MMP10 catalytic domain, mutant with improved stability

Human, recombinant.
residues 99-263, swissprot accession P09238
MW = 18500 Da.
EC #
CAT # G04MP10Cm

Packaging and prices - Technical Details - References

Packaging and Prices

Unlabeled Protein
Catalog n° Labeling Q.ty Price (€)
G04MP10Cm none 10 µg 200.00
G04MP10Cm none 5 x 10 µg 400.00

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

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MW = 18.5 kDa. Recombinant matrix metalloproteinase-10 (MMP-10, stromelysin-2, transin 2) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-10 (residues 99-263 swissprot accession P09238) with the mutation F170N. 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 < 20 kDa.

Specific activity
> 10U/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. J. Mol. Biol. (2004) 336, 707–716.
G. Murphy and V. Knäuper. Matrix Biol. 1997, 15, 511.
W. Bode et al. Cell. Mol. Life Sci. 1999, 55, 639.
V. Knäuper et al. J. Biol. Chem. 1997, 272, 7608.

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