MMP 7 Human
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| Amount : | 20 µg |
| Purification : | Greater than 90% as determined by SDS-PAGE. |
| Content : | MMP7 protein solution (1mg/ml) containing 20mM Tris 8.0 and 10% glycerol. |
| Storage condition : | Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. |
| AA sequence : | MYSLFPNSPK WTSKVVTYRI VSYTRDLPHI TVDRLVSKAL NMWGKEIPLH FRKVVWGTAD IMIGFARGAH GDSYPFDGPG NTLAHAFAPG TGLGGDAHFD EDERWTDGSS LGINFLYAAT HELGHSLGMG HSSDPNAVMY PTYGNGDPQN FKLSQDDIKG IQKLYGKRSN SRKK. |
| Alternative Name : | Matrilysin, EC 3.4.24.23, Pump-1 protease, Uterine metalloproteinase, Matrix metalloproteinase-7, MMP-7, Matrin, MPSL1, PUMP-1, MMP7. |
Source: Escherichia Coli.
Sterile Filtered colorless solution.
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.
MMP-7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (95-267 a.a) and having a molecular mass of 19.2kDa.MMP7 is purified by proprietary chromatographic techniques.
Sterile Filtered colorless solution.
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.
MMP-7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 174 amino acids (95-267 a.a) and having a molecular mass of 19.2kDa.MMP7 is purified by proprietary chromatographic techniques.
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