Aggrecan 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. 

During 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.

References/Citations:

Clement-Lacroix, P., Little, C. B., Smith, M. M., Cottereaux, C., Merciris, D., Meurisse, S., ... & Amantini, D. (2022). Pharmacological characterization of GLPG1972/S201086, a potent and selective small-molecule inhibitor of ADAMTS5. Osteoarthritis and Cartilage, 30(2), 291-301.

Brebion, F., Gosmini, R., Deprez, P., Varin, M., Peixoto, C., Alvey, L., ... & 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.

Powell, A. J., Little, C. B., & 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. Arthritis & Rheumatism: Official Journal of the American College of Rheumatology, 56(9), 3010-3019.

Little, C. B., Hughes, C. E., Curtis, C. L., Janusz, M. J., Bohne, R., Wang-Weigand, S., ... & Caterson, B. (2002). Matrix metalloproteinases are involved in C-terminal and interglobular domain processing of cartilage aggrecan in late stage cartilage degradation. Matrix biology, 21(3), 271-288.

Caterson, B., Flannery, C. R., Hughes, C. E., & Little, C. B. (2000). Mechanisms involved in cartilage proteoglycan catabolism. Matrix Biology, 19(4), 333-344.