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| Company | Aladdin Scientific Corporation | Aladdin Scientific Corporation | Aladdin Scientific Corporation | Aladdin Scientific Corporation | Aladdin Scientific Corporation |
| Item | α-Chymotrypsin−Agarose from bovine pancreas | Proteasome-activating peptide 1 TFA | PTHrP-(1-21)/PTH-(22-34) (human) | Recombinant Carboxypeptidase B | Recombinant Human IL-2 Receptor Alpha Protein |
| Catalog Number | C755291 | P658731 | rp174848 | R141077 | rp147480 |
| Price | Supplier Page | Supplier Page | Supplier Page | Supplier Page | Supplier Page |
| Quantity | 100U, 50U | 10mg, 5mg, 50mg, 1mg, 25mg | 500µg, 1mg | 100mg, 5mg, 50mg, 1mg, 10mg | 100µg, 10µg, 50µg, 1mg |
| Type | Proteins | Chelating Agents & Ligands | Chelating Agents & Ligands | Chelating Agents & Ligands | Chelating Agents & Ligands |
| Description | α-Chymotrypsin agarose from bovine pancreas has been used to study the purification and characterization of glucoamylase. α-Chymotrypsin agarose from bovine pancreas has also been used in a study to investigate molecular modeling for the design of a biomimetic chimeric ligand | Proteasome-activating peptide 1 TFA is a peptide and a potent proteasome activator. Proteasome-activating peptide 1 TFA increases the chymotrypsin-like proteasomal catalytic activity and, consequently, proteolytic rates both in vitro and in culture. Proteasome-activating peptide 1 TFA prevents Proteasome-activating peptide 1 TFA is a peptide and a potent proteasome activator. Proteasome-activating peptide 1 TFA increases the chymotrypsin-like proteasomal catalytic activity and, consequently, proteolytic rates both in vitro and in culture. Proteasome-activating peptide 1 TFA prevents protein aggregation in a cellular model of amyotrophic lateral sclerosis... Read More | Inquire | Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.Carboxypeptidase B is competitively inhibited by arginine and lysine. The enzyme is Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from theC-terminal end of polypeptides. The molecular weight is 34,500 daltons, 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 (EC 3.4.17.2) 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.Animal origin free:eliminate the risk of virus presence, or of 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. High purity:1) Recombinant carboxypeptidase B provides increased specific activity and eliminates contaminating protease 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... Read More | Purity>97% SDS-PAGE.FunctionReceptor for interleukin-2 |
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