Purified recombinant Human MMP1 protein Expression System: E.coli Bioactivity: MMP-1 activity was measured by its ability to cleave a chromogenic peptide MMP-1 substrate at room temperature. At an MMP-1 concentration of 2.5 µg/mL, 50 % cleavage was achieved at an incubation time of approximately 25 minutes
Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. These enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-1 is a secreted collagenase with specificity toward Type I, II, III, VII, and X collagens. Alternative Names: Matrix metalloproteinase-1, MMP-1 protein, MMP1, Fibroblast collagenase, MMP-1, MMP-1 protein, interstitial collagenase protein, MMP 1 protein, MMP 1