Analytical Data
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基因名
NDUFB2
- Application
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别名
CI-AGGG; Complex I-AGGG; mitochondrial; NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 2; NADH-ubiquinone oxidoreductase AGGG subunit; NDUB2_HUMAN; NDUFB2
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
O95178
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表达区间
34-105 aa
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氨基酸序列
AGGGVHI EPRYRQFPQL TRSQVFQSEF FSGLMWFWIL WRFWHDSEEV LGHFPYPDPS QWTDEELGIP PDDED
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分子量
12.0 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
NDUFB2, a crucial subunit of the mitochondrial NADH:ubiquinone oxidoreductase (Complex I), plays a significant role in cellular energy metabolism within the oxidative phosphorylation pathway. This protein is integral to the electron transport chain, facilitating the transfer of electrons from NADH to ubiquinone, ultimately contributing to ATP production. Mutations in NDUFB2 have been linked to various mitochondrial diseases, which can result in severe cellular dysfunction and a wide array of clinical manifestations. The study of recombinant NDUFB2 protein is essential for understanding its structure and function, as well as its interactions with other Complex I components. By expressing and purifying this protein, researchers can elucidate the mechanistic pathways involved in mitochondrial bioenergetics, assess the impact of genetic variations, and develop potential therapeutic strategies for disorders associated with Complex I deficiencies. Furthermore, investigating the biochemical properties of recombinant NDUFB2 provides insights into the design of targeted interventions aimed at ameliorating mitochondrial dysfunction, highlighting its relevance in both basic and applied biomedical research.
