Recombinant Human Matrix Metal

Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7.

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.

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

Escherichia Coli.

Sterile clear liquid solution.

The protein contains the following additives 10mM HEPES (pH 7.4), 5mM CaCl2 and 150mM NaCl.

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

The specific activity was found to be 9,100 U/mg.

One unit is defined as the digestion of 1 µg Azocoll/min at 37°C.