ADAMTS5 (a disintegrin and metalloproteinase with thrombospondin motifs 5), also known as Aggrecanase-2 and ADAMTS11, is a member of the family of secreted zinc proteases with a multi-domain structure (1, 2). The protein precursors consist of signal peptide and following domains: pro, catalytic, disintegrin-like, TS type 1 motif, cysteine-rich, spacer and a variable number of TS type 1 motifs. ADAMTS5 is an active protease effectively cleaving alpha 2-Macroglobulin (3), Aggrecan (4), and Brevican (5), and is inhibited by TIMP-3 with inhibition constants in the subnanomolar range (6). Based on the murine model studies (7, 8), this protease may be a key enzyme in the degradation of cartilage leading to osteoarthritis and rheumatoid arthritis. The purified recombinant human (rh) ADAMTS5 starts at the N-terminus of the catalytic domain and ends at the C-terminus of the TSP-1 domain. The amino acid sequence of rhADAMTS5 is 98%, 97%, and 96% identical to that of canine, bovine, and mouse/rat. The aggrecanase activity can be inhibited by 5 mM 1,10-phenanthroline and rhTIMP-3 (R&D Systems, Catalog # 973-TM).
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| Product By Gene ID | 11096 |
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