Isocitrate dehydrogenase (IDH1) (NM_005896) Human Recombinant Protein

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 cytoplasm and peroxisomes. It contains the PTS-1 peroxisomal targeting signal sequence. The presence of this enzyme in peroxisomes suggests roles 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 enzyme serves a significant role in cytoplasmic NADPH production. Alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Sep 2013]

Recombinant protein of human isocitrate dehydrogenase 1 (NADP+), soluble (IDH1) and mutant (R132C) heterodimer, with C-terminal polyhistidine and DDK tags, expressed in sf9 cells

Stable for 1 year at -20°C or below from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. For long-term storage, aliquot and store at -20°C or below. Avoid repeated freeze-thaw cycles.