Additional information
| Qty | 10 μg, 5 x 10 μg, 100 μg |
|---|---|
| Shipping in Dry Ice | yes |
MMP12 - catalytic domain, inactive mutant
210,00€ – 680,00€
Human, recombinant
Residues 106-263, UniProtKB accession P39900
MW = 17.6 kDa
EC # 3.4.24.65
CAT # G04MP12Ci
| Catalog n. | Qty | Price |
|---|---|---|
| 210,00€ | ||
| 420,00€ | ||
| 680,00€ | ||
| VAT not included | ||
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Description
Description
MW = 17.6 kDa. Recombinant matrix metalloproteinase-12 (MMP-12, metalloelastase, macrophage elastase) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-12 (residues 106-263, UniProtKB accession P39900).The enzyme has been inactivated by mutagenesis (E219A). This product is derived from MMP-12 Catalytic domain and contain also the mutation F171D to increase its stability. No residual enzyme activity has been detected using the method described in the specific activity section of this data sheet.
MW = 17.6 kDa. Recombinant matrix metalloproteinase-12 (MMP-12, metalloelastase, macrophage elastase) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-12 (residues 106-263, UniProtKB accession P39900).The enzyme has been inactivated by mutagenesis (E219A). This product is derived from MMP-12 Catalytic domain and contain also the mutation F171D to increase its stability. No residual enzyme activity has been detected using the method described in the specific activity section of this data sheet.
Sequence
110 120 130 140 150
M-GPVWR KHYITYRINN YTPDMNREDV DYAIRKAFQV WSNVTPLKFS
160 170 180 190 200
KINTGMADIL VVFARGAHGD DHAFDGKGGI LAHAFGPGSG IGGDAHFDED
210 220 230 240 250
EFWTTHSGGT NLFLTAVHEI GHSLGLGHSS DPKAVMFPTY KYVDINTFRL
260
SADDIRGIQS LYG
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.
> 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
0.2 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 = 26930 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 = 26930 M-1cm-1 calculated).
Specific activity
Not detected. 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.
Not detected. 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.
RELEATED RESEARCH FIELDS
- Cancer
- Lung cancer
- Cardiovascular disorders
- Aneurysm formation
- Coronary artery disease
- Myocardial infarction
- Neurodegenerative disease
- Alzheimer’s disease
- Multiple sclerosis
References
I. Bertini, et al. Proc Natl Acad Sci U S A. 2005 Apr 12; 102(15):5334-9.
S.D. Shapiro. Curr. Opin. Cell Biol. 1998, 10, 602.
S.D. Shapiro et al. J. Biol. Chem. 1993, 268, 23824.
A. Belaaouaj et al. J. Biol. Chem. 1995, 270, 14568.
S.D. Shapiro. Curr. Opin. Cell Biol. 1998, 10, 602.
S.D. Shapiro et al. J. Biol. Chem. 1993, 268, 23824.
A. Belaaouaj et al. J. Biol. Chem. 1995, 270, 14568.