{"title":"Antibodies","description":"\u003cp\u003e\u003cspan style=\"font-family: -apple-system, BlinkMacSystemFont, 'San Francisco', 'Segoe UI', Roboto, 'Helvetica Neue', sans-serif; font-size: 1.2em;\"\u003eMD Bioproducts has built its reputation over 30 years by supplying quality antibodies and antigens for research. Our proprietary products have been cited in thousands of publications and are used in all leading academic and industrial laboratories. Our products are manufactured to the highest degree of consistency with well established processes. \u003c\/span\u003e\u003ca href=\"https:\/\/mdbioproducts.myshopify.com\/pages\/contact-us\" style=\"font-family: -apple-system, BlinkMacSystemFont, 'San Francisco', 'Segoe UI', Roboto, 'Helvetica Neue', sans-serif; font-size: 1.2em;\"\u003eTalk to us\u003c\/a\u003e\u003cspan style=\"font-family: -apple-system, BlinkMacSystemFont, 'San Francisco', 'Segoe UI', Roboto, 'Helvetica Neue', sans-serif; font-size: 1.2em;\"\u003e about products that you would like to see on this list.\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv aria-hidden=\"true\" id=\"_IgbUYJ-LKZS4tQbohYHYCg31\" aria-labelledby=\"_IgbUYJ-LKZS4tQbohYHYCg32\" class=\"gy6Qzb S8PBwe\" data-mce-fragment=\"1\" jsaction=\"CQwlrf\" jsslot=\"\" jsname=\"dcydfb\"\u003e\n\u003cdiv data-mce-fragment=\"1\"\u003e\n\u003cdiv data-ved=\"2ahUKEwifpPrUs6_xAhUUXM0KHehCAKsQu04oAXoECAkQCg\" data-hveid=\"CAkQCg\" id=\"_IgbUYJ-LKZS4tQbohYHYCg33\" class=\"y8URue\" data-mce-fragment=\"1\" jsname=\"oQYOj\"\u003e\n\u003cdiv class=\"VWE0hc\" data-mce-fragment=\"1\"\u003e\n\u003cdiv id=\"6\" data-mce-fragment=\"1\"\u003e\n\u003cdiv class=\"g\" data-mce-fragment=\"1\"\u003e\n\u003cdiv data-ved=\"2ahUKEwifpPrUs6_xAhUUXM0KHehCAKsQFSgAMAJ6BAgIEAA\" data-hveid=\"CAgQAA\" data-mce-fragment=\"1\"\u003e\n\u003cdiv class=\"tF2Cxc\" data-mce-fragment=\"1\"\u003e\n\u003cdiv class=\"yuRUbf\" data-mce-fragment=\"1\"\u003e\n\u003cdiv class=\"B6fmyf\" data-mce-fragment=\"1\"\u003e\n\u003cdiv class=\"eFM0qc\" data-mce-fragment=\"1\"\u003e\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e","products":[{"product_id":"aggrecan-antibody-c-terminal-neoepitope-nitege","title":"Aggrecan Antibody, C-terminal neoepitope NITEGE, 100 ug","description":"\u003cp\u003eAggrecan monoclonal antibody to C-terminal neoepitope NITEGE (mouse, clone BC-13). This aggrecan degradation product usually remains within the tissue still complexed to hyaluronan and link protein. Its release from the cartilage usually signals that there has been extensive catabolism of aggrecan, which allows large complexes containing this metabolite to be released from the tissue.\u003c\/p\u003e\n\u003cp\u003eAggrecan is a member of a family of large, aggregating proteoglycans (also including versican, brevican and neurocan) which is found in articular cartilage. Aggrecan is composed of three major domains: G1, G2, and G3.\u003c\/p\u003e\n\u003cp\u003eBetween the G1 and G2 domains there is an interglobulin region (IGD). The IGD region is the major site of cleavage by specific proteases like metalloproteinases (MMPs) and aggrecanase. Aggrecan cleavage has been associated with a number of degenerative diseases including rheumatoid arthritis and osteoarthritis. There is evidence that this family of proteoglycans modulates cell adhesion, migration, and axonal outgrowth in the CNS. \u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cmeta charset=\"UTF-8\"\u003e\u003cspan\u003eXue, C., Tian, J., Cui, Z., Liu, Y., Sun, D., Xiong, M., Yi, N., Wang, K., Li, X., Wang, Y., Xu, H., Zhang, W., \u0026amp; Liang, Q. (2023). Reactive oxygen species (ROS)-mediated M1 macrophage-dependent nanomedicine remodels inflammatory microenvironment for osteoarthritis recession. \u003c\/span\u003e\u003ci\u003eBioactive materials\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e33\u003c\/i\u003e\u003cspan\u003e, 545–561. https:\/\/doi.org\/10.1016\/j.bioactmat.2023.10.032\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cmeta charset=\"UTF-8\"\u003e\u003cspan\u003eCaxaria, S., Kouvatsos, N., Eldridge, S. E., Alvarez-Fallas, M., Thorup, A. S., Cici, D., Barawi, A., Arshed, A., Strachan, D., Carletti, G., Huang, X., Bharde, S., Deniz, M., Wilson, J., Thomas, B. L., Pitzalis, C., Cantatore, F. P., Sayilekshmy, M., Sikandar, S., Luyten, F. P., … Dell'Accio, F. (2023). Disease modification and symptom relief in osteoarthritis using a mutated GCP-2\/CXCL6 chemokine. \u003c\/span\u003e\u003ci\u003eEMBO molecular medicine\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e15\u003c\/i\u003e\u003cspan\u003e(1), e16218.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eKang, D., Lee, J., Jung, J., Carlson, B. A., Chang, M. J., Chang, C. B., ... \u0026amp; Kim, J. H. (2022). Selenophosphate synthetase 1 deficiency exacerbates osteoarthritis by dysregulating redox homeostasis. \u003cem\u003eNature Communications\u003c\/em\u003e, \u003cem\u003e13\u003c\/em\u003e(1), 1-14.\u003c\/p\u003e\n\u003cp\u003eCollins, A.T., Hu, G., Newman, H. et al. Obesity alters the collagen organization and mechanical properties of murine cartilage. Sci Rep 11, 1626 (2021).\u003cbr\u003e\u003cbr\u003eAshinsky, B. G., Gullbrand, S. E., Bonnevie, E. D., Mandalapu, S. A., Wang, C., Elliott, D. M., ... \u0026amp; Smith, H. E. (2019). Multiscale and multimodal structure–function analysis of intervertebral disc degeneration in a rabbit model. Osteoarthritis and Cartilage, 27(12), 1860-1869.\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eMori, Y., Saito, T., Chang, S. H., Kobayashi, H., Ladel, C. H., Guehring, H., ... \u0026amp; Kawaguchi, H. (2014). Identification of fibroblast growth factor-18 as a molecule to protect adult articular cartilage by gene expression profiling. \u003c\/span\u003e\u003ci\u003eJournal of Biological Chemistry\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e289\u003c\/i\u003e\u003cspan\u003e(14), 10192-10200.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eStanton, H., Golub, S. B., Rogerson, F. M., Last, K., Little, C. B., \u0026amp; Fosang, A. J. (2011). Investigating ADAMTS-mediated aggrecanolysis in mouse cartilage. \u003c\/span\u003e\u003ci\u003eNature protocols\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e6\u003c\/i\u003e\u003cspan\u003e(3), 388-404.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eLittle, C. B., Hughes, C. E., Curtis, C. L., Janusz, M. J., Bohne, R., Wang-Weigand, S., ... \u0026amp; Caterson, B. (2002). Matrix metalloproteinases are involved in C-terminal and interglobular domain processing of cartilage aggrecan in late stage cartilage degradation. \u003c\/span\u003e\u003ci\u003eMatrix biology\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e21\u003c\/i\u003e\u003cspan\u003e(3), 271-288.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eCaterson, B., Flannery, C. R., Hughes, C. E., \u0026amp; Little, C. B. (2000). Mechanisms involved in cartilage proteoglycan catabolism. \u003c\/span\u003e\u003ci\u003eMatrix Biology\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e19\u003c\/i\u003e\u003cspan\u003e(4), 333-344.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39913602908349,"sku":"1042003","price":440.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Aggrecan_Antibody_C_Terminal_Neoepitope_NITEGE.png?v=1718876004"},{"product_id":"aggrecan-antibody-n-terminal-neoepitope-arg","title":"Aggrecan Antibody, N-terminal neoepitope ARG, 100 ug","description":"\u003cp\u003eAggrecan monoclonal antibody to N-terminal neoepitope ARG (mouse, clone BC-3).  Aggrecan degradation products containing this neoepitope are rapidly released from the tissue in model explant culture systems and are also present in the synovial fluids of patients with degenerative joint disease. \u003c\/p\u003e\n\u003cp\u003eDuring differentiation of neural precursor cells, neurospheres downregulate Chondroitin sulfate proteoglycans (CSPGs). Proliferating neural precursors synthesize lecticans, including aggrecan, which are downregulated with differentiation; suggesting a link between CSPGs and CNS precursor biology.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong style=\"box-sizing: border-box; font-weight: bold; caret-color: #000000; color: #000000; font-family: 'red Hat Display', sans-serif; font-size: 18px; font-style: normal; font-variant-caps: normal; letter-spacing: normal; orphans: auto; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; widows: auto; word-spacing: 0px; -webkit-text-size-adjust: auto; -webkit-text-stroke-width: 0px; text-decoration: none;\" data-mce-style=\"box-sizing: border-box; font-weight: bold; caret-color: #000000; color: #000000; font-family: 'red Hat Display', sans-serif; font-size: 18px; font-style: normal; font-variant-caps: normal; letter-spacing: normal; orphans: auto; text-align: start; text-indent: 0px; text-transform: none; white-space: normal; widows: auto; word-spacing: 0px; -webkit-text-size-adjust: auto; -webkit-text-stroke-width: 0px; text-decoration: none;\"\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eClement-Lacroix, P., Little, C. B., Smith, M. M., Cottereaux, C., Merciris, D., Meurisse, S., ... \u0026amp; Amantini, D. (2022). Pharmacological characterization of GLPG1972\/S201086, a potent and selective small-molecule inhibitor of ADAMTS5. \u003cem\u003eOsteoarthritis and Cartilage\u003c\/em\u003e, \u003cem\u003e30\u003c\/em\u003e(2), 291-301.\u003c\/p\u003e\n\u003cp\u003eBrebion, F., Gosmini, R., Deprez, P., Varin, M., Peixoto, C., Alvey, L., ... \u0026amp; Amantini, D. (2021). Discovery of GLPG1972\/S201086, a Potent, Selective, and Orally Bioavailable ADAMTS-5 Inhibitor for the Treatment of Osteoarthritis. Journal of Medicinal Chemistry, 64(6), 2937-2952.\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003ePowell, A. J., Little, C. B., \u0026amp; Hughes, C. E. (2007). Low molecular weight isoforms of the aggrecanases are responsible for the cytokine‐induced proteolysis of aggrecan in a porcine chondrocyte culture system. \u003c\/span\u003e\u003ci\u003eArthritis \u0026amp; Rheumatism: Official Journal of the American College of Rheumatology\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e56\u003c\/i\u003e\u003cspan\u003e(9), 3010-3019.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eLittle, C. B., Hughes, C. E., Curtis, C. L., Janusz, M. J., Bohne, R., Wang-Weigand, S., ... \u0026amp; Caterson, B. (2002). Matrix metalloproteinases are involved in C-terminal and interglobular domain processing of cartilage aggrecan in late stage cartilage degradation. \u003c\/span\u003e\u003ci\u003eMatrix biology\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e21\u003c\/i\u003e\u003cspan\u003e(3), 271-288.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eCaterson, B., Flannery, C. R., Hughes, C. E., \u0026amp; Little, C. B. (2000). Mechanisms involved in cartilage proteoglycan catabolism. \u003c\/span\u003e\u003ci\u003eMatrix Biology\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e19\u003c\/i\u003e\u003cspan\u003e(4), 333-344.\u003c\/span\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39913605562557,"sku":"1042001","price":440.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Aggrecan_Antibody_N-terminal_Neoepitope_ARG.png?v=1719223028"},{"product_id":"aggrecan-antibody-n-terminal-neoepitope-dipen","title":"Aggrecan Antibody, N-terminal neoepitope DIPEN, 100ug","description":"\u003cp\u003eAggrecan monoclonal antibody to N-terminal neoepitope DIPEN (mouse, clone BC-4).\u003c\/p\u003e\n\u003cp\u003eProteoglycans are categorized depending upon the nature of their glycosaminoglycan chains (chondroitin sulfate, dermatan sulfate, heparin sulphate and keratin sulfate) as well as characterized by size.\u003c\/p\u003e\n\u003cp\u003eAggrecan is a large aggregating proteoglycan of articular cartilage. It is found also in aorta tissue, discs, tendons and in the perineuronal net. It is responsible for hydrating cartilage, giving it compressibility and resilience during joint loading, thereby playing a major role in the normal function of cartilage. Depletion of glycosaminoglycan bearing aggrecan fragments is one of the earliest events in cartilage destruction.\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cmeta charset=\"UTF-8\"\u003e\u003cspan\u003eBelliveau, C., Rahimian, R., Fakhfouri, G., Hosdey, C., Simard, S., Davoli, M. A., ... \u0026amp; Mechawar, N. (2024). Evidence of microglial involvement in the childhood abuse-associated increase in perineuronal nets in the ventromedial prefrontal cortex. \u003c\/span\u003e\u003ci\u003eBioRxiv\u003c\/i\u003e\u003cspan\u003e, 2024-03.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eDupuis, L. E., Nelson, E. L., Hozik, B., Porto, S. C., Rogers-DeCotes, A., Fosang, A., \u0026amp; Kern, C. B. (2019). Adamts5−\/− mice exhibit altered aggrecan proteolytic profiles that correlate with ascending aortic anomalies. Arteriosclerosis, Thrombosis, and Vascular Biology, 39(10), 2067-2081.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eTodorov, A., Kreutz, M., Haumer, A., Scotti, C., Barbero, A., Bourgine, P. E., ... \u0026amp; Martin, I. (2016). Fat-derived stromal vascular fraction cells enhance the bone-forming capacity of devitalized engineered hypertrophic cartilage matrix. \u003c\/span\u003e\u003ci\u003eStem cells translational medicine\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e5\u003c\/i\u003e\u003cspan\u003e(12), 1684-1694.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003ePeffers, M. J., Thornton, D. J., \u0026amp; Clegg, P. D. (2016). Characterization of neopeptides in equine articular cartilage degradation. \u003c\/span\u003e\u003ci\u003eJournal of Orthopaedic Research\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e34\u003c\/i\u003e\u003cspan\u003e(1), 106-120.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eMori, Y., Saito, T., Chang, S. H., Kobayashi, H., Ladel, C. H., Guehring, H., ... \u0026amp; Kawaguchi, H. (2014). Identification of fibroblast growth factor-18 as a molecule to protect adult articular cartilage by gene expression profiling. \u003c\/span\u003e\u003ci\u003eJournal of Biological Chemistry\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e289\u003c\/i\u003e\u003cspan\u003e(14), 10192-10200.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eRussell, T. M., \u0026amp; Johnson, B. J. (2013). L yme disease spirochaetes possess an aggrecan‐binding protease with aggrecanase activity. \u003c\/span\u003e\u003ci\u003eMolecular microbiology\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e90\u003c\/i\u003e\u003cspan\u003e(2), 228-240.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eScotti, C., Tonnarelli, B., Papadimitropoulos, A., Scherberich, A., Schaeren, S., Schauerte, A., ... \u0026amp; Martin, I. (2010). Recapitulation of endochondral bone formation using human adult mesenchymal stem cells as a paradigm for developmental engineering. \u003c\/span\u003e\u003ci\u003eProceedings of the National Academy of Sciences\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e107\u003c\/i\u003e\u003cspan\u003e(16), 7251-7256. \u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eSupporting Literature: \u003cspan\u003eChamberland, A., Wang, E., Jones, A. R., Collins-Racie, L. A., LaVallie, E. R., Huang, Y., ... \u0026amp; Yang, Z. (2009). Identification of a novel HtrA1-susceptible cleavage site in human aggrecan: evidence for the involvement of HtrA1 in aggrecan proteolysis in vivo. \u003c\/span\u003e\u003ci\u003eJournal of Biological Chemistry\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e284\u003c\/i\u003e\u003cspan\u003e(40), 27352-27359.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eLittle, C. B., Hughes, C. E., Curtis, C. L., Janusz, M. J., Bohne, R., Wang-Weigand, S., ... \u0026amp; Caterson, B. (2002). Matrix metalloproteinases are involved in C-terminal and interglobular domain processing of cartilage aggrecan in late stage cartilage degradation. \u003c\/span\u003e\u003ci\u003eMatrix biology\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e21\u003c\/i\u003e\u003cspan\u003e(3), 271-288.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eCaterson, B., Flannery, C. R., Hughes, C. E., \u0026amp; Little, C. B. (2000). Mechanisms involved in cartilage proteoglycan catabolism. \u003c\/span\u003e\u003ci\u003eMatrix Biology\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e19\u003c\/i\u003e\u003cspan\u003e(4), 333-344.\u003c\/span\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39913604972733,"sku":"1042002","price":440.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Aggrecan_Antibody_N-terminal_Neoepitope_DIPEN.png?v=1719223162"},{"product_id":"aggrecan-antibody-n-terminal-neoepitope-ffgv","title":"Aggrecan Antibody, N-terminal neoepitope FFGV, 100 ug","description":"\u003cp\u003eAggrecan monoclonal antibody to N-terminal neoepitope FFGV (mouse, clone BC14). This fragment is rapidly released from the tissue when MMP catabolism of aggrecan occurs and has been identified in synovial fluid samples from patients with degenerative joint diseases.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eProteoglycans are categorized depending upon the nature of their glycosaminoglycan chains (chondroitin sulfate, dermatan sulfate, heparan sulphate and keratan sulphate) as well as characterized by size.\u003c\/p\u003e\n\u003cp\u003eAggrecan is a large aggregating proteoglycan of articular cartilage. It is found also in aorta tissue, discs, tendons and in the perineuronal net. It is responsible for hydrating cartilage, giving it compressibility and resilience during joint loading, thereby playing a major role in the normal function of cartilage. Depletion of glycosaminoglycan bearing aggrecan fragments is one of the earliest events in cartilage destruction.\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848191262909,"sku":"1042004","price":440.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Aggrecan_Antibody_N-terminal_Neoepitope_FFGV.png?v=1719223332"},{"product_id":"aggrecan-igd-antibody","title":"Aggrecan IGD Antibody, 100 ug","description":"\u003cp\u003eAggrecan IGD monoclonal antibody (mouse, clone 6B4). This antibody detects aggrecan metabolites (intact or matrix protease-catabolised) in human synovial fluid samples.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eProteoglycans are categorized depending upon the nature of their glycosaminoglycan chains (chondroitin sulfate, dermatan sulfate, heparan sulphate and keratan sulfate) as well as characterized by size. \u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eAggrecan is a large aggregating proteoglycan of articular cartilage. It is also found in aorta tissue, discs, tendons and in the perineuronal net. It is responsible for hydrating cartilage, giving it compressibility and resilience during joint loading, thereby playing a major role in the normal function of cartilage. Depletion of glycosaminoglycan-bearing aggrecan fragments is one of the earliest events in cartilage destruction.\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848191295677,"sku":"1042005","price":440.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Aggrecan_IGD_Antibody.png?v=1719223443"},{"product_id":"cartilage-link-protein-antibody","title":"Cartilage Link Protein, Antibody, 100 ug","description":"\u003cp\u003eCartilage-link protein (HAPLN1) monoclonal antibody (clone 8A4). Cartilage-link protein (LP) is a glycoprotein present in cartilage that stabilizes the interaction of aggrecan (versican) with hyaluronic acid (HA) in large proteoglycan aggregates.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eRelated Terms\/Symbols:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eAnti-HAPLN1 antibody\u003c\/li\u003e\n\u003cli\u003eCRTL1\u003c\/li\u003e\n\u003cli\u003eHyaluronan and proteoglycan link protein 1\u003c\/li\u003e\n\u003cli\u003eLP\u003c\/li\u003e\n\u003cli\u003eProteoglycan link protein\u003c\/li\u003e\n\u003cli\u003eCartilage-linking protein 1\u003c\/li\u003e\n\u003cli\u003eHAPLN1 gene\u003c\/li\u003e\n\u003cli\u003eP10915\u003c\/li\u003e\n\u003c\/ul\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848191361213,"sku":"1042013","price":450.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Cartilage_Link_Protein_Antibody.png?v=1719224139"},{"product_id":"chondroitin-sulphate-neoepitope-antibody","title":"Chondroitin Sulphate Neoepitope Antibody, 100ug","description":"\u003cp\u003eChondroitin sulfate monoclonal antibody (mouse, clone 1B5) to detect the zero sulphated Chondroitin Sulphate stub neoepitope generated by chondroitinase ABC treatment.\u003c\/p\u003e\n\u003cp\u003eRecognizes unsaturated disaccharide of unsulfated chondroitin generated by chondroitinase ABC digestion.\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eA.J. Hayes et al. (2008) Methods 45:10–21\u003cbr\u003e \u003cbr\u003eCouchman JR, Caterson B, Christner JB, Baker JR (1984) Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues. Nature 307:650–652\u003cbr\u003e \u003cbr\u003eCaterson B, Christner JE, Baker JR, Couchman JR (1985) Production and characterization of monoclonal antibodies directed against connective tissue proteoglycans. Fed Proc 44:386–393\u003cbr\u003e \u003cbr\u003eAnthony J. Hayes, Amanda Hall, Liesbeth Brown, Ross Tubo, and Bruce Caterson (2007) Macromolecular Organization and In Vitro Growth Characteristics of Scaffold-free Neocartilage GraftsJournal of Histochemistry \u0026amp; Cytochemistry Volume 55(8): 853–866 \u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848191459517,"sku":"1042014","price":450.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Chondroitin_Sulphate_Neoepitope_Antibody.png?v=1719224250"},{"product_id":"chondroitinase-generated-c-4-s-ds-antibody","title":"Chondroitinase generated C-4-S \u0026 DS Antibody, 100ug","description":"\u003cp\u003eChondroitin-4-sulfate (C-4-S) monoclonal antibody that's also specific to dermatan-sulfate (DS) neoepitope (mouse, clone 2B6).\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eMonoclonal antibody to delta-unsaturated glucuronic acid adjacent to N-acetylgalactosamine- 4-sulphate in the non-reducing terminal dissacharide ÒstubÓ of 4-sulphated chondroitin sulfate that is produced after chondroitinase digestion of chondroitin-4- sulphate glycosaminoglycan chains (chondroitinase ABC or ACII) or dermatan sulphate glycosaminoglycan chains (chondroitinase ABC or chondroitinase B).\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003cstrong\u003eRelated Terms\/Symbols:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eChondroitin-4-sulfate\u003c\/li\u003e\n\u003cli\u003eC-4-S\u003c\/li\u003e\n\u003cli\u003eDermatan-sulfate\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cul\u003e\u003c\/ul\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cmeta charset=\"UTF-8\"\u003e\u003cspan\u003eBrown, D. M., Yu, J., Kumar, P., Paulus, Q. M., Kowalski, M. A., Patel, J. M., Kane, M. A., Ethier, C. R., \u0026amp; Pardue, M. T. (2023). Exogenous All-Trans Retinoic Acid Induces Myopia and Alters Scleral Biomechanics in Mice. \u003c\/span\u003e\u003ci\u003eInvestigative ophthalmology \u0026amp; visual science\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e64\u003c\/i\u003e\u003cspan\u003e(5), 22. https:\/\/doi.org\/10.1167\/iovs.64.5.22\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003eRees SG, Flannery CR, Little CB, Hughes CE, Caterson B \u0026amp; Dent CM (2000). Catabolism of aggrecan, decorin and biglycan in tendon. Biochem J. 350: 181-188. \u003cbr\u003e\u003cbr\u003eHayes AJ, Hall A, Brown L, Tubo R \u0026amp; Caterson B (2007). Macromolecular organization and in vitro growth characteristics of scaffold-free neocartilage grafts. J Histochem Cytochem. 55(8):853-66. \u003cbr\u003e\u003cbr\u003eHayes AJ, Hughes CE \u0026amp; Caterson B (2008). Antibodies and immunohistochemisrty in extracellular matrix research. Methods 45: 10-21 \u003cbr\u003e\u003cbr\u003eStefan Milz, Frank Regner, Reinhard Putz, and Michael Benjamin. Expression of a Wide Range of Extracellular Matrix Molecules in the Tendon and Trochlea of the Human Superior Oblique MuscleInvestigative Ophthalmology and Visual Science. 2002;43:1330-1334 \u003cbr\u003e\u003cbr\u003eHedlund, H, Hedbom, E, Heinegard, D, Mengarelli-Widholm, S, Reinholt, FP, Svensson, O. (1999) Association of the aggrecan keratan sulfate-rich region with collagen in bovine articular cartilage J Biol Chem 274,5777-5781\u003c\/p\u003e\n\u003cp\u003eCaterson, B, Christner, JE, Baker, JR, Couchman, JR. (1985) Production and character- ization of monoclonal antibodies directed against connective tissue proteoglycans Fed Proc 44,386-393 \u003cbr\u003e\u003cbr\u003eCouchman, J.R., Caterson, B., Christner, J.E. and Baker, J.R. (1984). Mapping by Monoclonal Antibody Detection of Glycosaminoglycans in Connective Tissues. Nature 307: 650-652\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848192835773,"sku":"1042009","price":480.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Chondroitinase_Generated_C-4-S_DS_Antibody.png?v=1719223757"},{"product_id":"collagen-type-i-antibody-anti-mouse","title":"Collagen Type I Antibody, anti-Mouse, 100 uL","description":"\u003cp\u003eCollagen type I polyclonal antibody (rabbit anti-mouse) purified from rabbits injected with type I collagen that was extracted\/purified from mouse skin. Purified, freeze-dried antibody in a 0.1 mL vial. \u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant form of collagen in the human body and is synthesized mainly by fibroblasts, osteoblasts, odontoblasts and chondroblasts. It is located in the extracellular matrix of many tissues of the body including cartilage, bone, tendon, skin and the sclera of the eye. Type I collagen is composed of two pro-_1(I) chains, produced from the COL1A1 gene, and one pro-_2(I) chain, produced from the COL1A2 gene. Mutations in the genes that produce collagen type I are responsible for causing various health conditions including Ehlers-Danlos syndrome, osteogenesis imperfecta, osteoporosis and Caffey disease.\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eBorza, C. M., Bolas, G., Bock, F., Zhang, X., Akabogu, F. C., Zhang, M. Z., ... \u0026amp; Pozzi, A. (2022). DDR1 contributes to kidney inflammation and fibrosis by promoting the phosphorylation of BCR and STAT3. \u003cem\u003eJCI insight\u003c\/em\u003e, \u003cem\u003e7\u003c\/em\u003e(3).\u003c\/p\u003e\n\u003cp\u003eLu, C. L., Cain, J., Brudvig, J., Ortmeier, S., Boyadjiev, S. A., Weimer, J. M., \u0026amp; Kim, J. (2021). Collagen has a unique SEC24 preference for efficient export from the endoplasmic reticulum. bioRxiv.\u003c\/p\u003e\n\u003cp\u003eBota-Rabassedas, N., Guo, H. F., Banerjee, P., Chen, Y., Terajima, M., Yamauchi, M., \u0026amp; Kurie, J. M. (2020). Use of osteoblast-derived matrix to assess the influence of collagen modifications on cancer cells. Matrix Biology Plus, 8, 100047.\u003cbr\u003e\u003cbr\u003eSaraswati, S., Lietman, C. D., Li, B., Mathew, S., Zent, R., \u0026amp; Young, P. P. (2020). Small proline-rich repeat 3 is a novel coordinator of PDGFRβ and integrin β1 crosstalk to augment proliferation and matrix synthesis by cardiac fibroblasts. The FASEB Journal.\u003cbr\u003e\u003cbr\u003eFeng, Y., Li, M., Wang, S., Cong, W., Hu, G., Song, Y., ... \u0026amp; Zhang, Y. (2020). Paired box 6 inhibits cardiac fibroblast differentiation. Biochemical and Biophysical Research Communications, 528(3), 561-566.\u003cbr\u003e\u003cbr\u003eSaraswati, S., Marrow, S. M., Watch, L. A., \u0026amp; Young, P. P. (2019). Identification of a pro-angiogenic functional role for FSP1-positive fibroblast subtype in wound healing. Nature Communications, 10(1), 1-16.\u003cbr\u003e\u003cbr\u003eNawaito, S. A., Sahadevan, P., Sahmi, F., Gaestel, M., Calderone, A., \u0026amp; Allen, B. G. (2019). Transcript levels for extracellular matrix proteins are altered in MK5-deficient cardiac ventricular fibroblasts. Journal of Molecular and Cellular Cardiology, 132, 164-177.\u003cbr\u003e\u003cbr\u003ePesevski, Z., Kvasilova, A., Stopkova, T., Nanka, O., Drobna Krejci, E., Buffinton, C., ... \u0026amp; Sedmera, D. (2018). Endocardial fibroelastosis is secondary to hemodynamic alterations in the chick embryonic model of hypoplastic left heart syndrome. Developmental Dynamics, 247(3), 509-520.\u003cbr\u003e\u003cbr\u003eSurinkaew, S., Aflaki, M., Takawale, A., Chen, Y., Qi, X. Y., Gillis, M. A., ... \u0026amp; Nattel, S. (2018). Exchange protein activated by cyclic-adenosine monophosphate (Epac) regulates atrial fibroblast function and controls cardiac remodelling. Cardiovascular research, 115(1), 94-106.\u003cbr\u003e\u003cbr\u003eViquez, O. M., Yazlovitskaya, E. M., Tu, T., Mernaugh, G., Secades, P., McKee, K. K., ... \u0026amp; Gewin, L. C. (2017). Integrin alpha6 maintains the structural integrity of the kidney collecting system. Matrix Biology, 57, 244-257.\u003cbr\u003e\u003cbr\u003eFeng, Y., Wang, S., Zhang, Y., \u0026amp; Xiao, H. (2017). Metformin attenuates renal fibrosis in both AMPK α2‐dependent and independent manners. Clinical and Experimental Pharmacology and Physiology, 44(6), 648-655.\u003cbr\u003e\u003cbr\u003eChen, X., \u0026amp; Thibeault, S. L. (2016). Cell–cell interaction between vocal fold fibroblasts and bone marrow mesenchymal stromal cells in three‐dimensional hyaluronan hydrogel. Journal of tissue engineering and regenerative medicine, 10(5), 437-446.\u003cbr\u003e\u003cbr\u003eDupuis, L. E., Doucette, L., Rice, A. K., Lancaster, A. E., Berger, M. G., Chakravarti, S., \u0026amp; Kern, C. B. (2016). Development of myotendinous‐like junctions that anchor cardiac valves requires fibromodulin and lumican. Developmental Dynamics, 245(10), 1029-1042.\u003cbr\u003e\u003cbr\u003eSeet, L. F., Toh, L. Z., Finger, S. N., Chu, S. W., Stefanovic, B., \u0026amp; Wong, T. T. (2016). Valproic acid suppresses collagen by selective regulation of Smads in conjunctival fibrosis. Journal of Molecular Medicine, 94(3), 321-334.\u003cbr\u003e\u003cbr\u003ePankova, D., Chen, Y., Terajima, M., Schliekelman, M. J., Baird, B. N., Fahrenholtz, M., ... \u0026amp; Ahn, Y. H. (2016). Cancer-associated fibroblasts induce a collagen cross-link switch in tumor stroma. Molecular Cancer Research, 14(3), 287-295.\u003cbr\u003e\u003cbr\u003eNeelisetty, S., Alford, C., Reynolds, K., Woodbury, L., Nlandu-khodo, S., Yang, H., ... \u0026amp; Gewin, L. (2015). Renal fibrosis is not reduced by blocking transforming growth factor-β signaling in matrix-producing interstitial cells. Kidney international, 88(3), 503-514.\u003cbr\u003e\u003cbr\u003eWang, H., Chen, X., Su, Y., Paueksakon, P., Hu, W., Zhang, M. Z., ... \u0026amp; Pozzi, A. (2015). p47phox contributes to albuminuria and kidney fibrosis in mice. Kidney international, 87(5), 948-962.\u003cbr\u003e\u003cbr\u003eSingh, S. P., Tao, S., Fields, T. A., Webb, S., Harris, R. C., \u0026amp; Rao, R. (2015). Glycogen synthase kinase-3 inhibition attenuates fibroblast activation and development of fibrosis following renal ischemia-reperfusion in mice. Disease models \u0026amp; mechanisms, 8(8), 931-940.\u003cbr\u003e\u003cbr\u003eTrombetta‐eSilva, J., Rosset, E. A., Hepfer, R. G., Wright, G. J., Baicu, C., Yao, H., \u0026amp; Bradshaw, A. D. (2015). Decreased Mechanical Strength and Collagen Content in SPARC‐Null Periodontal Ligament Is Reversed by Inhibition of Transglutaminase Activity. Journal of bone and mineral research, 30(10), 1914-1924.\u003cbr\u003e\u003cbr\u003eZhu, M., Tao, J., Vasievich, M. P., Wei, W., Zhu, G., Khoriaty, R. N., \u0026amp; Zhang, B. (2015). Neural tube opening and abnormal extraembryonic membrane development in SEC23A deficient mice. Scientific reports, 5, 15471.\u003cbr\u003e\u003cbr\u003eManley Jr, E., Perosky, J. E., Khoury, B. M., Reddy, A. B., Kozloff, K. M., \u0026amp; Alford, A. I. (2015). Thrombospondin-2 deficiency in growing mice alters bone collagen ultrastructure and leads to a brittle bone phenotype. Journal of Applied Physiology, 119(8), 872-881.\u003cbr\u003e\u003cbr\u003eSochman, J., Peregrin, J. H., Pavcnik, D., Uchida, B. T., Timmermans, H. A., Sedmera, D., ... \u0026amp; Rosch, J. (2014). Reverse endoventricular artificial obturator in tricuspid valve position. Experimental feasibility research study. Physiological research, 63(2), 157.\u003cbr\u003e\u003cbr\u003eBohuslavova, R., Kolar, F., Sedmera, D., Skvorova, L., Papousek, F., Neckar, J., \u0026amp; Pavlinkova, G. (2014). Partial deficiency of HIF-1α stimulates pathological cardiac changes in streptozotocin-induced diabetic mice. BMC endocrine disorders, 14(1), 11.\u003cbr\u003e\u003cbr\u003eChen, X., Wang, H., Liao, H. J., Hu, W., Gewin, L., Mernaugh, G., ... \u0026amp; Fässler, R. (2014). Integrin-mediated type II TGF-β receptor tyrosine dephosphorylation controls SMAD-dependent profibrotic signaling. The Journal of clinical investigation, 124(8), 3295-3310.\u003cbr\u003e\u003cbr\u003eZimmerman, K. A., Graham, L. V., Pallero, M. A., \u0026amp; Murphy-Ullrich, J. E. (2013). Calreticulin (CRT) regulates Transforming Growth Factor-β (TGF-β) stimulated extracellular matrix production. Journal of Biological Chemistry, jbc-M112.\u003cbr\u003e\u003cbr\u003eRosa, R. G., Akgul, Y., Joazeiro, P. P., \u0026amp; Mahendroo, M. (2012). Changes of large molecular weight hyaluronan and versican in the mouse pubic symphysis through pregnancy. Biology of reproduction, 86(2).\u003cbr\u003e\u003cbr\u003eBaicu, C. F., Zhang, Y., Van Laer, A. O., Renaud, L., Zile, M. R., \u0026amp; Bradshaw, A. D. (2012). Effects of the absence of procollagen C-endopeptidase enhancer-2 on myocardial collagen accumulation in chronic pressure overload. American Journal of Physiology-Heart and Circulatory Physiology, 303(2), H234.\u003cbr\u003e\u003cbr\u003eDawson, K., Wu, C. T., Qi, X. Y., \u0026amp; Nattel, S. (2012). Congestive heart failure effects on atrial fibroblast phenotype: differences between freshly-isolated and cultured cells. PLoS One, 7(12), e52032.\u003cbr\u003e\u003cbr\u003eChen, J., Chen, J. K., Nagai, K., Plieth, D., Tan, M., Lee, T. C., ... \u0026amp; Harris, R. C. (2012). EGFR signaling promotes TGFβ-dependent renal fibrosis. Journal of the American Society of Nephrology, 23(2), 215-224.\u003cbr\u003e\u003cbr\u003eDagher, P. C., Mai, E. M., Hato, T., Lee, S. Y., Anderson, M. D., Karozos, S. C., ... \u0026amp; Sutton, T. A. (2011). The p53 inhibitor pifithrin-α can stimulate fibrosis in a rat model of ischemic acute kidney injury. American Journal of Physiology-Renal Physiology, 302(2), F284-F291.\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eAkins, M. L., Luby-Phelps, K., Bank, R. A., \u0026amp; Mahendroo, M. (2011). Cervical softening during pregnancy: regulated changes in collagen cross-linking and composition of matricellular proteins in the mouse. \u003c\/span\u003e\u003ci\u003eBiology of reproduction\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e84\u003c\/i\u003e\u003cspan\u003e(5), 1053-1062.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eHarris, B. S., Zhang, Y., Card, L., Rivera, L. B., Brekken, R. A., \u0026amp; Bradshaw, A. D. (2011). SPARC regulates collagen interaction with cardiac fibroblast cell surfaces. \u003ci\u003eAmerican Journal of Physiology-Heart and Circulatory Physiology\u003c\/i\u003e, \u003ci\u003e301\u003c\/i\u003e(3), H841-H847.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan data-mce-fragment=\"1\"\u003eGraham, L. V. D., Sweetwyne, M. T., Pallero, M. A., \u0026amp; Murphy-Ullrich, J. E. (2010). Intracellular calreticulin regulates multiple steps in fibrillar collagen expression, trafficking, and processing into the extracellular matrix. \u003c\/span\u003e\u003ci data-mce-fragment=\"1\"\u003eJournal of Biological Chemistry\u003c\/i\u003e\u003cspan data-mce-fragment=\"1\"\u003e, \u003c\/span\u003e\u003ci data-mce-fragment=\"1\"\u003e285\u003c\/i\u003e\u003cspan data-mce-fragment=\"1\"\u003e(10), 7067-7078.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan data-mce-fragment=\"1\"\u003eHe, W., Wang, Y., Zhang, M. Z., You, L., Davis, L. S., Fan, H., ... \u0026amp; Hao, C. M. (2010). Sirt1 activation protects the mouse renal medulla from oxidative injury. \u003c\/span\u003e\u003ci data-mce-fragment=\"1\"\u003eThe Journal of clinical investigation\u003c\/i\u003e\u003cspan data-mce-fragment=\"1\"\u003e, \u003c\/span\u003e\u003ci data-mce-fragment=\"1\"\u003e120\u003c\/i\u003e\u003cspan data-mce-fragment=\"1\"\u003e(4), 1056-1068.\u003c\/span\u003e\u003cbr\u003e\u003cbr\u003e\u003cbr\u003eCervical Softening During Pregnancy: Regulated Changes in Collagen Cross-Linking and Composition of Matricellular Proteins in the Mouse.Meredith L. Akins, Katherine Luby-Phelps, Ruud A. Bank, and Mala Mahendroo Biol Reprod, May 2011; 84: 1053 - 1062Intracellular Calreticulin Regulates Multiple Steps in Fibrillar Collagen Expression, Trafficking, and Processing into the Extracellular Matrix\u003cbr\u003eLauren Van Duyn Graham, et al. J. Biol. Chem., Mar 2010; 285: 7067 - 7078.Sirt1 activation protects the mouse renal medulla from oxidative injury.\u003cbr\u003eHe W, et al. J Clin Invest. 2010 Apr; 120(4):1056-68.Type XIV collagen regulates fibrillogenesis: premature collagen fibril growth and tissue dysfunction in null mice.\u003cbr\u003eAnsorge HL, et al. J Biol Chem. Mar 2009; 284(13): 8427-38.SPARC Regulates Processing of Procollagen I and Collagen Fibrillogenesis in Dermal Fibroblasts\u003cbr\u003eTyler J. Rentz et al., J. Biol. Chem., Jul 2007; 282: 22062 - 22071. \u003cbr\u003eThe Calreticulin-Binding Sequence of Thrombospondin 1 Regulates Collagen Expression and Organization During Tissue Remodeling\u003cbr\u003eMariya T. Sweetwyne, Manuel A. Pallero, Ailing Lu, Lauren Van Duyn Graham, and Joanne E. Murphy-Ullrich\u003cbr\u003eAm. J. Pathol., Oct 2010; 177: 1710 - 1724.\u003cbr\u003e\u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848193851581,"sku":"203002-1","price":790.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_Antibody_Anti-Mouse.png?v=1719222562"},{"product_id":"collagen-type-i-antibody-anti-rat","title":"Collagen Type I Antibody, anti-Rat, 100 uL","description":"\u003cp\u003eCollagen type I polyclonal antibody (rabbit anti-rat) purified from rabbits injected with type I collagen that was extracted\/purified from rat skin. \u003cmeta charset=\"utf-8\"\u003e\u003cspan data-mce-fragment=\"1\"\u003eIgG fraction, freeze-dried (0.5 ml). Reconstitute with 0.5 ml di H2O and store aliquots at -20°C.\u003c\/span\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant form of collagen in the human body and is synthesized mainly by fibroblasts, osteoblasts, odontoblasts and chondroblasts. It is located in the extracellular matrix of many tissues of the body including cartilage, bone, tendon, skin and the sclera of the eye. Type I collagen is composed of two pro-_1(I) chains, produced from the COL1A1 gene, and one pro-_2(I) chain, produced from the COL1A2 gene. Mutations in the genes that produce collagen type I are responsible for causing various health conditions including Ehlers-Danlos syndrome, osteogenesis imperfecta, osteoporosis and Caffey disease.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003c\/strong\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eDagher, P. C., Hato, T., Mang, H. E., Plotkin, Z., Richardson, Q. V., Massad, M., ... \u0026amp; Sutton, T. A. (2016). Inhibition of toll-like receptor 4 signaling mitigates microvascular loss but not fibrosis in a model of ischemic acute kidney injury. International journal of molecular sciences, 17(5), 647.\u003cbr\u003e \u003cbr\u003eSutton, T. A., Hato, T., Mai, E., Yoshimoto, M., Kuehl, S., Anderson, M., ... \u0026amp; Dagher, P. C. (2013). p53 is renoprotective after ischemic kidney injury by reducing inflammation. Journal of the American Society of Nephrology, 24(1), 113-124.\u003cbr\u003e \u003cbr\u003eDagher, P. C., Mai, E. M., Hato, T., Lee, S. Y., Anderson, M. D., Karozos, S. C., ... \u0026amp; Sutton, T. A. (2011). The p53 inhibitor pifithrin-α can stimulate fibrosis in a rat model of ischemic acute kidney injury. American Journal of Physiology-Renal Physiology, 302(2), F284-F291.\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848193884349,"sku":"203004-1","price":790.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_Antibody_Anti-Rat.png?v=1719222780"},{"product_id":"collagen-type-ii-antibody-anti-human","title":"Collagen Type II Antibody, anti-Human, 100 uL","description":"\u003cp\u003eCollagen Type II polyclonal antibody (rabbit anti-human) purified from rabbits injected with type II collagen that was extracted\/purified from human cartilage. IgG fraction, freeze-dried (0.5 ml).\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eType II collagen (CII) is a fibrillar collagen that is primarily located in cartilage tissue. The major molecular form of collagen in cartilage is type II collagen. Type II collagen is also located in the vitreous humor of the eye, the inner ear, the nose, and the intervertebral discs of the spine. The function of type II collagen is to provide tensile strength to the matrix and give cartilage the ability to resist shearing forces. Mutations of the COL2A1 gene affect the synthesis of type II collagen and cause chondrodysplasias. This is characterized by abnormal cartilage that leads to bone and joint deformities. The degradation of collagen type II is an early indicator of osteoarthritis.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003c\/strong\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eHoffman, J. K., Geraghty, S., \u0026amp; Protzman, N. M. (2015). Articular cartilage repair using marrow stimulation augmented with a viable chondral allograft: 9-month postoperative histological evaluation. Case reports in orthopedics, 2015.\u003cbr\u003e\u003cbr\u003eYadav, V., Sun, L., Panilaitis, B., \u0026amp; Kaplan, D. L. (2015). In vitro chondrogenesis with lysozyme susceptible bacterial cellulose as a scaffold. Journal of tissue engineering and regenerative medicine, 9(12), E276-E288.\u003cbr\u003e\u003cbr\u003eSutton, T. A., Hato, T., Mai, E., Yoshimoto, M., Kuehl, S., Anderson, M., ... \u0026amp; Dagher, P. C. (2013). p53 is renoprotective after ischemic kidney injury by reducing inflammation. Journal of the American Society of Nephrology, 24(1), 113-124.\u003cbr\u003e\u003cbr\u003eDagher, P. C., Mai, E. M., Hato, T., Lee, S. Y., Anderson, M. D., Karozos, S. C., ... \u0026amp; Sutton, T. A. (2011). The p53 inhibitor pifithrin-α can stimulate fibrosis in a rat model of ischemic acute kidney injury. American Journal of Physiology-Renal Physiology, 302(2), F284-F291.\u003cbr\u003e\u003cbr\u003eDynamic compression can inhibit chondrogenesis of mesenchymal stem cells.\u003cbr\u003eThorpe SD, et al. Biochem Biophys Res Commun. 2008 Dec; 377(2): 458-62.\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848194277565,"sku":"203001-1","price":790.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_II_Antibody_Anti-Human.png?v=1719222450"},{"product_id":"collagen-type-iv-antibody-anti-mouse","title":"Collagen Type IV Antibody, anti-Mouse, 100 uL","description":"\u003cp\u003eCollagen Type IV polyclonal antibody (rabbit anti-mouse) purified from rabbits injected with type IV collagen that was extracted\/purified from mouse tumor tissues. \u003cmeta charset=\"utf-8\"\u003e\u003cspan data-mce-fragment=\"1\"\u003eIgG fraction, freeze-dried (0.5 ml)\u003c\/span\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eType IV collagen (CIV) is a major structural component of the basal lamina that assembles as a sheetlike network in the underlying extracellular space of all epithelial cells and tubes. The basal lamina separates the epithelia from the underlying connective tissue. There are several different isoforms of type IV collagen, but all are composed in a triple helical structure. The different isoforms are synthesized from six genes: COL4A1, COL4A2, COL4A3, COL4A4, COL4A5 and COL4A6. Type 1V collagens are considerably more flexible than the fibrillar type collagens. Mutations in genes associated with type IV collagen are associated with Alport and Goodpasture syndrome.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations: \u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eLu, C. L., Ortmeier, S., Brudvig, J., Moretti, T., Cain, J., Boyadjiev, S. A., ... \u0026amp; Kim, J. (2022). Collagen has a unique SEC24 preference for efficient export from the endoplasmic reticulum. \u003cem\u003eTraffic\u003c\/em\u003e, \u003cem\u003e23\u003c\/em\u003e(1), 81-93.\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eBelle, M., Godefroy, D., Couly, G., Malone, S. A., Collier, F., Giacobini, P., \u0026amp; Chédotal, A. (2017). Tridimensional visualization and analysis of early human development. \u003c\/span\u003e\u003ci\u003eCell\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e169\u003c\/i\u003e\u003cspan\u003e(1), 161-173.\u003c\/span\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848196014269,"sku":"203003-1","price":790.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_IV_Antibody_Anti-Mouse.png?v=1719222683"},{"product_id":"collagen-type-iv-antibody-anti-rat","title":"Collagen Type IV Antibody, anti-Rat,  100 uL","description":"\u003cp\u003eAffinity chromatography purified rabbit antibody to rat type IV collagen extracted, purified from rodent tumor tissues.\u003c\/p\u003e\n\u003cp\u003ePurified, freeze-dried (0.5 ml). Reconstitute with 0.5 ml di H2O. Type IV collagen (CIV) is a major structural component of the basal lamina that assembles as a sheetlike network in the underlying extracellular space of all epithelial cells and tubes. The basal lamina separates the epithelia from the underlying connective tissue. There are several different isoforms of type IV collagen, but all are composed in a triple helical structure. The different isoforms are synthesized from six genes: COL4A1, COL4A2, COL4A3, COL4A4, COL4A5 and COL4A6. Type 1V collagens are considerably more flexible than the fibrillar type collagens. Mutations in genes associated with type IV collagen are associated with Alport and Goodpasture syndrome.\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848196079805,"sku":"203005-1","price":790.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_IV_Antibody_Anti-Rat.png?v=1719222893"},{"product_id":"goat-anti-mouse-igd-antiserum","title":"Goat anti-Mouse IgD, Antiserum, 1 mL","description":"\u003cp\u003eImmunoglobulin D activator for B-cells. Preservative-free for in vivo application.\u003c\/p\u003e\n\u003cp\u003eImmunoglobulin D (IgD) is an antibody isotype that is found primarily on mature B-cells as part of the B-cell receptor (BCR) complex. Clustering of the BCR due to antigen binding leads to activation of B-cells that can result in a number of outcomes including proliferation, differentiation, and tolerance.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eThe ability to activate B-lymphocytes using polyclonal antisera recognizing anti-IgD is useful for the study of B-cell function (Finkelman, et al., 1985; Nguyen, et al., 2014). Anti-IgD is particularly suited for this application because soluble IgD is present in extremely low levels in serum (\u0026lt;0.25% of total immunoglobulin) and will not interfere with B-cell activation in a whole blood-based or in vivo setting. (In contrast, high levels of circulating IgM will typically block B-cell activation by anti-IgM in whole blood.) Such a methodology can be used to rapidly test the efficacy of B-cell inhibitory agents in a cellular, ex vivo, or in vivo context (Coffey, et al., 2012).\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eLee, S., Yang, J. I., Lee, J. H., Lee, H. W., \u0026amp; Kim, T. J. (2022). Low-Level Expression of CD138 Marks Naturally Arising Anergic B Cells. Immune Network, 22.\u003c\/p\u003e\n\u003cp\u003eBame, E., Tang, H., Burns, J. C., Arefayene, M., Michelsen, K., Ma, B., ... \u0026amp; Mingueneau, M. (2021). Next-generation Bruton's tyrosine kinase inhibitor BIIB091 selectively and potently inhibits B cell and Fc receptor signaling and downstream functions in B cells and myeloid cells. Clinical \u0026amp; translational immunology, 10(6), e1295.\u003c\/p\u003e\n\u003cp\u003eAlvarenga, I. C. (2021). Extrusion process to retain resistant starch in a pet food for the purpose of altering colonic fermentation end products that benefit dog health (Doctoral dissertation, Kansas State University).\u003c\/p\u003e\n\u003cp\u003eTan, C., Hiwa, R., Mueller, J. L., Vykunta, V., Hibiya, K., Noviski, M., ... \u0026amp; Li, Z. (2020). A negative feedback loop mediated by the NR4A family of nuclear hormone receptors restrains expansion of B cells that receive signal one in the absence of signal two. bioRxiv.\u003cbr\u003e \u003cbr\u003eRip, J., de Bruijn, M. J., Kaptein, A., Hendriks, R. W., \u0026amp; Corneth, O. B. (2020). Phosphoflow Protocol for Signaling Studies in Human and Murine B Cell Subpopulations. The Journal of Immunology.\u003cbr\u003e \u003cbr\u003eNoviski, M., Mueller, J. L., Satterthwaite, A., Garrett-Sinha, L. A., Brombacher, F., \u0026amp; Zikherman, J. (2018). IgM and IgD B cell receptors differentially respond to endogenous antigens and control B cell fate. eLife, 7, e35074\u003cbr\u003e \u003cbr\u003eNguyen, T., \u0026amp; Morris J. (2014). Signals from activation of B-cell receptor with anti-IgD can override the stimulatory effects of excess BAFF on mature B cells in vivo. Immunology Lett., 161(1), 157-164.\u003cbr\u003e \u003cbr\u003eCoffey, G., DeGuzman, F., Inagaki, M., Pak, Y., Delaney, S., Ives, D., Betz, A., Jia, Z., Pandey, A., Baker, D., Hollenbach, S., Phillips, D., \u0026amp; Sinha, U. (2012). Specific Inhibition of Spleen Tyrosine Kinase Suppresses Leukocyte Immune Function and Inflammation in Animal Models of Rheumatoid Arthritis. J. Pharm. and Exp. Therapeutics., 340(2), 350-359.\u003cbr\u003e \u003cbr\u003eFinkelman, F., Smith, J., Villacreses, N., \u0026amp; Metcalf, E. (1985). Polyclonal activation of the murine immune system by an antibody to IgD. VI. Influence of doses of goat anti-mouse delta chain and normal goat IgG on B lymphocyte proliferation and differentiation. Eur J Immunol., 15(4), 315-320.\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848196702397,"sku":"2057001","price":390.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Goat_Anti_Mouse_IgD_Antiserum.png?v=1719322671"},{"product_id":"hyaluronic-acid-binding-region-antibody","title":"Hyaluronic Acid Binding Region, Antibody, 100 ug","description":"\u003cp\u003eHyaluronic acid binding region (HABR), clone 1C6, monoclonal antibody is used to detect the HA-binding region of Aggrecan. Clear liquidy, 0.1 mg\/mL.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e\n","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848196735165,"sku":"1042012","price":440.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Hyaluronic_Acid_Binding_Region_Antibody.png?v=1719224044"},{"product_id":"keratan-sulfate-antibody","title":"Keratan Sulfate Antibody, 100 ug","description":"\u003cp\u003eKeratan sulfate (KS) monoclonal antibody (mouse, clone 5D4) used to detect KS type I epitopes and KS type II epitopes. Liquid. Store at \u003cmeta charset=\"utf-8\"\u003e\u003cspan data-mce-fragment=\"1\"\u003e-20° C.\u003c\/span\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eKeratan Sulfate (KS) is a proteoglycan found in cornea (KS type I), cartilage and bone (KS type II). ItÕs KS chains are attached to extracellular matrix proteins or core proteins, which include lumican, keratocan, mimecan, fibromodulin, PRELP, osteoaheran and aggrecan. In the joints, keratan sulfate acts as a cushion to protect against mechanical shock. This monoclonal antibody has been raised against sulfated oligosaccharide present in corneal (KS I) and skeletal keratan sulfate (KS II).\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eRelated Terms\/Symbols:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eKeratan sulfate proteoglycans\u003c\/li\u003e\n\u003cli\u003eKS\u003c\/li\u003e\n\u003cli\u003eKS Type I\u003c\/li\u003e\n\u003cli\u003eKS Type II\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eCaterson B, Christner JE \u0026amp; Baker JR (1983). Identification of a monoclonal antibody that specifically recognizes corneal and skeletal keratan sulfate. Monoclonal antibod- ies to cartilage proteoglycan. J Biol Chem. 258(14): 8848-54. \u003cbr\u003e \u003cbr\u003eThonar EJ, Lenz ME, Klintworth GK, Caterson B, Pachman LM, Glickman P, Katz R, Huff J \u0026amp; Kuettner KE (1985). Quantification of keratan sulfate in blood as a marker of cartilage catabolism. Arthritis \u0026amp; Rheum. 28(12): 1367-76. \u003cbr\u003e \u003cbr\u003eMehmet H, Scudder P, Tang PW, Hounsell EF, Caterson B \u0026amp; Feizi T (1986). The anti- genic determinants recognized by three monoclonal antibodies to keratan sulphate involve sulphated hepta- or larger oligosaccharides of the poly(N-acetyllactosamine) series. Eur J Biochem. 157(2): 385-91. \u003cbr\u003e \u003cbr\u003eFunderburgh JL, Caterson B \u0026amp; Conrad GW (1987). Distribution of proteoglycans antigenically related to corneal keratan sulfate proteoglycan. J Biol Chem. 262(24):11634-40. \u003cbr\u003e \u003cbr\u003eRees SG, Flannery CR, Little CB, Hughes CE, Caterson B \u0026amp; Dent CM (2000). Catabolism of aggrecan, decorin and biglycan in tendon. Biochem J. 350: 181-188. \u003cbr\u003e \u003cbr\u003eYoung RD, Akama TO, Liskova P, Ebenezer ND, Allan B, Kerr B, Caterson B, Fukuda MN, Quantock AJ (2007a). Differential immunogold localisation of sulphated and unsul- phated keratan sulphate proteoglycans in normal and macular dystrophy cornea using sulphation motif-specific antibodies. Histochem Cell Biol. 127(1):115-20 \u003cbr\u003e \u003cbr\u003eYoung RD, Gealy EC, Liles M, Caterson B, Ralphs JR \u0026amp; Quantock AJ (2007b). Keratan sulfate glycosaminoglycan and the association with collagen fibrils in rudimen- tary lamellae in the developing avian cornea. Invest Ophthalmol Vis Sci. 2007 Jul;48(7):3083-8. \u003cbr\u003e \u003cbr\u003eHayes AJ, Hall A, Brown L, Tubo R \u0026amp; Caterson B (2007). Macromolecular organization and in vitro growth characteristics of scaffold-free neocartilage grafts. J Histochem Cytochem. 55(8):853-66. \u003cbr\u003e \u003cbr\u003eHayes AJ, Hughes CE \u0026amp; Caterson B (2008). Antibodies and immunohistochemisrty in extracellular matrix research. Methods 45: 10-21\u003c\/p\u003e\n","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848196866237,"sku":"1042010","price":440.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Keratan_Sulfate_Antibody.png?v=1719223853"},{"product_id":"keratocan-antibody","title":"Keratocan Antibody, 100 ug","description":"\u003cp\u003eKeratocan (KERA) monoclonal antibody (mouse, clone Ker-1) to detect keratocan. 1 mL\/vial. Concentration is 0.1 mg\/mL. \u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eNormal keratocan expression in adult tissues is limited to the corneal stroma and is considered a phenotypic marker for keratocytes. In keratocan knockout mice (Kera-\/-) the corneal stroma is thinner, the cornea-iris angles are narrower and the collagen fibers of the corneal stroma are disorganized when compared to wild-type animals. In humans, mutations of the keratocan gene (KERA) are associated with the human disease called Cornea plana (CNA2). This disease is characterized by a flattening of the forward convex curvature of the cornea and has been associated with glaucoma. Ultimately, this leads to a decrease in light refraction. Present research is focused on using adult stem cells to regenerate tissue and corneal transparency within knockout mice. Additionally, understanding keratocan in the corneal inflammatory response is a topic of interest.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eRelated Terms\/Symbols:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eKERA\u003c\/li\u003e\n\u003cli\u003eCNA2\u003c\/li\u003e\n\u003cli\u003eKeratan sulfate proteoglycans (KSPGs)\u003c\/li\u003e\n\u003cli\u003eO60938\u003c\/li\u003e\n\u003cli\u003eKTN\u003c\/li\u003e\n\u003cli\u003eSLRR2B\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eImmunolocalisation and expression of keratocan in tendon. Rees SG, Waggett AD, Kerr BC, Probert J, Gealy EC, Dent CM, Caterson B, Hughes CE. (2008) Osteoarthritis Cartilage. \u003cbr\u003e \u003cbr\u003eFragmentation of decorin, biglycan, lumican and keratocan is elevated in degener- ate human meniscus, knee and hip articular cartilages compared with age-matched macroscopically normal and control tissues. Melrose J, Fuller ES, Roughley PJ, Smith MM, Kerr B, Hughes CE, Caterson B, Little CB. (2008) Arthritis Res Ther. 10(4):R79. \u003cbr\u003e \u003cbr\u003eDifferential expression of the keratan sulphate proteoglycan, keratocan, during chick corneal embryogenesis. Gealy EC, Kerr BC, Young RD, Tudor D, Hayes AJ, Hughes CE, Caterson B, Quantock AJ, Ralphs JR. (2007) Histochem Cell Biol. Dec;128(6):551-5.\u003c\/p\u003e\n","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848196899005,"sku":"1042008","price":440.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Keratocan_Antibody.png?v=1719223610"},{"product_id":"lubricin-antibody-bovine","title":"Lubricin Antibody, Bovine, 100 ug","description":"\u003cp\u003eLubricin (PRG4) monoclonal antibody (mouse, clone 6A1) to detect superficial zone protein (SZP) from bovine articular cartilage and a non conformational epitope in the C terminus of lubricin. Clear-liquid. No preservatives. Concentration is 0.1 mg\/mL.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eLubricin is processed from the same gene as superficial zone protein, the proteoglycan 4 gene (PRG4). Lubricin is synthesized by synovial fibroblasts and secreted into the synovial fluid where its role is to regulate the lubrication of diarthrodial joints. Additionally, it is found in the meniscus, ligaments and tendons. Mutations in the lubricin gene are associated with camptodactyly-arthropathy-coxa vara-pericarditis syndrome.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eRelated Terms\/Symbols\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003ePRG4\u003c\/li\u003e\n\u003cli\u003eProteoglycan 4\u003c\/li\u003e\n\u003cli\u003eSZP\u003c\/li\u003e\n\u003cli\u003eArticular superficial zone protein\u003c\/li\u003e\n\u003cli\u003eMegakaryocyte stimulating factor\u003c\/li\u003e\n\u003cli\u003ePericarditis syndrome\u003c\/li\u003e\n\u003cli\u003eQ92954\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eSeol, D., McCabe, D. J., Choe, H., Zheng, H., Yu, Y., Jang, K., ... \u0026amp; Martin, J. A. (2012). Chondrogenic progenitor cells respond to cartilage injury. Arthritis \u0026amp; Rheumatism, 64(11), 3626-3637.\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848197030077,"sku":"1042015","price":440.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Lubricin_Antibody_Bovine.png?v=1719224337"},{"product_id":"lubricin-antibody-native-bovine","title":"Lubricin Antibody, Native Bovine, 100 ug","description":"\u003cp\u003eLubricin (PRG4) monoclonal antibody (mouse, clone 3A4) to detect the native form of bovine lubricin. \u003cmeta charset=\"utf-8\"\u003e\u003cspan data-mce-fragment=\"1\"\u003eDoes not recognize reduced or denatured lubricin.\u003c\/span\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eLubricin is processed from the same gene as superficial zone protein, the proteoglycan 4 gene (PRG4). Lubricin is synthesized by synovial fibroblasts and secreted into the synovial fluid where its role is to regulate the lubrication of diarthrodial joints. Additionally, it is found in the meniscus, ligaments and tendons of our body. Mutations in the lubricin gene are associated with camptodactyly-arthropathy-coxa vara-pericarditis syndrome.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eRelated Terms\/Symbols\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003ePRG4\u003c\/li\u003e\n\u003cli\u003eProteoglycan 4\u003c\/li\u003e\n\u003cli\u003eSZP\u003c\/li\u003e\n\u003cli\u003eArticular superficial zone protein\u003c\/li\u003e\n\u003cli\u003eMegakaryocyte stimulating factor\u003c\/li\u003e\n\u003cli\u003ePericarditis syndrome\u003c\/li\u003e\n\u003cli\u003eQ92954\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eWu, Y., Yang, Z., Denslin, V., Ren, X., Lee, C. S., Yap, F. L., \u0026amp; Lee, E. H. (2020). Repair of Osteochondral Defects With Predifferentiated Mesenchymal Stem Cells of Distinct Phenotypic Character Derived From a Nanotopographic Platform. The American Journal of Sports Medicine, 0363546520907137. \u003c\/p\u003e\n\u003cp\u003eParreno, J., Bianchi, V. J., Sermer, C., Regmi, S. C., Backstein, D., Schmidt, T. A., \u0026amp; Kandel, R. A. (2018). Adherent agarose mold cultures: An in vitro platform for multifactorial assessment of passaged chondrocyte redifferentiation. Journal of Orthopaedic Research®, 36(9), 2392-2405.\u003c\/p\u003e\n\u003cp\u003eWarnecke, D., Schild, N. B., Klose, S., Joos, H., Brenner, R. E., Kessler, O., ... \u0026amp; Dürselen, L. (2017). Friction properties of a new silk fibroin scaffold for meniscal replacement. Tribology international, 109, 586-592.\u003c\/p\u003e\n\u003cp\u003ePallante-Kichura, A. L., Chen, A. C., Temple-Wong, M. M., Bugbee, W. D., \u0026amp; Sah, R. L. (2013). In vivo efficacy of fresh versus frozen osteochondral allografts in the goat at 6 months is associated with PRG4 secretion. Journal of Orthopaedic Research, 31(6), 880-886.\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848197161149,"sku":"1042011","price":440.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Lubricin_Antibody_Native_Bovine.png?v=1719223964"},{"product_id":"lumican-antibody","title":"Lumican, Antibody, 100 ug","description":"\u003cp\u003eLumican (LUM) monoclonal antibody (mouse, clone Lum-1) to detect a protein epitope in lumican. Liquid, 1 mL\/vial. Concentration: 0.1 mg\/mL\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eLumican (LUM) is the major keratan sulfate proteoglycan of the cornea and it binds collagen fibrils. In noncorneal tissues, lumican is present as a low or nonsulfated glycoprotein and has been found in the aorta, cartilage, liver, skeletal muscle, kidney, pancreas, brain, placenta and lung. Complications of the cornea have been confirmed using lumican-null mice. These mice exhibit corneal opacity, skin fragility, and impaired collagen fibrillogenesis. More recent studies show lumican has an integral role in cell migration, adhesion and proliferation. The expression of lumican has also been examined in breast, pancreatic and colorectal cancer. The affect of lumican depends on the type of cancer as it has been shown to have both a positive and negative affect on tumor growth.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eRelated Terms\/Symbols\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eLUM\u003c\/li\u003e\n\u003cli\u003eLDC\u003c\/li\u003e\n\u003cli\u003eSLRR2D\u003c\/li\u003e\n\u003cli\u003eP51884\u003c\/li\u003e\n\u003cli\u003eLumican proteoglycan\u003c\/li\u003e\n\u003cli\u003emajor keratan sulfate proteoglycan\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003e\u003c\/strong\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eFragmentation of decorin, biglycan, lumican and keratocan is elevated in degener- ate human meniscus, knee and hip articular cartilages compared with age-matched macroscopically normal and control tissues. Melrose J, Fuller ES, Roughley PJ, Smith MM, Kerr B, Hughes CE, Caterson B, Little CB. (2008) Arthritis Res Ther. 10(4):R79. \u003cbr\u003e \u003cbr\u003eMatrix morphogenesis in cornea is mediated by the modification of keratan sulfate by GlcNAc 6-O-sulfotransferase. Hayashida Y, Akama TO, Beecher N, Lewis P, Young RD, Meek KM, Kerr B, Hughes CE, Caterson B, Tanigami A, Nakayama J, Fukada MN, Tano Y, Nishida K, Quantock AJ. (2006) Proc Natl Acad Sci U S A. 5;103(36):13333-8.\u003c\/p\u003e\n","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848197226685,"sku":"1042007","price":440.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Lumican_Antibody.png?v=1719223529"},{"product_id":"t1-st2-il-33-r-monoclonal-antibody-azide-free","title":"T1\/ST2 (IL-33 R) Monoclonal Antibody, azide-free, 0.5 mL","description":"\u003cp\u003eMouse T1\/ST2 (IL-33 R) monoclonal antibody (Clone DJ8, Host \/ Isotype Subclass: Rat IgG1, light chain not isotyped), azide-free,  for the identification and purification of murine T helper 2 (Th2) cells and all forms of murine mast cells.\u003c\/p\u003e\n\u003cp\u003eT1\/ST2 (also known as IL-1 R4 or IL-33Ra) is a transmembrane glycoprotein expressed on mast cells and Th2 cells. It is a selective marker for both murine and human Th2 lymphocytes and plays a role in regulating inflammatory responses. IL-33 is a recently identified member of the IL-1 family of cytokines and is involved in Th2 mediated immune responses. IL-33 mediates its biological effects via T1\/ST2 binding. The roles of IL-33 and T1\/ST2 (IL-33Ra) have been investigated in many immune responses such as allergy, asthma, rheumatoid arthritis and osteoarthritis.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003c\/strong\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cmeta charset=\"UTF-8\"\u003e\u003cspan\u003eYan, C., Kuang, W., Ma, G., Guo, F., Jin, L., Wan, H., ... \u0026amp; Wang, L. (2025). E3 ligase RNF128 restricts A. alternata-induced ILC2 activation and type 2 immune response in the murine lung. \u003c\/span\u003e\u003ci\u003eScientific Reports\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e15\u003c\/i\u003e\u003cspan\u003e(1), 1193.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eIL-33 induces IL-13-dependent cutaneous fibrosis.\u003cbr\u003eRankin A, et al. Journ. of Immunol., 2010; 184(3):1526-35\u003c\/p\u003e\n\u003cp\u003eIL-33 Enhances Lipopolysaccharide-Induced Inflammatory Cytokine Production from Mouse Macrophages by Regulating Lipopolysaccharide Receptor Complex\u003cbr\u003eQuentin Espinassous et al., J. Immunol., Jul 2009; 183: 1446 - 1455.\u003c\/p\u003e\n\u003cp\u003eInterleukin-1 receptor-related protein ST2 suppresses the initial stage of bleomycin-induced lung injury N. Mato et al., Eur. Respir. J., Jun 2009; 33: 1415 - 1428.\u003c\/p\u003e\n\u003cp\u003eIL-1 receptor accessory protein and ST2 comprise the IL-33 receptor complex. Chackerian A, et al. Journ. of Immunol., 2007; 179(4):2551-5.\u003c\/p\u003e\n\u003cp\u003eIL-17 Promotes Immune Privilege of Corneal Allografts Khrishen Cunnusamy, Peter W. Chen, and Jerry Y. Niederkorn\u003cbr\u003eJ. Immunol., Oct 2010; 185: 4651 - 4658.\u003c\/p\u003e\n\u003cp\u003ePredominance of Th2 response in human abdominal aortic aneurysm: Mistaken identity for IL-4-producing NK and NKT cells? Chan WL, et al. Cellular Immun (2005) 233:109-114Changes in systemic type 1 and type 2 immunity in normal pregnancy and pre-eclampsia may be mediated by natural killer cells Borzychowski, A.M. et al., Eur J Immunol (2005) 35:3054-3063.\u003c\/p\u003e\n\u003cp\u003eAtherosclerotic Abdominal Aortic Aneurysm and the Interaction Between Autologous Human Plaque-Derived Vascular Smooth Muscle Cells, Type-1 NKT, and Helper T-Cells Chan, W.L. et al., Circ Res (2005) 96:675-683NKT cell subsets in infection and inflammation Chan WL, et al. Immun Lett (2003) 85:159-163\u003c\/p\u003e\n\u003cp\u003eRegulation of ST2L expression on T helper (Th) type 2 cells Carter, R.W. et al., Eur. J. Immunol. (2001) 31:2979-2985Human IL-18 Receptor and ST@L Are Stable and Selective markers for the Respective Type 1 and Type 2 Circulating Lymphocytes Chan WL, et al. J Immunol. 2001 Aug 1; 167(3):1238-44.\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848199192765,"sku":"101001N","price":740.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/T1_ST2_IL-33R_Monoclonal_Antibody_Azide_Free.png?v=1719221696"},{"product_id":"t1-st2-il-33-r-mouse-monoclonal-antibody","title":"T1\/ST2 (IL-33 R) Mouse, Monoclonal Antibody, 0.5 mL","description":"\u003cp\u003eMouse T1\/ST2 (IL-33 R) monoclonal antibody (Clone: DJ8, Host \/ Isotype Subclass: Rat IgG1, light chain not isotyped) for the identification and purification of murine T helper 2 (Th2) cells and all forms of murine mast cells.\u003c\/p\u003e\n\u003cp\u003eT1\/ST2 (also known as IL-1 R4 or IL-33Ra) is a transmembrane glycoprotein expressed on mast cells and Th2 cells. It is a selective marker for murine Th2 lymphocytes and plays a role in regulating inflammatory responses. IL-33 is a recently identified member of the IL-1 family of cytokines and is involved in Th2 mediated immune responses. IL-33 mediates its biological effects via T1\/ST2 binding. The roles of IL-33 and T1\/ST2 (IL-33Ra) have been investigated in many immune responses such as allergy, asthma, rheumatoid arthritis and osteoarthritis.\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cmeta charset=\"UTF-8\"\u003eYan, C., Kuang, W., Ma, G., Guo, F., Jin, L., Wan, H., ... \u0026amp; Wang, L. (2025). E3 ligase RNF128 restricts A. alternata-induced ILC2 activation and type 2 immune response in the murine lung. \u003ci\u003eScientific Reports\u003c\/i\u003e, \u003ci\u003e15\u003c\/i\u003e(1), 1193.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eToutounchi, N. S., Braber, S., van‘t Land, B., Thijssen, S., Garssen, J., Folkerts, G., \u0026amp; Hogenkamp, A. (2022). Deoxynivalenol exposure during pregnancy has adverse effects on placental structure and immunity in mice model. \u003ci\u003eReproductive Toxicology\u003c\/i\u003e, \u003ci\u003e112\u003c\/i\u003e, 109-118.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eRobb, C. T., Zhou, Y., Felton, J. M., Zhang, B., Goepp, M., Jheeta, P., ... \u0026amp; Yao, C. (2022\u003c\/span\u003e\u003cspan\u003e). Metabolic regulation by prostaglandin E2 impairs lung group 2 innate lymphoid cell responses. \u003c\/span\u003e\u003ci\u003eAllergy\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e78\u003c\/i\u003e\u003cspan\u003e(3), 714-730.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eVan der Jeught, K., Sun, Y., Fang, Y., Zhou, Z., Jiang, H., Yu, T., ... \u0026amp; Eyvani, H. (2020). ST2 as checkpoint target for colorectal cancer immunotherapy. JCI insight, 5(9).\u003cbr\u003e\u003cbr\u003eMatsushita, K., Tanaka, H., Yasuda, K., Adachi, T., Fukuoka, A., Akasaki, S., ... \u0026amp; Yoshimoto, T. (2020). Regnase-1 degradation is crucial for IL-33–and IL-25–mediated ILC2 activation. JCI Insight, 5(4).\u003cbr\u003e\u003cbr\u003eRicardo-Gonzalez, R. R., Schneider, C., Liao, C., Lee, J., Liang, H. E., \u0026amp; Locksley, R. M. (2020). Tissue-specific pathways extrude activated ILC2s to disseminate type 2 immunity. Journal of Experimental Medicine, 217(4).\u003cbr\u003e\u003cbr\u003eD'Souza, S. S., Shen, X., Fung, I. T., Ye, L., Kuentzel, M., Chittur, S. V., ... \u0026amp; Yang, Q. (2019). Compartmentalized effects of aging on group 2 innate lymphoid cell development and function. Aging Cell, 18(6), e13019.\u003cbr\u003e\u003cbr\u003eYe, L., Pan, J., Liang, M., Pasha, M. A., Shen, X., D'Souza, S. S., ... \u0026amp; Yang, Q. (2019). A critical role for c-Myc in group 2 innate lymphoid cell activation. Allergy.\u003cbr\u003e\u003cbr\u003eCai, T., Qiu, J., Ji, Y., Li, W., Ding, Z., Suo, C., ... \u0026amp; Guo, X. (2018). IL-17–producing ST2+ group 2 innate lymphoid cells play a pathogenic role in lung inflammation. Journal of Allergy and Clinical Immunology.\u003cbr\u003e\u003cbr\u003eShen, X., Pasha, M. A., Hidde, K., Khan, A., Liang, M., Guan, W., ... \u0026amp; Yang, Q. (2018). Group 2 innate lymphoid cells promote airway hyperresponsiveness through production of VEGFA. Journal of Allergy and Clinical Immunology, 141(5), 1929-1931.\u003cbr\u003e\u003cbr\u003eGöpfert, C., Andreas, N., Weber, F., Häfner, N., Yakovleva, T., Gaestel, M., ... \u0026amp; Drube, S. (2018). The p38-MK2\/3 Module Is Critical for IL-33–Induced Signaling and Cytokine Production in Dendritic Cells. The Journal of Immunology, 200(3), 1198-1206.\u003cbr\u003e\u003cbr\u003eBartemes, K., Chen, C. C., Iijima, K., Drake, L., \u0026amp; Kita, H. (2018). IL-33–responsive group 2 innate lymphoid cells are regulated by female sex hormones in the uterus. The Journal of Immunology, 200(1), 229-236.\u003cbr\u003e\u003cbr\u003eYang, Y., Liu, H., Zhang, H., Ye, Q., Wang, J., Yang, B., ... \u0026amp; Lu, B. (2017). ST2\/IL-33-dependent microglial response limits acute ischemic brain injury. Journal of Neuroscience, 3233-16.\u003cbr\u003e\u003cbr\u003eMadouri, F., Chenuet, P., Beuraud, C., Fauconnier, L., Marchiol, T., Rouxel, N., ... \u0026amp; Marquant, Q. (2017). Protein kinase Cθ controls type 2 innate lymphoid cell and TH2 responses to house dust mite allergen. Journal of Allergy and Clinical Immunology, 139(5), 1650-1666.\u003cbr\u003e\u003cbr\u003eSilver, J. S., Kearley, J., Copenhaver, A. M., Sanden, C., Mori, M., Yu, L., ... \u0026amp; Erjefalt, J. S. (2016). Inflammatory triggers associated with exacerbations of COPD orchestrate plasticity of group 2 innate lymphoid cells in the lungs. Nature immunology, 17(6), 626.\u003cbr\u003e\u003cbr\u003eVannella, K. M., Ramalingam, T. R., Borthwick, L. A., Barron, L., Hart, K. M., Thompson, R. W., ... \u0026amp; Comeau, M. R. (2016). Combinatorial targeting of TSLP, IL-25, and IL-33 in type 2 cytokine–driven inflammation and fibrosis. Science translational medicine, 8(337), 337ra65-337ra65.\u003cbr\u003e\u003cbr\u003eMonticelli, L. A., Buck, M. D., Flamar, A. L., Saenz, S. A., Wojno, E. D. T., Yudanin, N. A., ... \u0026amp; Shah, H. (2016). Arginase 1 is an innate lymphoid-cell-intrinsic metabolic checkpoint controlling type 2 inflammation. Nature immunology, 17(6), 656.\u003cbr\u003e\u003cbr\u003eYoon, J., Leyva-Castillo, J. M., Wang, G., Galand, C., Oyoshi, M. K., Kumar, L., ... \u0026amp; Kuchroo, V. K. (2016). IL-23 induced in keratinocytes by endogenous TLR4 ligands polarizes dendritic cells to drive IL-22 responses to skin immunization. Journal of Experimental Medicine, 213(10), 2147-2166.\u003cbr\u003e\u003cbr\u003eGaland, C., Leyva-Castillo, J. M., Yoon, J., Han, A., Lee, M. S., McKenzie, A. N., ... \u0026amp; Geha, R. S. (2016). IL-33 promotes food anaphylaxis in epicutaneously sensitized mice by targeting mast cells. Journal of Allergy and Clinical Immunology, 138(5), 1356-1366.\u003cbr\u003e\u003cbr\u003eBando JK, Liang HE, Locksley RM (2015) Identification and distribution of developing innate lymphoid cells in the fetal mouse intestine. Nat Immunol. 2015 Feb;16(2):153-60\u003cbr\u003e\u003cbr\u003eFilbey KJ, Grainger JR, Smith KA, Boon L, van Rooijen N, Harcus Y, Jenkins S, Hewitson JP, Maizels RM (2014) Innate and adaptive type 2 immune cell responses in genetically controlled resistance to intestinal helminth infection. Immunol Cell Biol. 2014 May-Jun;92(5):436-48.\u003cbr\u003e\u003cbr\u003eBiethahn, K., Orinska, Z., Vigorito, E., Goyeneche‐Patino, D. A., Mirghomizadeh, F., Föger, N., \u0026amp; Bulfone‐Paus, S. (2014). miRNA‐155 controls mast cell activation by regulating the PI3Kγ pathway and anaphylaxis in a mouse model. Allergy, 69(6), 752-762.\u003cbr\u003e\u003cbr\u003eConnor, L. M., Tang, S. C., Camberis, M., Le Gros, G., \u0026amp; Ronchese, F. (2014). Helminth-conditioned dendritic cells prime CD4+ T cells to IL-4 production in vivo. The Journal of Immunology, 193(6), 2709-2717.\u003cbr\u003e\u003cbr\u003eBeale, J., Jayaraman, A., Jackson, D. J., Macintyre, J. D., Edwards, M. R., Walton, R. P., ... \u0026amp; Bartlett, N. W. (2014). Rhinovirus-induced IL-25 in asthma exacerbation drives type 2 immunity and allergic pulmonary inflammation. Science translational medicine, 6(256), 256ra134-256ra134.\u003cbr\u003e\u003cbr\u003eMatta, B. M., Lott, J. M., Mathews, L. R., Liu, Q., Rosborough, B. R., Blazar, B. R., \u0026amp; Turnquist, H. R. (2014). IL-33 is an unconventional alarmin that stimulates IL-2 secretion by dendritic cells to selectively expand IL-33R\/ST2+ regulatory T cells. The Journal of Immunology, 193(8), 4010-4020.\u003cbr\u003e\u003cbr\u003eFurusawa, J. I., Moro, K., Motomura, Y., Okamoto, K., Zhu, J., Takayanagi, H., ... \u0026amp; Koyasu, S. (2013). Critical role of p38 and GATA3 in natural helper cell function. The Journal of Immunology, 191(4), 1818-1826.\u003cbr\u003e\u003cbr\u003eImai, Y., Yasuda, K., Sakaguchi, Y., Haneda, T., Mizutani, H., Yoshimoto, T., ... \u0026amp; Yamanishi, K. (2013). Skin-specific expression of IL-33 activates group 2 innate lymphoid cells and elicits atopic dermatitis-like inflammation in mice. Proceedings of the National Academy of Sciences, 110(34), 13921-13926.\u003cbr\u003e\u003cbr\u003eLipsky, B. P., Toy, D. Y., Swart, D. A., Smithgall, M. D., \u0026amp; Smith, D. (2012). Deletion of the ST2 proximal promoter disrupts fibroblast‐specific expression but does not reduce the amount of soluble ST2 in circulation. European journal of immunology, 42(7), 1863-1869.\u003cbr\u003e\u003cbr\u003eBartemes, K. R., Iijima, K., Kobayashi, T., Kephart, G. M., McKenzie, A. N., \u0026amp; Kita, H. (2012). IL-33–Responsive Lineage− CD25+ CD44hi Lymphoid Cells Mediate Innate Type 2 Immunity and Allergic Inflammation in the Lungs. The Journal of Immunology, 188(3), 1503-1513.\u003cbr\u003e\u003cbr\u003eSeol, D., McCabe, D. J., Choe, H., Zheng, H., Yu, Y., Jang, K., \u0026amp; Martin, J. A. (2012). Chondrogenic progenitor cells respond to cartilage injury. Arthritis \u0026amp; Rheumatism, 64(11), 3626-3637.\u003cbr\u003e\u003cbr\u003eDoherty, T. A., Khorram, N., Chang, J. E., Kim, H. K., Rosenthal, P., Croft, M., \u0026amp; Broide, D. H. (2012). STAT6 regulates natural helper cell proliferation during lung inflammation initiated by Alternaria. American Journal of Physiology-Lung Cellular and Molecular Physiology, 303(7), L577-L588.\u003cbr\u003e\u003cbr\u003eTurnquist, H. R., Zhao, Z., Rosborough, B. R., Liu, Q., Castellaneta, A., Isse, K., ... \u0026amp; Thomson, A. W. (2011). IL-33 expands suppressive CD11b+ Gr-1int and regulatory T cells, including ST2L+ Foxp3+ cells, and mediates regulatory T cell-dependent promotion of cardiac allograft survival. The Journal of Immunology, 187(9), 4598-4610.\u003cbr\u003e\u003cbr\u003eAnthony, R. M., Kobayashi, T., Wermeling, F., \u0026amp; Ravetch, J. V. (2011). Intravenous gammaglobulin suppresses inflammation through a novel TH2 pathway. Nature, 475(7354), 110-113.\u003cbr\u003e\u003cbr\u003eNavarro, S., Cossalter, G., Chiavaroli, C., Kanda, A., Fleury, S., Lazzari, A., ... \u0026amp; Julia, V. (2011). The oral administration of bacterial extracts prevents asthma via the recruitment of regulatory T cells to the airways. Mucosal immunology, 4(1), 53-65.\u003cbr\u003e\u003cbr\u003eOhno, T., Oboki, K., Morita, H., Kajiwara, N., Arae, K., Tanaka, S., \u0026amp; Nakae, S. (2011). Paracrine IL-33 stimulation enhances lipopolysaccharide-mediated macrophage activation. PLoS One, 6(4), e18404.\u003cbr\u003e\u003cbr\u003eFöger, N., Jenckel, A., Orinska, Z., Lee, K. H., Chan, A. C., \u0026amp; Bulfone-Paus, S. (2011). Differential regulation of mast cell degranulation versus cytokine secretion by the actin regulatory proteins Coronin1a and Coronin1b. The Journal of experimental medicine, 208(9), 1777-1787.\u003cbr\u003e\u003cbr\u003eSchulze, J., Bickert, T., Beil, F. T., Zaiss, M. M., Albers, J., Wintges, K., \u0026amp; Schinke, T. (2011). Interleukin‐33 is expressed in differentiated osteoblasts and blocks osteoclast formation from bone marrow precursor cells. Journal of Bone and Mineral Research, 26(4), 704-717.\u003cbr\u003e\u003cbr\u003eRankin, A. L., Mumm, J. B., Murphy, E., Turner, S., Yu, N., McClanahan, T. K., ... \u0026amp; Pflanz, S. (2010). IL-33 induces IL-13–dependent cutaneous fibrosis. The journal of immunology, 184(3), 1526-1535.\u003cbr\u003e\u003cbr\u003eCunnusamy, K., Chen, P. W., \u0026amp; Niederkorn, J. Y. (2010). IL-17 promotes immune privilege of corneal allografts. The Journal of Immunology, 185(8), 4651-4658.\u003cbr\u003e\u003cbr\u003eAlves-Filho, J. C., Sônego, F., Souto, F. O., Freitas, A., Verri Jr, W. A., Auxiliadora-Martins, M., \u0026amp; Liew, F. Y. (2010). Interleukin-33 attenuates sepsis by enhancing neutrophil influx to the site of infection. Nature medicine, 16(6), 708-712.\u003cbr\u003e\u003cbr\u003eMoro, K., Yamada, T., Tanabe, M., Takeuchi, T., Ikawa, T., Kawamoto, H., \u0026amp; Koyasu, S. (2010). Innate production of TH2 cytokines by adipose tissue-associated c-Kit+ Sca-1+ lymphoid cells. Nature, 463(7280), 540-544.\u003cbr\u003e\u003cbr\u003e\u003cbr\u003eIL-33 induces IL-13-dependent cutaneous fibrosis.\u003cbr\u003eRankin A, et al. Journ. of Immunol., 2010; 184(3):1526-35.\u003c\/p\u003e\n\u003cp\u003eIL-33 Enhances Lipopolysaccharide-Induced Inflammatory Cytokine Production from Mouse Macrophages by Regulating Lipopolysaccharide Receptor Complex\u003cbr\u003eQuentin Espinassous et al., J. Immunol., Jul 2009; 183: 1446 - 1455.\u003c\/p\u003e\n\u003cp\u003eInterleukin-1 receptor-related protein ST2 suppresses the initial stage of bleomycin-induced lung injury N. Mato et al., Eur. Respir. J., Jun 2009; 33: 1415 - 1428.\u003c\/p\u003e\n\u003cp\u003eIL-1 receptor accessory protein and ST2 comprise the IL-33 receptor complex.\u003cbr\u003eChackerian A, et al. Journ. of Immunol., 2007; 179(4):2551-5.\u003c\/p\u003e\n\u003cp\u003eIL-17 Promotes Immune Privilege of Corneal Allografts Khrishen Cunnusamy, Peter W. Chen, and Jerry Y. Niederkorn J. Immunol., Oct 2010; 185: 4651 - 4658.\u003c\/p\u003e\n\u003cp\u003ePredominance of Th2 response in human abdominal aortic aneurysm: Mistaken identity for IL-4-producing NK and NKT cells? Chan WL, et al. Cellular Immun (2005) 233:109-114\u003c\/p\u003e\n\u003cp\u003eChanges in systemic type 1 and type 2 immunity in normal pregnancy and pre-eclampsia may be mediated by natural killer cells Borzychowski, A.M. et al., Eur J Immunol (2005) 35:3054-3063.\u003c\/p\u003e\n\u003cp\u003eAtherosclerotic Abdominal Aortic Aneurysm and the Interaction Between Autologous Human Plaque-Derived Vascular Smooth Muscle Cells, Type-1 NKT, and Helper T-Cells Chan, W.L. et al., Circ Res (2005) 96:675-683\u003c\/p\u003e\n\u003cp\u003eNKT cell subsets in infection and inflammation Chan WL, et al. Immun Lett (2003) 85:159-163\u003c\/p\u003e\n\u003cp\u003eRegulation of ST2L expression on T helper (Th) type 2 cells Carter, R.W. et al., Eur. J. Immunol. (2001) 31:2979-2985\u003c\/p\u003e\n\u003cp\u003eHuman IL-18 Receptor and ST@L Are Stable and Selective markers for the Respective Type 1 and Type 2 Circulating Lymphocytes Chan WL, et al. J Immunol. 2001 Aug 1; 167(3):1238-44.\u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848199422141,"sku":"101001","price":680.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/T1_ST2__IL-33R__Mouse_Monoclonal_Antibody.png?v=1719221040"},{"product_id":"t1-st2-il-33-r-mouse-monoclonal-antibody-biotinylated","title":"T1\/ST2 (IL-33 R) Mouse, Monoclonal Antibody, Biotinylated, 0.5 mL","description":"\u003cp\u003eMouse T1\/ST2 (IL-33 R) biotinylated monoclonal antibody (Clone: DJ8, Host \/ Isotype Subclass: Rat IgG1, light chain not isotyped) for the identification and purification of murine T helper 2 (Th2) cells and all forms of murine mast cells.\u003c\/p\u003e\n\u003cp\u003eT1\/ST2 (also known as IL-1 R4 or IL-33Ra) is a transmembrane glycoprotein expressed on mast cells and Th2 cells. It is a selective marker for murine Th2 lymphocytes and plays a role in regulating inflammatory responses. IL-33 is a recently identified member of the IL-1 family of cytokines and is involved in Th2 mediated immune responses. IL-33 mediates its biological effects via T1\/ST2 binding. The roles of IL-33 and T1\/ST2 (IL-33Ra) have been investigated in many immune responses such as allergy, asthma, rheumatoid arthritis and osteoarthritis.\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003cspan\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cmeta charset=\"UTF-8\"\u003eYan, C., Kuang, W., Ma, G., Guo, F., Jin, L., Wan, H., ... \u0026amp; Wang, L. (2025). E3 ligase RNF128 restricts A. alternata-induced ILC2 activation and type 2 immune response in the murine lung. \u003ci\u003eScientific Reports\u003c\/i\u003e, \u003ci\u003e15\u003c\/i\u003e(1), 1193.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cmeta charset=\"UTF-8\"\u003eSchmitt, P., Duval, A., Camus, M., Lefrançais, E., Roga, S., Dedieu, C., Ortega, N., Bellard, E., Mirey, E., Mouton-Barbosa, E., Burlet-Schiltz, O., Gonzalez-de-Peredo, A., Cayrol, C., \u0026amp; Girard, J. P. (2024). TL1A is an epithelial alarmin that cooperates with IL-33 for initiation of allergic airway inflammation. \u003ci\u003eThe Journal of experimental medicine\u003c\/i\u003e, \u003ci\u003e221\u003c\/i\u003e(6), e20231236. https:\/\/doi.org\/10.1084\/jem.20231236\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cmeta charset=\"UTF-8\"\u003eGupta, A., Lee, K., \u0026amp; Oh, K. (2023). mTORC1 Deficiency Prevents the Development of MC903-Induced Atopic Dermatitis through the Downregulation of Type 2 Inflammation. \u003ci\u003eInternational journal of molecular sciences\u003c\/i\u003e, \u003ci\u003e24\u003c\/i\u003e(6), 5968. https:\/\/doi.org\/10.3390\/ijms24065968\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eHosotani, Y., Yasuda, K., Nagai, M., Yamanishi, K., Kanazawa, N., Gomi, F., \u0026amp; Imai, Y. (2023). IL-33-induced keratoconjunctivitis is mediated by group 2 innate lymphoid cells in mice. \u003c\/span\u003e\u003ci\u003eAllergology International\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e72\u003c\/i\u003e\u003cspan\u003e(2), 324-331.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eGurram, R. K., Wei, D., Yu, Q., Butcher, M. J., Chen, X., Cui, K., ... \u0026amp; Zhu, J. (2023). Crosstalk between ILC2s and Th2 cells varies among mouse models. \u003ci\u003eCell Reports\u003c\/i\u003e, \u003ci\u003e42\u003c\/i\u003e(2).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eFerreira, A. C., Szeto, A. C., Clark, P. A., Crisp, A., Kozik, P., Jolin, H. E., \u0026amp; McKenzie, A. N. (2023). Neuroprotective protein ADNP-dependent histone remodeling complex promotes T helper 2 immune cell differentiation. \u003ci\u003eImmunity\u003c\/i\u003e.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eSong, M. H., Gupta, A., Nair, V. S., \u0026amp; Oh, K. (2022). CD4+ T cells play an essential role in chronic MC903-induced skin inflammation. Biochemical and Biophysical Research Communications, 612, 8-14.\u003c\/p\u003e\n\u003cp\u003eGschwend, J., Sherman, S. P., Ridder, F., Feng, X., Liang, H. E., Locksley, R. M., ... \u0026amp; Schneider, C. (2021). Alveolar macrophages rely on GM-CSF from alveolar epithelial type 2 cells before and after birth. Journal of Experimental Medicine, 218(10), e20210745.\u003c\/p\u003e\n\u003cp\u003eClark, J. T., Christian, D. A., Gullicksrud, J. A., Perry, J. A., Park, J., Jacquet, M., ... \u0026amp; Hunter, C. A. (2021). IL-33 promotes innate lymphoid cell-dependent IFN-γ production required for innate immunity to Toxoplasma gondii. Elife, 10, e65614.\u003c\/p\u003e\n\u003cp\u003eKato, Y., Morikawa, T., Kato, E., Yoshida, K., Imoto, Y., Sakashita, M., ... \u0026amp; Fujieda, S. (2021). Involvement of Activation of Mast Cells via IgE Signaling and Epithelial Cell–Derived Cytokines in the Pathogenesis of Pollen Food Allergy Syndrome in a Murine Model. The Journal of Immunology.\u003c\/p\u003e\n\u003cp\u003eMaes, B., Smole, U., Vanderkerken, M., Deswarte, K., Van Moorleghem, J., Vergote, K., ... \u0026amp; Hammad, H. (2021). The STE20 kinase TAOK3 controls the development house dust mite–induced asthma in mice. Journal of Allergy and Clinical Immunology.\u003c\/p\u003e\n\u003cp\u003eBlomme, E. E., Provoost, S., De Smet, E. G., De Grove, K. C., Van Eeckhoutte, H. P., De Volder, J., ... \u0026amp; Maes, T. (2021). Quantification and role of innate lymphoid cell subsets in Chronic Obstructive Pulmonary Disease. Clinical \u0026amp; translational immunology, 10(6), e1287.\u003c\/p\u003e\n\u003cp\u003eKamijo, S., Hara, M., Suzuki, M., Nakae, S., Ogawa, H., Okumura, K., \u0026amp; Takai, T. (2021). Innate IL-17A Enhances IL-33-Independent Skin Eosinophilia and IgE Response on Subcutaneous Papain Sensitization. The Journal of investigative dermatology, 141(1), 105-113.\u003c\/p\u003e\n\u003cp\u003eTomar, S., Ganesan, V., Sharma, A., Zeng, C., Waggoner, L., Smith, A., ... \u0026amp; Hogan, S. P. (2021). IL-4–BATF signaling directly modulates IL-9 producing mucosal mast cell (MMC9) function in experimental food allergy.Journal of Allergy and Clinical Immunology, 147(1), 280-295.\u003cbr\u003e\u003cbr\u003eAparicio-Domingo, P., Cannelle, H., Buechler, M. B., Nguyen, S., Kallert, S. M., Favre, S., ... \u0026amp; Pinschewer, D. D. (2020). Fibroblast-derived IL-33 is dispensable for lymph node homeostasis but critical for CD8 T-cell responses to acute and chronic viral infection. European Journal of Immunology.\u003cbr\u003e\u003cbr\u003eFeng, X., Li, L., Feng, J., He, W., Li, N., Shi, T., ... \u0026amp; Su, X. (2020). Vagal-a7nAChR signaling attenuates allergic asthma responses and facilitates asthma tolerance by regulating inflammatory group 2 innate lymphoid cells. Immunology and Cell Biology.\u003cbr\u003e\u003cbr\u003eSalomonsson, M., Dahlin, J. S., Ungerstedt, J., \u0026amp; Hallgren, J. (2020). Localization-Specific Expression of CCR1 and CCR5 by Mast Cell Progenitors. Frontiers in Immunology, 11, 321.\u003cbr\u003e\u003cbr\u003eKato, T., Yasuda, K., Matsushita, K., Ishii, K. J., Hirota, S., Yoshimoto, T., \u0026amp; Shibahara, H. (2019). Interleukin-1\/-33 signaling pathways as therapeutic targets for endometriosis. Frontiers in Immunology, 10, 2021.\u003cbr\u003e\u003cbr\u003eWalker, J. A., Clark, P. A., Crisp, A., Barlow, J. L., Szeto, A., Ferreira, A. C., ... \u0026amp; Pannell, R. (2019). Polychromic Reporter Mice Reveal Unappreciated Innate Lymphoid Cell Progenitor Heterogeneity and Elusive ILC3 Progenitors in Bone Marrow. Immunity.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eSchneider, C., Lee, J., Koga, S., Ricardo-Gonzalez, R. R., Nussbaum, J. C., Smith, L. K., ... \u0026amp; Locksley, R. M. (2019).\u003c\/p\u003e\n\u003cp\u003eTissue-Resident Group 2 Innate Lymphoid Cells Differentiate by Layered Ontogeny and In Situ Perinatal Priming. Immunity. Holgado, A., Braun, H., Van Nuffel, E., Detry, S., Schuijs, M. J., Deswarte, K., ... \u0026amp; Hammad, H. (2019).\u003c\/p\u003e\n\u003cp\u003eIL-33trap is a novel IL-33–neutralizing biologic that inhibits allergic airway inflammation. Journal of Allergy and Clinical Immunology.\u003cbr\u003eWalker, J. A., Clark, P. A., Crisp, A., Barlow, J. L., Szeto, A., Ferreira, A. C., ... \u0026amp; Pannell, R. (2019).\u003c\/p\u003e\n\u003cp\u003ePolychromic Reporter Mice Reveal Unappreciated Innate Lymphoid Cell Progenitor Heterogeneity and Elusive ILC3 Progenitors in Bone Marrow. Immunity. Schneider, C., Lee, J., Koga, S., Ricardo-Gonzalez, R. R., Nussbaum, J. C., Smith, L. K., ... \u0026amp; Locksley, R. M. (2019).\u003c\/p\u003e\n\u003cp\u003eTissue-Resident Group 2 Innate Lymphoid Cells Differentiate by Layered Ontogeny and In Situ Perinatal Priming. Immunity.\u003cbr\u003e\u003cbr\u003eHolgado, A., Braun, H., Van Nuffel, E., Detry, S., Schuijs, M. J., Deswarte, K., ... \u0026amp; Hammad, H. (2019). IL-33trap is a novel IL-33–neutralizing biologic that inhibits allergic airway inflammation. Journal of Allergy and Clinical Immunology.\u003cbr\u003e\u003cbr\u003eMiragaia, R. J., Gomes, T., Chomka, A., Jardine, L., Riedel, A., Hegazy, A. N., ... \u0026amp; Emerton, G. (2019). Single-cell transcriptomics of regulatory T cells reveals trajectories of tissue adaptation. Immunity, 50(2), 493-504\u003cbr\u003e\u003cbr\u003eWaddell, A., Vallance, J. E., Hummel, A., Alenghat, T., \u0026amp; Rosen, M. J. (2019). IL-33 Induces Murine Intestinal Goblet Cell Differentiation Indirectly via Innate Lymphoid Cell IL-13 Secretion. The Journal of Immunology, 202(2), 598-607.\u003cbr\u003e\u003cbr\u003eIto, M., Komai, K., Mise-Omata, S., Iizuka-Koga, M., Noguchi, Y., Kondo, T., ... \u0026amp; Nakatsukasa, H. (2019). Brain regulatory T cells suppress astrogliosis and potentiate neurological recovery. Nature, 1.c\u003cbr\u003e\u003cbr\u003eJin, R. M., Warunek, J., \u0026amp; Wohlfert, E. A. (2018).Therapeutic Administration of IL-10 and Amphiregulin Alleviates Chronic Skeletal Muscle Inflammation and Damage Induced by Infection. ImmunoHorizons, 2(5), 142-154.\u003cbr\u003e\u003cbr\u003eCayrol, C., Duval, A., Schmitt, P., Roga, S., Camus, M., Stella, A., ... \u0026amp; Girard, J. P. (2018). Environmental allergens induce allergic inflammation through proteolytic maturation of IL-33. Nature immunology, 19(4), 375.\u003cbr\u003e\u003cbr\u003eSchneider, C., O’Leary, C. E., von Moltke, J., Liang, H. E., Ang, Q. Y., Turnbaugh, P. J., ... \u0026amp; Locksley, R. M. (2018). A Metabolite-Triggered Tuft Cell-ILC2 Circuit Drives Small Intestinal Remodeling. Cell.\u003cbr\u003e\u003cbr\u003eLaman, J. D., Kooistra, S. M., \u0026amp; Clausen, B. E. (2017). Reproducibility issues: avoiding pitfalls in animal inflammation models. In Inflammation (pp. 1-17). Humana Press, New York, NY.\u003cbr\u003e\u003cbr\u003eTsuzuki, H., Arinobu, Y., Miyawaki, K., Takaki, A., Ota, S. I., Ota, Y., ... \u0026amp; Niiro, H. (2017). Functional interleukin‐33 receptors are expressed in early progenitor stages of allergy‐related granulocytes. Immunology, 150(1), 64-73.\u003cbr\u003e\u003cbr\u003eChen, C. C., Kobayashi, T., Iijima, K., Hsu, F. C., \u0026amp; Kita, H. (2017). IL-33 dysregulates regulatory T cells and impairs established immunologic tolerance in the lungs. Journal of Allergy and Clinical Immunology, 140(5), 1351-1363.\u003cbr\u003e\u003cbr\u003eDominguez, D., Ye, C., Geng, Z., Chen, S., Fan, J., Qin, L., ... \u0026amp; Fang, D. (2017). Exogenous IL-33 restores dendritic cell activation and maturation in established cancer. The Journal of Immunology, 198(3), 1365-1375.\u003cbr\u003e\u003cbr\u003eZarnegar, B., Mendez-Enriquez, E., Westin, A., Söderberg, C., Dahlin, J. S., Grönvik, K. O., \u0026amp; Hallgren, J. (2017). Influenza infection in mice induces accumulation of lung mast cells through the recruitment and maturation of mast cell progenitors. Frontiers in immunology, 8, 310.\u003cbr\u003e\u003cbr\u003eMorikawa, T., Fukuoka, A., Matsushita, K., Yasuda, K., Iwasaki, N., Akasaki, S., ... \u0026amp; Yoshimoto, T. (2017). Activation of group 2 innate lymphoid cells exacerbates and confers corticosteroid resistance to mouse nasal type 2 inflammation. International immunology, 29(5), 221-233.\u003cbr\u003e\u003cbr\u003eDullaers, M., Schuijs, M. J., Willart, M., Fierens, K., Van Moorleghem, J., Hammad, H., \u0026amp; Lambrecht, B. N. (2017). House dust mite–driven asthma and allergen-specific T cells depend on B cells when the amount of inhaled allergen is limiting. Journal of Allergy and Clinical Immunology, 140(1), 76-88.\u003cbr\u003e\u003cbr\u003eHe, Z., Chen, L., Souto, F. O., Canasto-Chibuque, C., Bongers, G., Deshpande, M., ... \u0026amp; Lira, S. A. (2017). Epithelial-derived IL-33 promotes intestinal tumorigenesis in Apc Min\/+ mice. Scientific reports, 7(1), 5520.\u003cbr\u003e\u003cbr\u003eMowel, W. K., McCright, S. J., Kotzin, J. J., Collet, M. A., Uyar, A., Chen, X., ... \u0026amp; Villarino, A. (2017). Group 1 innate lymphoid cell lineage identity is determined by a cis-regulatory element marked by a long non-coding RNA. Immunity, 47(3), 435-449.\u003cbr\u003e\u003cbr\u003eMinutti, C. M., Drube, S., Blair, N., Schwartz, C., McCrae, J. C., McKenzie, A. N., ... \u0026amp; Sijts, A. J. (2017). Epidermal growth factor receptor expression licenses type-2 helper T cells to function in a T cell receptor-independent fashion. Immunity, 47(4), 710-722.\u003cbr\u003e\u003cbr\u003eYang, Q., Moyar, Q. G., Kokalari, B., Redai, I. G., Wang, X., Kemeny, D. M., ... \u0026amp; Haczku, A. (2016). Group 2 innate lymphoid cells mediate ozone-induced airway inflammation and hyperresponsiveness in mice. Journal of Allergy and Clinical Immunology, 137(2), 571-578.\u003cbr\u003e\u003cbr\u003eRak, G. D., Osborne, L. C., Siracusa, M. C., Kim, B. S., Wang, K., Bayat, A., ... \u0026amp; Volk, S. W. (2016). IL-33-dependent group 2 innate lymphoid cells promote cutaneous wound healing. Journal of Investigative Dermatology, 136(2), 487-496.\u003cbr\u003e\u003cbr\u003eBiton, J., Athari, S. K., Thiolat, A., Santinon, F., Lemeiter, D., Hervé, R., ... \u0026amp; Girard, J. P. (2016). In vivo expansion of activated Foxp3+ regulatory T cells and establishment of a type 2 immune response upon IL-33 treatment protect against experimental arthritis. The Journal of Immunology, 1502124.\u003cbr\u003e\u003cbr\u003eGordon, E. D., Simpson, L. J., Rios, C. L., Ringel, L., Lachowicz-Scroggins, M. E., Peters, M. C., ... \u0026amp; Yuan, S. (2016). Alternative splicing of interleukin-33 and type 2 inflammation in asthma. Proceedings of the National Academy of Sciences, 113(31), 8765-8770.\u003cbr\u003e\u003cbr\u003eTsuzuki, H., Arinobu, Y., Miyawaki, K., Takaki, A., Ota, S. I., Ota, Y., ... \u0026amp; Niiro, H. (2017). Functional interleukin‐33 receptors are expressed in early progenitor stages of allergy‐related granulocytes. Immunology, 150(1), 64-73.\u003cbr\u003e\u003cbr\u003eYoon, J., Leyva-Castillo, J. M., Wang, G., Galand, C., Oyoshi, M. K., Kumar, L., ... \u0026amp; Kuchroo, V. K. (2016). IL-23 induced in keratinocytes by endogenous TLR4 ligands polarizes dendritic cells to drive IL-22 responses to skin immunization. Journal of Experimental Medicine, 213(10), 2147-2166.\u003cbr\u003e\u003cbr\u003eJackson-Jones, L. H., Duncan, S. M., Magalhaes, M. S., Campbell, S. M., Maizels, R. M., McSorley, H. J., ... \u0026amp; Bénézech, C. (2016). Fat-associated lymphoid clusters control local IgM secretion during pleural infection and lung inflammation. Nature communications, 7, 12651.\u003cbr\u003e\u003cbr\u003eValladao, A. C., Frevert, C. W., Koch, L. K., Campbell, D. J., \u0026amp; Ziegler, S. F. (2016). STAT6 regulates the development of eosinophilic versus neutrophilic asthma in response to Alternaria alternata. The Journal of Immunology, 1600007.\u003cbr\u003e\u003cbr\u003eVan Dyken, S. J., Nussbaum, J. C., Lee, J., Molofsky, A. B., Liang, H. E., Pollack, J. L., ... \u0026amp; Erle, D. J. (2016). A tissue checkpoint regulates type 2 immunity. Nature immunology, 17(12), 1381.\u003cbr\u003e\u003cbr\u003ePaclik, D., Stehle, C., Lahmann, A., Hutloff, A., \u0026amp; Romagnani, C. (2015). ICOS regulates the pool of group 2 innate lymphoid cells under homeostatic and inflammatory conditions in mice. European journal of immunology, 45(10), 2766-2772.\u003cbr\u003e\u003cbr\u003eWalker, J. A., Oliphant, C. J., Englezakis, A., Yu, Y., Clare, S., Rodewald, H. R., ... \u0026amp; McKenzie, A. N. (2015). Bcl11b is essential for group 2 innate lymphoid cell development. Journal of Experimental Medicine, 212(6), 875-882.\u003cbr\u003e\u003cbr\u003eZhang, J., Ramadan, A. M., Griesenauer, B., Li, W., Turner, M. J., Liu, C., ... \u0026amp; Paczesny, S. (2015). ST2 blockade reduces sST2-producing T cells while maintaining protective mST2-expressing T cells during graft-versus-host disease. Science translational medicine, 7(308), 308ra160-308ra160.\u003cbr\u003e\u003cbr\u003eCui, Y., Dahlin, J. S., Feinstein, R., Bankova, L. G., Xing, W., Shin, K., ... \u0026amp; Hallgren, J. (2014). Mouse mast cell protease-6 and MHC are involved in the development of experimental asthma. The Journal of Immunology, 193(10), 4783-4789.\u003cbr\u003e\u003cbr\u003eKim, B. S., Wang, K., Siracusa, M. C., Saenz, S. A., Brestoff, J. R., Monticelli, L. A., ... \u0026amp; Artis, D. (2014). Basophils promote innate lymphoid cell responses in inflamed skin. The Journal of Immunology, 193(7), 3717-3725\u003cbr\u003e\u003cbr\u003eKato, Y., Akasaki, S., Muto-Haenuki, Y., Fujieda, S., Matsushita, K., \u0026amp; Yoshimoto, T. (2014). Nasal sensitization with ragweed pollen induces local-allergic-rhinitis-like symptoms in mice.\u003cbr\u003e\u003cbr\u003eKomai‐Koma, M., Li, D., Wang, E., Vaughan, D., \u0026amp; Xu, D. (2014). Anti‐Toll‐like receptor 2 and 4 antibodies suppress inflammatory response in mice. Immunology, 143(3), 354-362.\u003cbr\u003e\u003cbr\u003eHeger, K., Seidler, B., Vahl, J. C., Schwartz, C., Kober, M., Klein, S., ... \u0026amp; Schmidt‐Supprian, M. (2014). CreERT2 expression from within the c‐Kit gene locus allows efficient inducible gene targeting in and ablation of mast cells. European journal of immunology, 44(1), 296-306.\u003cbr\u003e\u003cbr\u003eSpooner, C. J., Lesch, J., Yan, D., Khan, A. A., Abbas, A., Ramirez-Carrozzi, V., ... \u0026amp; Singh, H. (2013). Specification of type 2 innate lymphocytes by the transcriptional determinant Gfi1. Nature immunology, 14(12), 1229-1236.\u003cbr\u003e\u003cbr\u003eNussbaum, J. C., Van Dyken, S. J., von Moltke, J., Cheng, L. E., Mohapatra, A., Molofsky, A. B., ... \u0026amp; Locksley, R. M. (2013). Type 2 innate lymphoid cells control eosinophil homeostasis. Nature, 502(7470), 245-248.\u003cbr\u003e\u003cbr\u003eSaenz, S. A., Siracusa, M. C., Monticelli, L. A., Ziegler, C. G., Kim, B. S., Brestoff, J. R., ... \u0026amp; Artis, D. (2013). IL-25 simultaneously elicits distinct populations of innate lymphoid cells and multipotent progenitor type 2 (MPPtype2) cells. The Journal of experimental medicine, 210(9), 1823-1837.\u003cbr\u003e\u003cbr\u003eKamijo, S., Takeda, H., Tokura, T., Suzuki, M., Inui, K., Hara, M., ... \u0026amp; Takai, T. (2013). IL-33–Mediated Innate Response and Adaptive Immune Cells Contribute to Maximum Responses of Protease Allergen–Induced Allergic Airway Inflammation. The Journal of Immunology, 190(9), 4489-4499.\u003cbr\u003e\u003cbr\u003eMolofsky, A. B., Nussbaum, J. C., Liang, H. E., Van Dyken, S. J., Cheng, L. E., Mohapatra, A., ... \u0026amp; Locksley, R. M. (2013). Innate lymphoid type 2 cells sustain visceral adipose tissue eosinophils and alternatively activated macrophages. The Journal of experimental medicine, 210(3), 535-549.\u003cbr\u003e\u003cbr\u003eNussbaum, J. C., Van Dyken, S. J., von Moltke, J., Cheng, L. E., Mohapatra, A., Molofsky, A. B., ... \u0026amp; Locksley, R. M. (2013). Type 2 innate lymphoid cells control eosinophil homeostasis. Nature, 502(7470), 245-248.\u003cbr\u003e\u003cbr\u003eWong, S. H., Walker, J. A., Jolin, H. E., Drynan, L. F., Hams, E., Camelo, A., ... \u0026amp; McKenzie, A. N. (2012). Transcription factor ROR [alpha] is critical for nuocyte development. Nature immunology, 13(3), 229-236.\u003cbr\u003e\u003cbr\u003eChang, Y. J., Kim, H. Y., Albacker, L. A., Baumgarth, N., McKenzie, A. N., Smith, D. E., ... \u0026amp; Umetsu, D. T. (2011). Innate lymphoid cells mediate influenza-induced airway hyper-reactivity independently of adaptive immunity. Nature immunology, 12(7), 631-638.\u003cbr\u003e\u003cbr\u003eSaenz, S. A., Siracusa, M. C., Perrigoue, J. G., Spencer, S. P., Urban Jr, J. F., Tocker, J. E., ... \u0026amp; Artis, D. (2010). IL25 elicits a multipotent progenitor cell population that promotes TH2 cytokine responses. Nature, 464(7293), 1362-1366.\u003cbr\u003e\u003cbr\u003e\u003cbr\u003eCutting Edge: Atopy Promotes Th2 Responses to Alloantigens and Increases the Incidence and Tempo of Corneal Allograft Rejection\u003cbr\u003eClay Beauregard et al., J. Immunol., Jun 2005; 174: 6577 - 6581.Predominance of Th2 response in human abdominal aortic aneurysm: Mistaken identity for IL-4-producing NK and NKT cells? Chan WL, et al. Cellular Immun (2005) 233:109-114Changes in systemic type 1 and type 2 immunity in normal pregnancy and pre-eclampsia may be mediated by natural killer cells Borzychowski, A.M. et al., Eur J Immunol (2005) 35:3054-3063. Atherosclerotic Abdominal Aortic Aneurysm and the Interaction Between Autologous Human Plaque-Derived Vascular Smooth Muscle Cells, Type-1 NKT, and Helper T-Cells Chan, W.L. et al., Circ Res (2005) 96:675-683NKT cell subsets in infection and inflammation Chan WL, et al. Immun Lett (2003) 85:159-163Regulation of ST2L expression on T helper (Th) type 2 cells Carter, R.W. et al., Eur. J. Immunol. (2001) 31:2979-2985Human IL-18 Receptor and ST@L Are Stable and Selective markers for the Respective Type 1 and Type 2 Circulating Lymphocytes Chan WL, et al. J Immunol. 2001 Aug 1; 167(3):1238-44.\u003c\/p\u003e\n\u003cp class=\"p1\"\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp class=\"p1\"\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848199749821,"sku":"101001B","price":765.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/T1_ST2_IL-33R_Mouse_Monoclonal_Antibody_Biotinylated.png?v=1719221173"},{"product_id":"t1-st2-il-33-r-mouse-monoclonal-antibody-pe-conjugated","title":"T1\/ST2 (IL-33 R) Mouse, Monoclonal Antibody, PE Conjugated, 0.1 mL","description":"\u003cp\u003eMouse T1\/ST2 (IL-33 R) PE conjugated monoclonal antibody (Clone DJ8, Host \/ Isotype Subclass: Rat IgG1, light chain not isotyped) for the identification and purification of murine T helper 2 (Th2) cells and all forms of murine mast cells.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eT1\/ST2 (also known as IL-1 R4 or IL-33Ra) is a transmembrane glycoprotein expressed on mast cells and Th2 cells. It is a selective marker for murine Th2 lymphocytes and plays a role in regulating inflammatory responses. IL-33 is a recently identified member of the IL-1 family of cytokines and is involved in Th2 mediated immune responses. IL-33 mediates its biological effects via T1\/ST2 binding. The roles of IL-33 and T1\/ST2 (IL-33Ra) have been investigated in many immune responses such as allergy, asthma, rheumatoid arthritis and osteoarthritis.\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cmeta charset=\"UTF-8\"\u003eYan, C., Kuang, W., Ma, G., Guo, F., Jin, L., Wan, H., ... \u0026amp; Wang, L. (2025). E3 ligase RNF128 restricts A. alternata-induced ILC2 activation and type 2 immune response in the murine lung. \u003ci\u003eScientific Reports\u003c\/i\u003e, \u003ci\u003e15\u003c\/i\u003e(1), 1193.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eGurram, R. K., Wei, D., Yu, Q., Butcher, M. J., Chen, X., Cui, K., ... \u0026amp; Zhu, J. (2023). Crosstalk between ILC2s and Th2 cells varies among mouse models. \u003ci\u003eCell Reports\u003c\/i\u003e, \u003ci\u003e42\u003c\/i\u003e(2).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eSasse, C., Barinberg, D., Obermeyer, S., Debus, A., Schleicher, U., \u0026amp; Bogdan, C. (2022). Eosinophils, but not type 2 innate lymphoid cells, are the predominant source of interleukin 4 during the innate phase of Leishmania major infection. \u003c\/span\u003e\u003ci\u003ePathogens\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e11\u003c\/i\u003e\u003cspan\u003e(8), 828.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eLai, D., Chen, W., Zhang, K., Scott, M. J., Li, Y., Billiar, T. R., ... \u0026amp; Fan, J. (2022). GRK2 regulates group 2 innate lymphoid cell mobilization in sepsis. Molecular Medicine, 28(1), 1-12.\u003c\/p\u003e\n\u003cp\u003eCautivo, K. M., Matatia, P. R., Lizama, C. O., Mroz, N. M., Dahlgren, M. W., Yu, X., ... \u0026amp; Molofsky, A. B. (2022). Interferon gamma constrains type 2 lymphocyte niche boundaries during mixed inflammation. \u003cem\u003eImmunity\u003c\/em\u003e, \u003cem\u003e55\u003c\/em\u003e(2), 254-271.\u003c\/p\u003e\n\u003cp\u003eHuang, Y., Li, X., Zhu, L., Huang, C., Chen, W., Ling, Z., ... \u0026amp; Zhang, Y. (2022). Thrombin cleaves IL‐33 and modulates IL‐33‐activated allergic lung inflammation. \u003cem\u003eAllergy\u003c\/em\u003e.\u003c\/p\u003e\n\u003cp\u003eFrech, M., Omata, Y., Schmalzl, A., Wirtz, S., Taher, L., Schett, G., ... \u0026amp; Sarter, K. (2022). Btn2a2 Regulates ILC2–T Cell Cross Talk in Type 2 Immune Responses. \u003cem\u003eFrontiers in immunology\u003c\/em\u003e, \u003cem\u003e13\u003c\/em\u003e.\u003c\/p\u003e\n\u003cp\u003eO’Leary, C. E., Sbierski-Kind, J., Kotas, M. E., Wagner, J. C., Liang, H. E., Schroeder, A. W., ... \u0026amp; Locksley, R. M. (2022). Bile acid–sensitive tuft cells regulate biliary neutrophil influx. Science Immunology, 7(69), eabj1080.\u003c\/p\u003e\n\u003cp\u003e\u003cmeta charset=\"UTF-8\"\u003e\u003cspan\u003eSteele, H., Sachen, K., McKnight, A. J., Soloff, R., \u0026amp; Herro, R. (2021). Targeting TL1A\/DR3 Signaling Offers a Therapeutic Advantage to Neutralizing IL13\/IL4Rα in Muco-Secretory Fibrotic Disorders. \u003c\/span\u003e\u003ci\u003eFrontiers in immunology\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e12\u003c\/i\u003e\u003cspan\u003e, 692127. \u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eArora, P., Andersen, D., Moll, J. M., Danneskiold-Samsøe, N. B., Xu, L., Zhou, B., ... \u0026amp; Brix, S. (2021). Small Intestinal Tuft Cell Activity Associates With Energy Metabolism in Diet-Induced Obesity. \u003cem\u003eFrontiers in \u003c\/em\u003e\u003cem\u003eI\u003c\/em\u003e\u003cem\u003emmunology\u003c\/em\u003e, \u003cem\u003e12\u003c\/em\u003e.\u003c\/p\u003e\n\u003cp\u003eVan der Jeught, K., Sun, Y., Fang, Y., Zhou, Z., Jiang, H., Yu, T., ... \u0026amp; Eyvani, H. (2020). ST2 as checkpoint target for colorectal cancer immunotherapy. JCI insight, 5(9).\u003cbr\u003e\u003cbr\u003eSymowski, C., \u0026amp; Voehringer, D. (2019). Th2 cell-derived IL-4\/IL-13 promote ILC2 accumulation in the lung by ILC2-intrinsic STAT6 signaling in mice. European Journal of Immunology.\u003cbr\u003e\u003cbr\u003eKobayashi, T., Voisin, B., Kennedy, E. A., Jo, J. H., Shih, H. Y., Truong, A., ... \u0026amp; Moro, K. (2019). Homeostatic Control of Sebaceous Glands by Innate Lymphoid Cells Regulates Commensal Bacteria Equilibrium. Cell, 176(5), 982-997\u003cbr\u003e\u003cbr\u003eMoldaver, D. M., Bharhani, M. S., Rudulier, C. D., Wattie, J., Inman, M. D., \u0026amp; Larché, M. (2019). Induction of bystander tolerance and immune deviation after Fel d 1 peptide immunotherapy. Journal of Allergy and Clinical Immunology, 143(3), 1087-1099.\u003cbr\u003e\u003cbr\u003eLai, D., Tang, J., Chen, L., Fan, E. K., Scott, M. J., Li, Y., ... \u0026amp; Fan, J. (2018). Group 2 innate lymphoid cells protect lung endothelial cells from pyroptosis in sepsis. Cell death \u0026amp; disease, 9(3), 369.\u003cbr\u003e\u003cbr\u003eSchneider, C., O’Leary, C. E., von Moltke, J., Liang, H. E., Ang, Q. Y., Turnbaugh, P. J., ... \u0026amp; Locksley, R. M. (2018). A Metabolite-Triggered Tuft Cell-ILC2 Circuit Drives Small Intestinal Remodeling. Cell.\u003cbr\u003e\u003cbr\u003eOmata, Y., Frech, M., Primbs, T., Lucas, S., Andreev, D., Scholtysek, C., ... \u0026amp; Andreas, N. (2018). Group 2 Innate Lymphoid Cells Attenuate Inflammatory Arthritis and Protect from Bone Destruction in Mice. Cell reports, 24(1), 169-180.\u003cbr\u003e\u003cbr\u003eCutting Edge: Atopy Promotes Th2 Responses to Alloantigens and Increases the Incidence and Tempo of Corneal Allograft Rejection\u003cbr\u003eClay Beauregard et al., J. Immunol., Jun 2005; 174: 6577 - 6581.\u003c\/p\u003e\n\u003cp\u003ePredominance of Th2 response in human abdominal aortic aneurysm: Mistaken identity for IL-4-producing NK and NKT cells? Chan WL, et al. Cellular Immun (2005) 233:109-114\u003c\/p\u003e\n\u003cp\u003eChanges in systemic type 1 and type 2 immunity in normal pregnancy and pre-eclampsia may be mediated by natural killer cells Borzychowski, A.M. et al., Eur J Immunol (2005) 35:3054-3063.\u003c\/p\u003e\n\u003cp\u003eAtherosclerotic Abdominal Aortic Aneurysm and the Interaction Between Autologous Human Plaque-Derived Vascular Smooth Muscle Cells, Type-1 NKT, and Helper T-Cells Chan, W.L. et al., Circ Res (2005) 96:675-683\u003c\/p\u003e\n\u003cp\u003eNKT cell subsets in infection and inflammation Chan WL, et al. Immun Lett (2003) 85:159-163Regulation of ST2L expression on T helper (Th) type 2 cells Carter, R.W. et al., Eur. J. Immunol. (2001) 31:2979-2985\u003c\/p\u003e\n\u003cp\u003eHuman IL-18 Receptor and ST@L Are Stable and Selective markers for the Respective Type 1 and Type 2 Circulating Lymphocytes Chan WL, et al. J Immunol. 2001 Aug 1; 167(3):1238-44.\u003cbr\u003e\u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848199815357,"sku":"101001PE","price":570.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/T1_ST2_IL-33R_Mouse_Monoclonal_Antibody_PE_Conjugated.png?v=1719221843"},{"product_id":"t1-st2-il-33r-mouse-monoclonal-antibody-fitc","title":"T1\/ST2 (IL-33R) Mouse, Monoclonal Antibody, FITC,  0.5 mL","description":"\u003cp\u003eMouse T1\/ST2 (IL-33 R) FITC conjugated monoclonal antibody (Clone: DJ8, Host \/ Isotype Subclass: Rat IgG1, light chain not isotyped) for the identification and purification of murine T helper 2 (Th2) cells and all forms of murine mast cells.\u003c\/p\u003e\n\u003cp\u003eT1\/ST2 (also known as IL-1 R4 or IL-33Ra) is a transmembrane glycoprotein expressed on mast cells and Th2 cells. It is a selective marker for both murine and human Th2 lymphocytes and plays a role in regulating inflammatory responses. IL-33 is a recently identified member of the IL-1 family of cytokines and is involved in Th2 mediated immune responses. IL-33 mediates its biological effects via T1\/ST2 binding. The roles of IL-33 and T1\/ST2 (IL-33Ra) have been investigated in many immune responses such as allergy, asthma, rheumatoid arthritis and osteoarthritis.\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cmeta charset=\"UTF-8\"\u003ePrince, N., Peralta Marzal, L. N., Roussin, L., Monnoye, M., Philippe, C., Maximin, E., ... \u0026amp; Perez-Pardo, P. (2025). Mouse strain-specific responses along the gut-brain axis upon fecal microbiota transplantation from children with autism. \u003ci\u003eGut microbes\u003c\/i\u003e, \u003ci\u003e17\u003c\/i\u003e(1), 2447822.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cmeta charset=\"UTF-8\"\u003eYan, C., Kuang, W., Ma, G., Guo, F., Jin, L., Wan, H., ... \u0026amp; Wang, L. (2025). E3 ligase RNF128 restricts A. alternata-induced ILC2 activation and type 2 immune response in the murine lung. \u003ci\u003eScientific Reports\u003c\/i\u003e, \u003ci\u003e15\u003c\/i\u003e(1), 1193.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cmeta charset=\"UTF-8\"\u003eCapellmann, S., Kauffmann, M., Arock, M., \u0026amp; Huber, M. (2024). SR-BI regulates the synergistic mast cell response by modulating the plasma membrane-associated cholesterol pool. \u003ci\u003eEuropean journal of immunology\u003c\/i\u003e, \u003ci\u003e54\u003c\/i\u003e(8), e2350788. https:\/\/doi.org\/10.1002\/eji.202350788\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cmeta charset=\"UTF-8\"\u003eBartolacci, J. G., Behun, M. N., Warunek, J. P., Li, T., Sahu, A., Dwyer, G. K., Lucas, A., Rong, J., Ambrosio, F., Turnquist, H. R., \u0026amp; Badylak, S. F. (2024). Matrix-bound nanovesicle-associated IL-33 supports functional recovery after skeletal muscle injury by initiating a pro-regenerative macrophage phenotypic transition. \u003ci\u003eNPJ Regenerative medicine\u003c\/i\u003e, \u003ci\u003e9\u003c\/i\u003e(1), 7. https:\/\/doi.org\/10.1038\/s41536-024-00346-2\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eGurram, R. K., Wei, D., Yu, Q., Butcher, M. J., Chen, X., Cui, K., ... \u0026amp; Zhu, J. (2023). Crosstalk between ILC2s and Th2 cells varies among mouse models. \u003ci\u003eCell Reports\u003c\/i\u003e, \u003ci\u003e42\u003c\/i\u003e(2).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eFerreira, A. C., Szeto, A. C., Clark, P. A., Crisp, A., Kozik, P., Jolin, H. E., \u0026amp; McKenzie, A. N. (2023). Neuroprotective protein ADNP-dependent histone remodeling complex promotes T helper 2 immune cell differentiation. \u003ci\u003eImmunity\u003c\/i\u003e.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eSheikh, A., Lu, J., Melese, E., Seo, J. H., \u0026amp; Abraham, N. (2022). IL‐7 induces type 2 cytokine response in lung ILC2s and regulates GATA3 and CD25 expression. Journal of Leukocyte Biology\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003ePelgrim, C. E., van Ark, I., van Berkum, R. E., Schuitemaker-Borneman, A. M., Flier, I., Leusink-Muis, T., ... \u0026amp; Kraneveld, A. D. (2022). Effects of a nutritional intervention on impaired behavior and cognitive function in an emphysematous murine model of COPD with endotoxin-induced lung inflammation. \u003c\/span\u003e\u003ci\u003eFrontiers in nutrition\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e9\u003c\/i\u003e\u003cspan\u003e, 1010989.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eYe, L., Jin, K., Liao, Z., Xiao, Z., Xu, H., Lin, X., ... \u0026amp; Yu, X. (2022). Hypoxia-reprogrammed regulatory group 2 innate lymphoid cells promote immunosuppression in pancreatic cancer. EBioMedicine, 79, 104016.\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eHuang, Y., Li, X., Zhu, L., Huang, C., Chen, W., Ling, Z., ... \u0026amp; Zhang, Y. (2022). Thrombin cleaves IL‐33 and modulates IL‐33‐activated allergic lung inflammation. \u003c\/span\u003e\u003ci\u003eAllergy\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e77\u003c\/i\u003e\u003cspan\u003e(7), 2104-2120.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eLu, J. C. L. (2022). \u003ci\u003eTranscriptional regulation of type 2 innate lymphoid cells by interleukin-7 receptor signaling\u003c\/i\u003e (Doctoral dissertation, University of British Columbia).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eChen, W., Lai, D., Li, Y., Wang, X., Pan, Y., Fang, X., ... \u0026amp; Shu, Q. (2022). Neuronal-Activated ILC2s Promote IL-17A Production in Lung gd T Cells During Sepsis. \u003cem\u003eImmune Dysfunction: An Update of New Immune Cell Subsets and Cytokines in Sepsis\u003c\/em\u003e.\u003c\/p\u003e\n\u003cp\u003eO’Leary, C. E., Sbierski-Kind, J., Kotas, M. E., Wagner, J. C., Liang, H. E., Schroeder, A. W., ... \u0026amp; Locksley, R. M. (2022). Bile acid–sensitive tuft cells regulate biliary neutrophil influx. Science Immunology, 7(69), eabj1080.\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eChen, W., Lai, D., Li, Y., Wang, X., Pan, Y., Fang, X., ... \u0026amp; Shu, Q. (2022). Neuronal-Activated ILC2s Promote IL-17A Production in Lung gd T Cells During Sepsis. \u003c\/span\u003e\u003ci\u003eImmune Dysfunction: An Update of New Immune Cell Subsets and Cytokines in Sepsis\u003c\/i\u003e\u003cspan\u003e.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eSzklany, K., Engen, P. A., Naqib, A., Green, S. J., Keshavarzian, A., Lopez Rincon, A., ... \u0026amp; Kraneveld, A. D. (2021). Dietary Supplementation throughout Life with Non-Digestible Oligosaccharides and\/or n-3 Poly-Unsaturated Fatty Acids in Healthy Mice Modulates the Gut–Immune System–Brain Axis. \u003cem\u003eNutrients\u003c\/em\u003e, \u003cem\u003e14\u003c\/em\u003e(1), 173.\u003c\/p\u003e\n\u003cp\u003eNono, J. K., Mpotje, T., Mosala, P., Aziz, N. A., Musaigwa, F., Hlaka, L., ... \u0026amp; Brombacher, F. (2021). Treatment of Schistosoma mansoni Infected Mice Renders Them Less Susceptible to Reinfection. \u003cem\u003eFrontiers in Immunology\u003c\/em\u003e, \u003cem\u003e12\u003c\/em\u003e, 748387-748387.\u003c\/p\u003e\n\u003cp\u003eWilliams, C. M., Roy, S., Califano, D., McKenzie, A. N., Metzger, D. W., \u0026amp; Furuya, Y. (2021). The Interleukin-33–Group 2 Innate Lymphoid Cell Axis Represents a Potential Adjuvant Target To Increase the Cross-Protective Efficacy of Influenza Vaccine. Journal of Virology, 95(22), e00598-21.\u003c\/p\u003e\n\u003cp\u003eIijima, K., Kobayashi, T., Matsumoto, K., Ohara, K., Kita, H., \u0026amp; Drake, L. Y. (2021). Transient IL-33 upregulation in neonatal mouse lung promotes acute but not chronic type 2 immune responses induced by allergen later in life. Plos one, 16(5), e0252199.\u003cstrong\u003e\u003cbr\u003e\u003c\/strong\u003e\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e\n\u003cp\u003eKamijo, S., Hara, M., Suzuki, M., Nakae, S., Ogawa, H., Okumura, K., \u0026amp; Takai, T. (2021). Innate IL-17A enhances IL-33-independent skin eosinophilia and IgE response on subcutaneous papain sensitization. Journal of Investigative Dermatology, 141(1), 105-113\u003c\/p\u003e\n\u003cp\u003eFerreira, A. C., Szeto, A. C., Heycock, M. W., Clark, P. A., Walker, J. A., Crisp, A., ... \u0026amp; McKenzie, A. N. (2021). RORα  is a critical checkpoint for T cell and ILC2 commitment in the embryonic thymus. Nature Immunology, 1-13. \u003c\/p\u003e\n\u003cp\u003eSaunders, S. P., Floudas, A., Moran, T., Byrne, C. M., Rooney, M. D., Fahy, C. M., ... \u0026amp; Schwartz, C. (2020). Dysregulated skin barrier function in Tmem79 mutant mice promotes IL-17A-dependent spontaneous skin and lung inflammation. Allergy, 75(12), 3216-3227.\u003c\/p\u003e\n\u003cp\u003eAparicio-Domingo, P., Cannelle, H., Buechler, M. B., Nguyen, S., Kallert, S. M., Favre, S., ... \u0026amp; Pinschewer, D. D. (2020). Fibroblast-derived IL-33 is dispensable for lymph node homeostasis but critical for CD8 T-cell responses to acute and chronic viral infection. European Journal of Immunology.\u003c\/p\u003e\n\u003cp\u003eFeng, X., Zhao, C., Li, L., Feng, J., He, W., Shi, T., ... \u0026amp; Su, X. (2020). iNKT cells with high PLZF expression are recruited into the lung via CCL21-CCR7 signaling to facilitate the development of asthma tolerance in mice. European Journal of Immunology. \u003c\/p\u003e\n\u003cp\u003eZhang, K., Jin, Y., Lai, D., Wang, J., Wang, Y., Wu, X., ... \u0026amp; Wilson, M. (2020). RAGE-induced ILC2 expansion in acute lung injury due to haemorrhagic shock. Thorax.\u003c\/p\u003e\n\u003cp\u003eRomera-Hernández, M., Mathä, L., Steer, C. A., Ghaedi, M., \u0026amp; Takei, F. (2019). Identification of Group 2 Innate Lymphoid Cells in Mouse Lung, Liver, Small Intestine, Bone Marrow, and Mediastial and Mesenteric Lymph Nodes. Current Protocols in Immunology, e73. \u003c\/p\u003e\n\u003cp\u003eSasaki, T., Moro, K., Kubota, T., Kubota, N., Kato, T., Ohno, H., ... \u0026amp; Koyasu, S. (2019). Innate lymphoid cells in the induction of obesity. Cell Reports, 28(1), 202-217.\u003c\/p\u003e\n\u003cp\u003eAbbring, S., Ryan, J. T., Diks, M. A., Hols, G., Garssen, J., \u0026amp; van Esch, B. C. (2019). Suppression of Food Allergic Symptoms by Raw Cow’s Milk in Mice is Retained after Skimming but Abolished after Heating the Milk—A Promising Contribution of Alkaline Phosphatase. Nutrients, 11(7), 1499.\u003c\/p\u003e\n\u003cp\u003eBosnjak, B., Kazemi, S., Altenburger, L. M., Mokrovic, G., \u0026amp; Epstein, M. M. (2019). Th2-TRMs maintain life-long allergic memory in experimental asthma in mice. Frontiers in immunology, 10, 840.\u003c\/p\u003e\n\u003cp\u003eMathä, L., Shim, H., Steer, C. A., Yin, Y. H., Martinez-Gonzalez, I., \u0026amp; Takei, F. (2019). Female and male mouse lung group 2 innate lymphoid cells differ in gene expression profiles and cytokine production. PloS one, 14(3), e0214286. \u003c\/p\u003e\n\u003cp\u003eAbbring, S., Ryan, J. T., Diks, M. A., Hols, G., Garssen, J., \u0026amp; van Esch, B. C. (2019). Suppression of Food Allergic Symptoms by Raw Cow’s Milk in Mice is Retained after Skimming but Abolished after Heating the Milk—A Promising Contribution of Alkaline Phosphatase. Nutrients, 11(7), 1499. \u003c\/p\u003e\n\u003cp\u003eBosnjak, B., Kazemi, S., Altenburger, L. M., Mokrovic, G., \u0026amp; Epstein, M. M. (2019). Th2-TRMs maintain life-long allergic memory in experimental asthma in mice. Frontiers in Immunology, 10, 840.\u003c\/p\u003e\n\u003cp\u003eMathä, L., Shim, H., Steer, C. A., Yin, Y. H., Martinez-Gonzalez, I., \u0026amp; Takei, F. (2019). Female and male mouse lung group 2 innate lymphoid cells differ in gene expression profiles and cytokine production. PloS one, 14(3), e0214286.\u003c\/p\u003e\n\u003cp\u003eCui, W., Zhang, W., Yuan, X., Liu, S., Li, M., Niu, J., ... \u0026amp; Li, D. (2019). Vitamin A deficiency execrates Lewis lung carcinoma via induction of type 2 innate lymphoid cells and alternatively activates macrophages. Food Science \u0026amp; Nutrition.\u003c\/p\u003e\n\u003cp\u003eOkubo, Y., Tokumaru, S., Yamamoto, Y., Miyagawa, S. I., Sanjo, H., \u0026amp; Taki, S. (2019). Generation of a common innate lymphoid cell progenitor requires interferon regulatory factor 2. International immunology.\u003c\/p\u003e\n\u003cp\u003eKnolle, M. D., Chin, S. B., Rana, B. M., Englezakis, A., Nakagawa, R., Fallon, P. G., ... \u0026amp; McKenzie, A. N. (2018). MicroRNA-155 protects group 2 innate lymphoid cells from apoptosis to promote type-2 immunity. Frontiers in immunology, 9.\u003c\/p\u003e\n\u003cp\u003eMoldaver, D. M., Bharhani, M. S., Rudulier, C. D., Wattie, J., Inman, M. D., \u0026amp; Larché, M. (2019). Induction of bystander tolerance and immune deviation after Fel d 1 peptide immunotherapy. Journal of Allergy and Clinical Immunology, 143(3), 1087-1099. \u003c\/p\u003e\n\u003cp\u003eHiraishi, Y., Yamaguchi, S., Yoshizaki, T., Nambu, A., Shimura, E., Takamori, A., ... \u0026amp; Suzukawa, M. (2018). IL-33, IL-25 and TSLP contribute to development of fungal-associated protease-induced innate-type airway inflammation. Scientific reports, 8(1), 18052. \u003c\/p\u003e\n\u003cp\u003eZhou, Y., Wang, W., Zhao, C., Wang, Y., Wu, H., Sun, X., ... \u0026amp; Zhang, Y. (2018). Prostaglandin E2 Inhibits Group 2 Innate Lymphoid Cell Activation and Allergic Airway Inflammation Through E-Prostanoid 4-Cyclic Adenosine Monophosphate Signaling. Frontiers in immunology, 9, 501. \u003c\/p\u003e\n\u003cp\u003eBartemes, K., Chen, C. C., Iijima, K., Drake, L., \u0026amp; Kita, H. (2018). IL-33–responsive group 2 innate lymphoid cells are regulated by female sex hormones in the uterus. The Journal of Immunology, 200(1), 229-236.\u003c\/p\u003e\n\u003cp\u003eBall, D. H., Al-Riyami, L., Harnett, W., \u0026amp; Harnett, M. M. (2018). IL-33\/ST2 signalling and crosstalk with FcεRI and TLR4 is targeted by the parasitic worm product, ES-62. Scientific reports, 8(1), 4497. \u003c\/p\u003e\n\u003cp\u003eOgasawara, T., Kohashi, Y., Ikari, J., Taniguchi, T., Tsuruoka, N., Watanabe-Takano, H., ... \u0026amp; Fukushima, Y. (2018). Allergic TH2 Response Governed by B-Cell Lymphoma 6 Function in Naturally Occurring Memory Phenotype CD4+ T Cells. Frontiers in immunology, 9, 750.\u003c\/p\u003e\n\u003cp\u003eMoldaver, D. M., Bharhani, M. S., Rudulier, C. D., Wattie, J., Inman, M. D., \u0026amp; Larché, M. (2018). Induction of bystander tolerance and immune deviation following Fel d 1 Peptide Immunotherapy. Journal of Allergy and Clinical Immunology. \u003c\/p\u003e\n\u003cp\u003eShamji, M. H., Temblay, J. N., Cheng, W., Byrne, S. M., Macfarlane, E., Switzer, A. R., ... \u0026amp; Ashton-Rickardt, P. G. (2018). Antiapoptotic serine protease inhibitors contribute to survival of allergenic TH2 cells. Journal of Allergy and Clinical Immunology, 142(2), 569-581. \u003c\/p\u003e\n\u003cp\u003eCalifano, D., Furuya, Y., Roberts, S., Avram, D., McKenzie, A. N., \u0026amp; Metzger, D. W. (2018). IFN-γ increases susceptibility to influenza A infection through suppression of group II innate lymphoid cells. Mucosal immunology, 11(1), 209.\u003c\/p\u003e\n\u003cp\u003eMasuda, C., Miyasaka, T., Kawakami, K., Inokuchi, J., Kawano, T., Dobashi‐Okuyama, K., ... \u0026amp; Ohno, I. (2018). Sex‐based differences in CD103+ dendritic cells promote female‐predominant Th2 cytokine production during allergic asthma. Clinical \u0026amp; Experimental Allergy, 48(4), 379-393. \u003c\/p\u003e\n\u003cp\u003eLaman, J. D., Kooistra, S. M., \u0026amp; Clausen, B. E. (2017). Reproducibility issues: avoiding pitfalls in animal inflammation models. In Inflammation (pp. 1-17). Humana Press, New York, NY. \u003c\/p\u003e\n\u003cp\u003eNascimento, D. C., Melo, P. H., Pineros, A. R., Ferreira, R. G., Colón, D. F., Donate, P. B., ... \u0026amp; Borges, M. C. (2017). IL-33 contributes to sepsis-induced long-term immunosuppression by expanding the regulatory T cell population. Nature communications, 8, 14919.\u003c\/p\u003e\n\u003cp\u003eMadouri, F., Chenuet, P., Beuraud, C., Fauconnier, L., Marchiol, T., Rouxel, N., ... \u0026amp; Marquant, Q. (2017). Protein kinase Cθ controls type 2 innate lymphoid cell and TH2 responses to house dust mite allergen. Journal of Allergy and Clinical Immunology, 139(5), 1650-1666.\u003c\/p\u003e\n\u003cp\u003eSjöberg, L. C., Nilsson, A. Z., Lei, Y., Gregory, J. A., Adner, M., \u0026amp; Nilsson, G. P. (2017). Interleukin 33 exacerbates antigen driven airway hyperresponsiveness, inflammation and remodeling in a mouse model of asthma. Scientific Reports, 7(1), 4219 \u003c\/p\u003e\n\u003cp\u003eSugita, J., Asada, Y., Ishida, W., Iwamoto, S., Sudo, K., Suto, H., ... \u0026amp; Ohno, T. (2017). Contributions of Interleukin‐33 and TSLP in a papain‐soaked contact lens‐induced mouse conjunctival inflammation model. Immunity, inflammation and disease, 5(4), 515-525.\u003c\/p\u003e\n\u003cp\u003eSchwartz, C., Khan, A. R., Floudas, A., Saunders, S. P., Hams, E., Rodewald, H. R., ... \u0026amp; Fallon, P. G. (2017). ILC2s regulate adaptive Th2 cell functions via PD-L1 checkpoint control. Journal of Experimental Medicine, jem-20170051 \u003c\/p\u003e\n\u003cp\u003eImai, Y., Hosotani, Y., Ishikawa, H., Yasuda, K., Nagai, M., Jitsukawa, O., ... \u0026amp; Yamanishi, K. (2017). Expression of IL-33 in ocular surface epithelium induces atopic keratoconjunctivitis with activation of group 2 innate lymphoid cells in mice. Scientific Reports, 7(1), 10053.\u003c\/p\u003e\n\u003cp\u003eVonk, M. M., Wagenaar, L., Pieters, R. H., Knippels, L. M., Willemsen, L. E., Smit, J. J., ... \u0026amp; Garssen, J. (2017). The efficacy of oral and subcutaneous antigen-specific immunotherapy in murine cow’s milk-and peanut allergy models. Clinical and translational allergy, 7(1), 35.\u003c\/p\u003e\n\u003cp\u003eVonk, M. M., Diks, M. A., Wagenaar, L., Smit, J. J., Pieters, R. H., Garssen, J., ... \u0026amp; Knippels, L. M. (2017). Improved efficacy of oral immunotherapy using non-digestible oligosaccharides in a murine cow’s milk allergy model: a potential role for Foxp3+ regulatory T cells. Frontiers in immunology, 8, 1230.\u003c\/p\u003e\n\u003cp\u003eDrube, S., Grimlowski, R., Deppermann, C., Fröbel, J., Kraft, F., Andreas, N., ... \u0026amp; Göpfert, C. (2017). The Neurobeachin-like 2 protein regulates mast cell homeostasis. The Journal of Immunology, ji1700556.\u003c\/p\u003e\n\u003cp\u003eZoltowska Nilsson, A. M., Lei, Y., Adner, M., \u0026amp; Nilsson, G. P. (2017). Mast cell-dependent IL-33\/ST2 signaling is protective against the development of airway hyperresponsiveness in a house dust mite mouse model of asthma. American Journal of Physiology-Lung Cellular and Molecular Physiology, 314(3), L484-L492.\u003c\/p\u003e\n\u003cp\u003eDullaers, M., Schuijs, M. J., Willart, M., Fierens, K., Van Moorleghem, J., Hammad, H., \u0026amp; Lambrecht, B. N. (2017). House dust mite–driven asthma and allergen-specific T cells depend on B cells when the amount of inhaled allergen is limiting. Journal of Allergy and Clinical Immunology, 140(1), 76-88.\u003c\/p\u003e\n\u003cp\u003eXi, H., Katschke, K. J., Li, Y., Truong, T., Lee, W. P., Diehl, L., ... \u0026amp; Hackney, J. A. (2016). IL-33 amplifies an innate immune response in the degenerating retina. Journal of Experimental Medicine, 213(2), 189-207\u003c\/p\u003e\n\u003cp\u003eSchulze, B., Piehler, D., Eschke, M., Heyen, L., Protschka, M., Köhler, G., \u0026amp; Alber, G. (2016). Therapeutic expansion of CD4+ FoxP3+ regulatory T cells limits allergic airway inflammation during pulmonary fungal infection. FEMS Pathogens and Disease, 74(4), ftw020.\u003c\/p\u003e\n\u003cp\u003ede Miranda, S. M. N., Wilhelm, T., Huber, M., \u0026amp; Zorn, C. N. (2016). Differential Lyn-dependence of the SHIP1-deficient mast cell phenotype. Cell Communication and Signaling, 14(1), 12.\u003c\/p\u003e\n\u003cp\u003eVogel, K. U., Bell, L. S., Galloway, A., Ahlfors, H., \u0026amp; Turner, M. (2016). The RNA-binding proteins Zfp36l1 and Zfp36l2 enforce the thymic β-selection checkpoint by limiting DNA damage response signaling and cell cycle progression. The Journal of Immunology, 1600854.\u003c\/p\u003e\n\u003cp\u003eHams, E., Bermingham, R., Wurlod, F. A., Hogan, A. E., O’Shea, D., Preston, R. J., ... \u0026amp; Fallon, P. G. (2015). The helminth T2 RNase ω1 promotes metabolic homeostasis in an IL-33–and group 2 innate lymphoid cell–dependent mechanism. The FASEB Journal, 30(2), 824-835.\u003c\/p\u003e\n\u003cp\u003eBurrows, K. E., Dumont, C., Thompson, C. L., Catley, M. C., Dixon, K. L., \u0026amp; Marshall, D. (2015). OX40 blockade inhibits house dust mite driven allergic lung inflammation in mice and in vitro allergic responses in humans. European journal of immunology, 45(4), 1116-1128.\u003c\/p\u003e\n\u003cp\u003ePalomo, J., Reverchon, F., Piotet, J., Besnard, A. G., Couturier‐Maillard, A., Maillet, I., ... \u0026amp; Quesniaux, V. F. (2015). Critical role of IL‐33 receptor ST2 in experimental cerebral malaria development. European journal of immunology, 45(5), 1354-1365.\u003c\/p\u003e\n\u003cp\u003eHeger, K., Kober, M., Rieß, D., Drees, C., de Vries, I., Bertossi, A., ... \u0026amp; Schmidt‐Supprian, M. (2015). A novel Cre recombinase reporter mouse strain facilitates selective and efficient infection of primary immune cells with adenoviral vectors. European journal of immunology, 45(6), 1614-1620.\u003c\/p\u003e\n\u003cp\u003eSuzuki, M., Morita, R., Hirata, Y., Shichita, T., \u0026amp; Yoshimura, A. (2015). Spred1, a suppressor of the Ras–ERK pathway, negatively regulates expansion and function of group 2 innate lymphoid cells. The Journal of Immunology, 1500531.\u003c\/p\u003e\n\u003cp\u003eArshad, M. I., Guihard, P., Danger, Y., Noel, G., Le Seyec, J., Boutet, M. A., ... \u0026amp; Gascan, H. (2015). Oncostatin M induces IL-33 expression in liver endothelial cells in mice and expands ST2+ CD4+ lymphocytes. American Journal of Physiology-Gastrointestinal and Liver Physiology, 309(7), G542-G553.\u003c\/p\u003e\n\u003cp\u003eShim, D. H., Park, Y. A., Kim, M. J., Hong, J. Y., Baek, J. Y., Kim, K. W., ... \u0026amp; Hong, K. J. (2015). Pandemic influenza virus, pH 1N1, induces asthmatic symptoms via activation of innate lymphoid cells. Pediatric Allergy and Immunology, 26(8), 780-788.\u003c\/p\u003e\n\u003cp\u003eAhmed, A., \u0026amp; Koma, M. K. (2015). Interleukin‐33 Triggers B 1 Cell Expansion and Its Release of Monocyte\/Macrophage Chemoattractants and Growth Factors. Scandinavian journal of immunology, 82(2), 118-124.\u003c\/p\u003e\n\u003cp\u003eWojno, E. T., Monticelli, L. A., Tran, S. V., Alenghat, T., Osborne, L. C., Thome, J. J., ... \u0026amp; Artis, D. (2015). The prostaglandin D 2 receptor CRTH2 regulates accumulation of group 2 innate lymphoid cells in the inflamed lung. Mucosal immunology, 8(6), 1313.\u003c\/p\u003e\n\u003cp\u003eZhao, J., Wei, J., Bowser, R. K., Traister, R. S., Fan, M. H., \u0026amp; Zhao, Y. (2015). Focal Adhesion Kinase–Mediated Activation of Glycogen Synthase Kinase 3β Regulates IL-33 Receptor Internalization and IL-33 Signaling. The Journal of Immunology, 194(2), 795-802.\u003c\/p\u003e\n\u003cp\u003eMathie, S. A., Dixon, K. L., Walker, S. A., Tyrrell, V., Mondhe, M., O'Donnell, V. B., ... \u0026amp; Lloyd, C. M. (2015). Alveolar macrophages are sentinels of murine pulmonary homeostasis following inhaled antigen challenge. Allergy, 70(1), 80-89.\u003c\/p\u003e\n\u003cp\u003eYu, X., Pappu, R., Ramirez-Carrozzi, V., Ota, N., Caplazi, P., Zhang, J., \u0026amp; Grogan, J. L. (2014). TNF superfamily member TL1A elicits type 2 innate lymphoid cells at mucosal barriers. Mucosal immunology, 7(3), 730-740.\u003c\/p\u003e\n\u003cp\u003eMirchandani, A. S., Besnard, A. G., Yip, E., Scott, C., Bain, C. C., Cerovic, V., ... \u0026amp; Liew, F. Y. (2014). Type 2 innate lymphoid cells drive CD4+ Th2 cell responses. The Journal of Immunology, 192(5), 2442-2448.\u003c\/p\u003e\n\u003cp\u003eHams, E., Armstrong, M. E., Barlow, J. L., Saunders, S. P., Schwartz, C., Cooke, G., ... \u0026amp; Fallon, P. G. (2014). IL-25 and type 2 innate lymphoid cells induce pulmonary fibrosis. Proceedings of the National Academy of Sciences, 111(1), 367-372.\u003c\/p\u003e\n\u003cp\u003eHams, E., Locksley, R. M., McKenzie, A. N., \u0026amp; Fallon, P. G. (2013). Cutting edge: IL-25 elicits innate lymphoid type 2 and type II NKT cells that regulate obesity in mice. The Journal of Immunology, 191(11), 5349-5353.\u003c\/p\u003e\n\u003cp\u003eKabata, H., Moro, K., Fukunaga, K., Suzuki, Y., Miyata, J., Masaki, K., ... \u0026amp; Asano, K. (2013). Thymic stromal lymphopoietin induces corticosteroid resistance in natural helper cells during airway inflammation. Nature communications, 4.\u003c\/p\u003e\n\u003cp\u003eNussbaum, J. C., Van Dyken, S. J., von Moltke, J., Cheng, L. E., Mohapatra, A., Molofsky, A. B., ... \u0026amp; Locksley, R. M. (2013). Type 2 innate lymphoid cells control eosinophil homeostasis. Nature, 502(7470), 245-248.\u003c\/p\u003e\n\u003cp\u003eMaazi, H., Shirinbak, S., Boef, L. E., Fallarino, F., Volpi, C., Nawijn, M. C., \u0026amp; Oosterhout, A. J. M. (2013). Cytotoxic T lymphocyte antigen 4‐immunoglobulin G is a potent adjuvant for experimental allergen immunotherapy. Clinical \u0026amp; Experimental Immunology, 172(1), 113-120.\u003c\/p\u003e\n\u003cp\u003eElsen, L. W. J., Esch, B. C. A. M., Hofman, G. A., Kant, J., Heijning, B. J. M., Garssen, J., \u0026amp; Willemsen, L. E. M. (2013). Dietary long chain n‐3 polyunsaturated fatty acids prevent allergic sensitization to cow's milk protein in mice. Clinical \u0026amp; Experimental Allergy, 43(7), 798-810.\u003c\/p\u003e\n\u003cp\u003eMaazi, H., Shirinbak, S., Boef, L. E., Fallarino, F., Volpi, C., Nawijn, M. C., \u0026amp; Oosterhout, A. J. M. (2013). Cytotoxic T lymphocyte antigen 4‐immunoglobulin G is a potent adjuvant for experimental allergen immunotherapy. Clinical \u0026amp; Experimental Immunology, 172(1), 113-120.\u003c\/p\u003e\n\u003cp\u003eHalim, T. Y., MacLaren, A., Romanish, M. T., Gold, M. J., McNagny, K. M., \u0026amp; Takei, F. (2012). Retinoic-acid-receptor-related orphan nuclear receptor alpha is required for natural helper cell development and allergic inflammation. Immunity, 37(3), 463-474.\u003c\/p\u003e\n\u003cp\u003eZhao, J., Wei, J., Mialki, R. K., Mallampalli, D. F., Chen, B. B., Coon, T., ... \u0026amp; Zhao, Y. (2012). F-box protein FBXL19-mediated ubiquitination and degradation of the receptor for IL-33 limits pulmonary inflammation. Nature immunology, 13(7), 651-658.\u003c\/p\u003e\n\u003cp\u003eMüller, U., Piehler, D., Stenzel, W., Köhler, G., Frey, O., Held, J., ... \u0026amp; Alber, G. (2012). Lack of IL-4 receptor expression on T helper cells reduces T helper 2 cell polyfunctionality and confers resistance in allergic bronchopulmonary mycosis. Mucosal immunology, 5(3), 299-310.\u003c\/p\u003e\n\u003cp\u003eHalim, T. Y., Krass, R. H., Sun, A. C., \u0026amp; Takei, F. (2012). Lung natural helper cells are a critical source of Th2 cell-type cytokines in protease allergen-induced airway inflammation. Immunity, 36(3), 451-463.\u003c\/p\u003e\n\u003cp\u003eKim, H. Y., Chang, Y. J., Subramanian, S., Lee, H. H., Albacker, L. A., Matangkasombut, P., \u0026amp; Umetsu, D. T. (2012). Innate lymphoid cells responding to IL-33 mediate airway hyperreactivity independently of adaptive immunity. Journal of Allergy and Clinical Immunology, 129(1), 216-227.\u003c\/p\u003e\n\u003cp\u003eJiang, H. R., Milovanović, M., Allan, D., Niedbala, W., Besnard, A. G., Fukada, S. Y., ... \u0026amp; Liew, F. Y. (2012). IL‐33 attenuates EAE by suppressing IL‐17 and IFN‐γ production and inducing alternatively activated macrophages. European journal of immunology, 42(7), 1804-1814.\u003c\/p\u003e\n\u003cp\u003eMonticelli, L. A., Sonnenberg, G. F., Abt, M. C., Alenghat, T., Ziegler, C. G., Doering, T. A. \u0026amp; Artis, D. (2011). Innate lymphoid cells promote lung-tissue homeostasis after infection with influenza virus. Nature immunology, 12(11), 1045-1054.\u003c\/p\u003e\n\u003cp\u003e Al-Garawi, A., Fattouh, R., Botelho, F., Walker, T. D., Goncharova, S., Moore, C. L., \u0026amp; Jordana, M. (2011). Influenza A facilitates sensitization to house dust mite in infant mice leading to an asthma phenotype in adulthood. Mucosal immunology, 4(6), 682-694.\u003c\/p\u003e\n\u003cp\u003eIdentification of Semaphorin 4B as a Negative Regulator of Basophil-Mediated Immune Responses. Nakagawa, Y et al., J. Immunol. (2011) 186:2881\u003c\/p\u003e\n\u003cp\u003eContribution of IL-33 to induction and augmentation of experimental allergic conjuctivitis. Matsuba-Kitamura S, et al., International Immunology, May 2010\u003cbr\u003eEosinophils are dispensable for allergic remodeling and immunity in a model of house dust mite-induced airway disease. Fattouh R, et al. Am J Respir Crit Care Med. 2010 Aug 23.\u003c\/p\u003e\n\u003cp\u003eContribution of IL-33 to induction and augmentation of experimental allergic conjuctivitis. Matsuba-Kitamura S, et al., International Immunology, May 2010\u003cbr\u003eInterleukin-33 attenuates sepsis by enhancing neutrophil influx to the site of infection. Alves-Filho J, et al. Nature Medicine., 2010; 16(6):2-7.\u003c\/p\u003e\n\u003cp\u003eActivin-A induces regulatory T cells that suppress T helper cell immune responses and protect from allergic airway disease. Semitekolou M, et al. J. Exp. Med., 2009; 206(8):1769-85.\u003c\/p\u003e\n\u003cp\u003eIL-33 reduces the development of atherosclerosis. Ashley M. Miller et al., J. Exp. Med., Feb 2008; 205: 339 - 346.\u003c\/p\u003e\n\u003cp\u003eIL-1beta-driven ST2L expression promotes maturation resistance in rapamycin-conditioned dendritic cells. Turnquist H, et al. Journ. Immunol., 2008; 181(1):62-72.\u003c\/p\u003e\n\u003cp\u003eOsteopontin has a crucial role in allergic airway disease through regulation of dendritic cell subsets. Xanthou G, et al. Nature Medicine. 2007; 13(5):570-80\u003c\/p\u003e\n\u003cp\u003eSoluble ST2 Blocks Interleukin-33 Signaling in Allergic Airway Inflammation. Hiroko Hayakawa et al., J. Biol. Chem., Sep 2007; 282: 26369 - 26380.\u003c\/p\u003e\n\u003cp\u003ePhenotypic differences between Th1 and Th17 cells and negative regulation of Th1 cell differentiation by IL-17. Susumu Nakae et al., J. Leukoc. Biol., May 2007; 81: 1258 - 1268.\u003c\/p\u003e\n\u003cp\u003eAirway Epithelial STAT3 Is Required for Allergic Inflammation in a Murine Model of Asthma. Marina C. Simeone-Penney et al.,  J. Immunol., May 2007; 178: 6191 - 6199.\u003c\/p\u003e\n\u003cp\u003eCCR4 is a key modulator of innate immune responses. Ness T, et al. Journ. of immunol., 2006; 177(11): 7531-9.\u003c\/p\u003e\n\u003cp\u003eIFN- Induces Apoptosis in Developing Mast Cells, Meredith N. Mann-Chandler et al., J. Immunol., Sep 2005; 175: 3000 - 3005.\u003c\/p\u003e\n\u003cp\u003eIdentification of mast cell progenitors in adult mice, Ching-Cheng Chen et al.,  PNAS, Aug 2005; 102: 11408 - 11413.\u003c\/p\u003e\n\u003cp\u003ePredominance of Th2 response in human abdominal aortic aneurysm: Mistaken identity for IL-4-producing NK and NKT cells?  Chan WL, et al. Cellular Immun (2005) 233:109-114\u003c\/p\u003e\n\u003cp\u003eChanges in systemic type 1 and type 2 immunity in normal pregnancy and pre-eclampsia may be mediated by natural killer cells  Borzychowski, A.M. et al., Eur J Immunol (2005) 35:3054-3063.\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848199848125,"sku":"101001F","price":740.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/T1_ST2_IL-33R_Mouse_Monoclonal_Antibody_FITC.png?v=1719221286"},{"product_id":"arthritomab-antibody-cocktail-for-inducing-arthritis-50-mg","title":"ArthritoMab™ Antibody Cocktail for Balb\/c, DBA\/1, R10.RIII, 50 mg","description":"\u003cp\u003eArthritoMab™ Arthritis Inducing Antibody Cocktail is a cocktail of 4 arthritogenic monoclonal antibodies to collagen II (CII) used for inducing arthritis in the anti-Collagen Antibody Induced Arthritis (CAIA) model. It is an excellent alternative to both the K\/BxN and CIA models. Induction is rapid and results in a synchronized, steady and controlled disease progression that exhibits histological similarities to the classic CIA model. Download a protocol guide and data pack to learn more about the epitopes, protocol, optimization tips, positive controls and data.\u003c\/p\u003e\n\u003cp\u003eThe Collagen Antibody Induced Arthritis (CAIA) model is a relevant model for studying the efferent phase of RA, where leukocytes are attracted and respond to the immune complex in the joint. It is induced using a cocktail of antibodies to anti-CII and contains pathogenic features similar to that of RA such as pannus formation, cellular infiltration, synovitis and cartilage\/bone destruction.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003ca href=\"https:\/\/www.mdbioproducts.com\/pages\/arthritomab-antibody-cocktail-whitepaper\"\u003eDownload the whitepaper\u003c\/a\u003e\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003cmeta charset=\"UTF-8\"\u003eFor use with C57BL\/6, TG strains, see \u003ca href=\"https:\/\/www.mdbioproducts.com\/products\/arthritomab-antibody-cocktail-for-c57bl-6-50-mg?_pos=2\u0026amp;_sid=874b53f27\u0026amp;_ss=r\u0026amp;variant=39921477943485\" target=\"_blank\"\u003eArthritoMab™ Antibody Cocktail for C57BL\/6, TG, 50 mg\u003c\/a\u003e.\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cimg alt=\"\" src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/CIA-MAB-50-data_480x480.png?v=1625459580\"\u003e\u003c\/p\u003e\n\u003cp style=\"margin: 0in;\"\u003e\u003cem\u003e\u003cspan style=\"font-size: 10.0pt; font-family: 'Arial',sans-serif; color: #666666;\"\u003eFigure: Balb\/c were administered 2 mg of ArthritoMab antibody cocktail on day 0 followed by a LPS boost on day 3. Unlike competitor products, disease progression is steady and controlled for easy evaluation of prophylactic and therapeutic regimes.\u003c\/span\u003e\u003c\/em\u003e\u003cspan style=\"font-size: 10.0pt; font-family: 'Arial',sans-serif; color: #666666;\"\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cp style=\"margin: 0in;\"\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eBenefits of the CAIA model\u003c\/strong\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eLength of study:\u003c\/strong\u003e Arthritis develops in mice typically within 24-48 hr allowing the completion of a study within 2 weeks reducing the number of assessments and scoring periods.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReduced group size:\u003c\/strong\u003e Rate of incidence is nearly 100% depending on the strain allowing for smaller group sizes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSynchronization:\u003c\/strong\u003e onset of disease is synchronized between animals simplifying treatment schedules.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSteady \u0026amp; Controlled disease progression:\u003c\/strong\u003e No rapid \u0026amp; severe disease spikes enabling evaluation of all treatment schedules\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSusceptibility:\u003c\/strong\u003e Arthritis is induced not only in CIA-susceptible DBA\/1 and B10.RIII mice, but also in some CIA-resistant mice, such as Balb\/c.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eEliminates expensive colonies:\u003c\/strong\u003e Models such as the K\/BxN serum transfer model require labs to maintain expensive colonies and the sera can vary from batch to batch.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eComparison\u003c\/strong\u003e\u003c\/p\u003e\n\u003ctable\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003e\u003cstrong\u003eArthritoMab™\u003c\/strong\u003e\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003e\u003cstrong\u003eCompetitor\u003c\/strong\u003e\u003c\/p\u003e\n\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd\u003e\n\u003cp\u003eEpitopes Recognized\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003eCB11, CB10, CB8\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003eCB11 only\u003c\/p\u003e\n\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd\u003e\n\u003cp\u003eDisease Progression\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003eSteady \u0026amp; Controlled\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003eRapid \u0026amp; Severe\u003c\/p\u003e\n\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd\u003e\n\u003cp\u003ePaw involvement\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003eConsistent \u0026amp; Predominantely rear\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003eVariable \u0026amp; unpredictable\u003c\/p\u003e\n\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd\u003e\n\u003cp\u003eAnimals\/vial\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003e25\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003e20\u003c\/p\u003e\n\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eAbreviations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eAnti-Collagen Induced arthritis (ACIA)\u003c\/li\u003e\n\u003cli\u003eMonoclonal Antibody induced arthritis (mAb-RA)\u003c\/li\u003e\n\u003cli\u003eCollagen Antibody Induced Arthritis (CAIA) \u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cmeta charset=\"UTF-8\"\u003e\u003cspan\u003eTang, Y., Aleithan, F., Madahar, S. S., Mirzaesmaeili, A., Saran, S., Tang, J., ... \u0026amp; Abdul-Sater, A. A. (2024). Selective disruption of Traf1\/cIAP2 interaction attenuates inflammatory responses and limits sepsis and rheumatoid arthritis. \u003c\/span\u003e\u003ci\u003ebioRxiv\u003c\/i\u003e\u003cspan\u003e, 2024-08.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eMarin, A. A., Decker, R. E., Kumar, S., Lamantia, Z., Yokota, H., Emrick, T., \u0026amp; Figueiredo, M. L. (2022). Enhancing Arthritis Therapy with Targeted IL-27 Gene Delivery. Bioengineering, 9(6), 248.\u003c\/p\u003e\n\u003cp\u003eVan Mechelen, M., Hayer, S., Van Laere, K., Lories, R., \u0026amp; Neerinckx, B. (2022). AB0106 The Pattern of Joint Inflammation in the CAIA Mouse Model of Arthritis.\u003c\/p\u003e\n\u003cp\u003eSangaletti, S., Botti, L., Gulino, A., Lecis, D., Bassani, B., Portararo, P., ... \u0026amp; Colombo, M. P. (2020). SPARC regulation of PMN clearance protects from pristane induced lupus and rheumatoid arthritis. Available at SSRN 3678911.\u003cbr\u003e\u003cbr\u003eNandakumar, K. S., Collin, M., Happonen, K. E., Lundström, S. L., Croxford, A. M., Xu, B., ... \u0026amp; Holmdahl, R. (2018). Streptococcal endo--N-acetylglucosaminidase suppresses antibody mediated inflammation in vivo. Frontiers in immunology, 9, 1623.\u003cbr\u003e\u003cbr\u003eHamamura, K., Nishimura, A., Chen, A., Takigawa, S., Sudo, A., \u0026amp; Yokota, H. (2015). Salubrinal acts as a Dusp2 inhibitor and suppresses inflammation in anti-collagen antibody-induced arthritis. Cellular signalling, 27(4), 828-835\u003cbr\u003e\u003cbr\u003eAsnagli, H., Martire, D., Belmonte, N., Quentin, J., Bastian, H., Boucard-Jourdin, M., ... \u0026amp; Marchetti, I. (2014). Type 1 regulatory T cells specific for collagen type II as an efficient cell-based therapy in arthritis. Arthritis research \u0026amp; therapy, 16(3), R115\u003cbr\u003e\u003cbr\u003eOhtsubo-Yoshioka, M., Nunomura, S., Kataoka, T. R., Okayama, Y., \u0026amp; Ra, C. (2013). Fc receptor beta chain deficiency exacerbates murine arthritis in the anti-type II collagen antibody-induced experimental model. Modern rheumatology, 23(4), 804-810\u003cbr\u003e\u003cbr\u003eLeavenworth, J. W., Tang, X., Kim, H. J., Wang, X., \u0026amp; Cantor, H. (2013). Amelioration of arthritis through mobilization of peptide-specific CD8+ regulatory T cells. The Journal of clinical investigation, 123(3), 1382-1389.\u003cbr\u003e\u003cbr\u003eJacques, P., Lambrecht, S., Verheugen, E., Pauwels, E., Kollias, G., Armaka, M., ... \u0026amp; Elewaut, D. (2013). Proof of concept: enthesitis and new bone formation in spondyloarthritis are driven by mechanical strain and stromal cells. Annals of the rheumatic diseases, annrheumdis-2013\u003cbr\u003e\u003cbr\u003eKudryavtseva, E., Forde, T. S., Pucker, A. D., \u0026amp; Adarichev, V. A. (2012). Wnt signaling genes of murine chromosome 15 are involved in sex‐affected pathways of inflammatory arthritis. Arthritis \u0026amp; Rheumatism, 64(4), 1057-1068\u003cbr\u003e\u003cbr\u003eTe Boekhorst, B. C., Jensen, L. B., Colombo, S., Varkouhi, A. K., Schiffelers, R. M., Lammers, T., ... \u0026amp; Nicolay, K. (2012). MRI-assessed therapeutic effects of locally administered PLGA nanoparticles loaded with anti-inflammatory siRNA in a murine arthritis model. Journal of controlled release, 161(3), 772-780.\u003cbr\u003e\u003cbr\u003eDimitrova, P., Ivanovska, N., Belenska, L., Milanova, V., Schwaeble, W., \u0026amp; Stover, C. (2012). Abrogated RANKL expression in properdin-deficient mice is associated with better outcome from collagen-antibody-induced arthritis. Arthritis research \u0026amp; therapy, 14(4), R173.\u003cbr\u003e\u003cbr\u003eWruck, C. J., Fragoulis, A., Gurzynski, A., Brandenburg, L. O., Kan, Y. W., Chan, K., ... \u0026amp; Pufe, T. (2010). Role of oxidative stress in rheumatoid arthritis: insights from the Nrf2-knockout mice. Annals of the rheumatic diseases, annrheumdis132720\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eMin, S. H., Wang, Y., Gonsiorek, W., Anilkumar, G., Kozlowski, J., Lundell, D., ... \u0026amp; Grant, E. P. (2010). Pharmacological targeting reveals distinct roles for CXCR2\/CXCR1 and CCR2 in a mouse model of arthritis. \u003c\/span\u003e\u003ci\u003eBiochemical and biophysical research communications\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e391\u003c\/i\u003e\u003cspan\u003e(1), 1080-1086.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eHultqvist, M., Nandakumar, K. S., Björklund, U., \u0026amp; Holmdahl, R. (2009). The novel small molecule drug Rabeximod is effective in reducing disease severity of mouse models of autoimmune disorders. \u003c\/span\u003e\u003ci\u003eAnnals of the rheumatic diseases\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e68\u003c\/i\u003e\u003cspan\u003e(1), 130-135.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eZalevsky, J., Secher, T., Ezhevsky, S. A., Janot, L., Steed, P. M., O’Brien, C., ... \u0026amp; Szymkowski, D. E. (2007). Dominant-negative inhibitors of soluble TNF attenuate experimental arthritis without suppressing innate immunity to infection. \u003c\/span\u003e\u003ci\u003eThe Journal of Immunology\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e179\u003c\/i\u003e\u003cspan\u003e(3), 1872-1883.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eZalevsky, J., Secher, T., Janot, L., Wong, P., O'Brien, C., Ryffel, B., \u0026amp; Szymkowski, D. E. (2006, September). Preclinical efficacy of XPro (TM) 1595, a biologic dominant-negative inhibitor of soluble TNF that blocks inflammation without suppressing innate immunity. In \u003c\/span\u003e\u003ci\u003eARTHRITIS AND RHEUMATISM\u003c\/i\u003e\u003cspan\u003e (Vol. 54, No. 9, pp. S45-S45). DIV JOHN WILEY \u0026amp; SONS INC, 111 RIVER ST, HOBOKEN, NJ 07030 USA: WILEY-LISS.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eNandakumar, K. S., \u0026amp; Holmdahl, R. (2005). Efficient promotion of collagen antibody induced arthritis (CAIA) using four monoclonal antibodies specific for the major epitopes recognized in both collagen induced arthritis and rheumatoid arthritis. \u003c\/span\u003e\u003ci\u003eJournal of immunological methods\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e304\u003c\/i\u003e\u003cspan\u003e(1-2), 126-136.\u003c\/span\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39921464377533,"sku":"CIA-MAB-50","price":2400.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/ArthritoMab_Antibody_Cocktail_Balb7c_DBA_1_R10.RIII.png?v=1718879087"},{"product_id":"arthritomab-antibody-cocktail-for-c57bl-6-50-mg","title":"ArthritoMab™ Antibody Cocktail for C57BL\/6, TG, 50 mg","description":"\u003cp\u003eArthritoMab™ Antibody Cocktail is a reformulated cocktail of 4 monoclonal antibodies for the induction of arthritis as an alternative to the widely used collagen-induced arthritis (CIA) model. Many transgenic strains of mice are on a C57BL\/6 background. However this strain is refractory to arthritis induction either by CIA or CAIA. Traditionally to overcome this in the CAIA model an increased dose of antibody cocktail is given. This reformulated cocktail of antibodies is optimized for production of arthritis in C57BL\/6, inducing arthritis with lower doses of antibody. This new formulation can also be used in other strains of mouse, which traditionally require greater amounts of cocktail.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eThe Collagen Antibody Induced Arthritis (CAIA) model is a relevant model for studying the efferent phase of RA, where leukocytes are attracted and respond to the immune complex in the joint. It is induced using a cocktail of antibodies to anti-CII and contains pathogenic features similar to that of RA such as pannus formation, cellular infiltration, synovitis and cartilage\/bone destruction.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003e\u003ca href=\"https:\/\/www.mdbioproducts.com\/pages\/arthritomab-antibody-cocktail-whitepaper\"\u003eDownload the whitepaper. \u003c\/a\u003e\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eFor use with Balb\/c, DBA\/1, R10.RIII strains, see \u003ca href=\"https:\/\/www.mdbioproducts.com\/products\/arthritomab-antibody-cocktail-for-inducing-arthritis-50-mg?_pos=1\u0026amp;_sid=874b53f27\u0026amp;_ss=r\u0026amp;variant=39921464377533\" target=\"_blank\"\u003eArthritoMab™ Antibody Cocktail for Balb\/c, DBA\/1, R10.RIII, 50 mg\u003c\/a\u003e.\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cimg data-mce-fragment=\"1\" src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/CIA-MAB-2C-data_480x480.jpg?v=1625459730\" alt=\"\"\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eBenefits of the CAIA model\u003c\/strong\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003e\n\u003cstrong\u003eLength of study:\u003c\/strong\u003e Arthritis develops in mice typically within 24-48 hr allowing the completion of a study within 2 weeks reducing the number of assessments and scoring periods.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReduced group size:\u003c\/strong\u003e Rate of incidence is nearly 100% depending on the strain allowing for smaller group sizes.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSynchronization:\u003c\/strong\u003e onset of disease is synchronized between animals simplifying treatment schedules.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSteady \u0026amp; Controlled disease progression:\u003c\/strong\u003e No rapid \u0026amp; severe disease spikes enabling evaluation of all treatment schedules\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eSusceptibility:\u003c\/strong\u003e Induce arthritis in transgenic strains with as little as 2 mg of Antibody. \u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eComparison\u003c\/strong\u003e\u003c\/p\u003e\n\u003ctable\u003e\n\u003ctbody\u003e\n\u003ctr\u003e\n\u003ctd\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003e\u003cstrong\u003eArthritoMab™\u003c\/strong\u003e\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003e\u003cstrong\u003eCompetitor\u003c\/strong\u003e\u003c\/p\u003e\n\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd\u003e\n\u003cp\u003eEpitopes Recognized\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003eCB11, CB10, CB8\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003eCB11 only\u003c\/p\u003e\n\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd\u003e\n\u003cp\u003eDisease Progression\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003eSteady \u0026amp; Controlled\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003eRapid \u0026amp; Severe\u003c\/p\u003e\n\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd\u003e\n\u003cp\u003ePaw involvement\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003eConsistent \u0026amp; Predominantely rear\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003eVariable \u0026amp; unpredictable\u003c\/p\u003e\n\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr\u003e\n\u003ctd\u003e\n\u003cp\u003eAmount required for C57Bl\/6\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003e2 mg (25 animals per vial)\u003c\/p\u003e\n\u003c\/td\u003e\n\u003ctd\u003e\n\u003cp\u003e5 mg (8 animals per vial)\u003c\/p\u003e\n\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e\n\u003cp\u003e\u003cstrong\u003e\u003c\/strong\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eAbbreviations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eAnti-Collagen Induced arthritis (ACIA)\u003c\/li\u003e\n\u003cli\u003eMonoclonal Antibody induced arthritis (mAb-RA)\u003c\/li\u003e\n\u003cli\u003eCollagen Antibody Induced Arthritis (CAIA)\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cmeta charset=\"UTF-8\"\u003eRinotas V, Iliaki K, Pavlidi L, Meletakos T, Mosialos G, Armaka M. Cyld restrains the hyperactivation of synovial fibroblasts in inflammatory arthritis by regulating the TAK1\/IKK2 signaling axis. \u003ci\u003eCell Death Dis\u003c\/i\u003e. 2024;15(8):584. Published 2024 Aug 9. doi:10.1038\/s41419-024-06966-2\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eMoulin, D., Millard, M., Taïeb, M., Michaudel, C., Aucouturier, A., Lefèvre, A., ... \u0026amp; Sokol, H. (2024). Counteracting tryptophan metabolism alterations as a new therapeutic strategy for rheumatoid arthritis. \u003c\/span\u003e\u003ci\u003eAnnals of the Rheumatic Diseases\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e83\u003c\/i\u003e\u003cspan\u003e(3), 312-323.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eMaleitzke, T., Dietrich, T., Hildebrandt, A., Weber, J., Appelt, J., Jahn, D., ... \u0026amp; Keller, J. (2023). Inactivation of the gene encoding procalcitonin prevents antibody-mediated arthritis. Inflammation Research, 1-13.\u003c\/p\u003e\n\u003cp\u003eShoda, J., Tanaka, S., Etori, K., Hattori, K., Kasuya, T., Ikeda, K., ... \u0026amp; Nakajima, H. (2022). Semaphorin 3G exacerbates joint inflammation through the accumulation and proliferation of macrophages in the synovium. Arthritis Research \u0026amp; Therapy, 24(1), 1-12.\u003c\/p\u003e\n\u003cp\u003eMaleitzke, T., Weber, J., Hildebrandt, A., Dietrich, T., Zhou, S., Tsitsilonis, S., \u0026amp; Keller, J. (2022). Standardized protocol and outcome measurements for the collagen antibody-induced arthritis mouse model. STAR protocols, 3(4), 101718. \u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eMaleitzke, T., Hildebrandt, A., Dietrich, T., Appelt, J., Jahn, D., Otto, E., ... \u0026amp; Keller, J. (2022). The Calcitonin Receptor Protects Against Bone Loss and Excessive Inflammation in Collagen Antibody-Induced Arthritis. \u003cem\u003eiScience\u003c\/em\u003e, 103689.\u003c\/p\u003e\n\u003cp\u003eDaïen, C. I., Tan, J., Audo, R., Mielle, J., Quek, L. E., Krycer, J. R., ... \u0026amp; Macia, L. (2021). Gut-derived acetate promotes B10 cells with anti-inflammatory effects. JCI insight, 6(7).\u003c\/p\u003e\n\u003cp\u003eSangaletti, S., Botti, L., Gulino, A., Lecis, D., Bassani, B., Portararo, P., ... \u0026amp; Colombo, M. P. (2020). SPARC regulation of PMN clearance protects from pristane induced lupus and rheumatoid arthritis. Available at SSRN 3678911.\u003cbr\u003e\u003cbr\u003eNandakumar, K. S., Collin, M., Happonen, K. E., Lundström, S. L., Croxford, A. M., Xu, B., ... \u0026amp; Holmdahl, R. (2018). Streptococcal endo--N-acetylglucosaminidase suppresses antibody mediated inflammation in vivo. Frontiers in immunology, 9, 1623.\u003c\/p\u003e\n\u003cp\u003e\u003cspan data-mce-fragment=\"1\"\u003eJahagirdar, R., Attwell, S., Marusic, S., Bendele, A., Shenoy, N., McLure, K. G., ... \u0026amp; Kulikowski, E. (2017). RVX-297, a BET bromodomain inhibitor, has therapeutic effects in preclinical models of acute inflammation and autoimmune disease. \u003c\/span\u003e\u003ci data-mce-fragment=\"1\"\u003eMolecular Pharmacology\u003c\/i\u003e\u003cspan data-mce-fragment=\"1\"\u003e, \u003c\/span\u003e\u003ci data-mce-fragment=\"1\"\u003e92\u003c\/i\u003e\u003cspan data-mce-fragment=\"1\"\u003e(6), 694-706.\u003c\/span\u003e\u003cbr\u003e\u003cbr\u003eHamamura, K., Nishimura, A., Chen, A., Takigawa, S., Sudo, A., \u0026amp; Yokota, H. (2015). Salubrinal acts as a Dusp2 inhibitor and suppresses inflammation in anti-collagen antibody-induced arthritis. Cellular signalling, 27(4), 828-835\u003cbr\u003e\u003cbr\u003eAsnagli, H., Martire, D., Belmonte, N., Quentin, J., Bastian, H., Boucard-Jourdin, M., ... \u0026amp; Marchetti, I. (2014). Type 1 regulatory T cells specific for collagen type II as an efficient cell-based therapy in arthritis. Arthritis research \u0026amp; therapy, 16(3), R115\u003cbr\u003e\u003cbr\u003eOhtsubo-Yoshioka, M., Nunomura, S., Kataoka, T. R., Okayama, Y., \u0026amp; Ra, C. (2013). Fc receptor beta chain deficiency exacerbates murine arthritis in the anti-type II collagen antibody-induced experimental model. Modern rheumatology, 23(4), 804-810\u003cbr\u003e\u003cbr\u003eLeavenworth, J. W., Tang, X., Kim, H. J., Wang, X., \u0026amp; Cantor, H. (2013). Amelioration of arthritis through mobilization of peptide-specific CD8+ regulatory T cells. The Journal of clinical investigation, 123(3), 1382-1389.\u003cbr\u003e\u003cbr\u003eJacques, P., Lambrecht, S., Verheugen, E., Pauwels, E., Kollias, G., Armaka, M., ... \u0026amp; Elewaut, D. (2013). Proof of concept: enthesitis and new bone formation in spondyloarthritis are driven by mechanical strain and stromal cells. Annals of the rheumatic diseases, annrheumdis-2013\u003cbr\u003e\u003cbr\u003eKudryavtseva, E., Forde, T. S., Pucker, A. D., \u0026amp; Adarichev, V. A. (2012). Wnt signaling genes of murine chromosome 15 are involved in sex‐affected pathways of inflammatory arthritis. Arthritis \u0026amp; Rheumatism, 64(4), 1057-1068\u003cbr\u003e\u003cbr\u003eTe Boekhorst, B. C., Jensen, L. B., Colombo, S., Varkouhi, A. K., Schiffelers, R. M., Lammers, T., ... \u0026amp; Nicolay, K. (2012). MRI-assessed therapeutic effects of locally administered PLGA nanoparticles loaded with anti-inflammatory siRNA in a murine arthritis model. Journal of controlled release, 161(3), 772-780.\u003cbr\u003e\u003cbr\u003eDimitrova, P., Ivanovska, N., Belenska, L., Milanova, V., Schwaeble, W., \u0026amp; Stover, C. (2012). Abrogated RANKL expression in properdin-deficient mice is associated with better outcome from collagen-antibody-induced arthritis. Arthritis research \u0026amp; therapy, 14(4), R173.\u003cbr\u003e\u003cbr\u003eWruck, C. J., Fragoulis, A., Gurzynski, A., Brandenburg, L. O., Kan, Y. W., Chan, K., ... \u0026amp; Pufe, T. (2010). Role of oxidative stress in rheumatoid arthritis: insights from the Nrf2-knockout mice. Annals of the rheumatic diseases, annrheumdis132720.\u003cbr\u003e\u003cbr\u003e\u003cbr\u003e\u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39921477943485,"sku":"CIA-MAB-2C","price":2460.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/ArthritoMab_Antibody_Cocktail_C57BL_6_TG.png?v=1718879181"},{"product_id":"collagen-type-ii-monoclonal-antibody-clone-m2139-100ug","title":"Collagen Type II, Monoclonal Antibody (Clone M2139), 100ug","description":"\u003cdiv class=\"page\" title=\"Page 2\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003eThis antibody (clone 2139) recognizes the conformational J1 epitope on the triple-helical structure of the native Collagen Type II molecule. The J1 epitope on mouse collagen consists of residues 551–564. It cross-reacts with mouse, rat, human, bovine, and chicken.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eCollagen type II, encoded by the COL2A1 gene, is a crucial component of cartilage and plays a vital role in maintaining joint integrity. In mouse models of arthritis, such as collagen-induced arthritis, COL2A1 is studied for its role in cartilage degradation, a key feature of conditions like rheumatoid arthritis and osteoarthritis. Research on COL2A1 helps in understanding arthritis mechanisms and de\u003cimg\u003eveloping new treatments.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cstrong\u003eSynonyms:\u003c\/strong\u003e\u003cbr\u003eCollagen alpha-1(II) chain, COL2A1, Collagen Type II, Collagen Type 2, CII.\u003c\/span\u003e\u003cspan\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv class=\"page\" title=\"Page 2\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\" style=\"text-align: start;\"\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cimg alt=\"Collagen Type II, Monoclonal Antibody (Clone M2139), 100ug\" src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Image_1061001_-M2139_graph_6_wider.png?v=1732026475\" style=\"margin-bottom: 16px; float: none;\" data-mce-src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Image_1061001_-M2139_graph_6_wider.png?v=1732026475\"\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eM2139 binds to the triple helical J1 epitope on collagen II. Binding to collagen II epitopes was determined in bead-based flow immunoassay as median fluorescence intensity (MFI). Triple helical (Gly-Pro- Hyp)x11 is a synthetic control peptide with 11 repeats of the Gly-Pro-Hyp sequence and mimics the collagen II backbone structure.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cstrong\u003eReferences:\u003c\/strong\u003e\u003cbr\u003e\u003cmeta charset=\"UTF-8\"\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv class=\"page\" title=\"Page 2\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003e1. Mo JA, Holmdahl R. The B cell response to autologous type II collagen: biased V gene repertoire with V gene sharing and epitope shift. J Immunol. 1996 Sep 15;157(6):2440-8.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cbr\u003e2. Tong D, Lönnblom E, Yau ACY, Nandakumar KS, Liang B, Ge C, Viljanen J, Li L, Bãlan M, Klareskog L, Chagin AS, Gjertsson I, Kihlberg J, Zhao M, Holmdahl R. A Shared Epitope of Collagen Type XI and Type II Is Recognized by Pathogenic Antibodies in Mice and Humans with Arthritis. Front Immunol. 2018 Apr 12;9:451.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e3. Uysal H, Bockermann R, Nandakumar KS, Sehnert B, Bajtner E, Engström A, Serre G, Burkhardt H, Thunnissen MM, Holmdahl R. Structure and pathogenicity of antibodies specific for citrullinated collagen type II in experimental arthritis. J Exp Med. 2009 Feb 16;206(2):449- 62.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e4. Li Y, Tong D, Liang P, Lönnblom E, Viljanen J, Xu B, Nandakumar KS, Holmdahl R. Cartilage-binding antibodies initiate joint inflammation and promote chronic erosive arthritis. Arthritis Res Ther. 2020 May 24;22(1):120.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e5. Amirahmadi SF, Whittingham S, Crombie DE, Nandakumar KS, Holmdahl R, Mackay IR, van Damme MP, Rowley MJ. Arthritogenic anti- type II collagen antibodies are pathogenic for cartilage-derived chondrocytes independent of inflammatory cells. Arthritis Rheum. 2005 \u003c\/span\u003e\u003cspan\u003eJun; 52(6):1897-906.\u003c\/span\u003e\u003c\/p\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003cp\u003e\u003cspan\u003e\u003cbr\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":44656161226941,"sku":"1061001","price":490.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Monoclonal_Antibody_to_Collagen_Type_II_Clone_M2139_COL2A1_Affinity_Purified.png?v=1732184195"},{"product_id":"collagen-type-xi-monoclonal-antibody-100ug","title":"Collagen Type XI, Monoclonal Antibody, 100ug","description":"\u003cdiv title=\"Page 3\" class=\"page\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003eThis antibody (clone L10D9) binds to the triple-helical D3 epitope on collagen XI, which is shared with Collagen type II. The antibody binds to both Collagen Type XI (CXI) and Collagen Type II (CII), and CII is equally strong, with a specific binding for the D3 epitope region of the COL2A1 chain1. It cross-reacts with mouse and human.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eCollagen type XI is a minor fibrillar collagen that plays a crucial role in cartilage organization and structural integrity. It is a component of the extracellular matrix that regulates collagen fibril diameter and cartilage development. In mouse models of arthritis, such as collagen- induced and spontaneous arthritis models, collagen type XI is studied for its involvement in cartilage degradation and joint pathology. Understanding the role of collagen type XI in these models helps researchers explore its contribution to the progression of arthritis, providing insights into potential therapeutic targets for joint diseases.\u003c\/span\u003e\u003cspan\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv title=\"Page 3\" class=\"page\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv style=\"text-align: start;\" class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003e\u003cstrong\u003eSynonyms:\u003c\/strong\u003e\u003cbr\u003eCollagen XI, CXI, Collagen Type XI, Collagen Type 11.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cimg style=\"float: none;\" src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Image_1061002_L10D9-binding-to-D3-on-CII-and-CXI_MFI_linear_480x480.png?v=1732028185\" alt=\"Monoclonal Antibody to Collagen Type XI Affinity Purified\"\u003e\u003cspan\u003e\u003cimg\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv title=\"Page 2\" class=\"page\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003eL10D9 binds to the triple helical D3 \u003c\/span\u003e\u003cspan\u003eepitope on collagen. Binding to collagen epitopes was determined in bead-based \u003c\/span\u003e\u003cspan\u003eflow immunoassay as mean fluorescence intensity (MFI).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eReferences:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cdiv title=\"Page 2\" class=\"page\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003e1. Tong D, Lönnblom E, Yau ACY, Nandakumar KS, Liang B, Ge C, Viljanen J, Li L, Bãlan M, Klareskog L, Chagin AS, Gjertsson I, Kihlberg J, Zhao M, Holmdahl R. A Shared Epitope of Collagen Type XI and Type II Is Recognized by Pathogenic Antibodies in Mice and Humans with Arthritis. Front Immunol. 2018 Apr 12;9:451.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e2. Li Y, Tong D, Liang P, Lönnblom E, Viljanen J, Xu B, Nandakumar KS, Holmdahl R. Cartilage-binding antibodies initiate joint inflammation and promote chronic erosive arthritis. Arthritis Res Ther.\u003cbr\u003e2020 May 24;22(1):120.\u003c\/span\u003e\u003c\/p\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003cbr\u003e\n\u003c\/div\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":44656271327421,"sku":"1061002","price":490.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Monoclonal_Antibody_to_Collagen_Type_XI_Affinity_Purified.png?v=1732184449"},{"product_id":"acc1-monoclonal-antibody-100ug","title":"ACC1, Monoclonal Antibody, 100ug","description":"\u003cdiv class=\"page\" title=\"Page 4\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\" style=\"text-align: start;\" data-mce-style=\"text-align: start;\"\u003e\n\u003cp\u003e\u003cspan\u003eThis antibody binds ACC1 to the citrullinated triple-helical collagen type II (CII) epitope (position 359-369), the C1 epitope. The ACC1 antibody recognizes the second citrulline at position 365 in mouse Collagen Type II. The antibody binds to flexible triple-helical Collagen Type II determinants and many citrullinated CII peptides and was found to cross-react with several non-citrullinated epitopes on native Collagen Type II. It cross-reacts with mouse and human.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eCitrullination of proteins is a post-translational modification in which arginine is converted into citrulline by a family of enzymes called peptidylarginine deiminases (PADs). Proteins are susceptible to citrullination during inflammatory processes, and an autoantibody response to citrullinated proteins is a hallmark of Rheumatoid Arthritis.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cstrong\u003eSynonyms:\u003c\/strong\u003e\u003cbr\u003eCOL2A1, Collagen Type II, Collagen alpha-1(II) chain, CII, Col II, citrullinated CII; citrullinated Col II; citrullinated proteins.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cimg alt=\"Monoclonal Antibody to ACC1 Citrullinated Collagen Type II, Affinity Purified\" src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Image_1061003_ACC1_image_480x480.png?v=1732029100\" style=\"margin-bottom: 16px; float: none;\" data-mce-src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Image_1061003_ACC1_image_480x480.png?v=1732029100\" data-mce-style=\"margin-bottom: 16px; float: none;\"\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv class=\"page\" title=\"Page 2\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003eThe Mouse Anti-citrullinated COL2A1 Antibody clone ACC1 binds to the triple helical C1 epitope on collagen II when citrullinated. Binding to collagen type II epitopes was determined in bead-based flow immunoassay as median fluorescence intensity (MFI).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cstrong\u003eReferences:\u003c\/strong\u003e\u003cbr\u003e\u003cmeta charset=\"UTF-8\"\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv class=\"page\" title=\"Page 2\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003e1. Uysal H, Bockermann R, Nandakumar KS, Sehnert B, Bajtner E, Engström A, Serre G, Burkhardt H, Thunnissen MM, Holmdahl R. Structure and pathogenicity of antibodies specific for citrullinated collagen type II in experimental arthritis. J Exp Med. 2009 Feb 16;206(2):449-62.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e2. Ge C, Tong D, Liang B, Lönnblom E, Schneider N, Hagert C, Viljanen J, Ayoglu B, Stawikowska R, Nilsson P, Fields GB, Skogh T, Kastbom A, Kihlberg J, Burkhardt H, Dobritzsch D, Holmdahl R. Anti-citrullinated protein antibodies cause arthritis by cross-reactivity to joint cartilage. JCI Insight. 2017 Jul 6;2(13):e93688.\u003c\/span\u003e\u003c\/p\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003cp\u003e\u003cspan\u003e\u003cbr\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":44656281911485,"sku":"1061003","price":490.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Monoclonal_Antibody_to_ACC1_Citrullinated_Collagen_Type_II_Affinity_Purified.png?v=1732184794"},{"product_id":"acc4-igg1-monoclonal-antibody-100ug","title":"ACC4 (IgG1), Monoclonal Antibody, 100ug","description":"\u003cdiv class=\"page\" title=\"Page 5\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\" style=\"text-align: start;\" data-mce-style=\"text-align: start;\"\u003e\n\u003cp\u003e\u003cspan\u003eThis antibody is an anti-citrullinated protein antibody (ACPA) that, on Collagen alpha-1 (II) chain, binds specifically to citrullinated C1 epitope on alpha-chain (position 359–369). It cross-reacts with mouse, bovine, and potentially human.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eCitrullination of proteins is a post-translational modification in which arginine is converted into citrulline by a family of enzymes called peptidylarginine deiminases (PADs). Proteins are susceptible to citrullination during inflammatory processes, and an autoantibody response to citrullinated proteins is a hallmark of Rheumatoid Arthritis.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eSynonyms:\u003cbr\u003eCOL2A1, Collagen Type II, Collagen alpha-1(II) chain, CII, Col II, citrullinated CII; citrullinated Col II; citrullinated proteins.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cimg alt=\"Monoclonal Antibody to ACC4 (IgG1) Citrullinated Collagen Type II, Affinity Purified\" src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Image_1061004_image002_480x480.png?v=1732029827\" style=\"margin-bottom: 16px; float: none;\" data-mce-src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Image_1061004_image002_480x480.png?v=1732029827\" data-mce-style=\"margin-bottom: 16px; float: none;\"\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv class=\"page\" title=\"Page 2\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003eThe mouse Anti-citrullinated COL2A1 Antibody clone ACC4 binds to the C1 epitope on alpha-chain of collagen II when the first arginine in the epitope (position 359–369; is citrullinated (Cit- Arg). The antibody does not bind to the C1 epitope when the second arginine is citrullinated (Arg-Cit), neither when both arginines are citrullinated (Cit- Cit). The antibody binds to the epitope in both triple helical and cyclic form. Binding to collagen II epitopes was determined in bead-based flow immunoassay as median fluorescence intensity (MFI).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eReferences:\u003cmeta charset=\"UTF-8\"\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv title=\"Page 2\" class=\"page\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003e1. He, Y., Ge, C., Moreno-Giró, À. et al. A subset of antibodies targeting citrullinated proteins confers protection from rheumatoid arthritis. Nat Commun 14, 691 (2023).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cbr\u003e2. Uysal H, Bockermann R, Nandakumar KS, Sehnert B, Bajtner E, Engström A, Serre G, Burkhardt H, Thunnissen MM, Holmdahl R. Structure and pathogenicity of antibodies specific for citrullinated collagen type II in experimental arthritis. J Exp Med. 2009 Feb 16;206(2):449-62.\u003c\/span\u003e\u003c\/p\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":44656305799357,"sku":"1061004","price":490.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Monoclonal_Antibody_to_ACC4_IgG1_Citrullinated_Collagen_Type_II_Affinity_Purified.png?v=1732185071"},{"product_id":"acc4-igg2b-monoclonal-antibody-100ug","title":"ACC4 (IgG2b), Monoclonal Antibody, 100ug","description":"\u003cdiv title=\"Page 6\" class=\"page\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003eThis antibody is an anti-citrullinated protein antibody (ACPA) that on Collagen alpha-1 (II) chain binds specifically to citrullinated C1 epitope on alpha-chain (position 359–369). It cross-reacts with mouse, bovine, and potentially human.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eCitrullination of proteins is a post-translational modification in which arginine is converted into citrulline by a family of enzymes called peptidylarginine deiminases (PADs). Proteins are susceptible to citrullination during inflammatory processes, and an autoantibody response to citrullinated proteins is a hallmark of Rheumatoid Arthritis.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eSynonyms:\u003cbr\u003eCOL2A1, Collagen Type II, Collagen alpha-1(II) chain, CII, Col II, citrullinated CII; citrullinated Col II; citrullinated proteins.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eReferences:\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv title=\"Page 2\" class=\"page\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003e1. He, Y., Ge, C., Moreno-Giró, À. et al. A subset of antibodies targeting citrullinated proteins confers protection from rheumatoid arthritis. Nat Commun 14, 691 (2023).\u003cbr\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e2. Uysal H, Bockermann R, Nandakumar KS, Sehnert B, Bajtner E, Engström A, Serre G, Burkhardt H, Thunnissen MM, Holmdahl R. Structure and pathogenicity of antibodies specific for citrullinated collagen type II in experimental arthritis. J Exp Med. 2009 Feb 16;206(2):449-62.\u003c\/span\u003e\u003c\/p\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":44656327196861,"sku":"1061005","price":490.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Monoclonal_Antibody_to_ACC4_IgG2b_Citrullinated_Collagen_Type_II_Affinity_Purified.png?v=1732185318"},{"product_id":"acpa-monoclonal-antibody-clone-e4ng-100ug","title":"ACPA, Monoclonal Antibody (Clone E4NG), 100ug","description":"\u003cdiv class=\"page\" title=\"Page 7\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\" style=\"text-align: start;\"\u003e\n\u003cp\u003e\u003cspan\u003eThis antibody recognizes multiple citrullinated proteins\/peptides, including CCP2, citrullinated collagen type 2 (COL2) peptides, citrullinated human\/mouse alpha-enolase (citENO1), etc., and potentially other citrullinated proteins\/peptides typically manifested in rheumatoid arthritis, as a citrulline-specific antibody. E4NG has a mutation on glycosylation sites in the variable domain, prohibiting the expression of the Fab-glycan (no N-glycosylation on the variable domain). It cross-reacts with mouse and human.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eNote: For negative control antibody use Catalogue number \u003ca href=\"https:\/\/www.mdbioproducts.com\/products\/acpa-negative-control-monoclonal-antibody-clone-e4ng-mutant-100ug?_pos=2\u0026amp;_sid=064ebe571\u0026amp;_ss=r\u0026amp;variant=44659589218493\"\u003e1061006-NC\u003c\/a\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eAnti-citrullinated protein antibodies (ACPA) are autoantibodies linked to rheumatoid arthritis (RA). In RA research, collagen-induced arthritis (CIA) or CAIA mouse models are used to study ACPA's role in disease mechanisms like inflammation and joint damage.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eSynonyms:\u003cbr\u003eCitrullinated epitopes of COL2, Collagen alpha-1(II) chain, COL2A1, type II collagen, CII1; Citrullinated epitopes of ENO1, MPB\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cimg alt=\"Monoclonal Antibody to ACPA Anti–Citrullinated Protein Antibody, Affinity Purified\" src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/1061006_-_resized_600x600.png?v=1732031488\" style=\"margin-bottom: 16px; float: none;\"\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv class=\"page\" title=\"Page 2\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003eThe antibody clone E4NG (Catalogue number 1061006) binds to citrullinated collagen type II (COL2) epitopes. E4NG-mutant (Catalogue number 1061006-NC) is the control antibody that does not bind to citrulline. Binding to unmodified COL2 peptides is low by both E4NG and E4NG-mutant antibodies. A multiplex flow immunoassay determined binding. (Results published in He et al Nat Comm 2023)\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eReferences:\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv class=\"page\" title=\"Page 2\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003e1. He, Y., Ge, C., Moreno-Giró, À. et al. A subset of antibodies targeting citrullinated proteins confers protection from rheumatoid arthritis. Nat Commun 14, 691 (2023).\u003c\/span\u003e\u003c\/p\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":44656405774525,"sku":"1061006","price":980.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Monoclonal_Antibody_to_ACPA_Anti_Citrullinated_Protein_Antibody_Affinity_Purified.png?v=1732185552"},{"product_id":"acpa-negative-control-monoclonal-antibody-clone-e4ng-mutant-100ug","title":"ACPA (Negative Control), Monoclonal Antibody (Clone E4NG-Mutant), 100ug","description":"\u003cdiv class=\"page\" title=\"Page 8\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\" style=\"text-align: start;\"\u003e\n\u003cp\u003e\u003cspan\u003eThis antibody is a negative control for the E4NG antibody (product number 1061006). It is the mutated version of the E4NG antibody, with identical sequence, methods of production\/purification and format to E4NG except two mutations in the paratope (W48M \u0026amp; S51A).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eThis antibody has neglectable or no affinity to citrulline and has no known cross-reactivity to other antigens. It may have minimal non- specific binding to CCP2, the cyclic citrullinated peptide(s) of the second generation of the anti-CCP test.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eThis antibody can be paired as a negative control with E4NG antibody (product number \u003ca href=\"https:\/\/www.mdbioproducts.com\/products\/acpa-monoclonal-antibody-clone-e4ng-100ug?_pos=2\u0026amp;_sid=dad76faf9\u0026amp;_ss=r\u0026amp;variant=44656405774525\"\u003e1061006\u003c\/a\u003e) for detecting citrullinated antigens. This negative control antibody is not sold separately.\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eAnti-citrullinated protein antibodies (ACPA) are autoantibodies linked to rheumatoid arthritis (RA). In RA research, collagen-induced arthritis (CIA) or CAIA mouse models are used to study ACPA's role in disease mechanisms like inflammation and joint damage.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eSynonyms:\u003cbr\u003eCitrullinated epitopes of COL2, Collagen alpha-1(II) chain, COL2A1, type II collagen, CII1; Citrullinated epitopes of ENO1, MPB1\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cimg alt=\"Monoclonal Antibody to ACPA (Negative Control) Anti–Citrullinated Protein Antibody, Affinity Purified\" src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/1061006_-_resized_600x600.png?v=1732031488\" style=\"margin-bottom: 16px; float: none;\"\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eThe antibody clone E4NG (Catalogue number 1061006) binds to citrullinated collagen type II (COL2) epitopes. E4NG-mutant (Catalogue number 1061006-NC) is the control antibody that does not bind to citrulline. Binding to unmodified COL2 peptides is low by both E4NG and E4NG-mutant antibodies. A multiplex flow immunoassay determined binding. (Results published in He et al Nat Comm 2023)\u003c\/span\u003e\u003cspan\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eReferences:\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv class=\"page\" title=\"Page 2\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003e1. He, Y., Ge, C., Moreno-Giró, À. et al. A subset of antibodies targeting citrullinated proteins confers protection from rheumatoid arthritis. Nat Commun 14, 691 (2023).\u003c\/span\u003e\u003c\/p\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":44659589218493,"sku":"1061006-NC","price":0.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Monoclonal_Antibody_to_ACPA_Negative_Control_Anti_Citrullinated_Protein_Antibody_Affinity_Purified.png?v=1732185748"},{"product_id":"cartilage-oligomeric-matrix-protein-comp-monoclonal-antibody-clone-15a11-100ug","title":"Cartilage Oligomeric Matrix Protein (COMP) , Monoclonal Antibody (Clone 15A11), 100ug","description":"\u003cdiv title=\"Page 9\" class=\"page\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv style=\"text-align: start;\" class=\"column\" data-mce-style=\"text-align: start;\"\u003e\n\u003cp\u003e\u003cspan\u003eThis antibody binds to the fourth EGF (Epithelial Growth Factor) -like domain of mouse COMP, comprising residues 232–252, called the P6 epitope.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eCartilage Oligomeric Matrix Protein (COMP) is a disulfide-linked pentameric proteoglycan primarily found in cartilage, but also present in other joint tissues such as meniscus, tendon, synovial fibroblasts, and osteoblasts. As a member of the thrombospondin family, COMP stimulates type II collagen fibril formation. It is released into the blood when cartilage is damaged, making it a valuable biomarker for predicting cartilage destruction in inflammatory joint diseases like rheumatoid arthritis (RA) and osteoarthritis (OA).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eSynonyms:\u003cbr\u003eCartilage Oligomeric Matrix Protein, COMP\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cimg style=\"margin-bottom: 16px; float: none;\" src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Image_1061007_Non-log_480x480.png?v=1732096698\" alt=\"Monoclonal Antibody to COMP (Clone 15A11) Cartilage Oligomeric Matrix Protein, Affinity Purified\" data-mce-style=\"margin-bottom: 16px; float: none;\" data-mce-src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Image_1061007_Non-log_480x480.png?v=1732096698\"\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv title=\"Page 2\" class=\"page\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003eThe mouse monoclonal anti-Cartilage Oligomeric Matrix Protein (COMP) antibody clone 15A11 binds to the fourth EGF (Epithelial Growth Factor) -like domain of murine COMP, comprising residues 232– 252, called the P6 epitope. Binding to recombinant human COMP was determined in enzyme linked immunosorbent assay (ELISA) as absorbance at 405nm.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eReferences:\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv title=\"Page 2\" class=\"page\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003e1. Geng H, Nandakumar KS, Pramhed A, Aspberg A, Mattsson R, Holmdahl R. Cartilage oligomeric matrix protein specific antibodies are pathogenic. Arthritis Res Ther. 2012 Aug 20;14(4):R191.\u003cbr\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e2. Li Y, Tong D, Liang P, Lönnblom E, Viljanen J, Xu B, Nandakumar KS, Holmdahl R. Cartilage-binding antibodies initiate joint inflammation and promote chronic erosive arthritis. Arthritis Res Ther. \u003c\/span\u003e\u003cspan\u003e2020 May 24;22(1):120.\u003c\/span\u003e\u003c\/p\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":44659607732413,"sku":"1061007","price":490.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Monoclonal_Antibody_to_COMP_Clone_15A11_Cartilage_Oligomeric_Matrix_Protein_Affinity_Purified.png?v=1732186037"},{"product_id":"cartilage-oligomeric-matrix-protein-comp-monoclonal-antibody-clone-16b5-100ug","title":"Cartilage Oligomeric Matrix Protein (COMP), Monoclonal Antibody (Clone 16B5), 100ug","description":"\u003cdiv title=\"Page 10\" class=\"page\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv style=\"text-align: start;\" class=\"column\" data-mce-style=\"text-align: start;\"\u003e\n\u003cp\u003e\u003cspan\u003eThis antibody binds to the coiled-coil domain or pentamer COMP. It cross-reacts with mouse, rat and human.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eCartilage Oligomeric Matrix Protein (COMP) is a disulfide-linked pentameric proteoglycan primarily found in cartilage, but also present in other joint tissues such as meniscus, tendon, synovial fibroblasts, and osteoblasts. As a member of the thrombospondin family, COMP\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003estimulates type II collagen fibril formation. It is released into the blood when cartilage is damaged, making it a valuable biomarker for predicting cartilage destruction in inflammatory joint diseases like rheumatoid arthritis (RA) and osteoarthritis (OA).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eSynonyms:\u003cbr\u003eCartilage Oligomeric Matrix Protein, COMP\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cimg style=\"margin-bottom: 16px; float: none;\" src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Image_1061008_16B5_480x480.png?v=1732097157\" alt=\"Monoclonal Antibody to COMP (Clone 16B5) Cartilage Oligomeric Matrix Protein, Affinity Purified\" data-mce-style=\"margin-bottom: 16px; float: none;\" data-mce-src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Image_1061008_16B5_480x480.png?v=1732097157\"\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv title=\"Page 2\" class=\"page\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003e16B5 binds to COMP (hCOMP, recombinant human COMP) but not to denatured COMP. Binding was determined in bead-based flow immunoassay as median fluorescence intensity (MFI). Bovine serum albumin (BSA) was used as the negative control.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eReferences:\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv title=\"Page 2\" class=\"page\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003e1. Geng H, Nandakumar KS, Pramhed A, Aspberg A, Mattsson R, Holmdahl R. Cartilage oligomeric matrix protein specific antibodies are pathogenic. Arthritis Res Ther. 2012 Aug 20;14(4):R191.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cbr\u003e2. Geng H, Nandakumar KS, Xiong L, Jie R, Dong J, Holmdahl R. Incomplete B cell tolerance to cartilage oligomeric matrix protein in mice. Arthritis Rheum. 2013 Sep;65(9):2301-9.\u003c\/span\u003e\u003c\/p\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":44659625853117,"sku":"1061008","price":490.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Monoclonal_Antibody_to_COMP_Clone_16B5_Cartilage_Oligomeric_Matrix_Protein_Affinity_Purified.png?v=1732186243"},{"product_id":"collagen-type-ii-monoclonal-antibody-clone-ciic1-100ug","title":"Collagen Type II, Monoclonal Antibody (Clone CIIC1), 100ug","description":"\u003cdiv class=\"page\" title=\"Page 11\"\u003e\n\u003cdiv class=\"section\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\" style=\"text-align: start;\" data-mce-style=\"text-align: start;\"\u003e\n\u003cp\u003e\u003cspan\u003eThis antibody binds specifically to the C1 epitope on triple helica collagen type 2. It cross-reacts with mouse, rat, chicken, baboon and horse.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eCollagen type II, encoded by the COL2A1 gene, is a crucial component of cartilage and plays a vital role in maintaining joint integrity. In mouse models of arthritis, such as collagen-induced arthritis, COL2A1 is studied for its role in cartilage degradation, a key feature of conditions like rheumatoid arthritis and osteoarthritis. Research on COL2A1 helps in understanding arthritis mechanisms and developing new treatments.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eSynonyms:\u003cbr\u003eCollagen alpha-1(II) chain, COL2A1, Collagen Type II, Collagen Type 2, CII.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cimg alt=\"Monoclonal Antibody to Collagen Type II (Clone CIIC1) (COL2A1), Affinity Purified\" src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Image_1061009_image001-2_480x480.png?v=1732097616\" style=\"margin-bottom: 16px; float: none;\" data-mce-src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Image_1061009_image001-2_480x480.png?v=1732097616\" data-mce-style=\"margin-bottom: 16px; float: none;\"\u003e\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv class=\"page\" title=\"Page 2\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003eAnti-COL2A1 Antibody (CIIC1) binds to the triple helical C1 epitope on collagen type 2 (CII) but not when the epitope is double-citrullinated (Cit-Cit). CIIC1 can be used in studies of collagen citrullination together with mouse Anti-citrullinated COL2A1 ACC4 Antibody (Catalogue number 1061004). Binding specificity to triple helical C1 peptide epitopes was determined by bead-based flow immunoassay as median fluorescence intensity (MFI).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eReferences:\u003c\/span\u003e\u003c\/p\u003e\n\u003cdiv class=\"page\" title=\"Page 2\"\u003e\n\u003cdiv class=\"layoutArea\"\u003e\n\u003cdiv class=\"column\"\u003e\n\u003cp\u003e\u003cspan\u003e1. Holmdahl, R., et al. Characterization of the antibody response in mice with type II collagen-induced arthritis, using monoclonal anti- type II collagen antibodies. Arthritis Rheum. 1986. 29: 400–410.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e2. Nandakumar KS, et al. Collagen type II-specific monoclonal antibody- induced arthritis in mice: description of the disease and the influence of age, sex, and genes. Am J Pathol. 2003 Nov;163(5):1827-37.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e3. Nandakumar KS, et al. Collagen type II (CII)-specific antibodies induce arthritis in the absence of T or B cells but the arthritis progression is enhanced by CII-reactive T cells. Arthritis Res Ther. 2004;6(6):R544-50. \u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e4. Uysal H, et al. The crystal structure of the pathogenic collagen type II- specific mouse monoclonal antibody CIIC1 Fab: structure to function analysis. Mol Immunol. 2008 Apr;45(8):2196-204.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e5. Böiers U, et al. Collagen type II is recognized by a pathogenic antibody through germline encoded structures. Eur J Immunol. 2008 Oct;38(10):2784-95.\u003c\/span\u003e\u003c\/p\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e\n\u003c\/div\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":44659632537789,"sku":"1061009","price":490.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Monoclonal_Antibody_to_Collagen_Type_II_Clone_CIIC1_COL2A1_Affinity_Purified.png?v=1732186686"}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/collections\/MD-Bioproducts-Antibodies.jpg?v=1718720223","url":"https:\/\/www.mdbioproducts.com\/collections\/antibodies.oembed?page=3","provider":"MD Bioproducts","version":"1.0","type":"link"}