MMP20 - catalytic domain

200,00400,00

Human, recombinant
Residues 113-271, UniProtKB accession O60882
MW = 17.5 kDa
EC # 3.4.24.-
CAT # G04MP20C

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SKU: G04MP20C Categories: , Tags: , , , , ,
Catalog n.QtyPrice
200,00
400,00
VAT not included

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Description

Description
MW = 17.5 kDa calculated. 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). UniProtKB accession O60882.
 
Sequence
       120        130        140        150        160
M-GEPKWKKN TLTYRISKYT PSMSSVEVDK AVEMALQAWS SAVPLSFVRI 
       170        180        190        200        210
NSGEADIMIS FENGDHGDSY PFDGPRGTLA HAFAPGEGLG GDTHFDNAEK
       220        230        240        250        260
WTMGTNGFNL FTVAAHEFGH ALGLAHSTDP SALMYPTYKY KNPYGFHLPK
       270
DDVKGIQALY G
 
Purity
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight between 14.4 and 18.4 kDa.
 
Supplied as
0.1 mg/mL solution in Tris 20 mM pH 7.2, CaCl2 10 mM, ZnCl2 0.1 mM, NaCl 0.3 M, acetohydroxamic acid (AHA) 0.5 M. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 28420 M-1cm-1 calculated).

Specific activity
> 50 U/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.

Storage
-80°C. After initial defrost, aliquot the product into individual tubes and refreeze at -80°C.
Avoid repeated freeze/thaw cycles.

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

References
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.

Additional information

Qty

10 μg, 5 x 10 μg

Shipping in Dry Ice

yes

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