Isocitrate dehydrogenase/IDH1 Recombinant Protein | IDH1 recombinant protein

Isocitrate dehydrogenase/IDH1 Protein, Human, Recombinant (His Tag)

Cat. Num. AAA8121067

• Gene Names: IDH1; IDH; IDP; IDCD; IDPC; PICD; HEL-216; HEL-S-26
• Purity: >95% as determined by SDS-PAGE
• Synonyms: Isocitrate dehydrogenase/IDH1; Isocitrate dehydrogenase/IDH1 Protein; Human; Recombinant (His Tag); Human IDH1 Protein (His Tag); HEL-216 Protein; HEL-S-26 Protein; IDCD Protein; IDH Protein; IDP Protein; IDPC Protein; PICD Protein; isocitrate dehydrogenase 1 (NADP+); soluble; IDH1 recombinant protein

• Host: E Coli
• Purity/Purification: >95% as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile 50mM Tris, 200mM NaCl, 1mM DTT, 10% Glycerol, pH7.5. Normally 5%-8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hard copy of CoA.
• Sequence: Met1-Leu414

• Species: Human
• Predicted N Terminal: Met 1
• Tag: C-His
• Protein Construction: A DNA sequence encoding the human IDH1 (O75874)(Met 1-Leu 414) was fused with a polyhistidine tag at the C-terminus.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -20 degree C to -80 degree C. Store it under sterile conditions at -20 degree C to -80 degree C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.; In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid.; They are shipped out with blue ice.

SDS-Page

References

Takano S, et al. (2011) Detection of IDH1 mutation in human gliomas: comparison of immunohistochemistry and sequencing. Brain Tumor Pathol. 28(2): 115-23.Geisbrecht BV, et al. (1999) The human PICD gene encodes a cytoplasmic and peroxisomal NADP(+)-dependent isocitrate dehydrogenase. J Biol Chem. 274(43): 30527-30533.Nekrutenko A, et al. (1998) Cytosolic isocitrate dehydrogenase in humans, mice, and voles and phylogenetic analysis of the enzyme family. Mol Biol Evol. 15(12): 1674-1684.Henke B, et al. (1998) IDP3 encodes a peroxisomal NADP-dependent isocitrate dehydrogenase required for the beta-oxidation of unsaturated fatty acids. J Biol Chem. 273(6): 3702-3711.Gabriel JL, et al. (1986) Activity of purified NAD-specific isocitrate dehydrogenase at modulator and substrate concentrations approximating conditions in mitochondria. Metabolism. 35(7): 661-667.

NCBI and Uniprot Product Information

• NCBI GI #: 119590846
• NCBI GeneID: 3417
• UniProt Accession #: O75874; Q567U4; Q6FHQ6; Q7Z3V0; Q93090; Q9NTJ9; Q9UKW8
• Molecular Weight: 46,659 Da
• NCBI Official Full Name: isocitrate dehydrogenase 1 (NADP+), soluble, isoform CRA_b
• NCBI Official Synonym Full Names: isocitrate dehydrogenase 1 (NADP+), soluble
• 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; isocitrate dehydrogenase [NADP] cytoplasmic; NADP(+)-specific ICDH; oxalosuccinate decarboxylase; epididymis luminal protein 216; epididymis secretory protein Li 26; NADP-dependent isocitrate dehydrogenase, cyt
• UniProt Protein Name: Isocitrate dehydrogenase [NADP] cytoplasmic
• Protein Family: Isocitrate dehydrogenase
• UniProt Gene Name: IDH1
• UniProt Synonym Gene Names: PICD; IDH
• UniProt Entry Name: IDHC_HUMAN

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

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