nterstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, MMP1, CLG, CLGN.

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, IGFBP-3, IGFBP-5, casein, gelatin, 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.

MMP1 (24-207) Human Recombinant is a single, glycosylated polypeptide chain containing 190 amino acids and having a molecular mass of 21.2kDa. MMP1 (24-207) is fused to a 6 a.a C-terminal His tag.

HEK293 Cells.

MMP1 (24-207) filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS, pH7.5 and 5% (w/v) Threalose.

It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.

Greater than 95.0% as determined by SDS-PAGE.

CTCVPPHPQT AFCNSDLVIR AKFVGTPEVN QTTLYQRYEI KMTKMYKGFQ ALGDAADIRF VYTPAMESVC GYFHRSHNRS EEFLIAGKLQ DGLLHITTCS FVAPWNSLSL AQRRGFTKTY TVGCEECTVF PCLSIPCKLQ SGTHCLWTDQ LLQGSEKGFQ SRHLACLPRE PGLCTWQSLR SQIAHHHHHH.

SDS

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