Isocitrate dehydrogenase 1 (IDH1) is an isoform of IDH enzyme. It is a cytoplasmic NADP+-dependent enzyme, localized both in the cytoplasm and peroxisomes.
Immunogen
synthetic peptide corresponding to an internal sequence of human IDH1, conjugated to KLH. The corresponding sequence is highly conserved in mouse (single amino acid substitution) and highly conserved in rat IDH1 (89% sequence identity).
Biochem/physiol Actions
Isocitrate dehydrogenase (IDH) is a key metabolic enzyme that catalyzes the oxidative decarboxylation of isocitrate into α-ketoglutarate (αKG) in the cytosol, by using either NAD+ or NADP+ as co-substrates. IDH1 appears to have a tumor suppressor activity and its inactivation leads to tumorigenesis partially mediated by induction of the HIF1 pathway. A genome-wide mutation study has shown that IDH1 is mutated in glioblastoma, acute myeloid leukemia (AML) and chondrosarcoma. Mutations in IDH1 specific to Arg132 (R132) impart the enzyme′s ability to generate 2- hydroxyglutarate (2HG) instead of αKG. Several IDH1 mutations have been identified in gliomas, including R132H, R132C, R132S, R132G and R132L, each may result in different tumor type with varied malignant progression.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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Mutations in the enzyme cytosolic isocitrate dehydrogenase 1 (IDH1) are a common feature of a major subset of primary human brain cancers. These mutations occur at a single amino acid residue of the IDH1 active site, resulting in loss of
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