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.

Western

Western blot analysis of IDH1 in HepG2 (1), NIH/3T3 (2), C2C12 (3), COS7 (4), and SW480 (5) cell lysate using IDH1 antibody.

Immunocytochemistry

Immunocytochemistry analysis of IDH1 in Hela cells using IDH1 antibody (green),and DAPI(blue). Red: Actin filaments have been labeled with Alexa Fluor- 555 phalloidin.

Flow

Flow Cytometry analysis of Hela cells using IDH1 antibody (green) and negative control (red).

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