Additional information
| Qty | 10 μg, 5 x 10 μg, 100 μg |
|---|---|
| Shipping in Dry Ice | yes |
MMP13 - catalytic domain, inactive mutant
210,00€ – 680,00€
Human, recombinant.
Residues 104-268, F175D mutant, UniProtKB accession P45452
MW = 18.6 kDa.
EC # 3.4.24.24
CAT # G04MP13Ci
| Catalog n. | Qty | Price |
|---|---|---|
| 210,00€ | ||
| 420,00€ | ||
| 680,00€ | ||
| VAT not included | ||
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Description
Description
MW = 18.6 kDa. 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). The enzyme has been inactivated by mutagenesis (E223A). This product is derived from MMP-13 Catalytic domain and contain also the mutation F175D 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 = 18.6 kDa. 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). The enzyme has been inactivated by mutagenesis (E223A). This product is derived from MMP-13 Catalytic domain and contain also the mutation F175D 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
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
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
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, and screening of inhibitors.
RELATED RESEARCH FIELDS
- Biomaterials
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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.