| Description | ATP6V1G3 Human Pre-designed siRNA Set A contains three designed siRNAs for ATP6V1G3 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ATP6V1G3 siRNA-1: 5 nmol (HPLC) ATP6V1G3 siRNA-2: 5 nmol (HPLC) ATP6V1G3 siRNA-3: 5 nmol (HPLC) siRNA ATP6V1G3 Human Pre-designed siRNA Set A contains three designed siRNAs for ATP6V1G3 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ATP6V1G3 siRNA-1: 5 nmol (HPLC) ATP6V1G3 siRNA-2: 5 nmol (HPLC) ATP6V1G3 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 | H-7 dihydrochloride blocks human immunodeficiency virus (HIV-1) replication in MOLT-4 (clone No. 8) cell line. It increases the secretion of interleukin 1β (IL-1β).Application:H-7 dihydrochloride has been used to study H-7-induced inhibition of contractility in rat embryo H-7 dihydrochloride blocks human immunodeficiency virus (HIV-1) replication in MOLT-4 (clone No. 8) cell line. It increases the secretion of interleukin 1β (IL-1β).Application:H-7 dihydrochloride has been used to study H-7-induced inhibition of contractility in rat embryo fibroblasts (REF52) cells and acts as a kinase inhibitor... Read More | 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 | Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA. Recombinant Human Trypsin is a genetically engineered protein expressed in E.coli and purified by high pressure liquid chromatography. There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparation.Animal origin free:The use of recombinant Human Trypsin eliminates the risk of virus presence, and of any other potential adventitious agents found in animal pancreas-derived trypsin. Recombinant human trypsin:The amino acid sequence is the same as the Human Trypsin 2.Stable:A sterile recombinant human trypsin lyophilized eliminates the contamination risks and decreases the chance of activity loss in the process of transport and storage.High purity:(1) Recombinant human trypsin provides increased specificity and eliminates contaminating activities found in lower purity enzymes.(2) No other contaminating proteases such as chymotrypsin or carboxypeptidase A... Read More |