MMP20 - catalytic domain

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.

       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, 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 = 28420 M^-1cm^-1 calculated).

Specific activity
> 50 U/μg. Activity described as U = 100 pmol/min at 25°C using a colorimetric assay 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.

Usage
Enzyme kinetic studies, cleavage of target substrates and screening of inhibitors.

RELATED RESEARCH FIELDS

• Cancer
  • Lung cancer
• Dental diseases
  • • Amelogenesis Imperfecta
• Osteoarthritis

Arendt, Y., et al. FEBS Lett. 2007 Oct 2;581(24):4723-6. Epub 2007 Sep 6.
Yamakoshi, Y., et al. J Biol Chem. 2006 Dec 15;281(50):38235-43. Epub 2006 Oct 17.