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Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. Additionally we are shipping Isocitrate Dehydrogenase 3 (NAD+) beta Proteins (8) and many more products for this protein.
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Human Monoclonal IDH3B Primary Antibody for ELISA - ABIN395755
Dange, Colman: Each conserved active site tyr in the three subunits of human isocitrate dehydrogenase has a different function. in The Journal of biological chemistry 2010
Show all 5 references for ABIN395755
Human Polyclonal IDH3B Primary Antibody for WB - ABIN1944754
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
Show all 4 references for ABIN1944754
Human NAD-dependent isocitrate dehydrogenase (IDH) is a heterotetrameric mitochondrial enzyme with 2alpha:1beta:1gamma subunit ratio subunits shich share 40-52% identity in amino acid sequence.
IDPm (show IDH2 Antibodies) activity appears to be modulated through enzymatic glutathionylation and deglutathionylation during oxidative stress
active sites of the human NAD-IDH are shared between alpha and gamma subunits and between alpha and beta subunits
Asp192 is needed for optimal affinity of IDH (show IDH1 Antibodies) beta subunit (show POLG Antibodies) for nicotinamide-adenine dinucleotide (NAD) substrate, but is not critical for catalysis.
Homozygous for loss-of-function mutations in IDH3B is associated with retinitis pigmentosa.
The point mutations of isocitrate dehydrogenase (show IDH1 Antibodies) are essentially unique to gliomas.
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 beta subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase. Three alternatively spliced transcript variants encoding different isoforms have been described for this gene.
isocitrate dehydrogenase 3 (NAD+) beta
, isocitrate dehydrogenase 3, beta subunit
, isocitrate dehydrogenase [NAD] subunit beta, mitochondrial-like
, N14A tumor-related protein
, isocitrate dehydrogenase 3 beta
, NAD(+)-specific ICDH subunit beta
, NAD+-specific ICDH
, NAD+-specific isocitrate dehydrogenase b subunit
, NAD+-specific isocitrate dehydrogenase beta
, isocitrate dehydrogenase [NAD] subunit beta, mitochondrial
, isocitrate dehydrogenase, NAD(+)-specific, mitochondrial, beta subunit
, isocitric dehydrogenase subunit beta
, NAD(+)-dependent isocitrate dehydrogenase subunit 3
, NAD(+)-isocitrate dehydrogenase subunit 1
, mitochondrial NAD+isocitrate dehydrogenase 3 beta variant 2