Isocitrate dehydrogenases (IDHs) are NAD+ and NADP+-dependent enzymes that catalyze the third step of the tricarboxylic acid cycle. IDHs catalyze oxidative decarboxylation of isocitrate producing -ketoglutarate (-KG) and carbon dioxide. IDH1 (cytosolic) and IDH2 (mitochondrial) are NADP+-dependent enzymes that catalyze reversible rEActions. The IDH3 isoform, a NAD+-dependent multisubunit enzyme, is irreversible and allosterically regulated by a variety of positive (calcium, ADP, and citrate) and negative (ATP, NADH, and NADPH) effectors.1 IDH1 and IDH2 are mutated in >70% of lower grade gliomas.2 The most common IDH mutation, Arg132His, imparts new gain of function catalytic activity lEAding to the NADPH-dependent conversion of -KG to 2-hydroxyglutarate.3,4 Astrocytes expressing IDH1 R132H mutant have been shown to produce markedly incrEAsed levels of the R-2-hydroxyglutarate enantiomer, lEAding to transformation of cells through the HIF prolyl 4-hydroxylase, EGLN.5Technical InformationSynonymsIsocitrate Dehydrogenase (NADP) CytoplasmicPurity95% estimated by SDS-PAGESourceActive recombinant C-terminal His-tagged protein expressed in E. coliAmino Acids2-414 (full-length)MW47.9 kDaFormulation50 mM Tris-HCl, pH 7.5, containing 200 mM sodium chloride, 5 mM -mercaptoethanol, and 10% glycerolUniProt Accession O75874