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| Introduction | 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. |
| Synonyms | Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7. |
| Source | Escherichia Coli. |
| Physical Appearance | Sterile clear liquid solution. |
| Formulation | The protein contains the following additives 10mM HEPES (pH 7.4), 5mM CaCl2 and 150mM NaCl. |
| Stability | Matrilysin althoµgh stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. |
| Purity | Greater than 95.0% as determined by(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE. |
| Biological Activity | The specific activity was found to be 6,900 U/mg. |
| Usage | NeoScientific's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drµgs, agricultural or pesticidal products, food additives or household chemicals. |
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