IDH1 R132H mutant (human recombinant)

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 alpha-ketoglutarate (alpha-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. IDH1 and IDH2 are mutated in >70% of lower grade gliomas. The most common IDH mutation, Arg132His, imparts new gain of function catalytic activity leading to the NADPH-dependent conversion of alpha-KG to 2-hydroxyglutarate. 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.Synonyms: Isocitrate Dehydrogenase (NADP) Cytoplasmic. Purity: >95% estimated by SDS-PAGE. Source: Active recombinant C-terminal His-tagged protein expressed in E. coli. Amino Acids: 2-414 (full-length). MW: 47.9 kDa. Formulation: (Request formulation change), 50 mM Tris-HCl, pH 7.5, containing 200 mM sodium chloride, 5 mM beta-mercaptoethanol, and 10% glycerol. UniProt Accession #: O75874.