MMP3 catalytic domain, mutant with improved stability

Human, recombinant.
residues 105-265, swissprot accession P08254
MW = 18000 Da.
EC #
CAT # G04MP03Cm

Packaging and prices - Technical Details - References

Packaging and Prices

Unlabeled Protein
Catalog n° Labeling Q.ty Price (€)
G04MP03Cm none 10 µg 200.00
G04MP03Cm none 5 x 10 µg 400.00

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

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MW = 18 kDa. Recombinant matrix metalloproteinase-3 (MMP-3, stromelysin-1, transin) cloned from human cDNA, expressed in E.coli. The enzyme consists of the catalytic domain of human MMP-3, residues 105-265 (swissprot accession P08254) 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 protein was observed as a single band migrating at a molecular weight between 19.5 and 14.4 kDa.

Specific activity
> 30U/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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L.A. Alcaraz et al. J Biol Inorg Chem. 2007, 12, 1197.
L.L. Johnson et al. J. Biol. Chem. 2000, 275, 11026.
L. Chen et al. J. Mol. Biol. 1999, 293, 545-557.

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