{"title":"Inflammation","description":"\u003cp\u003e\u003cspan\u003eMD Bioproducts provides a specialized range of products designed to support inflammation research. The offerings enable researchers to study the molecular mechanisms driving inflammatory responses, immune cell signaling, and tissue damage. From chronic inflammatory diseases to acute responses, high-quality products help advance research into conditions such as arthritis, inflammatory bowel disease, and other inflammation-related disorders.\u003c\/span\u003e\u003c\/p\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-atelocollagen-bovine","title":"Collagen Type I (Atelocollagen), Bovine, 30 mg","description":"\u003cp\u003ePurified Bovine Collagen Type I (Atelocollagen) from bovine tendons. \u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. It is the major component and the primary determinant of tensile strength of the extracelluar matrix (ECM). It is widely used as a thin layer on tissue-culture surfaces to enhance the attachment and proliferation of a variety of cells including endothelial cells, fibroblasts, hepatocytes, epithelial cells etc. In addition, collagen I can self-assemble into a 3-D superamolecular gel in vitro, making it an ideal biological scaffold to promote more in vivo-like cellular morphology and function.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL1A1\u003c\/li\u003e\n\u003cli\u003eCOL1A2\u003c\/li\u003e\n\u003cli\u003eosteogenesis imperfecta\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848192868541,"sku":"8052013","price":680.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_Atelocollagen_Bovine.png?v=1721220554"},{"product_id":"collagen-type-i-atelocollagen-mouse","title":"Collagen Type I (Atelocollagen), Mouse, 1 mg","description":"\u003cp\u003ePurified Mouse Collagen Type I (Atelocollagen) from mouse tail tendon.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. It is the major component and the primary determinant of tensile strength of the extracelluar matrix (ECM). It is widely used as a thin layer on tissue-culture surfaces to enhance the attachment and proliferation of a variety of cells including endothelial cells, fibroblasts, hepatocytes, epithelial cells etc. In addition, collagen I can self-assemble into a 3-D superamolecular gel in vitro, making it an ideal biological scaffold to promote more in vivo-like cellular morphology and function.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL1A1\u003c\/li\u003e\n\u003cli\u003eCOL1A2\u003c\/li\u003e\n\u003cli\u003eosteogenesis imperfecta\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e \u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848192901309,"sku":"8052015","price":740.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_Atelocollagen_Mouse.png?v=1718964016"},{"product_id":"collagen-type-i-atelocollagen-rat","title":"Collagen Type I (Atelocollagen), Rat, 30 mg","description":"\u003cp\u003ePurified Rat Collagen Type I (Atelocollagen) from rat tail tendon.\u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. It is the major component and the primary determinant of tensile strength of the extracelluar matrix (ECM). It is widely used as a thin layer on tissue-culture surfaces to enhance the attachment and proliferation of a variety of cells including endothelial cells, fibroblasts, hepatocytes, epithelial cells etc. In addition, collagen I can self-assemble into a 3-D superamolecular gel in vitro, making it an ideal biological scaffold to promote more in vivo-like cellular morphology and function.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL1A1\u003c\/li\u003e\n\u003cli\u003eCOL1A2\u003c\/li\u003e\n\u003cli\u003eosteogenesis imperfecta\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e \u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848193097917,"sku":"8052016","price":790.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_Atelocollagen_Rat.png?v=1721220706"},{"product_id":"collagen-type-i-and-iii-bovine","title":"Collagen Type I and III, Bovine, 10 mg","description":"\u003cp\u003ePurified type I \u0026amp; III bovine collagen from calf skin.\u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. It is the major component and the primary determinant of tensile strength of the extracelluar matrix (ECM). It is widely used as a thin layer on tissue-culture surfaces to enhance the attachment and proliferation of a variety of cells including endothelial cells, fibroblasts, hepatocytes, epithelial cells etc. In addition, collagen I can self-assemble into a 3-D superamolecular gel in vitro, making it an ideal biological scaffold to promote more in vivo-like cellular morphology and function.\u003cbr\u003e\u003cbr\u003eType III collagen is the second most abundant collagen in tissues and is found most commonly in tissues exhibiting elastic properties such as skin, lungs, intestinal walls and walls of blood vessels. It is a homotrimer comprised of three alpha-1 chains and resembles other fibrillar collagens in structure and function. It is synthesized as procollagen, similary to collagen I, but the N-terminal propeptide remains attached in the mature fibrillar type III form.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL1A1\u003c\/li\u003e\n\u003cli\u003eCOL1A2\u003c\/li\u003e\n\u003cli\u003eCOL3A1\u003c\/li\u003e\n\u003cli\u003eCollagen type III, alpha 1\u003c\/li\u003e\n\u003cli\u003eosteogenesis imperfecta\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848193130685,"sku":"8052011","price":560.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_and_Bovine.png?v=1721220411"},{"product_id":"collagen-type-i-and-iii-canine","title":"Collagen Type I and III, Canine,  10 mg","description":"\u003cp\u003ePurified type I \u0026amp; III canine collagen.\u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. It is the major component and the primary determinant of tensile strength of the extracelluar matrix (ECM). It is widely used as a thin layer on tissue-culture surfaces to enhance the attachment and proliferation of a variety of cells including endothelial cells, fibroblasts, hepatocytes, epithelial cells etc. In addition, collagen I can self-assemble into a 3-D superamolecular gel in vitro, making it an ideal biological scaffold to promote more in vivo-like cellular morphology and function.\u003cbr\u003e\u003cbr\u003eType III collagen is the second most abundant collagen in tissues and is found most commonly in tissues exhibiting elastic properties such as skin, lungs, intestinal walls and walls of blood vessels. It is a homotrimer comprised of three alpha-1 chains and resembles other fibrillar collagens in structure and function. It is synthesized as procollagen, similary to collagen I, but the N-terminal propeptide remains attached in the mature fibrillar type III form.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL1A1\u003c\/li\u003e\n\u003cli\u003eCOL1A2\u003c\/li\u003e\n\u003cli\u003eCOL3A1\u003c\/li\u003e\n\u003cli\u003eCollagen type III, alpha 1\u003c\/li\u003e\n\u003cli\u003eosteogenesis imperfecta\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e \u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848193163453,"sku":"8052008","price":560.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_and_III_Canine.png?v=1721220025"},{"product_id":"collagen-type-i-and-iii-mouse","title":"Collagen Type I and III, Mouse, 5 mg","description":"\u003cp\u003ePurified native collagen type I and III from tail tendons of the mouse, 5 mg. \u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. It is the major component and the primary determinant of tensile strength of the extracelluar matrix (ECM). It is widely used as a thin layer on tissue-culture surfaces to enhance the attachment and proliferation of a variety of cells including endothelial cells, fibroblasts, hepatocytes, epithelial cells etc. In addition, collagen I can self-assemble into a 3-D superamolecular gel in vitro, making it an ideal biological scaffold to promote more in vivo-like cellular morphology and function.\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e Type III collagen is the second most abundant collagen in tissues and is found most commonly in tissues exhibiting elastic properties such as skin, lungs, intestinal walls and walls of blood vessels. It is a homotrimer comprised of three alpha-1 chains and resembles other fibrillar collagens in structure and function. It is synthesized as procollagen, similary to collagen I, but the N-terminal propeptide remains attached in the mature fibrillar type III form.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL1A1\u003c\/li\u003e\n\u003cli\u003eCOL1A2\u003c\/li\u003e\n\u003cli\u003eCOL3A1\u003c\/li\u003e\n\u003cli\u003eCollagen type III, alpha 1\u003c\/li\u003e\n\u003cli\u003eosteogenesis imperfecta\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\u003eCivitarese, R. A., Talior-Volodarsky, I., Desjardins, J. F., Kabir, G., Switzer, J., Mitchell, M., ... \u0026amp; Connelly, K. A. (2016). The α11 integrin mediates fibroblast–extracellular matrix–cardiomyocyte interactions in health and disease. American Journal of Physiology-Heart and Circulatory Physiology, 311(1), H96-H106.\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848193622205,"sku":"8052006","price":560.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_and_III_Mouse.png?v=1721219135"},{"product_id":"collagen-type-i-and-iii-porcine","title":"Collagen Type I and III, Porcine, 10 mg","description":"\u003cp\u003ePurified type I \u0026amp; III native porcine collagen from pig’s tissue, 10 mg. Highest quality collagen for research use. \u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. It is the major component and the primary determinant of tensile strength of the extracelluar matrix (ECM). It is widely used as a thin layer on tissue-culture surfaces to enhance the attachment and proliferation of a variety of cells including endothelial cells, fibroblasts, hepatocytes, epithelial cells etc. In addition, collagen I can self-assemble into a 3-D superamolecular gel in vitro, making it an ideal biological scaffold to promote more in vivo-like cellular morphology and function.\u003cbr\u003e\u003cbr\u003e Type III collagen is the second most abundant collagen in tissues and is found most commonly in tissues exhibiting elastic properties such as skin, lungs, intestinal walls and walls of blood vessels. It is a homotrimer comprised of three alpha-1 chains and resembles other fibrillar collagens in structure and function. It is synthesized as procollagen, similary to collagen I, but the N-terminal propeptide remains attached in the mature fibrillar type III form.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL1A1\u003c\/li\u003e\n\u003cli\u003eCOL1A2\u003c\/li\u003e\n\u003cli\u003eCOL3A1\u003c\/li\u003e\n\u003cli\u003eCollagen type III, alpha 1\u003c\/li\u003e\n\u003cli\u003eosteogenesis imperfecta\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e \u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848193654973,"sku":"8052004","price":560.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_and_III_Porcine.png?v=1721218895"},{"product_id":"collagen-type-i-and-iii-rat","title":"Collagen Type I and III, Rat, 10 mg","description":"\u003cp\u003ePurified type I \u0026amp; III native rat collagen purified from rat tissue. Highest quality collagen for research use. \u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. It is the major component and the primary determinant of tensile strength of the extracelluar matrix (ECM). It is widely used as a thin layer on tissue-culture surfaces to enhance the attachment and proliferation of a variety of cells including endothelial cells, fibroblasts, hepatocytes, epithelial cells etc. In addition, collagen I can self-assemble into a 3-D superamolecular gel in vitro, making it an ideal biological scaffold to promote more in vivo-like cellular morphology and function.\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e Type III collagen is the second most abundant collagen in tissues and is found most commonly in tissues exhibiting elastic properties such as skin, lungs, intestinal walls and walls of blood vessels. It is a homotrimer comprised of three alpha-1 chains and resembles other fibrillar collagens in structure and function. It is synthesized as procollagen, similary to collagen I, but the N-terminal propeptide remains attached in the mature fibrillar type III form.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL1A1\u003c\/li\u003e\n\u003cli\u003eCOL1A2\u003c\/li\u003e\n\u003cli\u003eCOL3A1\u003c\/li\u003e\n\u003cli\u003eCollagen type III, alpha 1\u003c\/li\u003e\n\u003cli\u003eosteogenesis imperfecta\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e \u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848193818813,"sku":"8052003","price":560.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_and_III_Rat.png?v=1721218773"},{"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-i-bovine","title":"Collagen Type I, Bovine, 10 mg","description":"\u003cp\u003eHighly Purified type I native collagen from bovine skin. Lyophilized\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. It is the major component and the primary determinant of tensile strength of the extracelluar matrix (ECM). It is widely used as a thin layer on tissue-culture surfaces to enhance the attachment and proliferation of a variety of cells including endothelial cells, fibroblasts, hepatocytes, epithelial cells etc. In addition, collagen I can self-assemble into a 3-D superamolecular gel in vitro, making it an ideal biological scaffold to promote more in vivo-like cellular morphology and function.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL1A1\u003c\/li\u003e\n\u003cli\u003eCOL1A2\u003c\/li\u003e\n\u003cli\u003eosteogenesis imperfecta\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e\u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848193917117,"sku":"8052010","price":530.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_Bovine.png?v=1721220254"},{"product_id":"collagen-type-i-goat","title":"Collagen Type I, Goat, 10 mg","description":"\u003cp\u003eHighly Purified type I native goat collagen. Lyophilized. Reconstitute to 10 mg\/mL\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. It is the major component and the primary determinant of tensile strength of the extracelluar matrix (ECM). It is widely used as a thin layer on tissue-culture surfaces to enhance the attachment and proliferation of a variety of cells including endothelial cells, fibroblasts, hepatocytes, epithelial cells etc. In addition, collagen I can self-assemble into a 3-D superamolecular gel in vitro, making it an ideal biological scaffold to promote more in vivo-like cellular morphology and function.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL1A1\u003c\/li\u003e\n\u003cli\u003eCOL1A2\u003c\/li\u003e\n\u003cli\u003eosteogenesis imperfecta\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp\u003e \u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848193982653,"sku":"8052007","price":590.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_Goat.png?v=1721219903"},{"product_id":"collagen-type-i-mouse","title":"Collagen Type I, Mouse, 1 mg","description":"\u003cp\u003ePurified type I native mouse collagen from mouse tail tendon. Lyophilized. Reconstitute to yield 1-5 mg\/mL collagen solution. \u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. It is the major component and the primary determinant of tensile strength of the extracelluar matrix (ECM). It is widely used as a thin layer on tissue-culture surfaces to enhance the attachment and proliferation of a variety of cells including endothelial cells, fibroblasts, hepatocytes, epithelial cells etc. In addition, collagen I can self-assemble into a 3-D superamolecular gel in vitro, making it an ideal biological scaffold to promote more in vivo-like cellular morphology and function.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL1A1\u003c\/li\u003e\n\u003cli\u003eCOL1A2\u003c\/li\u003e\n\u003cli\u003eosteogenesis imperfecta\u003c\/li\u003e\n\u003c\/ul\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":39848194048189,"sku":"8052005","price":590.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_Mouse.png?v=1721219012"},{"product_id":"collagen-type-i-porcine","title":"Collagen Type I (Atelocollagen) Porcine, 30 mg","description":"\u003cp\u003eHighly Purified Porcine Collagen Type I from porcine tendon. Lyophilized. Reconstitute to a concentration of 1-5 mg\/mL. \u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eType I collagen is the most abundant collagen and is found in connective tissues including tendon, ligament, dermis and blood vessel. It is the major component and the primary determinant of tensile strength of the extracelluar matrix (ECM). It is widely used as a thin layer on tissue-culture surfaces to enhance the attachment and proliferation of a variety of cells including endothelial cells, fibroblasts, hepatocytes, epithelial cells etc. In addition, collagen I can self-assemble into a 3-D superamolecular gel in vitro, making it an ideal biological scaffold to promote more in vivo-like cellular morphology and function.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL1A1\u003c\/li\u003e\n\u003cli\u003eCOL1A2\u003c\/li\u003e\n\u003cli\u003eosteogenesis imperfecta\u003c\/li\u003e\n\u003c\/ul\u003e\n","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848194080957,"sku":"8052017","price":740.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_I_Atelocollagen_Porcine.png?v=1721220884"},{"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-ii-bovine-lyophilized","title":"Collagen Type II, Bovine, Immunization Grade, Lyophilized, 10 mg","description":"\u003cp\u003eImmunization Grade Collagen type II (CII) protein, purified from fetal bovine articular cartilage, for the induction of arthritis in the Collagen-Induced Arthritis (CIA) model.\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 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.\u003cbr\u003e\u003cbr\u003eType II Collagen and Adjuvent Susceptibility to CIA is linked to MHC class II molecules and is dependent upon the species of type II collagen used for immunization. Various species of highly purified Type II Collagen are supplied lyophilized and in solution for use in the induction of arthritis in vivo.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL2A1\u003c\/li\u003e\n\u003cli\u003epro-alpha 1(II) chain\u003c\/li\u003e\n\u003cli\u003eAchondrogenesis\u003c\/li\u003e\n\u003cli\u003eHypochondrogenesis\u003c\/li\u003e\n\u003cli\u003eSpondyloepimetaphyseal dysplasia\u003c\/li\u003e\n\u003cli\u003eOsteoarthritis (OA)\u003c\/li\u003e\n\u003cli\u003eCollagen Induced Arthritis (CIA)\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cul\u003e\u003c\/ul\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eRosillo, M. Á., Villegas, I., Vázquez-Román, V., Fernández-Santos, J. M., Ortega-Vidal, J., Salido, S., ... \u0026amp; Alarcón-de-la-Lastra, C. (2024). Dietary oleacein, a secoiridoid from extra virgin olive oil, prevents collagen-induced arthritis in mice. \u003c\/span\u003e\u003ci\u003eFood \u0026amp; Function\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e15\u003c\/i\u003e\u003cspan\u003e(2), 838-852.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cmeta charset=\"UTF-8\"\u003e\u003cspan\u003eLibánská, A., Randárová, E., Skoroplyas, S., Bartoš, M., Luňáčková, J., Lager, F., Renault, G., Scherman, D., \u0026amp; Etrych, T. (2023). Size-switchable polymer-based nanomedicines in the advanced therapy of rheumatoid arthritis. \u003c\/span\u003e\u003ci\u003eJournal of controlled release : official journal of the Controlled Release Society\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e353\u003c\/i\u003e\u003cspan\u003e, 30–41.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eKeller, C. R., Ruud, K. F., Martinez, S. R., \u0026amp; Li, W. (2022). Identification of the Collagen Types Essential for Mammalian Breast Acinar Structures. \u003ci\u003eGels\u003c\/i\u003e, \u003ci\u003e8\u003c\/i\u003e(12).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eScanu, A., Luisetto, R., Oliviero, F., Galuppini, F., Lazzarin, V., Pennelli, G., ... \u0026amp; Punzi, L. (2022). Bactericidal\/Permeability-Increasing Protein Downregulates the Inflammatory Response in In Vivo Models of Arthritis. \u003c\/span\u003e\u003ci\u003eInternational Journal of Molecular Sciences\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e23\u003c\/i\u003e\u003cspan\u003e(21), 13066.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eRodríguez-Martínez, L., Regueiro, C., Amhaz-Escanlar, S., Pena, C., Herbello-Hermelo, P., Moreda-Piñeiro, A., ... \u0026amp; González, A. (2022). Antibodies against 4 Atypical Post-Translational Protein Modifications in Patients with Rheumatoid Arthritis. \u003cem\u003eDiagnostics\u003c\/em\u003e, \u003cem\u003e12\u003c\/em\u003e(2), 352.\u003c\/p\u003e\n\u003cp\u003eLord, A. E., Zhang, L., Erickson, J. E., Bryant, S., Nelson, C. M., Gaudette, S. M., ... \u0026amp; Mitra, S. (2022). Quantitative in vivo micro-computed tomography for monitoring disease activity and treatment response in a collagen-induced arthritis mouse model. \u003cem\u003eScientific reports\u003c\/em\u003e, \u003cem\u003e12\u003c\/em\u003e(1), 1-8.\u003c\/p\u003e\n\u003cp\u003eLeblond, A., Pezet, S., Cauvet, A., Casas, C., \u0026amp; Da, J. P. (2020). Decreased expression and Activity of the desacetylase Sirtuin-1 contribute to the activated and proangiogenic profile of endothelial cells in rheumatoid arthritis and promote the persistence of experimental arthritis by increasing synovial angiogenesis. Ann Rheum Dis, 891, 79.\u003cbr\u003e\u003cbr\u003eAlvarez, P., Augustín, J. J., Tamayo, E., Iglesias, M., Acinas, O., Mendiguren, M. A., Merino, R. (2020). Therapeutic effects of anti-Bone Morphogenetic Protein and Activin Membrane-Bound Inhibitor treatment in psoriasis and arthritis. Arthritis \u0026amp; Rheumatology.\u003cbr\u003e\u003cbr\u003eCasanova-Vallve, N., Constantin-Teodosiu, D., Filer, A., Hardy, R. S., Greenhaff, P. L.,Chapman, V. (2020). Skeletal muscle dysregulation in rheumatoid arthritis: Metabolic and molecular markers in a rodent model and patients. PloS one, 15(7), e0235702.\u003cbr\u003e\u003cbr\u003eLückemann, L., Stangl, H., Straub, R. H., Schedlowski, M., \u0026amp; Hadamitzky, M. (2020). Learned immunosuppressive placebo response attenuates disease progression in a rodent model of rheumatoid arthritis. Arthritis \u0026amp; Rheumatology, 72(4), 588-597.\u003cbr\u003e\u003cbr\u003eZhou, J., Chen, P., Li, Z., \u0026amp; Zuo, Q. (2020). Gene delivery of TIPE2 attenuates collagen-induced arthritis by modulating inflammation. International Immunopharmacology, 79, 106044.\u003cbr\u003e\u003cbr\u003eMausset-Bonnefont, A. L., Cren, M., Vicente, R., Quentin, J., Jorgensen, C., Apparailly, F., \u0026amp; Louis-Plence, P. (2019). Arthritis sensory and motor scale: predicting functional deficits from the clinical score in collagen-induced arthritis. Arthritis Research \u0026amp; Therapy, 21(1), 1-12.\u003cbr\u003e\u003cbr\u003eCoppard, C., Bonnefoy, F., Hannani, D., Gabert, F., Manches, O., Plumas, J., ... \u0026amp; Chaperot, L. (2019). Photopheresis efficacy in the treatment of rheumatoid arthritis: a pre-clinical proof of concept. Journal of Translational Medicine, 17(1), 1-10.\u003cbr\u003e\u003cbr\u003eCao, L., Yu, M., Wang, C., Bao, Y., Zhang, M., He, P., ... \u0026amp; Gong, Y. (2019). Cellulase-Assisted Extraction, Characterization, and Bioactivity against Rheumatoid Arthritis of Astragalus Polysaccharides. International Journal of Polymer Science, 2019.\u003cbr\u003e\u003cbr\u003eEbbers, M., Lübcke, P. M., Volzke, J., Kriebel, K., Hieke, C., Engelmann, R., ... \u0026amp; Müller-Hilke, B. (2018). Interplay between P. gingivalis, F. nucleatum and A. actinomycetemcomitans in murine alveolar bone loss, arthritis onset and progression. Scientific Reports, 8(1), 15129.\u003cbr\u003e\u003cbr\u003eRuzek, M. C., Huang, L., Zhang, T. T., Bryant, S., Slivka, P. F., Cuff, C. A., ... \u0026amp; Blaich, G. (2018). Dual Blockade of Interleukin-1β and Interleukin-17A Reduces Murine Arthritis Pathogenesis but Also Leads to Spontaneous Skin Infections in Nonhuman Primates. Journal of Pharmacology and Experimental Therapeutics, 364(3), 474-484.\u003cbr\u003e\u003cbr\u003eDoonan, J., Lumb, F. E., Pineda, M. A., Tarafdar, A., Crowe, J., Khan, A. M., ... \u0026amp; Harnett, W. (2018). Protection against arthritis by the parasitic worm product ES-62, and its drug-like small molecule analogues, is associated with inhibition of osteoclastogenesis. Frontiers in immunology, 9\u003cbr\u003e\u003cbr\u003eLin, Y. Y., Jean, Y. H., Lee, H. P., Lin, S. C., Pan, C. Y., Chen, W. F., ... \u0026amp; Sung, P. J. (2017). Excavatolide B attenuates rheumatoid arthritis through the inhibition of osteoclastogenesis. Marine drugs, 15(1), 9.\u003cbr\u003e\u003cbr\u003eEngelmann, R., \u0026amp; Müller-Hilke, B. (2017). Experimental silicosis does not aggravate collagen-induced arthritis in mice. Journal of negative results in biomedicine, 16(1), 5.\u003cbr\u003e\u003cbr\u003eOehler, B., Kistner, K., Martin, C., Schiller, J., Mayer, R., Mohammadi, M., ... \u0026amp; Pflücke, D. (2017). Inflammatory pain control by blocking oxidized phospholipid-mediated TRP channel activation. Scientific reports, 7(1), 5447.\u003cbr\u003e\u003cbr\u003eDel Prete, A., Martínez-Muñoz, L., Mazzon, C., Toffali, L., Sozio, F., Za, L., ... \u0026amp; Liberati, C. (2017). The atypical receptor CCRL2 is required for CXCR2-dependent neutrophil recruitment and tissue damage. Blood, blood-2017.\u003cbr\u003e\u003cbr\u003eHablot, J., Peyrin-Biroulet, L., Kokten, T., El Omar, R., Netter, P., Bastien, C., ... \u0026amp; Moulin, D. (2017). Experimental colitis delays and reduces the severity of collagen-induced arthritis in mice. PloS one, 12(9), e0184624.\u003cbr\u003e\u003cbr\u003eNieto, F. R., Clark, A. K., Grist, J., Hathway, G. J., Chapman, V., \u0026amp; Malcangio, M. (2016). Neuron-immune mechanisms contribute to pain in early stages of arthritis. Journal of neuroinflammation, 13(1), 96.\u003cbr\u003e\u003cbr\u003eHansson, C., Schön, K., Kalbina, I., Strid, Å., Andersson, S., Bokarewa, M. I., \u0026amp; Lycke, N. Y. (2016). Feeding transgenic plants that express a tolerogenic fusion protein effectively protects against arthritis. Plant biotechnology journal, 14(4), 1106-1115.\u003cbr\u003e\u003cbr\u003ePostigo, J., Iglesias, M., Álvarez, P., Jesus Augustin, J., Buelta, L., Merino, J., \u0026amp; Merino, R. (2016). Bone Morphogenetic Protein and Activin Membrane–Bound Inhibitor, a Transforming Growth Factor β Rheostat That Controls Murine Treg Cell\/Th17 Cell Differentiation and the Development of Autoimmune Arthritis by Reducing Interleukin‐2 Signaling. Arthritis \u0026amp; Rheumatology, 68(6), 1551-1562.\u003cbr\u003e\u003cbr\u003eIglesias, M., Augustin, J. J., Alvarez, P., Santiuste, I., Postigo, J., Merino, J., \u0026amp; Merino, R. (2016). Selective impairment of TH17-differentiation and protection against autoimmune arthritis after overexpression of BCL2A1 in T lymphocytes. PloS one, 11(7), e0159714.\u003cbr\u003e\u003cbr\u003eBonnefoy, F., Daoui, A., Valmary-Degano, S., Toussirot, E., Saas, P., \u0026amp; Perruche, S. (2016). Apoptotic cell infusion treats ongoing collagen-induced arthritis, even in the presence of methotrexate, and is synergic with anti-TNF therapy. Arthritis research \u0026amp; therapy, 18(1), 184.\u003cbr\u003e\u003cbr\u003eÁlvarez, P., Genre, F., Iglesias, M., Augustin, J. J., Tamayo, E., Escolà‐Gil, J. C., ... \u0026amp; Merino, J. (2016). Modulation of autoimmune arthritis severity in mice by apolipoprotein E (ApoE) and cholesterol. Clinical \u0026amp; Experimental Immunology, 186(3), 292-303.\u003cbr\u003e\u003cbr\u003eKiyeko, G. W., Hatterer, E., Herren, S., Di Ceglie, I., van Lent, P. L., Reith, W., ... \u0026amp; Shang, L. (2016). Spatiotemporal expression of endogenous TLR4 ligands leads to inflammation and bone erosion in mouse collagen‐induced arthritis. European journal of immunology, 46(11), 2629-2638.\u003cbr\u003e\u003cbr\u003ePapadaki, G., Kambas, K., Choulaki, C., Vlachou, K., Drakos, E., Bertsias, G., ... \u0026amp; Sidiropoulos, P. (2016). Neutrophil extracellular traps exacerbate Th1‐mediated autoimmune responses in rheumatoid arthritis by promoting DC maturation. European journal of immunology, 46(11), 2542-2554.\u003cbr\u003e\u003cbr\u003eVicente, R., Quentin, J., Mausset-Bonnefont, A. L., Chuchana, P., Martire, D., Cren, M., ... \u0026amp; Louis-Plence, P. (2015). Nonclassical CD4+ CD49b+ regulatory T cells as a better alternative to conventional CD4+ CD25+ T cells to dampen arthritis severity. The Journal of Immunology, 1501069.\u003cbr\u003e\u003cbr\u003eMcRae, B. L., Levin, A. D., Wildenberg, M. E., Koelink, P. J., Bousquet, P., Mikaelian, I., ... \u0026amp; Salfeld, J. (2015). Fc receptor-mediated effector function contributes to the therapeutic response of anti-TNF monoclonal antibodies in a mouse model of inflammatory bowel disease. Journal of Crohn's and Colitis, 10(1), 69-76.\u003cbr\u003e\u003cbr\u003eScales, H. E., Ierna, M., Smith, K. M., Ross, K., Meiklejohn, G. R., Patterson-Kane, J. C., ... \u0026amp; Maffia, P. (2015). Assessment of murine collagen-induced arthritis by longitudinal non-invasive duplexed molecular optical imaging. Rheumatology, 55(3), 564-572.\u003cbr\u003e\u003cbr\u003eElhai, M., Chiocchia, G., Marchiol, C., Lager, F., Renault, G., Colonna, M., ... \u0026amp; Avouac, J. (2015). Targeting CD226\/DNAX accessory molecule-1 (DNAM-1) in collagen-induced arthritis mouse models. Journal of Inflammation, 12(1), 9.\u003cbr\u003e\u003cbr\u003eBrühl, H., Cihak, J., Talke, Y., Gomez, M. R., Hermann, F., Goebel, N., ... \u0026amp; Nimmerjahn, F. (2015). B‐cell inhibition by cross‐linking CD79b is superior to B‐cell depletion with anti‐CD20 antibodies in treating murine collagen‐induced arthritis. European journal of immunology, 45(3), 705-715.\u003cbr\u003e\u003cbr\u003eRzepecka, J., Pineda, M. A., Al-Riyami, L., Rodgers, D. T., Huggan, J. K., Lumb, F. E., ... \u0026amp; Suckling, C. J. (2015). Prophylactic and therapeutic treatment with a synthetic analogue of a parasitic worm product prevents experimental arthritis and inhibits IL-1β production via NRF2-mediated counter-regulation of the inflammasome. Journal of autoimmunity, 60, 59-73.\u003cbr\u003e\u003cbr\u003eNissinen, L., Ojala, M., Langen, B., Dost, R., Pihlavisto, M., Käpylä, J., ... \u0026amp; Heino, J. (2015). Sulfonamide inhibitors of α2β1 integrin reveal the essential role of collagen receptors in in vivo models of inflammation. Pharmacology research \u0026amp; perspectives, 3(3).\u003cbr\u003e\u003cbr\u003eMuschter, D., Göttl, C., Vogel, M., Grifka, J., Straub, R. H., \u0026amp; Grässel, S. (2015). Reactivity of rat bone marrow-derived macrophages to neurotransmitter stimulation in the context of collagen II-induced arthritis. Arthritis research \u0026amp; therapy, 17(1), 169.\u003cbr\u003e\u003cbr\u003eBaddack, U., Frahm, S., Antolin‐Fontes, B., Grobe, J., Lipp, M., Müller, G., \u0026amp; Ibañez‐Tallon, I. (2015). Suppression of peripheral pain by blockade of voltage‐Gated calcium 2.2 channels in nociceptors induces RANKL and impairs recovery from inflammatory arthritis in a mouse model. Arthritis \u0026amp; Rheumatology, 67(6), 1657-1667.\u003cbr\u003e\u003cbr\u003eHerman, S., Fischer, A., Presumey, J., Hoffmann, M., Koenders, M. I., Escriou, V., ... \u0026amp; Steiner, G. (2015). Inhibition of Inflammation and Bone Erosion by RNA Interference–Mediated Silencing of Heterogeneous Nuclear RNP A2\/B1 in Two Experimental Models of Rheumatoid Arthritis. Arthritis \u0026amp; Rheumatology, 67(9), 2536-2546.\u003cbr\u003e\u003cbr\u003eMcRae, B. L., Levin, A. D., Wildenberg, M. E., Koelink, P. J., Bousquet, P., Mikaelian, I., ... \u0026amp; Salfeld, J. (2015). Fc receptor-mediated effector function contributes to the therapeutic response of anti-TNF monoclonal antibodies in a mouse model of inflammatory bowel disease. Journal of Crohn's and Colitis, 10(1), 69-76.\u003cbr\u003e\u003cbr\u003ePostigo, J. (2015). BAMBI a TGF β rheostat that controls regulatory T\/TH 17 differentiation and the development of autoimmune arthritis by reducing IL-2 signaling. Arthritis \u0026amp; Rheumatology, n\/an\/a.\u003cbr\u003e\u003cbr\u003eNieto, F. R., Clark, A. K., Grist, J., Chapman, V., \u0026amp; Malcangio, M. (2015). Calcitonin Gene‐Related Peptide–Expressing Sensory Neurons and Spinal Microglial Reactivity Contribute to Pain States in Collagen‐Induced Arthritis. Arthritis \u0026amp; Rheumatology, 67(6), 1668-1677.\u003cbr\u003e\u003cbr\u003eHansell, C. A., MacLellan, L. M., Oldham, R. S., Doonan, J., Chapple, K. J., Anderson, E. J., \u0026amp; Goodyear, C. S. (2015). The atypical chemokine receptor ACKR2 suppresses Th17 responses to protein autoantigens. Immunology and cell biology, 93(2), 167-176.\u003cbr\u003e\u003cbr\u003eLopes, J. L., Miles, A. J., Whitmore, L., \u0026amp; Wallace, B. A. (2014). Distinct circular dichroism spectroscopic signatures of polyproline II and unordered secondary structures: Applications in secondary structure analyses. Protein Science, 23(12), 1765-1772.\u003cbr\u003e\u003cbr\u003eVogl, T., Eisenblätter, M., Völler, T., Zenker, S., Hermann, S., van Lent, P., \u0026amp; Roth, J. (2014). Alarmin S100A8\/S100A9 as a biomarker for molecular imaging of local inflammatory activity. Nature communications, 5.\u003cbr\u003e\u003cbr\u003eBrühl, H., Cihak, J., Goebel, N., Talke, Y., Renner, K., Hermann, F., \u0026amp; Mack, M. (2014). Chondroitin sulfate activates B cells in vitro, expands CD138+ cells in vivo, and interferes with established humoral immune responses. Journal of leukocyte biology, 96(1), 65-72.\u003cbr\u003e\u003cbr\u003eLindh, I., Snir, O., Lönnblom, E., Uysal, H., Andersson, I., Nandakumar, K. S., \u0026amp; Holmdahl, R. (2014). Type II collagen antibody response is enriched in the synovial fluid of rheumatoid joints and directed to the same major epitopes as in collagen induced arthritis in primates and mice. Arthritis Res Ther, 16(4), R143.\u003cbr\u003e\u003cbr\u003ePineda, M. A., Rodgers, D. T., Al‐Riyami, L., Harnett, W., \u0026amp; Harnett, M. M. (2014). ES‐62 Protects Against Collagen‐Induced Arthritis by Resetting Interleukin‐22 Toward Resolution of Inflammation in the Joints. Arthritis \u0026amp; Rheumatology, 66(6), 1492-1503.\u003cbr\u003e\u003cbr\u003eYilmaz-Elis, A. S., Ramirez, J. M., Asmawidjaja, P., van der Kaa, J., Mus, A. M., Brem, M. D., \u0026amp; Verbeek, J. S. (2014). FcγRIIb on myeloid cells rather than on B cells protects from collagen-induced arthritis. The Journal of Immunology, 192(12), 5540-5547.\u003cbr\u003e\u003cbr\u003eYoshimura, S., Asano, K., \u0026amp; Nakane, A. (2014). Attenuation of collagen-induced arthritis in mice by salmon proteoglycan. BioMed research international, 2014.\u003cbr\u003e\u003cbr\u003eRodgers, D. T., Pineda, M. A., McGrath, M. A., Al‐Riyami, L., Harnett, W., \u0026amp; Harnett, M. M. (2014). Protection against collagen‐induced arthritis in mice afforded by the parasitic worm product, ES‐62, is associated with restoration of the levels of interleukin‐10‐producing B cells and reduced plasma cell infiltration of the joints. Immunology, 141(3), 457-466.\u003cbr\u003e\u003cbr\u003eThiolat, A., Semerano, L., Pers, Y. M., Biton, J., Lemeiter, D., Portales, P. \u0026amp; Bessis, N. (2014). Interleukin‐6 Receptor Blockade Enhances CD39+ Regulatory T Cell Development in Rheumatoid Arthritis and in Experimental Arthritis. Arthritis \u0026amp; Rheumatology, 66(2), 273-283.\u003cbr\u003e\u003cbr\u003eAl-Riyami, L., Pineda, M. A., Rzepecka, J., Huggan, J. K., Khalaf, A. I., Suckling, C. J., \u0026amp; Harnett, W. (2013). Designing anti-inflammatory drugs from parasitic worms: a synthetic small molecule analogue of the Acanthocheilonema viteae product ES-62 prevents development of collagen-induced arthritis. Journal of medicinal chemistry, 56(24), 9982-10002.\u003cbr\u003e\u003cbr\u003eCampo, G. M., Avenoso, A., D’Ascola, A., Nastasi, G., Micali, A., Puzzolo, D., \u0026amp; Campo, S. (2013). Combined treatment with hyaluronan inhibitor Pep-1 and a selective adenosine A2 receptor agonist reduces inflammation in experimental arthritis. Innate immunity, 19(5), 462-478.\u003cbr\u003e\u003cbr\u003eShashidharamurthy, R., Machiah, D., Aitken, J. D., Putty, K., Srinivasan, G., Chassaing, B., \u0026amp; Vijay‐Kumar, M. (2013). Differential Role of Lipocalin 2 During Immune Complex–Mediated Acute and Chronic Inflammation in Mice. Arthritis \u0026amp; Rheumatism, 65(4), 1064-1073.\u003cbr\u003e\u003cbr\u003eIglesias, M., Postigo, J., Santiuste, I., González, J., Buelta, L., Tamayo, E. \u0026amp; Merino, R. (2013). p27Kip1 inhibits systemic autoimmunity through the control of Treg cell activity and differentiation. Arthritis \u0026amp; Rheumatism, 65(2), 343-354.\u003cbr\u003e\u003cbr\u003eDépis, F., Hatterer, E., Lamacchia, C., Waldburger, J. M., Gabay, C., Reith, W. \u0026amp; Dean, Y. (2012). Long‐term amelioration of established collagen‐induced arthritis achieved with short‐term therapy combining anti‐CD3 and anti–tumor necrosis factor treatments. Arthritis \u0026amp; Rheumatism, 64(10), 3189-3198.\u003cbr\u003e\u003cbr\u003ePineda, M. A., McGrath, M. A., Smith, P. C., Al-Riyami, L., Rzepecka, J., Gracie, J. A., \u0026amp; Harnett, M. M. (2012). The parasitic helminth product ES-62 suppresses pathogenesis in CIA by targeting of the IL-17-producing cellular network at multiple sites. Arthritis Rheum, 64(10), 3168-3178.\u003cbr\u003e\u003cbr\u003ePresumey, J., Salzano, G., Courties, G., Shires, M., Ponchel, F., Jorgensen, C \u0026amp; De Rosa, G. (2012). PLGA microspheres encapsulating siRNA anti-TNFalpha: efficient RNAi-mediated treatment of arthritic joints. European Journal of Pharmaceutics and Biopharmaceutics, 82(3), 457-464.\u003cbr\u003e\u003cbr\u003eClark, A. K., Grist, J., Al‐Kashi, A., Perretti, M., \u0026amp; Malcangio, M. (2012). Spinal cathepsin S and fractalkine contribute to chronic pain in the collagen‐induced arthritis model. Arthritis \u0026amp; Rheumatism, 64(6), 2038-2047.\u003cbr\u003e\u003cbr\u003eCrilly, A., Palmer, H., Nickdel, M. B., Dunning, L., Lockhart, J. C.Plevin, R., \u0026amp; Ferrell, W. R. (2012). Immunomodulatory role of proteinase-activated receptor-2. Annals of the rheumatic diseases, 71(9), 1559-1566.\u003cbr\u003e\u003cbr\u003eRoy, L. D., Ghosh, S., Pathangey, L. B., Tinder, T. L., Gruber, H. E., \u0026amp; Mukherjee, P. (2011). Collagen induced arthritis increases secondary metastasis in MMTV-PyV MT mouse model of mammary cancer. Bmc Cancer, 11(1), 365.\u003cbr\u003e\u003cbr\u003eCampo, G. M., Avenoso, A., Nastasi, G., Micali, A., Prestipino, V., Vaccaro, M., \u0026amp; Campo, S. (2011). Hyaluronan reduces inflammation in experimental arthritis by modulating TLR-2 and TLR-4 cartilage expression. Biochimica et Biophysica Acta (BBA)-Molecular Basis of Disease, 1812(9), 1170-1181.\u003cbr\u003e\u003cbr\u003e\u003cbr\u003eThe TNF family member APRIL dampens collagen-induced arthritis. Fernandez,L et al.(2012) Ann Rheum Dis doi:10.1136\/annrheumdis-2012-202382TGF-β–Exposed Plasmacytoid Dendritic Cells Participate in Th17 Commitment\u003cbr\u003eBonnefoy, F et al., J Immunol., Jun 2011; 166:6157.A Virus-Like Particle-Based Anti-Nerve Growth Factor Vaccine Reduces Inflammatory Hyperalgesia: Potential Long-Term Therapy for Chronic Pain\u003cbr\u003eRohn, T et al., J. Immunol., Feb 2011; 186: 1769Pan-CC chemokine neutralization restricts splenocyte egress and reduces inflammation in a model of arthritis.\u003cbr\u003eBuatois V, et al. J immunol. 2010 Aug 15; 185(4):2544-54.Liver X Receptor Agonism Promotes Articular Inflammation in Murine Collagen-Induced Arthritis\u003cbr\u003eAsquith DL, Miller AM, et al. Arthritis Rheum.2009 Sep; 60(9):2655-65.Destructive Arthritis in the Absence of Both FcRI and FcRIII\u003cbr\u003ePeter Boross et al., J. Immunol., Apr 2008; 180: 5083 - 5091.Efficient suppression of murine arthritis by combined anticytokine small interfering RNA lipoplexes.\u003cbr\u003eKhoury M, et al. Arthritis Rheum. 2008 Aug; 58(8):2356-67Immunomodulatory Dendritic Cells Inhibit Th1 Responses and Arthritis via Different Mechanisms\u003cbr\u003eLeonie M. van Duivenvoorde et al., J. Immunol., Aug 2007; 179: 1506 - 1515.Antibody-mediated delivery of IL-10 inhibits the progression of established collagen-induced arthritis.\u003cbr\u003eTrachsel E, et al. Arthritis Res Ther. 2007;9(1):R9The non-thiol angiotensin-converting enzyme inhibitor quinapril suppresses inflammatory arthritis\u003cbr\u003eN. Dalbeth et al., Rheumatology, Jan 2005; 44: 24 - 31.Inflammatory arthritis and dermatitis in thymectomized, CD25+ cell-depleted adult mice\u003cbr\u003eA. Loughry et al., Rheumatology, Mar 2005; 44: 299 - 308.Tracking of Proinflammatory Collagen-Specific T Cells in Early and Late Collagen-Induced Arthritis in Humanized Mice\u003cbr\u003ePia Svendsen et al., J. Immunol., Dec 2004; 173: 7037 - 7045. \u003cbr\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\u003c\/ul\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848194834621,"sku":"804001-lyo","price":285.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_II_Bovine_Lyophilzed.png?v=1718875493"},{"product_id":"collagen-type-ii-bovine-soluble","title":"Collagen Type II, Bovine, Immunization Grade, Soluble, 2 mg\/mL","description":"\u003cp\u003eImmunization Grade Collagen type II (CII) protein, purified from fetal bovine articular cartilage, for the induction of arthritis in the Collagen-Induced Arthritis (CIA) model. Soluble 5 mL (2 mg\/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 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.\u003cbr\u003e\u003cbr\u003eType II Collagen and Adjuvent Susceptibility to CIA is linked to MHC class II molecules and is dependent upon the species of type II collagen used for immunization. Various species of highly purified Type II Collagen are supplied lyophilized and in solution for use in the induction of arthritis in vivo.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL2A1\u003c\/li\u003e\n\u003cli\u003epro-alpha 1(II) chain\u003c\/li\u003e\n\u003cli\u003eAchondrogenesis\u003c\/li\u003e\n\u003cli\u003eHypochondrogenesis\u003c\/li\u003e\n\u003cli\u003eSpondyloepimetaphyseal dysplasia\u003c\/li\u003e\n\u003cli\u003eOsteoarthritis (OA)\u003c\/li\u003e\n\u003cli\u003eCollagen Induced Arthritis (CIA)\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\u003e\u003cmeta charset=\"UTF-8\"\u003e\u003cspan\u003eHarnett, M. M., Doonan, J., Tarafdar, A., Pineda, M. A., Duncombe-Moore, J., Buitrago, G., Pan, P., Hoskisson, P. A., Selman, C., \u0026amp; Harnett, W. (2024). The parasitic worm product ES-62 protects against collagen-induced arthritis by resetting the gut-bone marrow axis in a microbiome-dependent manner. \u003c\/span\u003e\u003ci\u003eFrontiers in tropical diseases\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e4\u003c\/i\u003e\u003cspan\u003e, fitd.2023.1334705. https:\/\/doi.org\/10.3389\/fitd.2023.1334705\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eSimpkins, D. A., Downton, P., Gray, K. J., Dickson, S. H., Maidstone, R. J., Konkel, J. E., Hepworth, M. R., Ray, D. W., Bechtold, D. A., \u0026amp; Gibbs, J. E. (2023). Consequences of collagen induced inflammatory arthritis on circadian regulation of the gut microbiome. \u003ci\u003eFASEB journal : official publication of the Federation of American Societies for Experimental Biology\u003c\/i\u003e, \u003ci\u003e37\u003c\/i\u003e(1), e22704.\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eKeller, C. R., Ruud, K. F., Martinez, S. R., \u0026amp; Li, W. (2022). Identification of the Collagen Types Essential for Mammalian Breast Acinar Structures. \u003c\/span\u003e\u003ci\u003eGels\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e8\u003c\/i\u003e\u003cspan\u003e(12).\u003c\/span\u003e \u003cbr\u003e\u003cspan\u003eScanu, A., Luisetto, R., Oliviero, F., Galuppini, F., Lazzarin, V., Pennelli, G., ... \u0026amp; Punzi, L. (2022). Bactericidal\/Permeability-Increasing Protein Downregulates the Inflammatory Response in In Vivo Models of Arthritis. \u003c\/span\u003e\u003ci\u003eInternational Journal of Molecular Sciences\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e23\u003c\/i\u003e\u003cspan\u003e(21), 13066.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eLord, A. E., Zhang, L., Erickson, J. E., Bryant, S., Nelson, C. M., Gaudette, S. M., ... \u0026amp; Mitra, S. (2022). 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A., M Harnett, M., \u0026amp; Harnett, W. (2020). Development of Acanthocheilonema viteae in Meriones shawi: Absence of microfilariae and production of active ES-62. Parasite Immunology, e12803.\u003cbr\u003e\u003cbr\u003eAlvarez, P., Augustín, J. J., Tamayo, E., Iglesias, M., Acinas, O., Mendiguren, M. A., ... \u0026amp; Merino, R. (2020). Therapeutic effects of anti-Bone Morphogenetic Protein and Activin Membrane-Bound Inhibitor treatment in psoriasis and arthritis. Arthritis \u0026amp; Rheumatology.\u003cbr\u003e\u003cbr\u003eZhou, J., Chen, P., Li, Z., \u0026amp; Zuo, Q. (2020). Gene delivery of TIPE2 attenuates collagen-induced arthritis by modulating inflammation. International Immunopharmacology, 79, 106044. \u003cbr\u003e\u003cbr\u003eLückemann, L., Stangl, H., Straub, R. H., Schedlowski, M., \u0026amp; Hadamitzky, M. (2019). Learned immunosuppressive placebo response attenuates disease progression in a rodent model of rheumatoid arthritis. Arthritis \u0026amp; Rheumatology\u003cbr\u003eLeblond, A., Pezet, S., Cauvet, A., Casas, C., \u0026amp; Da, J. P. (2020). Decreased expression and Activity of the desacetylase Sirtuin-1 contribute to the activated and proangiogenic profile of endothelial cells in rheumatoid arthritis and promote the persistence of experimental arthritis by increasing synovial angiogenesis. Ann Rheum Dis, 891, 79.\u003cbr\u003e\u003cbr\u003eCasanova-Vallve, N., Constantin-Teodosiu, D., Filer, A., Hardy, R. S., Greenhaff, P. L.,Chapman, V. (2020). Skeletal muscle dysregulation in rheumatoid arthritis: Metabolic and molecular markers in a rodent model and patients. PloS one, 15(7), e0235702.\u003cbr\u003e\u003cbr\u003eLückemann, L., Stangl, H., Straub, R. H., Schedlowski, M., \u0026amp; Hadamitzky, M. (2020). Learned immunosuppressive placebo response attenuates disease progression in a rodent model of rheumatoid arthritis. Arthritis \u0026amp; Rheumatology.\u003cbr\u003e\u003cbr\u003eMausset-Bonnefont, A. L., Cren, M., Vicente, R., Quentin, J., Jorgensen, C., Apparailly, F., \u0026amp; Louis-Plence, P. (2019). Arthritis sensory and motor scale: predicting functional deficits from the clinical score in collagen-induced arthritis. Arthritis Research \u0026amp; Therapy, 21(1), 1-12.\u003cbr\u003e\u003cbr\u003ePoolman, T. M., Gibbs, J., Walker, A. L., Dickson, S., Farrell, L., Hensman, J., ... \u0026amp; Rattray, M. (2019). Rheumatoid arthritis reprograms circadian output pathways. Arthritis Research \u0026amp; Therapy, 21(1), 47.\u003cbr\u003e\u003cbr\u003eEbbers, M., Lübcke, P. M., Volzke, J., Kriebel, K., Hieke, C., Engelmann, R., ... \u0026amp; Müller-Hilke, B. (2018). Interplay between P. gingivalis, F. nucleatum and A. actinomycetemcomitans in murine alveolar bone loss, arthritis onset and progression. Scientific reports, 8(1), 15129.\u003cbr\u003e\u003cbr\u003eRuzek, M. C., Huang, L., Zhang, T. T., Bryant, S., Slivka, P. F., Cuff, C. A., ... \u0026amp; Blaich, G. (2018). Dual Blockade of Interleukin-1β and Interleukin-17A Reduces Murine Arthritis Pathogenesis but Also Leads to Spontaneous Skin Infections in Nonhuman Primates. Journal of Pharmacology and Experimental Therapeutics, 364(3), 474-484.\u003cbr\u003e\u003cbr\u003eDoonan, J., Lumb, F. E., Pineda, M. A., Tarafdar, A., Crowe, J., Khan, A. M., ... \u0026amp; Harnett, W. (2018). Protection against arthritis by the parasitic worm product ES-62, and its drug-like small molecule analogues, is associated with inhibition of osteoclastogenesis. Frontiers in immunology, 9\u003cbr\u003e\u003cbr\u003eLin, Y. Y., Jean, Y. H., Lee, H. P., Lin, S. C., Pan, C. Y., Chen, W. F., ... \u0026amp; Sung, P. J. (2017). Excavatolide B attenuates rheumatoid arthritis through the inhibition of osteoclastogenesis. Marine drugs, 15(1), 9.\u003cbr\u003e\u003cbr\u003eEngelmann, R., \u0026amp; Müller-Hilke, B. (2017). Experimental silicosis does not aggravate collagen-induced arthritis in mice. Journal of negative results in biomedicine, 16(1), 5.\u003cbr\u003e\u003cbr\u003eOehler, B., Kistner, K., Martin, C., Schiller, J., Mayer, R., Mohammadi, M., ... \u0026amp; Pflücke, D. (2017). Inflammatory pain control by blocking oxidized phospholipid-mediated TRP channel activation. Scientific reports, 7(1), 5447.\u003cbr\u003e\u003cbr\u003eDel Prete, A., Martínez-Muñoz, L., Mazzon, C., Toffali, L., Sozio, F., Za, L., ... \u0026amp; Liberati, C. (2017). The atypical receptor CCRL2 is required for CXCR2-dependent neutrophil recruitment and tissue damage. Blood, blood-2017.\u003cbr\u003e\u003cbr\u003eHablot, J., Peyrin-Biroulet, L., Kokten, T., El Omar, R., Netter, P., Bastien, C., ... \u0026amp; Moulin, D. (2017). Experimental colitis delays and reduces the severity of collagen-induced arthritis in mice. PloS one, 12(9), e0184624.\u003cbr\u003e\u003cbr\u003eVicente, R., Quentin, J., Mausset-Bonnefont, A. L., Chuchana, P., Martire, D., Cren, M., ... \u0026amp; Louis-Plence, P. (2015). Nonclassical CD4+ CD49b+ regulatory T cells as a better alternative to conventional CD4+ CD25+ T cells to dampen arthritis severity. The Journal of Immunology, 1501069.\u003cbr\u003e\u003cbr\u003eMcRae, B. L., Levin, A. D., Wildenberg, M. E., Koelink, P. J., Bousquet, P., Mikaelian, I., ... \u0026amp; Salfeld, J. (2015). Fc receptor-mediated effector function contributes to the therapeutic response of anti-TNF monoclonal antibodies in a mouse model of inflammatory bowel disease. Journal of Crohn's and Colitis, 10(1), 69-76.\u003cbr\u003e\u003cbr\u003eNieto, F. R., Clark, A. K., Grist, J., Hathway, G. J., Chapman, V., \u0026amp; Malcangio, M. (2016). Neuron-immune mechanisms contribute to pain in early stages of arthritis. Journal of neuroinflammation, 13(1), 96.\u003cbr\u003e\u003cbr\u003eHansson, C., Schön, K., Kalbina, I., Strid, Å., Andersson, S., Bokarewa, M. I., \u0026amp; Lycke, N. Y. (2016). 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J immunol. 2010 Aug 15; 185(4):2544-54.Liver X Receptor Agonism Promotes Articular Inflammation in Murine Collagen-Induced Arthritis\u003cbr\u003eAsquith DL, Miller AM, et al. Arthritis Rheum.2009 Sep; 60(9):2655-65.Destructive Arthritis in the Absence of Both FcRI and FcRIII\u003cbr\u003ePeter Boross et al., J. Immunol., Apr 2008; 180: 5083 - 5091.Efficient suppression of murine arthritis by combined anticytokine small interfering RNA lipoplexes.\u003cbr\u003eKhoury M, et al. Arthritis Rheum. 2008 Aug; 58(8):2356-67Immunomodulatory Dendritic Cells Inhibit Th1 Responses and Arthritis via Different Mechanisms\u003cbr\u003eLeonie M. van Duivenvoorde et al., J. Immunol., Aug 2007; 179: 1506 - 1515.Antibody-mediated delivery of IL-10 inhibits the progression of established collagen-induced arthritis.\u003cbr\u003eTrachsel E, et al. Arthritis Res Ther. 2007;9(1):R9The non-thiol angiotensin-converting enzyme inhibitor quinapril suppresses inflammatory arthritis\u003cbr\u003eN. Dalbeth et al., Rheumatology, Jan 2005; 44: 24 - 31.Inflammatory arthritis and dermatitis in thymectomized, CD25+ cell-depleted adult mice\u003cbr\u003eA. Loughry et al., Rheumatology, Mar 2005; 44: 299 - 308.Tracking of Proinflammatory Collagen-Specific T Cells in Early and Late Collagen-Induced Arthritis in Humanized Mice\u003cbr\u003ePia Svendsen et al., J. Immunol., Dec 2004; 173: 7037 - 7045. \u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848195686589,"sku":"804001-sol","price":285.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_II_Bovine_Solution.png?v=1718875581"},{"product_id":"collagen-type-ii-chicken-lyophilized","title":"Collagen Type II, Chicken, Lyophilized, 10 mg","description":"\u003cp\u003eHighest quality (\u0026gt;99%) Collagen type II (CII) protein, purified from chicken sternum, for the induction of arthritis in the Collagen-Induced Arthritis (CIA) model. Lyophilized. Can be reconstituted to desired concentration.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\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 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.\u003cbr\u003e\u003cbr\u003eType II Collagen and Adjuvent Susceptibility to CIA is linked to MHC class II molecules and is dependent upon the species of type II collagen used for immunization. Various species of highly purified Type II Collagen are supplied lyophilized and in solution for use in the induction of arthritis in vivo.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbol\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL2A1\u003c\/li\u003e\n\u003cli\u003epro-alpha 1(II) chain\u003c\/li\u003e\n\u003cli\u003eAchondrogenesis\u003c\/li\u003e\n\u003cli\u003eHypochondrogenesis\u003c\/li\u003e\n\u003cli\u003eSpondyloepiphyseal dysplasia\u003c\/li\u003e\n\u003cli\u003eOsteoarthritis (OA)\u003c\/li\u003e\n\u003cli\u003eCollagen Induced Arthritis (CIA)\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cp data-mce-fragment=\"1\"\u003e\u003cstrong\u003eReferences\/Citations:\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cmeta charset=\"UTF-8\"\u003e\u003cspan\u003eBiesemann, N., Margerie, D., Asbrand, C., Rehberg, M., Savova, V., Agueusop, I., Klemmer, D., Ding-Pfennigdorff, D., Schwahn, U., Dudek, M., Heyninck, K., De Tavernier, E., Cornelis, S., Kohlmann, M., Nestle, F. 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Clinical \u0026amp; Experimental Immunology, 183(3), 405-418.\u2028\u2028 \u003cbr\u003e  \u003cbr\u003ePerez, J., Dansou, B., Hervé, R., Levi, C., Tamouza, H., Vandermeersch, S., ... \u0026amp; Boissier, M. C. (2015). Calpains released by T lymphocytes cleave TLR2 to control IL-17 expression. The Journal of Immunology, 1500749.\u2028\u2028 \u003cbr\u003e  \u003cbr\u003eVicente, R., Quentin, J., Mausset-Bonnefont, A. L., Chuchana, P., Martire, D., Cren, M., ... \u0026amp; Louis-Plence, P. (2015). Nonclassical CD4+ CD49b+ regulatory T cells as a better alternative to conventional CD4+ CD25+ T cells to dampen arthritis severity. The Journal of Immunology, 1501069.\u2028\u2028 \u003cbr\u003e  \u003cbr\u003eVan Roy, M., Ververken, C., Beirnaert, E., Hoefman, S., Kolkman, J., Vierboom, M., ... \u0026amp; Jacobs, S. (2015). The preclinical pharmacology of the high affinity anti-IL-6R Nanobody® ALX-0061 supports its clinical development in rheumatoid arthritis. Arthritis research \u0026amp; therapy, 17(1), 135.\u2028\u2028Lindh, I., Snir, O., Lönnblom, E., Uysal, H., Andersson, I., Nandakumar, K. S., ... \u0026amp; Holmdahl, R. (2014). Type II collagen antibody response is enriched in the synovial fluid of rheumatoid joints and directed to the same major epitopes as in collagen induced arthritis in primates and mice. Arthritis research \u0026amp; therapy, 16(4), R143.\u2028\u2028 \u003cbr\u003e  \u003cbr\u003eRoy, L. D., Sahraei, M., Schettini, J. L., Gruber, H. E., Besmer, D. M., \u0026amp; Mukherjee, P. (2014). Systemic neutralization of IL-17A significantly reduces breast cancer associated metastasis in arthritic mice by reducing CXCL12\/SDF-1 expression in the metastatic niches. BMC cancer, 14(1), 225.\u2028\u2028 \u003cbr\u003e  \u003cbr\u003eChen, Y. M., Chuang, H. C., Lin, W. C., Tsai, C. Y., Wu, C. W., Gong, N. R., ... \u0026amp; Chen, D. Y. (2013). Germinal Center Kinase–like Kinase Overexpression in T Cells as a Novel Biomarker in Rheumatoid Arthritis. Arthritis \u0026amp; Rheumatism, 65(10), 2573-2582.\u2028\u2028 \u003cbr\u003e  \u003cbr\u003eMarenzana, M., Vugler, A., Moore, A., \u0026amp; Robinson, M. (2013). Effect of sclerostin-neutralising antibody on periarticular and systemic bone in a murine model of rheumatoid arthritis: a microCT study. Arthritis Res Ther, 15(5), R125.\u2028\u2028 \u003cbr\u003e  \u003cbr\u003eIqbal, A. J., Cooper, D., Vugler, A., Gittens, B. R., Moore, A., \u0026amp; Perretti, M. (2013). Endogenous galectin-1 exerts tonic inhibition on experimental arthritis. The Journal of Immunology, 191(1), 171-177.\u2028\u2028 \u003cbr\u003e  \u003cbr\u003eVierboom, M., Breedveld, E., Kondova, I., \u0026amp; 't Hart, B. (2010). Collagen-induced arthritis in common marmosets: a new nonhuman primate model for chronic arthritis. Arthritis Research and Therapy, 12(5), R200.\u2028\u2028 \u003cbr\u003e  \u003cbr\u003eAsquith, D. L., Miller, A. M., Hueber, A. J., Liew, F. Y., Sattar, N., \u0026amp; McInnes, I. B. (2010). Apolipoprotein E–deficient mice are resistant to the development of collagen‐induced arthritis. Arthritis \u0026amp; Rheumatism, 62(2), 472-477.\u2028\u2028 \u003cbr\u003e  \u003cbr\u003ePufe, T., Petersen, W., Kurz, B., Tsokos, M., Tillmann, B., \u0026amp; Mentlein, R. (2003). Mechanical factors influence the expression of endostatin—an inhibitor of angiogenesis—in tendons. Journal of orthopaedic research, 21(4), 610-616.\u2028\u2028 \u003cbr\u003e  \u003cbr\u003eBäcklund, J., Treschow, A., Bockermann, R., Holm, B., Holm, L., Issazadeh‐Navikas, S., ... \u0026amp; Holmdahl, R. (2002). Glycosylation of type II collagen is of major importance for T cell tolerance and pathology in collagen‐induced arthritis. European journal of immunology, 32(12), 3776-3784.\u2028\u2028\u2028 \u003cbr\u003e  \u003cbr\u003eApolipoprotein E-deficient mice are resistant to the development of collagen-induced arthritis.\u2028Asquith DL, Miller AM, et al. Arthritis Rheum. 2010 Feb; 62(2):472-7. \u003cbr\u003e  \u003cbr\u003eReversible changes in serum immunoglobulin galactosylation during the immune response and treatment of inflammatory autoimmune arthritis.Van Beneden K, et al. Annals of the rheumatic diseases. 2009; 68(8):1360-5. \u003cbr\u003e \u003cbr\u003e\u003cbr\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848195883197,"sku":"804002-lyo","price":285.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_II_Chicken_Lyophilized.png?v=1718875702"},{"product_id":"collagen-type-ii-chicken-soluble","title":"Collagen Type II, Chicken, Soluble, 2 mg\/mL","description":"\u003cp\u003eHighest quality (\u0026gt;99%) Collagen type II (CII) protein, purified from chicken sternum, for the induction of arthritis in the Collagen-Induced Arthritis (CIA) model. Soluble 10 mg (2 mg\/mL).\u003cbr\u003e\u003c\/p\u003e\n\u003cp\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 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.\u003cbr\u003e\u003cbr\u003e Type II Collagen and Adjuvent Susceptibility to CIA is linked to MHC class II molecules and is dependent upon the species of type II collagen used for immunization. Various species of highly purified Type II Collagen are supplied lyophilized and in solution for use in the induction of arthritis in vivo.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL2A1\u003c\/li\u003e\n\u003cli\u003epro-alpha 1(II) chain\u003c\/li\u003e\n\u003cli\u003eAchondrogenesis\u003c\/li\u003e\n\u003cli\u003eHypochondrogenesis\u003c\/li\u003e\n\u003cli\u003eSpondyloepiphyseal dysplasia\u003c\/li\u003e\n\u003cli\u003eOsteoarthritis (OA)\u003c\/li\u003e\n\u003cli\u003eCollagen Induced Arthritis (CIA)\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cul\u003e\u003c\/ul\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. Traffic, 23(1), 81-93.\u003c\/p\u003e\n\u003cp\u003eLi, L., Freitag, J., Asbrand, C., Munteanu, B., Wang, B. T., Zezina, E., ... \u0026amp; Biesemann, N. (2022). Multi-omics profiling of collagen-induced arthritis mouse model reveals early metabolic dysregulation via SIRT1 axis. bioRxiv.\u003c\/p\u003e\n\u003cp\u003eWang, Y., Pan, P., Khan, A., Çil, Ç., \u0026amp; Pineda, M. A. (2022). Synovial Fibroblast Sialylation Regulates Cell Migration and Activation of Inflammatory Pathways in Arthritogenesis. Frontiers in Immunology, 13.\u003c\/p\u003e\n\u003cp\u003eGilis, E., Gaublomme, D., Staal, J., Venken, K., Dhaenens, M., Lambrecht, S., ... \u0026amp; Dumas, E. (2019). Deletion of Mucosa-Associated Lymphoid Tissue Lymphoma Translocation Protein 1 in Mouse T Cells Protects Against Development of Autoimmune Arthritis but Leads to Spontaneous Osteoporosis. Arthritis \u0026amp; Rheumatology, 71(12), 2005-2015.\u003cbr\u003e \u003cbr\u003eChuang, H. C., Chen, Y. M., Chen, M. H., Hung, W. T., Yang, H. Y., Tseng, Y. H., \u0026amp; Tan, T. H. (2019). AhR–ROR-γt complex is a therapeutic target for MAP4K3\/GLKhighIL-17A high subpopulation of systemic lupus erythematosus. The FASEB Journal, 33(10), 11469-11480.\u003cbr\u003e \u003cbr\u003eMoschovakis, G. L., Bubke, A., Friedrichsen, M., Ristenpart, J., Back, J. W., Falk, C. S., ... \u0026amp; Förster, R. (2018). The chemokine receptor CCR7 is a promising target for rheumatoid arthritis therapy. Cellular \u0026amp; molecular immunology\u003cbr\u003e\u003cbr\u003eVierboom, M. P., Breedveld, E., Keehnen, M., Klomp, R., \u0026amp; Bakker, J. (2017). Pain Relief in Nonhuman Primate Models of Arthritis. In Inflammation (pp. 411-417). Humana Press, New York, NY\u003cbr\u003e \u003cbr\u003eKurowska-Stolarska, M., Alivernini, S., Melchor, E. G., Elmesmari, A., Tolusso, B., Tange, C., ... \u0026amp; Stewart, L. (2017). MicroRNA-34a dependent regulation of AXL controls the activation of dendritic cells in inflammatory arthritis. Nature communications, 8, 15877.\u003cbr\u003e \u003cbr\u003eMoschovakis, G. L., Bubke, A., Friedrichsen, M., Falk, C. S., Feederle, R., \u0026amp; Förster, R. (2017). T cell specific Cxcr5 deficiency prevents rheumatoid arthritis. Scientific Reports, 7(1), 8933.\u003cbr\u003e \u003cbr\u003eVerheul, M. K., Vierboom, M. P., Bert, A., Toes, R. E., \u0026amp; Trouw, L. A. (2017). Anti-carbamylated protein antibodies precede disease onset in monkeys with collagen-induced arthritis. Arthritis research \u0026amp; therapy, 19(1), 246.\u003cbr\u003e \u003cbr\u003eAthari, S. K., Poirier, E., Biton, J., Semerano, L., Hervé, R., Raffaillac, A., ... \u0026amp; Boissier, M. C. (2016). Collagen-induced arthritis and imiquimod-induced psoriasis develop independently of interleukin-33. Arthritis research \u0026amp; therapy, 18(1), 143.\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\u003eVierboom, M. P. M., Breedveld, E., Kap, Y. S., Mary, C., Poirier, N., 't Hart, B. A., \u0026amp; Vanhove, B. (2016). Clinical efficacy of a new CD28‐targeting antagonist of T cell co‐stimulation in a non‐human primate model of collagen‐induced arthritis. Clinical \u0026amp; Experimental Immunology, 183(3), 405-418.\u003cbr\u003e \u003cbr\u003eVan Roy, M., Ververken, C., Beirnaert, E., Hoefman, S., Kolkman, J., Vierboom, M., ... \u0026amp; Jacobs, S. (2015). The preclinical pharmacology of the high affinity anti-IL-6R Nanobody® ALX-0061 supports its clinical development in rheumatoid arthritis. Arthritis research \u0026amp; therapy, 17(1), 135.\u003cbr\u003e \u003cbr\u003eVicente, R., Quentin, J., Mausset-Bonnefont, A. L., Chuchana, P., Martire, D., Cren, M., ... \u0026amp; Louis-Plence, P. (2015). Nonclassical CD4+ CD49b+ regulatory T cells as a better alternative to conventional CD4+ CD25+ T cells to dampen arthritis severity. The Journal of Immunology, 1501069.\u003cbr\u003e \u003cbr\u003ePerez, J., Dansou, B., Hervé, R., Levi, C., Tamouza, H., Vandermeersch, S., ... \u0026amp; Boissier, M. C. (2015). Calpains released by T lymphocytes cleave TLR2 to control IL-17 expression. The Journal of Immunology, 1500749.\u003cbr\u003e \u003cbr\u003eLindh, I., Snir, O., Lönnblom, E., Uysal, H., Andersson, I., Nandakumar, K. S., ... \u0026amp; Holmdahl, R. (2014). Type II collagen antibody response is enriched in the synovial fluid of rheumatoid joints and directed to the same major epitopes as in collagen induced arthritis in primates and mice. Arthritis research \u0026amp; therapy, 16(4), R143.\u003cbr\u003e \u003cbr\u003eRoy, L. D., Sahraei, M., Schettini, J. L., Gruber, H. E., Besmer, D. M., \u0026amp; Mukherjee, P. (2014). Systemic neutralization of IL-17A significantly reduces breast cancer associated metastasis in arthritic mice by reducing CXCL12\/SDF-1 expression in the metastatic niches. BMC cancer, 14(1), 225.\u003cbr\u003e \u003cbr\u003eChen, Y. M., Chuang, H. C., Lin, W. C., Tsai, C. Y., Wu, C. W., Gong, N. R., ... \u0026amp; Chen, D. Y. (2013). Germinal Center Kinase–like Kinase Overexpression in T Cells as a Novel Biomarker in Rheumatoid Arthritis. Arthritis \u0026amp; Rheumatism, 65(10), 2573-2582.\u003cbr\u003e \u003cbr\u003eMarenzana, M., Vugler, A., Moore, A., \u0026amp; Robinson, M. (2013). Effect of sclerostin-neutralising antibody on periarticular and systemic bone in a murine model of rheumatoid arthritis: a microCT study. Arthritis Res Ther, 15(5), R125.\u003cbr\u003e \u003cbr\u003eIqbal, A. J., Cooper, D., Vugler, A., Gittens, B. R., Moore, A., \u0026amp; Perretti, M. (2013). Endogenous galectin-1 exerts tonic inhibition on experimental arthritis. The Journal of Immunology, 191(1), 171-177.\u003cbr\u003e \u003cbr\u003eVierboom, M., Breedveld, E., Kondova, I., \u0026amp; 't Hart, B. (2010). Collagen-induced arthritis in common marmosets: a new nonhuman primate model for chronic arthritis. Arthritis Research and Therapy, 12(5), R200.\u003cbr\u003e \u003cbr\u003eAsquith, D. L., Miller, A. M., Hueber, A. J., Liew, F. Y., Sattar, N., \u0026amp; McInnes, I. B. (2010). Apolipoprotein E–deficient mice are resistant to the development of collagen‐induced arthritis. Arthritis \u0026amp; Rheumatism, 62(2), 472-477.\u003cbr\u003e \u003cbr\u003ePufe, T., Petersen, W., Kurz, B., Tsokos, M., Tillmann, B., \u0026amp; Mentlein, R. (2003). Mechanical factors influence the expression of endostatin—an inhibitor of angiogenesis—in tendons. Journal of orthopaedic research, 21(4), 610-616.\u003cbr\u003e \u003cbr\u003eBäcklund, J., Treschow, A., Bockermann, R., Holm, B., Holm, L., Issazadeh‐Navikas, S., ... \u0026amp; Holmdahl, R. (2002). Glycosylation of type II collagen is of major importance for T cell tolerance and pathology in collagen‐induced arthritis. European journal of immunology, 32(12), 3776-3784.\u003cbr\u003e \u003cbr\u003e\u003cbr\u003eApolipoprotein E-deficient mice are resistant to the development of collagen-induced arthritis.\u003cbr\u003eAsquith DL, Miller AM, et al. Arthritis Rheum. 2010 Feb; 62(2):472-7.Reversible changes in serum immunoglobulin galactosylation during the immune response and treatment of inflammatory autoimmune arthritis.Van Beneden K, et al. Annals of the rheumatic diseases. 2009; 68(8):1360-5.\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848195915965,"sku":"804002-sol","price":285.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_II_Chicken_Solution.png?v=1718875804"},{"product_id":"collagen-type-iii-bovine","title":"Collagen Type III, Bovine, 10 mg","description":"\u003cp\u003ePurified type III bovine collagen. 10 mg. Lyophilized.\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eType III collagen is the second most abundant collagen in tissues and is found most commonly in tissues exhibiting elastic properties such as skin, lungs, intestinal walls and walls of blood vessels. It is a homotrimer comprised of three alpha-1 chains and resembles other fibrillar collagens in structure and function. It is synthesized as procollagen, similary to collagen I, but the N-terminal propeptide remains attached in the mature fibrillar type III form.\u003cbr\u003e\u003cbr\u003e Mutations of type III collagen causes Ehlers-Danlos syndrome, EDS IV, which affect arteries, internal organs, joints and skin, and may cause sudden death when the large arteries rupture.\u003cbr\u003e\u003cbr\u003e\u003cstrong\u003eSymbols\/Related Terms:\u003c\/strong\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eCOL3A1\u003c\/li\u003e\n\u003cli\u003eCollagen type III, alpha 1\u003c\/li\u003e\n\u003cli\u003eCollagen III, alpha-1 polypeptide\u003c\/li\u003e\n\u003cli\u003ecollagen, type III, alpha 1 (Ehlers-Danlos syndrome type IV, autosomal dominant)\u003c\/li\u003e\n\u003cli\u003eEDS4A\u003c\/li\u003e\n\u003c\/ul\u003e\n","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848195981501,"sku":"8052009","price":530.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_III_Bovine.png?v=1721220148"},{"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":"collagen-type-v-atelocollagen-bovine","title":"Collagen Type V (Atelocollagen), Bovine, 1 mg","description":"\u003cp\u003e\u003cspan\u003ePurified Bovine Collagen Type V from bovine placenta (atelocollagen)\u003c\/span\u003e\u003cspan lang=\"EN-US\"\u003e.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cbr\u003e\u003cspan\u003eType V collagen is a fibrillar collagen that plays a vital role in the fibrillation of types I and III collagen, ultimately contributing to optimal fibrillary formation and tissue quality. It is an essential component of the bone matrix, corneal stroma, and the interstitial matrix of muscles, liver, lungs, and placenta. However, dysregulation of collagen fibrillogenesis is a hallmark of several subtypes of Ehlers-Danlos syndrome (EDS). \u003c\/span\u003e\u003cbr\u003e\u003cspan\u003e \u003c\/span\u003e\u003cbr\u003e\u003cspan\u003eStudies have shown that Type V collagen is responsible for regulating the heterotypic fiber diameter and \u003c\/span\u003e\u003cspan lang=\"EN-US\"\u003eis \u003c\/span\u003e\u003cspan\u003econsidered a regulatory fibril-forming collagen. It is a part of the family of collagen proteins consisting of Collagen I- Collagen XXVIII, which support and strengthen many tissues including skin, bones, muscles, and ligaments. \u003c\/span\u003e\u003cbr\u003e\u003cspan\u003e \u003c\/span\u003e\u003cbr\u003e\u003cspan\u003eType V collagen is associated with the COL5A1 gene which provides instructions to produce Collagen V. Like other collagens, it is made up of procollagen molecules. \u003c\/span\u003e\u003cbr\u003e\u003cspan\u003e \u003c\/span\u003e\u003cbr\u003e\u003cspan\u003eUnderstanding the importance of Type V collagen in the body can help \u003c\/span\u003e\u003cspan lang=\"EN-US\"\u003eresearchers understand\u003c\/span\u003e\u003cspan\u003e the role it plays in maintaining tissue quality and preventing the onset of EDS. \u003c\/span\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848196178109,"sku":"8052012","price":790.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Collagen_Type_V_Atelocollagen_Bovine.png?v=1722412643"},{"product_id":"complete-freund-adjuvant","title":"Complete Freund's Adjuvant, 4 mg\/mL (5 mL)","description":"\u003cp\u003eComplete Freund's Adjuvant (CFA or FCA) is 4 mg\/ml M. Tuberculosis (non-viable) in mineral oil. \u003cmeta charset=\"utf-8\"\u003e\u003cspan data-mce-fragment=\"1\"\u003eFor in-vivo\/in-vitro studies. Typically used for the boost of an immune response.\u003c\/span\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eComplete Freund's Aduvant (CFA or FCA) is widely used in immunological research for the preparation of antigen-adjuvant emulsions in laboratory animal studies. CFA contains cell wall components of heat killed Mycobacterium tuberculosis and is often used for the initial injection that stimulates an enhanced immune response.\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\u003eHarnett, M. M., Doonan, J., Tarafdar, A., Pineda, M. A., Duncombe-Moore, J., Buitrago, G., Pan, P., Hoskisson, P. A., Selman, C., \u0026amp; Harnett, W. (2024). The parasitic worm product ES-62 protects against collagen-induced arthritis by resetting the gut-bone marrow axis in a microbiome-dependent manner. \u003c\/span\u003e\u003ci\u003eFrontiers in tropical diseases\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e4\u003c\/i\u003e\u003cspan\u003e, fitd.2023.1334705. https:\/\/doi.org\/10.3389\/fitd.2023.1334705\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cmeta charset=\"UTF-8\"\u003e\u003cspan\u003eMalcolm, J., Nyirenda, M. H., Brown, J. L., Adrados-Planell, A., Campbell, L., Butcher, J. P., Glass, D. G., Piela, K., Goodyear, C. S., Wright, A. J., McInnes, I. B., Millington, O. R., \u0026amp; Culshaw, S. (2023). C-terminal citrullinated peptide alters antigen-specific APC:T cell interactions leading to breach of immune tolerance. \u003c\/span\u003e\u003ci\u003eJournal of autoimmunity\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e135\u003c\/i\u003e\u003cspan\u003e, 102994.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003e\u003cmeta charset=\"UTF-8\"\u003eLibánská, A., Randárová, E., Skoroplyas, S., Bartoš, M., Luňáčková, J., Lager, F., Renault, G., Scherman, D., \u0026amp; Etrych, T. (2023). Size-switchable polymer-based nanomedicines in the advanced therapy of rheumatoid arthritis. \u003ci\u003eJournal of controlled release : official journal of the Controlled Release Society\u003c\/i\u003e, \u003ci\u003e353\u003c\/i\u003e, 30–41. \u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eHansson, C., Lebrero-Fernández, C., Schön, K., Angeletti, D., \u0026amp; Lycke, N. (2023). Tr1 cell-mediated protection against autoimmune disease by intranasal administration of a fusion protein targeting cDC1 cells. Mucosal Immunology.\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. Traffic, 23(1), 81-93.\u003c\/p\u003e\n\u003cp\u003eWang, Y., Pan, P., Khan, A., Çil, Ç., \u0026amp; Pineda, M. A. (2022). Synovial Fibroblast Sialylation Regulates Cell Migration and Activation of Inflammatory Pathways in Arthritogenesis. Frontiers in Immunology, 13.\u003cstrong\u003e\u003cbr\u003e\u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eSimpkins, D. A., Downton, P., Gray, K. J., Dickson, S. H., Maidstone, R. J., Konkel, J. E., ... \u0026amp; Gibbs, J. E. (2022). Consequences of collagen induced inflammatory arthritis on circadian regulation of the gut microbiome. \u003c\/span\u003e\u003ci\u003eThe FASEB Journal\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e37\u003c\/i\u003e\u003cspan\u003e(1).\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eCasanova-Vallve, N., Constantin-Teodosiu, D., Filer, A., Hardy, R. S., Greenhaff, P. L., \u0026amp; Chapman, V. (2020). Skeletal muscle dysregulation in rheumatoid arthritis: Metabolic and molecular markers in a rodent model and patients. PloS one, 15(7), e0235702.\u003cbr\u003e\u003cbr\u003eAlvarez, P., Augustín, J. J., Tamayo, E., Iglesias, M., Acinas, O., Mendiguren, M. A., ... \u0026amp; Merino, R. (2020). Therapeutic effects of anti-Bone Morphogenetic Protein and Activin Membrane-Bound Inhibitor treatment in psoriasis and arthritis. Arthritis \u0026amp; Rheumatology.\u003cbr\u003e\u003cbr\u003ePoolman, T. M., Gibbs, J., Walker, A. L., Dickson, S., Farrell, L., Hensman, J., ... \u0026amp; Rattray, M. (2019). Rheumatoid arthritis reprograms circadian output pathways. Arthritis Research \u0026amp; Therapy, 21(1), 47.\u003cbr\u003e\u003cbr\u003eChuang, H. C., Chen, Y. M., Chen, M. H., Hung, W. T., Yang, H. Y., Tseng, Y. H., \u0026amp; Tan, T. H. (2019). AhR–ROR-γt complex is a therapeutic target for MAP4K3\/GLKhighIL-17A high subpopulation of systemic lupus erythematosus. The FASEB Journal, 33(10), 11469-11480.\u003cbr\u003e\u003cbr\u003eMariola Kurowska-Stolarska, Stefano Alivernini, Emma Garcia Melchor, et. al. MicroRNA-34a dependent regulation of AXL controls the activation of dendritic cells in inflammatory arthritis. Nature Communications (2017) 8, Article number 15877 \u003cbr\u003e77 \u003cbr\u003e\u003cbr\u003eChris AH Hansel, Lindsay M MacLellan, Rachek S Oldham, et. al. The atypical chemokine receptor ACKR2 suppresses Th17 responses to protein autoantigens. Immunology and Cell Biology (2014), 1-10\u003cbr\u003e\u003cbr\u003eCampo GM, Avenoso A, D'Ascola A, Nastasi G, et.al. Combined Treatment With Hyaluronan Inhibitor Pep-1 and a Selective Adenosine A2 Receptor Agonist Reduces Inflammation in Experimental Arthritis. Innate Immun. 2013;19(5):462-478\u003cbr\u003e\u003cbr\u003eEveline Trachsel, Frank Bootz, Michela Silacci, et. al. Antibody-mediated delivery of IL-10 inhibits the progression of established collagen-induced arthritis. Arthritis Research \u0026amp; Therapy (2007), 9:R9\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848196636861,"sku":"501009","price":75.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Complete_Freunds_Adjuvant.png?v=1718873673"},{"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":"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":"lipopolysaccharide-lps","title":"Lipopolysaccharide (LPS), 5.0 mg","description":"\u003cp class=\"p1\"\u003eHighly purified LPS for in vivo and in vitro use. \u003cbr\u003e\u003c\/p\u003e\n\u003cp class=\"p1\"\u003e \u003c\/p\u003e\n\u003cp class=\"p1\"\u003eLipopolysaccharides (LPS), also known as lipoglyans and endotoxins, are large molecules consisting of a lipid and a polysaccharide composed of O-antigen outer core and inner core joined by a covalent bond. They are found in the outer membrane of Gram-negative bacteria and elicit strong immune responses in normal mammalian cells. LPS from E. coli is particularly potent in systemic inflammation and have long been recongnized as a key factor in septic shock and also used in research to induce synthesis and secretion of growth promoting factors such as interleukins. \u003cbr\u003e \u003cbr\u003e MD Bioproducts provides lyophilized lipopolysaccharide (LPS) for in vivo and in vitro use. The LPS is isolated from Escherichia coli by a modification of the phenol extraction method of Westphal and Jann. This material has been extracted from bacterial cells walls of E. coli 055:B5. The endotoxin has been futher purified to remove traces of residual protein and nucleic acids, producing highly purified LPS. The LPS is essentially free of nucleic acid and protein and is chemically characterized with respect to their phosphate and KDO(2-keto-3-deoxyoctonate) contents. The highly purified LPS has been then re-extracted by the method of Manthey and Vogel to eliminate residual protein contamination.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong data-mce-fragment=\"1\"\u003eReferences\/Citations:\u003c\/strong\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, \u003cem\u003e25\u003c\/em\u003e(1), 103689.\u003c\/p\u003e\n\u003cp class=\"p1\"\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848196931773,"sku":"MDLPS5-0","price":320.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Lipopolysaccharide_LPS.png?v=1721218577"},{"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":"mouse-igg1-isotype-control-biotin-conjugated-antibody","title":"Mouse IgG1 Isotype Control, Biotin-conjugated Antibody, 0.5 mg","description":"\u003cp\u003eMouse IgG1 Isotype control, Biotin Conjugated. \u003cmeta charset=\"utf-8\"\u003e\u003cspan data-mce-fragment=\"1\"\u003eThe biotin conjugate is supplied as 0.5 mg in 1.0 mL of PBS\/NaN3. \u003cmeta charset=\"utf-8\"\u003eStore at 2 – 8 °C.\u003c\/span\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eIsotype controls are most commonly used in flow cytometry and immunohistochemistry experiments as negative controls that measure the level of non-specific background signal caused by primary antibodies. Background signal is due to Igs binding to non-specifcally to Fc receptors present on a cell surface (ex. mice antibodies binding to human leukocytes non-specifically in which investigators would want to use a mouse isotype control when working with human cells or tissues).\u003c\/p\u003e\n","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848197259453,"sku":"1053002B","price":370.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Mouse_IgG1_Isotype_Control_Biotin-conjugated_Antibody.png?v=1722414917"},{"product_id":"mouse-igg1-isotype-control-fitc-conjugated-antibody","title":"Mouse IgG1 Isotype Control, FITC-conjugated Antibody, 0.1 mg","description":"\u003cp\u003eMouse IgG1 Isotype control, FITC-conjugated. \u003cmeta charset=\"utf-8\"\u003e\u003cspan data-mce-fragment=\"1\"\u003eThe fluorescein (FITC) conjugate is supplied in 1.0 mL PBS\/NaN3. \u003c\/span\u003e\u003cspan data-mce-fragment=\"1\"\u003eStore at 2 – 8 °C.\u003c\/span\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eIsotype controls are most commonly used in flow cytometry and immunohistochemistry experiments as negative controls that measure the level of non-specific background signal caused by primary antibodies. Background signal is due to Igs binding to non-specifcally to Fc receptors present on a cell surface (ex. mice antibodies binding to human leukocytes non-specifically in which investigators would want to use a mouse isotype control when working with human cells or tissues).\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848197292221,"sku":"1053002F","price":370.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Mouse_IgG1_Isotype_Control_FITC-conjugated_Antibody.png?v=1722415049"},{"product_id":"mouse-igg1-isotype-control-low-endotoxin-azide-free","title":"Mouse IgG1 Isotype Control, low endotoxin, azide-free, 0.5 mg","description":"\u003cp\u003eMouse IgG1 Isotype control, Low endotoxin, azide-free. \u003cmeta charset=\"utf-8\"\u003e\u003cspan data-mce-fragment=\"1\"\u003eThe low endotoxin, azide-free antibody is supplied as 0.5 mg purified immunoglobulin in 1.0 mL of PBS.\u003c\/span\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eIsotype controls are most commonly used in flow cytometry and immunohistochemistry experiments as negative controls that measure the level of non-specific background signal caused by primary antibodies. Background signal is due to Igs binding to non-specifcally to Fc receptors present on a cell surface (ex. mice antibodies binding to human leukocytes non-specifically in which investigators would want to use a mouse isotype control when working with human cells or tissues).\u003c\/p\u003e\n","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848197357757,"sku":"1053002N","price":340.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Mouse_IgG1_Isotype_Control_low_endotoxin_azide-free.png?v=1722415336"},{"product_id":"mouse-igg1-isotype-control-purified-antibody","title":"Mouse IgG1 Isotype Control, Purified Antibody, 1 mg","description":"\u003cp\u003eMouse IgG1 Isotype control, purified. \u003cmeta charset=\"utf-8\"\u003e\u003cspan data-mce-fragment=\"1\"\u003eThis product supplied as 1.0 mg of purified immunoglobulin in 1.0 mL of borate buffered saline, pH 8.2.\u003c\/span\u003e\u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003e \u003c\/p\u003e\n\u003cp\u003eIsotype controls are most commonly used in flow cytometry and immunohistochemistry experiments as negative controls that measure the level of non-specific background signal caused by primary antibodies. Background signal is due to Igs binding to non-specifcally to Fc receptors present on a cell surface (ex. mice antibodies binding to human leukocytes non-specifically in which investigators would want to use a mouse isotype control when working with human cells or tissues).\u003c\/p\u003e\n","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848197488829,"sku":"1053002","price":390.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Mouse_IgG1_Isotype_Control_Purified_Antibody.png?v=1722414449"},{"product_id":"myelin-oligodendrocyte-glycoprotein-mog-35-55","title":"Myelin Oligodendrocyte Glycoprotein (MOG 35-55), 25 mg","description":"\u003cp\u003ePurified myelin oligodendrocyte glycoprotein (MOG) for MOG-induced EAE models in mouse and rat. \u003cbr\u003e\u003c\/p\u003e\n\u003cp\u003eMultiple Sclerosis (MS) is a demyelinating disease of the central nervous system (CNS). The main characteristics of the disease are focal areas of demyelination and inflammation, however the pathogenesis is unclear. Although no animal model thus far establishes all facets of human MS, Experimental Autoimmune Encephalomyelitis (EAE) represents the model most studied for the disease. Initially brain homogenates were used as antigens for immunization. Today, myelin related proteins or peptides are used in the disease.\u003c\/p\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\u003eWørzner, K., Zimmermann, J., Buhl, R., Desoi, A., Christensen, D., Dietrich, J., Nguyen, N. D. N. T., Lindenstrøm, T., Woodworth, J. S., Alhakeem, R. S., Yu, S., Ødum, N., Mortensen, R., Ashouri, J. F., \u0026amp; Pedersen, G. K. (2024). Repeated immunization with ATRA-containing liposomal adjuvant transdifferentiates Th17 cells to a Tr1-like phenotype. \u003c\/span\u003e\u003ci\u003eJournal of autoimmunity\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e144\u003c\/i\u003e\u003cspan\u003e, 103174. https:\/\/doi.org\/10.1016\/j.jaut.2024.103174\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003eGauthier, T., Martin-Rodriguez, O., Chagué, C., Daoui, A., Ceroi, A., Varin, A., ... \u0026amp; Perruche, S. (2023). Amelioration of experimental autoimmune encephalomyelitis by in vivo reprogramming of macrophages using pro-resolving factors. \u003ci\u003eJournal of Neuroinflammation\u003c\/i\u003e, \u003ci\u003e20\u003c\/i\u003e(1), 307.\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eHe, Y., Ge, C., Moreno-Giró, À., Xu, B., Beusch, C. M., Sandor, K., ... \u0026amp; Holmdahl, R. (2023). A subset of antibodies targeting citrullinated proteins confers protection from rheumatoid arthritis. \u003c\/span\u003e\u003ci\u003eNature communications\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e14\u003c\/i\u003e\u003cspan\u003e(1), 691.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eHansson, C., Lebrero-Fernández, C., Schön, K., Angeletti, D., \u0026amp; Lycke, N. (2023). Tr1 cell-mediated protection against autoimmune disease by intranasal administration of a fusion protein targeting cDC1 cells. \u003ci\u003eMucosal Immunology\u003c\/i\u003e.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eKap, Y. S., van Driel, N., Arends, R., Rouwendal, G., Verolin, M., Blezer, E., ... \u0026amp; 't Hart, B. A. (2015). Immune modulation by a tolerogenic myelin oligodendrocyte glycoprotein (MOG) 10–60 containing fusion protein in the marmoset experimental autoimmune encephalomyelitis model. \u003c\/span\u003e\u003ci\u003eClinical \u0026amp; Experimental Immunology\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e180\u003c\/i\u003e\u003cspan\u003e(1), 28-39.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eIchikawa, M., Koh, C. S., Inaba, Y., Seki, C., Inoue, A., Itoh, M., ... \u0026amp; Komiyama, A. (1999). IgG subclass switching is associated with the severity of experimental autoimmune encephalomyelitis induced with myelin oligodendrocyte glycoprotein peptide in NOD mice. \u003c\/span\u003e\u003ci\u003eCellular immunology\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e191\u003c\/i\u003e\u003cspan\u003e(2), 97-104.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eScolding. (1999). Mechanisms of damage to myelin and oligodendrocytes and their relevance to disease. \u003ci\u003eNeuropathology and applied neurobiology\u003c\/i\u003e, \u003ci\u003e25\u003c\/i\u003e(6), 435-458.\u003c\/span\u003e\u003c\/p\u003e\n\u003cp\u003e\u003cspan\u003eBernard, C. C. A., Johns, T. G., Slavin, A., Ichikawa, M., Ewing, C., Liu, J., \u0026amp; Bettadapura, J. D. (1997). Myelin oligodendrocyte glycoprotein: a novel candidate autoantigen in multiple sclerosis. \u003ci\u003eJournal of molecular medicine\u003c\/i\u003e, \u003ci\u003e75\u003c\/i\u003e, 77-88.\u003c\/span\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848197554365,"sku":"3038001","price":3250.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Myelin_Oligodendrocyte_Glycoprotein_MOG_35_55.png?v=1718877763"},{"product_id":"myelin-proteolipid-protein-plp-139-151","title":"Myelin Proteolipid Protein (PLP 139-151), 15 mg","description":"\u003cp\u003ePurified myelin proteolipid protein (PLP) for PLP-induced EAE models in mouse and rat. \u003c\/p\u003e\n\u003cp\u003eMultiple Sclerosis (MS) is a demyelinating disease of the central nervous system (CNS). The main characteristics of the disease are focal areas of demyelination and inflammation, however the pathogenesis is unclear.\u003cbr\u003e\u003cbr\u003eAlthough no animal model thus far establishes all facets of human MS, Experimental Autoimmune Encephalomyelitis (EAE) represents the model most studied for the disease. Initially brain homogenates were used as antigens for immunization. Today, myelin related proteins or peptides are used in the disease.\u003c\/p\u003e\n\u003cp\u003e\u003cstrong\u003eReferences\/Citations: \u003c\/strong\u003e\u003c\/p\u003e\n\u003cp\u003eHansson, C., Lebrero-Fernández, C., Schön, K., Angeletti, D., \u0026amp; Lycke, N. (2023). Tr1 cell-mediated protection against autoimmune disease by intranasal administration of a fusion protein targeting cDC1 cells. Mucosal Immunology.\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\u003eMcRae, B. L., Kennedy, M. K., Tan, L. J., Dal Canto, M. C., Picha, K. S., \u0026amp; Miller, S. D. (1992). Induction of active and adoptive relapsing experimental autoimmune encephalomyelitis (EAE) using an encephalitogenic epitope of proteolipid protein. \u003c\/span\u003e\u003ci\u003eJournal of neuroimmunology\u003c\/i\u003e\u003cspan\u003e, \u003c\/span\u003e\u003ci\u003e38\u003c\/i\u003e\u003cspan\u003e(3), 229-240.\u003c\/span\u003e\u003c\/p\u003e","brand":"MD Bioproducts","offers":[{"title":"Default Title","offer_id":39848197619901,"sku":"301008","price":1680.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0554\/5485\/9453\/files\/Myelin_Proteolipid_Protein_PLP_139_151.png?v=1718876371"},{"product_id":"rat-igg1-isotype-control-biotin-conjugated-antibody","title":"Rat IgG1 Isotype Control, Biotin Conjugated Antibody,  0.5 mg","description":"\u003cp\u003eIsotype controls are most commonly used in flow cytometry and immunohistochemistry experiments as negative controls that measure the level of non-specific background signal caused by primary antibodies. 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