Description
MW = 19.3 kDa calculated. Recombinant Matrix Metalloproteinase-7 (MMP-7, Matrilysin, Uterine metalloproteinase) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-7 (residues 95-267, UniProtKB accession P09237).

 100        110        120        130        140  M-YSLFPN SPKWTSKVVT YRIVSYTRDL PHITVDRLVS KALNMWGKEI  150        160        170        180        190  PLHFRKVVWG TADIMIGFAR GAHGDSYPFD GPGNTLAHAF APGTGLGGDA 
       200        210        220        230        240
HFDEDERWTD GSSLGINFLY AATHELGHSL GMGHSSDPNA VMYPTYGNGD 
       250        260
PQNFKLSQDD IKGIQKLYGK RSNSRKK

Purity
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight between 18.8 kDa and 25.0 kDa.

Supplied As
0.1 mg/mL solution in Tris 20 mM pH 7.2, CaCl2 10 mM, ZnCl2 0.1 mM, NaCl 0.3 M, acetohydroxamic acid (AHA) 0.5 M. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 33920 M-1cm-1 calculated).

Specific activity
> 8U/μg. Activity described as U=100 pmol/min at 25°C using a colorimetric ***** with thiopeptide Ac-Pro-Leu-Gly-[2- mercapto-4-methyl-pentanoyl]-Leu-Gly-OC2H5 (Biomol) as substrate.

Storage
-80°C. After initial defrost, aliquot the product into individual tubes and refreeze at -80°C.
Avoid repeated freeze/thaw cycles.