|Place of Origin:||China, Shanghai|
|Certification:||NSF ISO 9001:2015|
|Minimum Order Quantity:||1mg|
|Packaging Details:||ice packaging, carton|
|Supply Ability:||1000g per week|
|Source:||E. Coli||Purified By:||HPLC|
|Physical Form:||Lyophilized Powder||Specific Activity:||NLT 200 Units/mg Pro|
|Contaminant Activity:||No Trypsin, Chymotrypsin, Carboxypeptidase A, Or Other Proteases Contaminant.||Cas:||9025-24-5|
sequencing grade modified trypsin,
Carboxypeptidase B, Sequencing Grade, For Mass Spectrometry Analysising lysine Peak Antibody
Recombinant Carboxypeptidase B
Source:Rat carboxypeptidase B, expressed in E. Coli.
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.
Protein structure and sequence analysis, such as hydrolyze basic amino acids lysine, arginine and histidine from the C-terminal end of polypeptides.
Antibody quality control.
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