IDH1 (D2H1) Rabbit mAb recognizes endogenous levels of total IDH1 protein. This antibody does not recognize endogenous IDH2 protein, but does recognize IDH2 when recombinantly overexpresssed.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg222 of human IDH1 protein.

IDH1 is one of three isocitrate dehydrogenases that catalyze the oxidative decarboxylation of isocitrate to α-ketoglutarate (α-KG). These enzymes exist in two distinct subclasses that utilize either NAD or NADP⁺ respectively, as an electron acceptor (1). IDH1 is the NADP⁺-dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. IDH2 and 3 are mitochondrial enzymes that also function in the Krebs cycle. IDH1 is inactivated by phosphorylation at Ser113 and contains a clasp-like domain wherein both polypeptide chains in the dimer interlock (2,3). IDH1 is expressed in a wide range of species and also in organisms that lack a complete citric acid cycle. Mutations in IDH1 have been reported in glioblastoma (4), acute myeloid leukemia (5,6), and other malignancies (7). IDH1 appears to function as a tumor suppressor that, when mutationally inactivated, contributes to tumorigenesis in part through induction of the HIF-1 pathway (8).