MMP1 HEK

ENZYMES

Recombinant Human Matrix Metalloproteinase-1, HEK

MMP-1 (interstitial collagenase) can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1, IGFBP-3, IGFBP-5, casein, gelatin, 1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

The activity was measured by its ability to cleave a fluorogenic peptide substrate Mca-KPLGL-Dpa-AR-NH2. The specific activity is 400 pmoles/min/ug.