Human MMP-1 - 100 µL

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

The apparent Mr on SDS-PAGE is approximately 56kDa/52 kDa. The pro-MMP-1 can be fully activated by incubating with 1 mM APMA at 37°C for 3 hr. Its activity can be measured by FRET peptides. 10-20 ng of enzyme is sufficient for FRET-based assay

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