Analytical Data
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Gene name
IDH2
- Application
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Alternative Names
IDH2；Isocitrate dehydrogenase [NADP]. mitochondrial
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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
P48735
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Expression Region
1-452aa
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AA Sequence
MAGYLRVVRSLCRASGSRPAWAPAALTAPTSQEQPRRHYADKRIKVAKPV VEMDGDEMTRIIWQFIKEKLILPHVDIQLKYFDLGLPNRDQTDDQVTIDS ALATQKYSVAVKCATITPDEARVEEFKLKKMWKSPNGTIRNILGGTVFRE PIICKNIPRLVPGWTKPITIGRHAHGDQYKATDFVADRAGTFKMVFTPKD GSGVKEWEVYNFPAGGVGMGMYNTDESISGFAHSCFQYAIQKKWPLYMST KNTILKAYDGRFKDIFQEIFDKHYKTDFDKNKIWYEHRLIDDMVAQVLKS SGGFVWACKNYDGDVQSDILAQGFGSLGLMTSVLVCPDGKTIEAEAAHGT VTRHYREHQKGRPTSTNPIASIFAWTRGLEHRGKLDGNQDLIRFAQMLEK VCVETVESGAMTKDLAGCIHGLSNVKLNEHFLNTTDFLDTIKSNLDRALG RQDYKDDDDK
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Molecular Weight
52 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
IDH2 (Isocitrate dehydrogenase 2) is an enzyme that plays a crucial role in cellular metabolism, specifically within the mitochondria, where it catalyzes the conversion of isocitrate to alpha-ketoglutarate while reducing NADP+ to NADPH. Research into IDH2 has gained significant attention due to its involvement in various metabolic processes and its implications in cancer biology. Mutations in IDH2 are frequently associated with several types of cancer, particularly acute myeloid leukemia (AML) and gliomas, where they result in the production of 2-hydroxyglutarate (2-HG), an oncometabolite that disrupts cellular differentiation and contributes to tumorigenesis. The exploration of IDH2 as a therapeutic target has led to the development of IDH2 inhibitors, aiming to reverse the effects of these mutations and restore normal metabolic function. Additionally, the expression patterns of IDH2 and its role in regulating oxidative stress and cell survival add layers of complexity to its function in health and disease. Given its pivotal role in metabolic pathways and tumor biology, the recombinant protein study of IDH2 is essential for advancing our understanding of cancer metabolism and for developing novel therapeutic strategies that could improve outcomes for patients with IDH2-related malignancies.
