MMP20 catalytic domain

Human, recombinant.
residues 113-271, swissprot accession O60882
MW = 17500 Da.
EC # 3.4.24.-
CAT # G04MP20C

Packaging and prices - Technical Details - References

Packaging and Prices

Unlabeled Protein
Catalog n° Labeling Q.ty Price (€)
G04MP20C none 10 µg 200.00
G04MP20C none 5 x 10 µg 400.00

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

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MW = 17.5 kDa. Matrix Metalloproteinase-20 (MMP-20, Enamelysin, enamel metalloproteinase) catalytic domain cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-20 (residues 113-271). Residues numbers are based on the unprocessed precursor). Swiss prot. accession: O60882.

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

Specific activity
> 50U/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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Arendt, Y., et al. FEBS Lett. 2007 Oct 2;581(24):4723-6. Epub 2007 Sep 6.
Yamakoshi, Y., et al. J Biol Chem. 2006 Dec 15;281(50):38235-43. Epub 2006 Oct 17.

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