| Description | KCNRG Human Pre-designed siRNA Set A contains three designed siRNAs for KCNRG gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components KCNRG siRNA-1: 5 nmol (HPLC) KCNRG siRNA-2: 5 nmol (HPLC) KCNRG siRNA-3: 5 nmol (HPLC) siRNA Negative Control:KCNRG Human Pre-designed siRNA Set A contains three designed siRNAs for KCNRG gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components KCNRG siRNA-1: 5 nmol (HPLC) KCNRG siRNA-2: 5 nmol (HPLC) KCNRG siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 nmol (HPLC) FAM-labeled siRNA Negative Control: 5 nmol (HPLC) GAPDH siRNA Positive Control:5 nmol (HPLC)... 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:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Implicated in the control of cell proliferation and cellular aging. May also act as a chaperone | Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SMT3 to its mature form and deconjugation of SMT3 from targeted proteins. Has an essential role in the G2/M Purity:>90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SMT3 to its mature form and deconjugation of SMT3 from targeted proteins. Has an essential role in the G2/M phase of the cell cycle. Probable centromere protein from the fission yeast (Schizosaccharomyces pombe). Similar to yeast Smt3p-specific protease, degrades conjugated ubiquitin-like protein [S. pombe]... Read More |