Anti-Isocitrate dehydrogenase/IDH1 Antibody Picoband® Fluoro488 Conjugated

Isocitrate dehydrogenase 1 (NADP+), soluble is an enzyme that in humans is encoded by the IDH1 gene. Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD (+) as the electron acceptor and the other NADP (+) . Five isocitrate dehydrogenases have been reported: three NAD (+) -dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP (+) -dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. Each NADP (+) -dependent isozyme is a homodimer. The protein encoded by this gene is the NADP (+) -dependent isocitrate dehydrogenase found in the cytoplasm and peroxisomes. It contains the PTS-1 peroxisomal targeting signal sequence. The presence of this enzyme in peroxisomes suggests roles in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid. The cytoplasmic enzyme serves a significant role in cytoplasmic NADPH production. Alternatively spliced transcript variants encoding the same protein have been found for this gene.

Isocitrate dehydrogenase [NADP] cytoplasmic; IDH;1.1.1.42; Cytosolic NADP-isocitrate dehydrogenase; IDP; NADP (+) -specific ICDH; Oxalosuccinate decarboxylase; IDH1; PICD

Cancer, Cancer Metabolism, Energy Metabolism, Energy Transfer Pathways, Lipid and Lipoprotein Metabolism, Lipid Metabolism, Metabolic Signaling Pathway, Metabolic Signaling Pathways, Metabolism, Metabolism of Lipids and Lipoproteins, Pathways and Processes, Signal Transduction

1. Entrez Gene: Isocitrate dehydrogenase 1 (NADP+), soluble. 2. Watanabe T, Nobusawa S, Kleihues P, Ohgaki H (April 2009) . IDH1 mutations are early events in the development of astrocytomas and oligodendrogliomas.. Am J Pathol. 174 issue = 4 (4) : 1149–53.