Analytical Data
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Gene name
IDH2
- Application
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Alternative Names
IDH; IDP; ICD-M; IDHM; mNADP-IDH; Isocitrate dehydrogenase [NADP], mitochondrial; Oxalosuccinate decarboxylase
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Species
Human
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Source
E. coli
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Tag
N-His
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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
Ala40~Gln452
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Molecular Weight
50kDa
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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
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Protein Description
IDH2 (isocitrate dehydrogenase 2) is a crucial enzyme involved in the tricarboxylic acid (TCA) cycle, primarily located in the mitochondria, where it plays a vital role in cellular metabolism and energy production. Research has highlighted its significance in various metabolic pathways and its implications in cancer biology, particularly the role of IDH2 mutations in tumorigenesis. These mutations can lead to the production of 2-hydroxyglutarate, an oncometabolite that disrupts cellular processes and promotes tumorigenic activity. Moreover, IDH2 has been implicated in the regulation of reactive oxygen species (ROS) and mitochondrial function, positioning it as a potential therapeutic target for metabolic diseases and cancers. The study of IDH2 recombinant proteins is essential for understanding its enzymatic activity, structural properties, and regulatory mechanisms. Furthermore, generating and characterizing IDH2 recombinant proteins can facilitate drug discovery efforts aimed at developing specific inhibitors or modulators to combat IDH2-related malignancies. As such, extensive research into IDH2 recombinant proteins can provide insights into its cellular functions, the consequences of its mutations, and the potential for targeted therapies in oncology, making it a significant focus within cancer research and metabolic studies.
