IDH1 (R132H) Inhibitor Screening Kit (Colorimetric) IDH1 R132H Mutant oxidizes NADPH into NADP+, which decreases the absorbance at 340 nm. In the presence of IDH1 R132H Mutant inhibitor, the reaction is impeded. An IDH1 R132H Mutant Inhibitor Control is included to compare the efficacy of the sample inhibitors. The assay is high-throughput adaptable and can be completed in less than 1 hr.
Storage Instruction:
Store the kit at -20°C. Avoid repeated freezing and thawing.
Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. Each NADP(+)-dependent isozyme is a homodimer. The protein encoded by this gene is the NADP(+)-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. It contains the PTS-1 peroxisomal targeting signal sequence. The presence of this enzyme in peroxisomes suggests roles in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid. The cytoplasmic enzyme serves a significant role in cytoplasmic NADPH production. [provided by RefSeq