MMP12 - catalytic domain

Description
MW = 17.6 kDa calculated. Recombinant Matrix Metalloproteinase-12 (MMP-12, Metalloelastase, Macrophage elastase) cloned from human cDNA, expressed in E. coli. The enzyme consists of the wild type catalytic domain of human MMP-12 (residues 106-263, UniProtKB accession P39900).

       110        120        130        140        150
   M-GPVWR KHYITYRINN YTPDMNREDV DYAIRKAFQV WSNVTPLKFS
       160        170        180        190        200 
KINTGMADIL VVFARGAHGD FHAFDGKGGI LAHAFGPGSG IGGDAHFDED
       210        210        220        230        240
EFWTTHSGGT NLFLTAVHEI GHSLGLGHSS DPKAVMFPTY KYVDINTFRL
       250 
SADDIRGIQS LYG

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
0.2 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 = 26930 M^-1cm^-1 calculated).

Specific activity
> 40 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.

RELEATED RESEARCH FIELDS

• Cancer
  • Lung cancer
• Cardiovascular disorders
  • Aneurysm formation
  • Coronary artery disease
  • Myocardial infarction
• Neurodegenerative disease
  • Alzheimer’s disease
  • Multiple sclerosis

I. Bertini, et al. Proc Natl Acad Sci U S A. 2005 Apr 12; 102(15):5334-9.
S.D. Shapiro. Curr. Opin. Cell Biol. 1998, 10, 602.
S.D. Shapiro et al. J. Biol. Chem. 1993, 268, 23824.
A. Belaaouaj et al. J. Biol. Chem. 1995, 270, 14568.