Recombinant Human MMP1 Protein (His Tag)

C-His

Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.

56 kDa

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, α1 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.

< 1.0 EU per μg of the protein as determined by the LAL method.

Supplied as a 0.2 μm filtered solution of 20mM MES, 150mM NaCl, 2mM CaCl₂, 1mM DTT, 0.05%Brij35, 10% Glycerol, pH 5.0.