|Place of Origin:||China, Shanghai|
|Certification:||NQA ISO 9001:2015|
|Minimum Order Quantity:||10mg|
|Packaging Details:||1mg, 10mg, 100mg, 1g; ice packaging, carton|
|Supply Ability:||1000g per week|
|Manufacturer:||YaxinBio||Product:||Recombinant Carboxypeptidase B|
|Cat. No.:||RCPB01||Source:||E. Coli|
|Purified By:||HPLC||Physical Form:||White Or White-like Lyophilized Powder|
|Product Advantage:||High Purity||Impact:||Produce Recombinant Polypeptide|
High Purity Recombinant Carboxypeptidase B,
170USP Units/Mg Pro Recombinant Carboxypeptidase B
Recombinant Carboxypeptidase B ≥170 USP units/mg pro.
Recombinant Carboxypeptidase B
Pancreatic or tissue Carboxypeptidase B (CPB), a key enzyme involved in insulin conversion and highly specific for excising C-terminal Lys and Arg residues from peptides and proteins, was expressed at high level and purified from a recombinant Pichia pastoris strain. A cDNA containing the porcine pancreatic pro-Carboxypeptidase B (proCPB) fused to the Saccharomyces cerevisiae alpha factor secretion signal was cloned into the pPIC3K vector under control of P. pastoris AOX1 promoter. After 72 h of growth on methanol, procarboxypeptidase B accumulated until 320 mg L−1, representing 70% of total proteins in culture supernatant. A single stepwise ion exchange purification process with Q-Sepharose at increasing concentrations of ammonium acetate allowed recovery of 65% procarboxypeptidase B in a single fraction. 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.
Physical form:Lyophilized from 20 mM Tris, pH 8.0 + 50 mM NaCl.
Animal origin free:YaxinBio recombinant carboxypeptidase B belongs to the AOF level 3, eliminate the risk of virus presence, or any other potential adventitious agents found in animal-derived carboxypeptitase B
Stability:A sterile recombinant carboxypeptidase B lyophilized eliminates the risk of contamination and decreases the chances of activity loss in the process of transport and storage.
1) Recombinant carboxypeptidase B provides increased specific activity and eliminates contaminating proteases activities found in extracted enzymes with lower purity level.
2) No other contaminating proteases such as chymotrypsin and carboxypeptidase A.
3) Less than 10ppm of recombinant trypsin.
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.
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
Physical Form Lyophilized Powder
Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Carboxypeptidase-B sequentially cleaves C terminal K and R residues. Recombinant rat Carboxypeptidase-B is a 35.1 kDa protein consisting of 307 amino acids.
Contact Person: Miss Eland