Description
Description
MW = 17.5 kDa calculated. Matrix Metalloproteinase-20 (MMP-20, Enamelysin, Enamel metalloproteinase) catalytic domain cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-20 (residues 113-271). Residues numbers are based on the unprocessed precursor). UniProtKB accession O60882.
Sequence
120 130 140 150 160
M-GEPKWKKN TLTYRISKYT PSMSSVEVDK AVEMALQAWS SAVPLSFVRI
170 180 190 200 210
NSGEADIMIS FENGDHGDSY PFDGPRGTLA HAFAPGEGLG GDTHFDNAEK
220 230 240 250 260
WTMGTNGFNL FTVAAHEFGH ALGLAHSTDP SALMYPTYKY KNPYGFHLPK
270
DDVKGIQALY G
Purity
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight between 14.4 and 18.4 kDa.
Supplied as
0.1 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 = 28420 M
-1cm
-1 calculated).
Specific activity
> 50 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.