| Description | CYP3A43 Human Pre-designed siRNA Set A contains three designed siRNAs for CYP3A43 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CYP3A43 siRNA-1: 5 nmol (HPLC) CYP3A43 siRNA-2: 5 nmol (HPLC) CYP3A43 siRNA-3: 5 nmol (HPLC) siRNA CYP3A43 Human Pre-designed siRNA Set A contains three designed siRNAs for CYP3A43 gene (Human), as well as a negative control, a positive control, and a FAM-labeled negative control. Components CYP3A43 siRNA-1: 5 nmol (HPLC) CYP3A43 siRNA-2: 5 nmol (HPLC) CYP3A43 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 | Malic Dehydrogenase is a ubiquitous enzyme, which exists in two isoforms in eukaryotic cells.Malic dehydrogenase exists as a dimer with each subunit containing an NAD-binding domain and a substrate-binding carboxy-terminal domain required for activity. Malic dehydrogenase is a cytoplasmic isozyme Malic Dehydrogenase is a ubiquitous enzyme, which exists in two isoforms in eukaryotic cells.Malic dehydrogenase exists as a dimer with each subunit containing an NAD-binding domain and a substrate-binding carboxy-terminal domain required for activity. Malic dehydrogenase is a cytoplasmic isozyme and an important catalyst in the tricarboxylic acid cycle.ReagentsA. 0.1 M Tris-HCl buffer (pH7.8)B. 0.01 M Phosphate buffer (KH2PO4-NaOH, pH 7.0)C. Triton X-100 solution (50 mg/ml)D. 0.01 M Phosphate buffer containing 0.1% Triton X-100 (KH2PO4-NaOH, pH 7.0)Dilute 20 ml of Triton X-100 solution (C) with approx. 800 ml of 0.01M Phosphate buffer (B). Fill up to 1,000 ml with 0.01M Phosphate buffer (B).E. NADH soluton Weigh 9 mg of NADH and dissolve in 0.1M Tris-HCl bufer (A). Fill up to 50 ml with 0.1M Tris-HCl Buffer (A). (Can be used for 5 days if kept refrigerated)F. Substrate solutionWeigh 11 mg of oxaloacetic acid and dissolve in 0.1M Tris-HCl buffer (A). Fill up to 50 ml with 0.1M Tris-HCl buffer (A) (Make a fresh solution for each use.)G. Enzyme solutionWeigh out Malate Dehydrogenase and dissolve in chilled 0.01M Phosphate Bufer containing 0.1% Triton X-100 (D). Enzyme solution should be prepared so that the value of AOD/minute becomes in the range of 0.025 ± 0.010.ProcedurePipette 2.0 ml of NADH solution (E) and 0.90 ml of Substrate solution (F) respectively into a quartz cell (d=10 mm) and keep at 25 + 0.5'℃ for 5 minutes. Then, pipete 0.10 ml of Enzyme solution (G) into the quartz cell and mix well immediately. Keep the reaction mixture at 25 ±0.5'C.Exaclly at 2 minutes and 5 minutes after the addition of Enzyme solution (G), measure the absorbances of the reaction mixture at 340 nm(A2 and A5).As a blank, pipette 0.01M Phosphate buffer (D) into another quartz cel (d=10 mm) instead of the Enzyme solution (G) and follow the same procedure described above (Ab2 and Ab5).CalculationMalate dehydrogenase activity (u/mg)=[(A2-A5)-(Ab2-Ab5)]/3*(1/6.22)*(n/0.1) ApplicationThis enzyme is used for the enzymatic determination of L-malate and gluamate oxalo-acetate transaminase(GOT)in clinical diagnosis... Read More | Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments: pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA.ApplicationUseful for the proteolytic inactivation of nucleases during the isolation of DNA and RNA.Removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease A.Reported useful for the isolation of hepatic, yeast, and mung bean mitochondriaDetermination of enzyme localization on membranesTreatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling.Digestion of proteins from brain tissue samples for prions in Transmissible Spongiform Encephalopathies (TSE) research... 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