Analytical Data
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基因名
NDUFB1
- Application
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别名
Complex I-MNLL;CI-MNLL;NADH-ubiquinone oxidoreductase MNLL subunit
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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
O75438
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表达区间
2-58 aa
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氨基酸序列
VNLLQIVRDHWVHVLVPMGFVIGCYLDRKSDERLTAFRNKSMLFKRELQPSEEVTWK
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分子量
33.7 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
NDUFB1, a critical subunit of the mitochondrial respiratory chain complex I, plays an essential role in aerobic energy production via oxidative phosphorylation. Mutations or deficiencies in the NDUFB1 gene are linked to a range of neurodegenerative disorders, characterized by impaired ATP synthesis and increased reactive oxygen species (ROS) production. This has generated significant interest in studying NDUFB1 to better understand mitochondrial dysfunction in various diseases. The recombinant protein of NDUFB1 can be produced in model organisms or expression systems, facilitating investigations into its structure, function, and interactions within the mitochondrial complex. By elucidating the biochemical properties and regulatory mechanisms of NDUFB1, researchers aim to uncover potential therapeutic targets and strategies for combating mitochondrial diseases. Additionally, advanced techniques such as cryo-electron microscopy and mass spectrometry are being employed to study the protein's conformation and dynamics in response to cellular stress. Overall, the research surrounding NDUFB1 recombinant protein not only enhances our understanding of mitochondrial bioenergetics but also provides insights into the molecular underpinnings of metabolic diseases, potentially guiding the development of novel interventions.
