Additional information
| Qty | 10 μg, 5 x 10 μg, 100 μg |
|---|---|
| Shipping in Dry Ice | yes |
MMP10 - catalytic domain, mutant with improved stability
210,00€ – 680,00€
Human, recombinant
Residues 99-263, F170N mutant, UniProtKB accession P09238
MW = 18.6 kDa
EC # 3.4.24.24
CAT # G04MP10Cm
| Catalog n. | Qty | Price |
|---|---|---|
| 210,00€ | ||
| 420,00€ | ||
| 680,00€ | ||
| VAT not included | ||
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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.
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.
> 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).
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.
> 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
- Dental diseases
- caries
- Neurodegenerative disease
- Huntington disease
- Wound healing
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).
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).