|Application ||WB, E|
|Other Accession||NP_005887, 28178825|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||46659 Da|
|Application Notes||IDH1 antibody can be used for detection of IDH1 by Western blot at 1 - 2 µg/mL.|
|Reconstitution & Storage||IDH1 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||IDH1 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Cellular Location||Cytoplasm. Peroxisome|
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Provided below are standard protocols that you may find useful for product applications.
IDH1 Antibody: 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(+). Two NADP(+)-dependent isocitrate dehydrogenases have been found as homodimer: IDH1 is predominantly cytosolic and peroxisomal and IDH2 is mitochondrial. The presence of IDH1 in peroxisomes suggests it may play a role 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 IDH1 serves a significant role in cytoplasmic NADPH production. Defects in IDH1 are involved in the development of glioma.
Geisbrecht BV and Gould SJ. The human PICD gene encodes a cytoplasmic and peroxisomal NADP(+)-dependent isocitrate dehydrogenase. J. Biol. Chem.1999; 274:30527-33.
Xu X, Zhao J, Xu Z, et al. Structures of human cytosolic NADP-dependent isocitrate dehydrogenase reveal a novel self-regulatory mechanism of activity. J. Biol. Chem.2004; 279:33946-57.
Dang L, White DW, and Gross S. Cancer-associated IDH1 mutations produce 2-hydroxyglutarate. Nature2009; 462:739-44.
Smeitink J. Metabolism, gliomas, and IDH1. N. Engl. J. Med.2010; 362:1144-5.
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