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Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. Additionally we are shipping Isocitrate Dehydrogenase 3 (NAD+) alpha Proteins (10) and Isocitrate Dehydrogenase 3 (NAD+) alpha Kits (3) and many more products for this protein.
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Human Polyclonal IDH3A Primary Antibody for ELISA - ABIN544693
Kim, Koh, Kim, Jo, Huh, Jeong, Lee, Song, Huh: Identification and functional characterization of a novel, tissue-specific NAD(+)-dependent isocitrate dehydrogenase beta subunit isoform. in The Journal of biological chemistry 2000
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Human Monoclonal IDH3A Primary Antibody for FACS, IF - ABIN2723868
Zhang, Wang, Shi, Liu, Sun, Hou, Zhang, Zhao, Zhou, Mi: Metabolic reprogramming of cancer-associated fibroblasts by IDH3? downregulation. in Cell reports 2015
Cow (Bovine) Polyclonal IDH3A Primary Antibody for IHC, WB - ABIN2775312
Soundar, Park, Huh, Colman: Evaluation by mutagenesis of the importance of 3 arginines in alpha, beta, and gamma subunits of human NAD-dependent isocitrate dehydrogenase. in The Journal of biological chemistry 2003
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Human Polyclonal IDH3A Primary Antibody for IF (p), IHC (p) - ABIN751543
Xing, Yuan, Xu, Gu, Liang, Lu: Proteomic identification of mitochondrial targets involved in andrographolide sodium bisulfite-induced nephrotoxicity in a rat model. in Environmental toxicology and pharmacology 2015
The silencing of IDH3a significantly delayed tumor growth by suppressing the HIF-1-mediated Warburg effect and angiogenesis.
for IDH, a normal alpha subunit is required for catalytic activity and alpha-Arg88 likely participates in the isocitrate site, whereas the beta and gamma subunits have roles in the nucleotide functions of this allosteric enzyme
active sites of the human NAD-IDH are shared between alpha and gamma subunits and between alpha and beta subunits
Asp181 is essential for nicotinamide-adenine dinucleotide (NAD)-specific IDH alpha subunit catalysis and may also facilitate the binding of substrates.
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. NAD(+)-dependent isocitrate dehydrogenases catalyze the allosterically regulated rate-limiting step of the tricarboxylic acid cycle. Each isozyme is a heterotetramer that is composed of two alpha subunits, one beta subunit, and one gamma subunit. The protein encoded by this gene is the alpha subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase.
isocitrate dehydrogenase 3 (NAD+) alpha
, isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial
, mitochondrial isocitrate dehydrogenase (nad) subunit alpha
, H-IDH alpha
, NAD(+)-specific ICDH subunit alpha
, NAD(H)-specific isocitrate dehydrogenase alpha subunit
, NAD+-specific ICDH
, isocitrate dehydrogenase (NAD+) alpha chain
, isocitric dehydrogenase subunit alpha
, isocitrate dehydrogenase subunits 3/4