Description
MW = 19.5 kDa calculated. Recombinant Matrix Metalloproteinase-3 (MMP-3, Stromelysin-1, Transin) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-3 (residues 100-272, UniProtKB accession P08254).

Sequence

                                        100        110        120
                                        M-F RTFPGIPKWR KTHLTYRIVN
       130        140        150        160        170        180
YTPDLPKDAV DSAVEKALKV WEEVTPLTFS RLYEGEADIM ISFAVREHGD FYPFDGPGNV
       190        200        210        220        230        240
LAHAYAPGPG INGDAHFDDD EQWTKDTTGT NLFLVAAHEI GHSLGLFHSA NTEALMYPLY
       250        260        270
HSLTDLTRFR LSQDDINGIQ SLYGPPPDSP ET

Available mutants
F171D – mutant with improved stability – CAT # G04MP03Cm
F171D, E219A – inactive mutant with improved stability – CAT # G04MP03Ci

Purity
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight between 18.4 and 25.0 kDa.

Suppied As
0.2 mg/mL solution in Tris 20 mM, pH 7.2, CaCl2 10 mM, ZnCl2 0.1 mM, NaCl 0.3 M, acetohydroxamic acid (AHA) 0.2 M. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 28420 M-1cm-1 calculated).

Specific activity
> 30U/μg. Activity described as U=100 pmol/min at 37°C using a colorimetric ***** with thiopeptolide 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.