Isocitrate Dehydrogenase 1 R132H mutant Active Protein | IDH1 active protein

Isocitrate Dehydrogenase 1 R132H mutant; Recombinant Human

Cat. Num. AAA846998

• Gene Names: IDH1; IDH; IDP; IDCD; IDPC; PICD; HEL-216; HEL-S-26
• Applications: SDS-Page
• Purity: > 90% by SDS-PAGE
• Synonyms: Isocitrate Dehydrogenase 1 R132H mutant; Recombinant Human; Isocitrate dehydrogenase [NADP] cytoplasmic; R132H; IDH 1 R132H; IDH1 active protein

• Host: E. coli
• Purity/Purification: > 90% by SDS-PAGE
• Form/Format: Lyophilized

• Applicable Applications for IDH1 active protein: SDS-PAGE
• Sequence: Full-length human IDH1 (452 amino acids) with N-Terminal HAT-tag. Arginine 132 is mutated to histidine.
• Reconstitution: Centrifuge the vial prior to opening. Reconstitute the lyophilized protein in deionized water to the final concentration 0.5 mg/ml and incubate the reconstituted protein at 25°C for 15 minutes.
• Specific Activity: The enzyme has a specific activity > 300 mU/mg based on measuring the oxidation of NADPH to NADP* at wavelength 340 nm from the following reaction using MyBioSource, Inc.'s Isocitrate Dehydrogenase Mutant assay Kit (MBS846916).; ; alpha-ketogluturate + NADPH + H⁺ --> 2HG + NADP⁺
• Unit Definition: One unit is the amount of enzyme that will convert 1.0 umole of NADPH to NADP⁺ per minute at pH 7.4 at 25°C.
• Preparation and Storage: Lyophilized protein can be stored at 4°C. Once reconstituted aliquot and store at -20°C. Avoid repeated freeze/thaw cycles.

SDS-PAGE

Testing Data

Related Product Information for IDH1 active protein

Mutations of the cytosolic IDH 1 are a common feature in primary human brain cancers. Arginine 132 (R132) of IDH is highly conserved among different isoforms of IDH and is most commonly mutated to Histidine. Mutation of IDH1 R132H leads to accumulation of R (-)-2-hydroxyglutarate (2HG); which correlates with an increased risk for malignant brain tumors.

NCBI and Uniprot Product Information

• NCBI GI #: 538917488
• NCBI GeneID: 3417
• NCBI Accession #: NP_001269315.1
• NCBI GenBank Nucleotide #: NM_001282386.1
• UniProt Accession #: O75874; Q567U4; Q6FHQ6; Q7Z3V0; Q93090; Q9NTJ9; Q9UKW8
• Molecular Weight: ~50.9 kDa (SDS-PAGE)
• NCBI Official Full Name: isocitrate dehydrogenase
• NCBI Official Synonym Full Names: isocitrate dehydrogenase (NADP(+)) 1, cytosolic
• NCBI Official Symbol: IDH1
• NCBI Official Synonym Symbols: IDH; IDP; IDCD; IDPC; PICD; HEL-216; HEL-S-26
• NCBI Protein Information: isocitrate dehydrogenase [NADP] cytoplasmic
• UniProt Protein Name: Isocitrate dehydrogenase [NADP] cytoplasmic
• Protein Family: Isocitrate dehydrogenase
• UniProt Gene Name: IDH1
• UniProt Synonym Gene Names: PICD; IDH

NCBI Description

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]

Uniprot Description

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

Chromosomal Location of Human Ortholog: 2q34

Cellular Component: cytoplasm; cytosol; extracellular region; peroxisomal matrix; peroxisome

Molecular Function: (R)-2-hydroxyglutarate dehydrogenase activity; cadherin binding; isocitrate dehydrogenase (NADP+) activity; magnesium ion binding; protein homodimerization activity; receptor binding

Biological Process: 2-oxoglutarate metabolic process; isocitrate metabolic process; NADPH regeneration; neutrophil degranulation

Disease: Glioma Susceptibility 1