Description
Description
MW = 20.0 kDa calculated. Recombinant Matrix Metalloproteinase-14 (MMP-14, Membrane-Type Matrix Metalloproteinase1, MT1- MMP) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-14 (residues 114-290, UniProtKB accession P50281). The protein has the mutation C127S to increase its stability. The catalytic activity rates are not affected by the mutation.
Sequence
120 130 140 150 160
IQGLKWQ HNEITFSIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR
170 180 190 200 210
EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA HAYFPGPNIG
220 230 240 250 260
GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS SDPSAIMAPF
270 280 290
YQWMDTENFV LPDDDRRGIQ QLYGGESGFP
Purity
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight between 18.8 and 25.0 kDa.
Supplied as
0.2 mg/mL solution in Tris 20 mM pH 7.2, CaCl
2 10 mM, ZnCl
2 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 (ε
280 = 33920 M
-1cm
-1 calculated).
Specific activity
> 150 U/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.
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