Recombinant Human Matrix Metalloproteinase-1/MMP-1 (C-6His)

Source: Human Cells. MW :52.88kD. Recombinant Human Matrix Metalloproteinase-1 is produced by our Mammalian expression system and the target gene encoding Phe20-Asn469 is expressed with a 6His tag at the C-terminus. Matrix Metalloproteinase-1 (MMP-1) is expressed by fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 contains several distinct domains: a prodomain that is cleaved upon activation, a catalytic domain containing the zinc binding site, a short hinge region, and a carboxyl terminal (hemopexin like) domain. MMP-1 can degrade a broad range of substrates including types I, II, III, VII, VIII, and X collagens as well as casein, gelatin, a1 antitrypsin, myelin basic protein, L-Selectin, pro-TNF, IL1, IGFBP3, IGFBP5, pro-MMP2, and pro-MMP9. A significant role of MMP1 is the degradation of fibrillar collagens in extracellular matrix remodeling, characterized by the cleavage of the interstitial collagen triple helix into 3/4, 1/4 fragments. MMP1 may also be involved in enzyme cascades, cytokine regulation and cell surface molecule modulation.