MMP12 catalytic domain, mutant with improved stability

Human, recombinant.
residues 106-263, swissprot accession P39900
MW = 17600 Da.
EC #
CAT # G04MP12Cm

Packaging and prices - Technical Details - References

Packaging and Prices

Unlabeled Protein
Catalog n° Labeling Q.ty Price (€)
G04MP12Cm none 10 µg 200.00
G04MP12Cm none 5 x 10 µg 400.00

Special prices for bulk quantities, or labelled samples, available upon request.

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MW = 17.6 kDa. Recombinant matrix metalloproteinase-12 (MMP-12, metalloelastase, macrophage elastase) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-12 (residues 106-263 swissprot accession P39900) with the mutation F171D. The protein has been mutated to increase its stability, as the mutation drastically reduces the enzyme’s rate of autoproteolysis. The catalytic activity rates are not affected by the mutation.

> 95% by SDS-PAGE. The enzyme was observed as a single band migrating at a molecular weight of between 19.5 and 14.4 kDa.

Specific activity
> 40U/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.

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

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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.

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