MMP12 catalytic domain, inactive mutant

Human, recombinant.
residues 106-263, swissprot accession P39900
MW = 17600 Da.
EC #
CAT # G04MP12Ci

Packaging and prices - Technical Details - References

Packaging and Prices

Unlabeled Protein
Catalog n° Labeling Q.ty Price (€)
G04MP12Ci none 10 µg 200.00
G04MP12Ci 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).The enzyme has been inactivated by mutagenesis (E219A). This product is derived from MMP-12 Catalytic domain and contain also the mutation F171D to increase its stability and solubility. No residual enzyme activity has been detected using the method described in the specific activity section of this data sheet.

> 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
Not detected. 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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