| Description | Lrp6 Mouse Pre-designed siRNA Set A contains three designed siRNAs for Lrp6 gene (Mouse), as well as a negative control, a positive control, and a FAM-labeled negative control. Components Lrp6 siRNA-1: 5 nmol (HPLC) Lrp6 siRNA-2: 5 nmol (HPLC) Lrp6 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 Lrp6 Mouse Pre-designed siRNA Set A contains three designed siRNAs for Lrp6 gene (Mouse), as well as a negative control, a positive control, and a FAM-labeled negative control. Components Lrp6 siRNA-1: 5 nmol (HPLC) Lrp6 siRNA-2: 5 nmol (HPLC) Lrp6 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 | Product introduction:The additive contains a variety of cytokines, human albumin and other components. In order to ensure the activity, it is recommended that the additive part be thawed once and then sub packaged and frozen again. It is not advisable to freeze and thaw repeatedly. The Product introduction:The additive contains a variety of cytokines, human albumin and other components. In order to ensure the activity, it is recommended that the additive part be thawed once and then sub packaged and frozen again. It is not advisable to freeze and thaw repeatedly. The product contains no animal serum or animal serum components, no animal protein components, and no antibiotics.Matters needing attention:1. try to reduce the number of repeated freezing and thawing to avoid efficiency decline. 2. it is not suitable to place it at room temperature for a long time. 3. pay attention to aseptic operation and try to avoid pollution. 4. please wear experimental clothes and disposable gloves for operationScope of application:Cell culture additives... 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 | Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide. Pyridoxal 5'-phosphate is a necessary cofactor. By using the apoenzyme prepared from cells grown on a vitamin B6 deficient medium pyridoxal phosphate may be determined. The Tyrosine decarboxylase catalyzes the removal of the carboxyl group from tyrosine to produce tyramine and carbon dioxide. Pyridoxal 5'-phosphate is a necessary cofactor. By using the apoenzyme prepared from cells grown on a vitamin B6 deficient medium pyridoxal phosphate may be determined. The HOLOenzyme may be used to determine tyrosine, phenylalanine and dihydroxyphenylalanine either manometrically or colorimetrically.L-Tyrosine decarboxylase apoenzyme from Streptococcus faecalis has been used in a study to purify and characterize tyrosine decarboxylase and aromatic-L-amino-acid decarboxylase.L-Tyrosine decarboxylase apoenzyme from Streptococcus faecalis has also been used in a study to investigate the stereospecificity of sodium borohydride reduction of tyrosine decarboxylase.One Unit yields 1µmole of CO2 per minute from L-tyrosine at 37°C, pH 5.5. The APOenzyme activity is measured in the presence of excess pyridoxal phosphate... Read More |