| Description | CITED1 Human Pre-designed siRNA Set A contains three designed siRNAs for CITED1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CITED1 siRNA-1: 5 nmol (HPLC) CITED1 siRNA-2: 5 nmol (HPLC) CITED1 siRNA-3: 5 nmol (HPLC) siRNA Negative CITED1 Human Pre-designed siRNA Set A contains three designed siRNAs for CITED1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CITED1 siRNA-1: 5 nmol (HPLC) CITED1 siRNA-2: 5 nmol (HPLC) CITED1 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 | Inquire | Store at +4°C. Store under desiccating conditions. The product can be stored for up to 12 months | 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 |