| Description | CSTA Human Pre-designed siRNA Set A contains three designed siRNAs for CSTA gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CSTA siRNA-1: 5 nmol (HPLC) CSTA siRNA-2: 5 nmol (HPLC) CSTA siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 CSTA Human Pre-designed siRNA Set A contains three designed siRNAs for CSTA gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CSTA siRNA-1: 5 nmol (HPLC) CSTA siRNA-2: 5 nmol (HPLC) CSTA 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 | Copper tripeptide (GHK-Cu) is a naturally occurring tripeptide that is first isolated from human plasma but can also be found in saliva and urine. During wound healing, Copper tripeptide can be removed from existing extracellular proteins by protein hydrolysis and used as a chemical lure for Copper tripeptide (GHK-Cu) is a naturally occurring tripeptide that is first isolated from human plasma but can also be found in saliva and urine. During wound healing, Copper tripeptide can be removed from existing extracellular proteins by protein hydrolysis and used as a chemical lure for inflammatory and endothelial cells. Copper tripeptide can increase the production of messenger RNA in collagen, elastin, protein polysaccharides and glycosamine polysaccharides in fibroblasts. Copper tripeptide is a natural regulator of many cellular pathways in skin regeneration... Read More | Biochemical Test:SDS-PAGE (purity > 80%); Western blot with patient sample.Calculated Isoelectric Point:pH 5.68 | 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 pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa Trypsin is a pancreatic serine protease with substrate specificity based upon positively charged lysine and arginine side chains. It is derived from a 34 kDa inactive precursor zymogen, trypsinogen, after enzymatic removal of an N-terminal 6-amino acid leader sequence resulting in the 23.8 kDa trypsin molecule. The optimum pH is 8.0. Trypsin is inhibited by organophosphorus compounds such as diisopropylfluorophosphate and natural inhibitors from pancreas. Soybean, lima bean, and egg white are also sources of natural inhibitors. Trypsin cleaves amide and ester bonds of Arg and Lys. The Aladdin Sequencing Grade Trypsin has been further purified to remove trace contaminating proteases and autolysis products which could interfere in trypsin digestion experiments, and exhibits a single band on PAGE.Trypsin is a serine protease used to hydrolyze proteins. Trypsin from bovine pancreas has a molecular weight of 23.8 kDa. Trypsins are used for the re-suspension of cells during cell culture and in proteomics research for the digestion of various proteins... Read More |