| Description | ANK1 Human Pre-designed siRNA Set A contains three designed siRNAs for ANK1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ANK1 siRNA-1: 5 nmol (HPLC) ANK1 siRNA-2: 5 nmol (HPLC) ANK1 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 ANK1 Human Pre-designed siRNA Set A contains three designed siRNAs for ANK1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components ANK1 siRNA-1: 5 nmol (HPLC) ANK1 siRNA-2: 5 nmol (HPLC) ANK1 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 | Bovine pancreatic deoxyribonuclease is an endonuclease which splits phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide yielding polynucleotides with free hydroxyl group at the 3' position and phosphate group at the 5' position. The average chain length of a limit digest is aBovine pancreatic deoxyribonuclease is an endonuclease which splits phosphodiester linkages, preferentially adjacent to a pyrimidine nucleotide yielding polynucleotides with free hydroxyl group at the 3' position and phosphate group at the 5' position. The average chain length of a limit digest is a tetranucleotide.Used for the removal of DNA from protein samples. Deoxyribonuclease I from bovine pancreas has been used in a study to compare several procedures for reducing RNase contamination in preparations of DNase. Deoxyribonuclease I from bovine pancreas has also been used in a study to investigate the effect of the composition of sodium dodecyl sulfate preparations on the renaturation of enzymes after polyacrylamide gel electrophoresis... Read More | Inquire | Purity>97% SDS-PAGE.FunctionReceptor for interleukin-2 | 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 |