Analytical Data
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Gene name
IDH3B
- Application
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Alternative Names
Isocitric dehydrogenase subunit betaNAD(+)-specific ICDH subunit beta
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43837
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Expression Region
35-385aa
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Molecular Weight
65.8 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
IDH3B (Isocitrate Dehydrogenase 3 Beta) is a critical enzyme in the citric acid cycle, playing a vital role in cellular energy production by catalyzing the oxidative decarboxylation of isocitrate to alpha-ketoglutarate. Recent studies have highlighted the significance of IDH3B in various metabolic processes and its potential links to several diseases, including cancer and neurodegenerative disorders. Mutations or alterations in IDH3B expression have been associated with disrupted metabolic pathways, leading to oncogenic transformations and impaired cellular functions. Given its essential role, researchers have been increasingly focused on the enzymatic properties, structural biology, and regulatory mechanisms of IDH3B, aiming to elucidate its function in health and disease. Additionally, the development of IDH3B recombinant proteins has enabled advanced studies into its enzymatic activity and interaction with potential inhibitors, providing insights that may lead to therapeutic strategies targeting metabolic dysregulation. The ongoing research into IDH3B not only contributes to our understanding of fundamental metabolic processes but also holds promise for novel interventions in related pathological conditions.











