| Description | EMC1 Human Pre-designed siRNA Set A contains three designed siRNAs for EMC1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components EMC1 siRNA-1: 5 nmol (HPLC) EMC1 siRNA-2: 5 nmol (HPLC) EMC1 siRNA-3: 5 nmol (HPLC) siRNA Negative Control: 5 EMC1 Human Pre-designed siRNA Set A contains three designed siRNAs for EMC1 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components EMC1 siRNA-1: 5 nmol (HPLC) EMC1 siRNA-2: 5 nmol (HPLC) EMC1 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 | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:CNN1 is a member of the calponin family. CNN1 is a thin filament-associated protein which is involved in the regulation and modulation of smooth muscle contraction. CNN1 is able to bind to actin, calmodulinPurity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description:CNN1 is a member of the calponin family. CNN1 is a thin filament-associated protein which is involved in the regulation and modulation of smooth muscle contraction. CNN1 is able to bind to actin, calmodulin, troponin C and tropomyosin. Prevention of actomyosin Mg-ATPase activity is a result of interaction between calponin and actin... Read More | Format:1-ComponentEnzyme:Horseradish peroxidase | 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 |