≥90% by SDS-PAGE
56
Matrix metalloproteinases (MMP’s) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-1 (collagenase-1) is involved in tumor development and metastasis and rheumatoid arthritis. It is proposed as a therapeutic target for these diseases. Native pro-MMP-1 is prepared from culture medium of human rheumatoid synovial fibroblasts. MMP-1 is secreted as pro-enzyme, which consists of a propeptide of 80 amino acids, a catalytic domain of 162 amino acids, a 16-residue linker region, and a hemopexin domain of 189 amino acids. The native pro-MMP-1 has a major Mr 52-kDa unglycosylated and a minor Mr 57-kDa glycosylated form. The proteolytic activation of the 57/52-kDa species will form 47/42-kDa active collagenase, and a 22-kDa C-terminal fragment
-78°C