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MMP13 - catalytic domain, inactive mutant
货号：G04MP13Ci
品牌：Giotto Biotech
规格：10 μg
目录价：询价
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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.
 
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.
 
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).
 
Specific activity
Not detected. Activity described as U=100 pmol/min at 25°C using a colorimetric ***** 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.