Recombinant Human ADAMTS1 Protein, CF

ADAMTS1 (a disintegrin and metalloproteinase with thrombospondin motifs 1), also known as METH1, is the founding member of the family of secreted zinc proteases with a multi-domain structure (1-3). 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. Based on their substrate specificity, ADAMTS1 and associated family members may be key enzymes in degradation of cartilage leading to inflammation and arthritis (4). It is an active protease cleaving alpha-2-macroglobulin (5), aggrecan (6), and versican (7). Compared to ADAMTS4 (aggrecanase 1) and ADAMTS5 (aggrecanase 2), the aggrecanase activity of ADAMTS1 is lower. However, its activity can be enhanced by the binding of cofactor such as fibulin-1 (8). The aggrecanase activity can be inhibited using 5 mM 1,10 Phenanthroline. ADAMTS1 is essential for normal growth and the structure and function of the kidneys, adrenal glands and female reproductive organs (9). It also plays an important role in atherosclerosis (10). It has been shown to inhibit endothelial cell proliferation by direct binding and sequestration of VEGF165 and to inhibit fibroblast migration at high concentrations by binding to FGF-2 (11, 12). The purified recombinant human ADAMTS1 starts at the N‑terminus of the catalytic domain and ends in the beginning of the spacer region.