MMP10 - catalytic domain, mutant with improved stability

210,00680,00

Human, recombinant
Residues 99-263, F170N mutant, UniProtKB accession P09238
MW = 18.6 kDa
EC # 3.4.24.24
CAT # G04MP10Cm

SKU: G04MP10Cm Categories: , Tags: , , , , , ,
Catalog n.QtyPrice
210,00
420,00
680,00
VAT not included

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Additional information

Qty

10 μg, 5 x 10 μg, 100 μg

Shipping in Dry Ice

yes

Description

Description
MW = 18.6 kDa calculated. 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 UniProtKB 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.
 
Sequence
       100        110        120        130        140
      M-FS SFPGMPKWRK THLTYRIVNY TPDLPRDAVD SAIEKALKVW
       150        160        170        180        190 
EEVTPLTFSR LYEGEADIMI SFAVKEHGDN YSFDGPGHSL AHAYPPGPGL
       200        210        220        230        240
YGDIHFDDDE KWTEDASGTN LFLVAAHELG HSLGLFHSAN TEALMYPLYN 
       250        260
SFTELAQFRL SQDDVNGIQS LYG
 
Purity
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight between 18.4 and 25.0 kDa.
 
Supplied as
0.2 mg/mL solution in Tris 20 mM pH 7.2, CaCl2 10 mM, ZnCl2 0.1 mM, NaCl 0.3 M, acetohydroxamic acid (AHA) 0.2 M. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 29910 M-1cm-1 calculated).
 
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.

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.

RELATED RESEARCH FIELDS

References
Bertini, I. et al. J. Mol. Biol. 336 (3), 707-716 (2004).
Bode, W. et al. Cell. Mol. Life Sci. 55 (4), 639-652 (1999).
Murphy, G. & Knäuper, V. Matrix Biol. 15 (8-9), 511-518 (1997).
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