Additional information
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MMP13 - catalytic domain, mutant with improved stability
210,00€ – 680,00€
Human, recombinant
Residues 104-268, F175D mutant, UniProtKB accession P45452
MW = 18.6 kDa
EC # 3.4.24.24
CAT # G04MP13Cm
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Description
Description
MW = 18.6 kDa calculated. Recombinant Matrix Metalloproteinase-13 (MMP-13, Collagenase-3, Col3) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-13 (residues 104-268, UniProtKB accession P45452). This product is derived from MMP-13 catalytic domain and contains also the mutation F175D to increase its stability.
MW = 18.6 kDa calculated. Recombinant Matrix Metalloproteinase-13 (MMP-13, Collagenase-3, Col3) cloned from human cDNA, expressed in E. coli. The enzyme consists of the catalytic domain of human MMP-13 (residues 104-268, UniProtKB accession P45452). This product is derived from MMP-13 catalytic domain and contains also the mutation F175D to increase its stability.
Sequence
110 120 130 140 150
YNVFPRT LKWSKMNLTY RIVNYTPDMT HSEVEKAFKK AFKVWSDVTP
160 170 180 190 200
LNFTRLHDGI ADIMISFGIK EHGDDYPFDG PSGLLAHAFP PGPNYGGDAH
210 220 230 240 250
FDDDETWTSS SKGYNLFLVA AHEFGHSLGL DHSKDPGALM FPIYTYTGKS
260
HFMLPDDDVQ GIQSLYGP
Available mutants
F171D, E223A – inactive mutant with improved stability – CAT # G04MP13Ci
F171D, E223A – inactive mutant with improved stability – CAT # G04MP13Ci
Purity
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight of about 18.4 kDa.
> 95% by SDS-PAGE. The protein is observed, in denaturing conditions, as a single band migrating at a molecular weight of about 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) 0.5 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) 0.5 M. The concentration is calculated by the analysis of the absorbance at 280 nm (ε280 = 29910 M-1cm-1 calculated).
Specific activity
> 100 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.
> 100 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.
RELATED RESEARCH FIELDS
- Biomaterials
- Cancer
- breast cancer
- lung cancer
- prostate cancer
- Dental diseases
- periodontitis
- Diabetes Mellitus
- Neurodegenerative disease
- Alzheimer’s disease
- Osteoarthritis
References
V. Knäuper et al. J. Biol. Chem. 1997, 272, 7608.
F.J.Moy et al. J Mol Biol. 2000 Sep 22; 302(3):671-89.
S. Cowell et al. Biochem. J. 1998, 331, 453.
G. Murphy and V. Knäuper Matrix Biol. 1997, 15, 51.
F.J.Moy et al. J Mol Biol. 2000 Sep 22; 302(3):671-89.
S. Cowell et al. Biochem. J. 1998, 331, 453.
G. Murphy and V. Knäuper Matrix Biol. 1997, 15, 51.