| Description | ATP5F1A Human Pre-designed siRNA Set A contains three designed siRNAs for ATP5F1A gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ATP5F1A siRNA-1: 5 nmol (HPLC) ATP5F1A siRNA-2: 5 nmol (HPLC) ATP5F1A siRNA-3: 5 nmol (HPLC) siRNA ATP5F1A Human Pre-designed siRNA Set A contains three designed siRNAs for ATP5F1A gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ATP5F1A siRNA-1: 5 nmol (HPLC) ATP5F1A siRNA-2: 5 nmol (HPLC) ATP5F1A 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 | The Leuconostoc GPDH exhibits dual coenzyme specificity, namely NAD and NADP (Olive and Levy, Biochem., 6, 730 730, 1967). When assayed under conditions that are optimal for the particular coenzyme, the ratio of observed catalytic activity is NAD/NADP = 1.8 | 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 |