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GiottoBiotech/MMP10 - catalytic domain, mutant with improved stability/10 μg/G04MP10Cm

Additional information

Qty

10 μg, 5 x 10 μg

Shipping in Dry Ice

yes

Description

DescriptionMW = 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
 100110120130140M-FS SFPGMPKWRK THLTYRIVNY TPDLPRDAVD SAIEKALKVW 150160170180190 EEVTPLTFSR LYEGEADIMI SFAVKEHGDN YSFDGPGHSL AHAYPPGPGL 200210220230240YGDIHFDDDE KWTEDASGTN LFLVAAHELG HSLGLFHSAN TEALMYPLYN250260SFTELAQFRL 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 as0.2 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.

UsageEnzyme kinetic studies, cleavage of target substrates and screening of inhibitors.

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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