| Description | Adora1 Mouse Pre-designed siRNA Set A contains three designed siRNAs for Adora1 gene (Mouse), as well as a negative control, a positive control, and a FAM-labeled negative control. Components Adora1 siRNA-1: 5 nmol (HPLC) Adora1 siRNA-2: 5 nmol (HPLC) Adora1 siRNA-3: 5 nmol (HPLC) siRNA Negative Adora1 Mouse Pre-designed siRNA Set A contains three designed siRNAs for Adora1 gene (Mouse), as well as a negative control, a positive control, and a FAM-labeled negative control. Components Adora1 siRNA-1: 5 nmol (HPLC) Adora1 siRNA-2: 5 nmol (HPLC) Adora1 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 | Amine-Reactive probe which passively diffuse into cells and it is nonfluorescent until the acetate groups are cleaved by intracellular esterases to yield the highly fluorescent, amine-reactive fluorophore. Upon reaction with amine-containing residues of intracellular proteins, these probes form dye Amine-Reactive probe which passively diffuse into cells and it is nonfluorescent until the acetate groups are cleaved by intracellular esterases to yield the highly fluorescent, amine-reactive fluorophore. Upon reaction with amine-containing residues of intracellular proteins, these probes form dye protein adducts that are well retained in cells as they move and divide during embryonic development.A Non-fluorescent cell permeant amine-reactive probe for long term tracing of cell... Read More | Inquire | SHP2 protein degrader-2 (SHP2-D26) is a SHP2 protein PROTAC degrader. SHP2 protein degrader-2 reduces expression level of SHP2 in various cancer cells.In VitroSHP2 protein degrader-2 (SHP2-D26) achieves excellent degradation of SHP2 with the DC 50 (the concentration where 50% of the protein has beenSHP2 protein degrader-2 (SHP2-D26) is a SHP2 protein PROTAC degrader. SHP2 protein degrader-2 reduces expression level of SHP2 in various cancer cells.In VitroSHP2 protein degrader-2 (SHP2-D26) achieves excellent degradation of SHP2 with the DC 50 (the concentration where 50% of the protein has been degraded) values of 2.6 nM and 6.0 nM for MV4;11 and KYSE520 cells, respectively. MCE has not independently confirmed the accuracy of these methods. They are for reference only.Form:Solid... 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 |