MMP 7 Human, Active

Matrix Metalloproteinase-7 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing having a molecular mass of 19.13 kDa.The MMP-7 is purified by proprietary chromatographic techniques.

Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.

The specific activity was found to be 6,200 U/mg.

Western Blotting (1:1K-5K for neat serum and 1-10 ug/ml for affinity pure antibody using ECL technique). ELISA: Control peptide can be used to coat ELISA plates at 1 ug/ml and detected with antibodies (1:10-50K for neat serum and 0.5-1 ug/ml for affinity pure).Histochemistry & Immunofluorescence: Not tested.

Matrilysin although stable at 4°C for 3 weeks, should be stored below -18°C . Please prevent freeze-thaw cycles.