Analytical Data
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Gene name
IDH3G
- Application
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Alternative Names
Isocitric dehydrogenase subunit gammaNAD(+)-specific ICDH subunit gamma
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P51553
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Expression Region
40-393aa
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Molecular Weight
54.8 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
IDH3G (Isocitrate Dehydrogenase 3 gamma) is an important enzyme in the tricarboxylic acid (TCA) cycle, playing a crucial role in cellular metabolism by catalyzing the oxidative decarboxylation of isocitrate to α-ketoglutarate. This enzymatic activity not only contributes to energy production but also influences various biosynthetic pathways and cellular signaling processes. Research into IDH3G has gained particular interest due to its potential implications in cancer biology and metabolic disorders. Abnormalities in the IDH enzymes, particularly in their isoforms, have been linked to altered metabolic states in tumors, which can promote tumorigenesis and affect treatment responses. Recent advances in molecular biology techniques have facilitated the recombination and expression of IDH3G, allowing scientists to produce recombinant proteins for detailed biochemical analysis. This includes investigating the enzyme's structural properties, substrate specificity, and regulatory mechanisms. Understanding the functional dynamics of IDH3G through recombinant protein studies could pave the way for novel therapeutic strategies targeting metabolic pathways in cancer and other diseases, making it a significant focus of ongoing research in the fields of biochemistry and molecular medicine.
