ProteoSure™ Recombinant Carboxypeptidase B, Sequencing Grade
Ultra pure Carboxypeptidase B contains high specific enzymatic activity. Suitable for protein structure research, sequencing analysis, and antibody quality control. ... Read more
Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from the C-terminal end of polypeptides. The molecular weight is 34,500 daltons, optimum pH 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 used during the manufacturing process.
- Protein structure and sequence analysis, such as hydrolyze basic amino acids lysine, arginine and histidine from the C-terminal of polypeptides.
- Antibody quality control.
Prepare 1-10mg/mL carboxypeptidase B with sterile water or 25 mM Tris-HCl pH 7.5. The recommended ratio to the sample protein is 1:50 to 1:1000 (w/w), the optimum pH is pH 7 - 9.
Storage and stability
|Enzyme Commission #||184.108.40.206|
|Molecular weight||34.5 kDa|
||≥200 units/mg protein|
|Unit definition||One Unit of carboxypeptidase B activity hydrolyzes one micromole of hippuryl-L-arginine per minute at 25°C, pH 7.65.|
||No trypsin, chymotrypsin, carboxypeptidase A, or other protease contaminants.|
|Storage||Store in a sealed container at 2 - 8°C. Once reconstituted, it should be aliquoted and stored at -20°C. The product is stable for 24 months with no detectable loss of enzymatic activity after 10 repeated freeze-and-thaw cycles.|
|Intended use||For research only. Not intended for any human or animal diagnostic or therapeutic use.|
Product Information Sheet
🗎 Recombinant Rat Carboxypeptidase B, Sequencing Grade
Marvelgent Biosciences Inc.
116 Will Drive, Canton, MA 02021, USA
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