|Place of Origin:||China|
|Certification:||ISO 9001 2015|
|Minimum Order Quantity:||100ug|
|Packaging Details:||ice packaging|
|Supply Ability:||1000 per week|
|Product:||Sequencing Grade Carboxypeptidase B||Manufacturer:||YaxinBio|
|Source:||E. Coli||Specific Activity:||NLT 200 Units/mg Pro|
|Contaminant Activity:||No Trypsin, Chymotrypsin, Carboxypeptidase A, Or Other Proteases Contaminant.||RELATED PRODUCT:||Sequencing Grade Chymotrypsin|
Carboxypeptidase B Proteomics Grade Producing Recombinant Insulin
Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from the C-terminal end of polypeptides. The molecular weight is 33.8kD, the pH optimum is 8.0, and pI is 6.0. Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is also inhibited by metal chelating agents, e.g., EDTA. Recombinant Carboxypeptidase B is expressed in E.Coli and purified by high pressure liquid chromatography. There is no trace of other enzyme (such as carboxypeptidase A and chymotrypsin) activity. No protease inhibitors such as PMSF are present in the preparation.
|Source||Recombinant E. coli|
|Appearance||White or off white, or yellowish powder|
|Specific activity||≥170 units/mg pro|
|Purity(SDS-PAGE)||Single major band|
|Molecular Weight(SDS-PAGE)||33.8±3.4 kDa|
UNIT DEFINITION:One unit of carboxypeptidase B activity hydrolyzes one micromole ofhippuryl-L-arginine per minute at 25℃, pH 7.65.
Prepare 1-10mg/ml recombinant carboxypeptidase B with sterile water or 25mM Tris-HCl pH 7.65. The ratio to aimed protein is 1:50 to 1:1000 (w/w), the optimum pH is pH 7.5-9.0.
Prepare 1-10mg/ml carboxypeptidase B with sterile water or 25mM Tris-HCl pH 7.65. The ratio to aimed protein is 1:50 to 1:1000 (w/w), the optimum pH is pH 7-9.
Recommend recombinant carboxypeptidase B lyophilized should be stored under 2-8℃ in sealed container. It is stable within 24 months.After dissolved, it should be stored under -20℃, It is stable within 24 months and no activity lose after 10 times repeated freezing and thawing.
Contact Person: Miss Eland