- CITATIONS: 1
|Application ||WB, E|
|Other Accession||Q99NA5, Q9D6R2, Q28480, P41563|
|Predicted||Bovine, Monkey, Mouse, Rat|
|Calculated MW||39592 Da|
|Antigen Region||317-346 aa|
|Other Names||Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial, Isocitric dehydrogenase subunit alpha, NAD(+)-specific ICDH subunit alpha, IDH3A|
|Target/Specificity||This Isocitrate dehydrogenase (IDH3) antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 317-346 amino acids from the C-terminal region of human Isocitrate dehydrogenase (IDH3).|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||IsocitRe dehydrogenase (IDH3) Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
Provided below are standard protocols that you may find useful for product applications.
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 described here is the alpha subunit of one isozyme of NAD(+)-dependent isocitrate dehydrogenase.
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Huh, T.L., et al., Genomics 32(2):295-296 (1996).
Kim, Y.O., et al., Biochem. J. 308 (PT 1), 63-68 (1995) (): ().
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