IDH1, Polyclonal Antibody

Oxalosuccinate decarboxylase, Cytosolic NADP-isocitrate dehydrogenase, NADP(+)-specific ICDH, IDCD, IDH, IDP, PICD

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

Rabbit

Affinity chromatography purified via peptide column

Supplied in PBS containing 0.02% sodium azide.

Can be stored at -20 degree C, stable for 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.

Small volumes of anti-IDH1 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

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.

Total protein Ab

ELISA (EIA), Western Blot (WB)

Western blot analysis of IDH1 in HepG2 cell lysate with IDH1 antibody at (A) 1 and (B) 2 ug/mL.

46,659 Da

isocitrate dehydrogenase 1 (NADP+), soluble

isocitrate dehydrogenase [NADP] cytoplasmic

Isocitrate dehydrogenase [NADP] cytoplasmic

PICD; IDH  [Similar Products]

IDHC_HUMAN

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]

IDH1: an oxidoreductase that catalyzes the third step of the TCA cycle: the oxidative decarboxylation of isocitrate, consuming NADP(+), and producing alpha-ketoglutarate (alpha-KG) and CO2. Alpha-KG is an activator the dioxygenases that hydroxylate the transcription factor HIF and lead to its degradation by VHL. Since HIF turns on oncogenic pathways, IDH1 has apparent tumor suppressor activity. Homo-dimerization is required for activity. Each subunit binds 1 magnesium or manganese ion. IDH1 is located in the cytosol and peroxisomes. Somatic mutations affecting arginine 132 (R132) are found in 80% of grade II?III gliomas and secondary glioblastomas in humans, and cause disease in a tissue-specific fashion. Only a single copy of the gene has been found to be mutated in tumours. Mutations of R132 to H, C, S, G, V, or L have been reported to be neomorphic, abolishing the conversion of isocitrate to alpha-KG. Instead, alpha-KG is converted to R(-)-2-hydroxyglutarate (2HG). Elevated levels of 2HG correlate with an elevated risk of malignant brain tumors. Neomorphic mutations in IDH1 and IDH2 convert alpha-KG to 2-hydroxyglutarate (2-HG) occur in a high percentage of patients with cytogenetically normal acute myeloid leukemia (AML).

Protein type: Other Amino Acids Metabolism - glutathione; Oxidoreductase; Carbohydrate Metabolism - citrate (TCA) cycle; EC 1.1.1.42

Chromosomal Location of Human Ortholog: 2q33.3

Cellular Component: peroxisomal matrix; mitochondrion; cytoplasm; peroxisome; cytosol

Molecular Function: protein homodimerization activity; magnesium ion binding; isocitrate dehydrogenase (NADP+) activity; NADP binding; NAD binding; receptor binding

Biological Process: isocitrate metabolic process; NADPH regeneration; glyoxylate cycle; glutathione metabolic process; response to steroid hormone stimulus; tricarboxylic acid cycle; response to oxidative stress; cellular lipid metabolic process; female gonad development; 2-oxoglutarate metabolic process

Disease: Glioma Susceptibility 1

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