Further Information
Interstitial Collagenase, Fibroblast Collagenase, Matrix Metalloproteinase-1, MMP-1, MMP1, CLG
This recombinant protein can be used for biological assays. For research use only.
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, alpha1 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.
Supplied as a 0.2 um filtered solution of 20mM MES, 150mM NaCl, 0.05% Brij35, pH 5.5. It is not recommended to reconstitute to a concentration less than 100 ug/ml.
C-6 His tag
4312
matrix metallopeptidase 1
MMP1
Homo sapiens
Liquid
Predicted Molecular Weight:
52.88 kD
P03956
Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test.
Recombinant Protein Sequence:
Thr32-Gly402
Human Cells
P03956
