Analytical Data
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Gene name
IDH1
- Application
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Alternative Names
IDH1；PICD；Isocitrate dehydrogenase [NADP] cytoplasmic
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75874
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Expression Region
1-414aa
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AA Sequence
MSKKISGGSVVEMQGDEMTRIIWELIKEKLIFPYVELDLHSYDLGIENRD ATNDQVTKDAAEAIKKHNVGVKCATITPDEKRVEEFKLKQMWKSPNGTIR NILGGTVFREAIICKNIPRLVSGWVKPIIIGHHAYGDQYRATDFVVPGPG KVEITYTPSDGTQKVTYLVHNFEEGGGVAMGMYNQDKSIEDFAHSSFQMA LSKGWPLYLSTKNTILKKYDGRFKDIFQEIYDKQYKSQFEAQKIWYEHRL IDDMVAQAMKSEGGFIWACKNYDGDVQSDSVAQGYGSLGMMTSVLVCPDG KTVEAEAAHGTVTRHYRMYQKGQETSTNPIASIFAWTRGLAHRAKLDNNK ELAFFANALEEVSIETIEAGFMTKDLAACIKGLPNVQRSDYLNTFEFMDK LGENLKIKLAQAKLDYKDDDDK
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Molecular Weight
48 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
IDH1 (isocitrate dehydrogenase 1) is an enzyme critically involved in the citric acid cycle, responsible for converting isocitrate to alpha-ketoglutarate while reducing NADP+ to NADPH. Mutations in the IDH1 gene are frequently associated with various cancers, particularly gliomas and acute myeloid leukemia (AML), leading to the production of the oncometabolite 2-hydroxyglutarate (2-HG). This metabolic shift alters cellular differentiation pathways and contributes to tumorigenesis. The study of IDH1 recombinant proteins has gained significant attention due to their dual role as potential biomarkers for cancer diagnosis and as targets for therapeutic intervention. Understanding the structural and functional properties of mutant IDH1 enzymes can help elucidate their role in carcinogenesis and support the development of small molecules that inhibit their activity or mitigate the effects of 2-HG accumulation. Recent advances in biochemistry and structural biology have facilitated the production of recombinant IDH1 proteins, enabling detailed studies of their enzymatic mechanisms, interactions with inhibitors, and implications in cancer metabolism. This research not only enhances our understanding of IDH1's pathological functions but also lays the groundwork for the design of novel therapeutic strategies aimed at targeting IDH1 mutations in cancer treatment.
