Additional information
| Qty | 10 μg, 5 x 10 μg, 100 μg |
|---|---|
| Shipping in Dry Ice | yes |
MMP14 - catalytic domain, mutant with improved stability
210,00€ – 680,00€
Human, recombinant
Residues 114-290, C127S mutant, UniProtKB accession P50281
MW = 20.1 kDa.
EC # 3.4.24.80
CAT # G04MP14Cm
| Catalog n. | Qty | Price |
|---|---|---|
| 210,00€ | ||
| 420,00€ | ||
| 680,00€ | ||
| VAT not included | ||
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Description
Description
MW = 20.0 kDa calculated. Recombinant Matrix Metalloproteinase-14 (MMP-14, Membrane-Type Matrix Metalloproteinase1, MT1- MMP) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-14 (residues 114-290, UniProtKB accession P50281). The protein has the mutation C127S to increase its stability. The catalytic activity rates are not affected by the mutation.
MW = 20.0 kDa calculated. Recombinant Matrix Metalloproteinase-14 (MMP-14, Membrane-Type Matrix Metalloproteinase1, MT1- MMP) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-14 (residues 114-290, UniProtKB accession P50281). The protein has the mutation C127S to increase its stability. The catalytic activity rates are not affected by the mutation.
Sequence
120 130 140 150 160
IQGLKWQ HNEITFSIQN YTPKVGEYAT YEAIRKAFRV WESATPLRFR
170 180 190 200 210
EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA HAYFPGPNIG
220 230 240 250 260
GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS SDPSAIMAPF
270 280 290
YQWMDTENFV LPDDDRRGIQ QLYGGESGFP
Purity
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight between 18.8 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 18.8 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) 0.5 M. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 33920 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) 0.5 M. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 33920 M-1cm-1 calculated).
Specific activity
> 150 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.
Releated researh fields
- Cancer
- Pancreatic cancer
- Cardiovascular disorders
- Aneurysm formation
- Coronary artery disease
- Myocardial infarction
- Dental diseases
- Periodontitis
- Neurodegenerative disease
- Huntington disease
- Pathogenesis of pterygium, a benign ocular tumor
- Renal pathologies
- Chronic allograft nephropathy
- Diabetic nephropathy
- Glomerulosclerosis/tubulointerstitial fibrosis
- Polycystic kidney disease
- Renal cell carcinoma
References
M. Gioia et al. J Mol Biol. 2007 May 11;368(4):1101-13.
K. Lehti et al. J. Biol. Chem. 2000, 275:15006-13.
G. Murphy and V. Knäuper Matrix Biol. 1997, 15, 511.
W. Bode et al. Cell Mol Life Sci 1999, 55:639-52.
K. Lehti et al. J. Biol. Chem. 2000, 275:15006-13.
G. Murphy and V. Knäuper Matrix Biol. 1997, 15, 511.
W. Bode et al. Cell Mol Life Sci 1999, 55:639-52.