IDH2 / Unconjugated /

Product Details
Description Rabbit polyclonal to IDH2.Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate.These enzymes belong to two distinct subclasses, one utilizes NAD(+) as the electron acceptor andthe other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependentwhich localize to the mitochondrial matrix; and two NADP(+)-dependent, one of which is mitochondrialand the other predominantly cytosolic. Each NADP(+)-dependent isozyme is a homodimer. IDH2 isthe NADP(+)-dependent isocitrate dehydrogenase found in the mitochondria, which plays a role inintermediary metabolism and energy production. IDH2 may tightly associate or interact with thepyruvate dehydrogenase complex. Defects in IDH2 are the cause of D-2-hydroxyglutaric aciduria type2 (D2HGA2), a neurometabolic disorder causing developmental delay, epilepsy, hypotonia, anddysmorphic features. -
Conjugate Unconjugated
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Target Species Human, Mouse
Applications WB
Supplier Biorbyt
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About IDH2
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 mitochondria. It plays a role in intermediary metabolism and energy production. This protein may tightly associate or interact with the pyruvate dehydrogenase complex. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2014]
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