Analytical Data
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基因名
IDH3G
- Application
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别名
Isocitric dehydrogenase subunit gammaNAD(+)-specific ICDH subunit gamma
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种属
Human
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P51553
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表达区间
40-393aa
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分子量
54.8 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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.
