IDH1 Mouse Monoclonal Antibody [A11-B4]

Function

Isocitrate dehydrogenase (IDH) is an enzyme that catalyzes the oxidative decarboxylation of isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. In humans, IDH exists in three isoforms: IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead of NAD+. They localize to the cytosol as well as the mitochondrion and peroxisome. Mutations in IDH1 are also implicated in cancer. Originally mutations in IDH1 were detected in an integrated genomic analysis of human glioblastoma multiforme. In addition to being mutated in diffuse gliomas, IDH1 has also been shown to harbor mutations in human acute myeloid leukemia (AML).

Background References

1. "Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity." Xu X., Zhao J., Xu Z., Peng B., Huang Q., Arnold E., Ding J. J. Biol. Chem. 279:33946-33957(2004)

2. "Cancer-associated IDH1 mutations produce 2-hydroxyglutarate." Dang L., et al. Nature 462:739-744(2009)

3. "IDH1 mutations at residue p.R132 (IDH1(R132)) occur frequently in high-grade gliomas but not in other solid tumors." Bleeker F.E., et al. Hum. Mutat. 30:7-11(2009)

Sequence Similarity

Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Post-translational Modification

Acetylation at Lys-374 dramatically reduces catalytic activity.

Subcellular Location

Cytoplasm.

UNIPROT

SwissProt: O75874 Human

SwissProt: O88844 Mouse

SwissProt: P41562 Rat

Synonyms