| Description | LHFPL2 Human Pre-designed siRNA Set A contains three designed siRNAs for LHFPL2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components LHFPL2 siRNA-1: 5 nmol (HPLC) LHFPL2 siRNA-2: 5 nmol (HPLC) LHFPL2 siRNA-3: 5 nmol (HPLC) siRNA Negative LHFPL2 Human Pre-designed siRNA Set A contains three designed siRNAs for LHFPL2 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components LHFPL2 siRNA-1: 5 nmol (HPLC) LHFPL2 siRNA-2: 5 nmol (HPLC) LHFPL2 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 | Fumarate hydratase-IN-2 sodium salt (compound 3) is a cell-permeable and competitive fumarate hydratase inhibitor ( K i =4.5 µM) with nutrient-dependent cytotoxicity.Appearance:SolidIC50& Target:Ki: 4.5 µM (Fumarate hydratase)Biological Activity:Fumarate hydratase-IN-2 sodium salt (Fumarate hydratase-IN-2 sodium salt (compound 3) is a cell-permeable and competitive fumarate hydratase inhibitor ( K i =4.5 µM) with nutrient-dependent cytotoxicity.Appearance:SolidIC50& Target:Ki: 4.5 µM (Fumarate hydratase)Biological Activity:Fumarate hydratase-IN-2 sodium salt (compound 3) is a cell-permeable and competitive fumarate hydratase inhibitor ( K i =4.5 µM) with nutrient-dependent cytotoxicity... Read More | Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with Mammalian lactate dehydrogenases (LDH) exist as five tetrameric isozymes composed of combinations of two different subunits. The H subunit predominates in heart muscle, which is geared for aerobic oxidation of pyruvate. The M subunit predominates in skeletal muscle and is concerned more with anaerobic metabolism and pyruvate reduction.Catalyzes the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+Recombinant rabbit muscle Lactate Dehydrogenase produced in E.Coli. Chromatographically purified. A lyophilized powder... Read More | Purity>98% SDS-PAGE. purified using conventional chromatography techniques.FunctionChemotactic activity for lymphocytes but not for monocytes or neutrophils.Chemokine (C motif) ligand (XCL1), as known as lymphotactin, is the only known member of the C-chemokine family and signals through the Purity>98% SDS-PAGE. purified using conventional chromatography techniques.FunctionChemotactic activity for lymphocytes but not for monocytes or neutrophils.Chemokine (C motif) ligand (XCL1), as known as lymphotactin, is the only known member of the C-chemokine family and signals through the receptor XCR1, formally known as GPR5. The expression of lymphotactin is abundant in some activated T cells such as activated CD8+ T cells and other class I MHC restricted T cells. It is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. XCL1 induces its chemotactic function by binding to a chemokine receptor called XCR1. Recombinant Human XCL1 which is a single non-glycosylated polypeptide chains containing 92 amino acids and it shares approximately 60 % amino acid sequence homology with the murine and rat protein... 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 |