Analytical Data
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基因名
NDUFB10
- Application
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别名
Complex I-PDSW
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种属
Human
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表达系统
E. coli
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标签
N- GST
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O96000
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表达区间
1-172aa
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分子量
47.8 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
NDUFB10, a nuclear-encoded subunit of the mitochondrial NADH:ubiquinone oxidoreductase complex (Complex I), plays a crucial role in cellular energy metabolism. This protein is integral to the electron transport chain, facilitating the transfer of electrons from NADH to ubiquinone, ultimately supporting ATP production through oxidative phosphorylation. Mutations in the NDUFB10 gene have been linked to various mitochondrial diseases, characterized by impaired energy production and associated with symptoms such as muscle weakness, neurological deficits, and metabolic dysfunction. The study of NDUFB10 recombinant protein is significant for understanding the molecular mechanisms underlying these mitochondrial disorders. By expressing and purifying recombinant NDUFB10, researchers aim to investigate its structure, function, and interaction with other Complex I components, thereby gaining insights into its role in mitochondrial bioenergetics. Furthermore, developing a reliable supply of this protein opens avenues for potential therapeutic strategies aimed at correcting the functional deficits caused by NDUFB10 mutations. Ultimately, advancing our understanding of NDUFB10's biochemical properties and its contributions to mitochondrial function may lead to improved diagnostic tools and targeted treatments for mitochondrial diseases.
