纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | NDUFB5 |
Uniprot No | O43674 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 94-189aa |
氨基酸序列 | GQAELAEIPEGYVPEHWEYYKHPISRWIARNFYDSPEKIYERTMAVLQIEAEKAELRVKELEVRKLMHVRGDGPWYYYETIDKELIDHSPKATPDN |
预测分子量 | 27.5 kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于NDUFB5重组蛋白的参考文献示例(注:部分文献信息为模拟虚构,仅作参考示例):
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1. **文献名称**: *Recombinant expression and functional characterization of human NDUFB5 in mitochondrial complex I assembly*
**作者**: Smith JL, et al.
**期刊**: Biochimica et Biophysica Acta (BBA) - Bioenergetics
**摘要**: 本研究在大肠杆菌中成功表达并纯化了重组人源NDUFB5蛋白,通过体外重构实验证明其与复合物I核心亚基的相互作用,揭示了NDUFB5在复合物I组装中的关键作用。
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2. **文献名称**: *Structural insights into NDUFB5 within the mitochondrial respiratory chain*
**作者**: Tanaka K, et al.
**期刊**: Journal of Molecular Biology
**摘要**: 利用X射线晶体学解析了重组NDUFB5蛋白的晶体结构,结合分子动力学模拟,提出其在电子传递链中参与质子转移的分子机制,为复合物I功能异常相关疾病提供结构基础。
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3. **文献名称**: *NDUFB5 mutations impair mitochondrial function: Analysis via recombinant protein rescue in patient-derived cells*
**作者**: Lee S, et al.
**期刊**: Human Molecular Genetics
**摘要**: 通过构建NDUFB5突变体重组蛋白,在患者细胞中验证其功能缺陷,发现重组野生型NDUFB5可恢复复合物I活性,表明其突变与线粒体脑肌病的直接关联。
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4. **文献名称**: *Targeting NDUFB5 in cancer: Recombinant protein-based screening identifies novel inhibitors*
**作者**: Zhang Y, et al.
**期刊**: Cellular Signalling
**摘要**: 研究利用重组NDUFB5蛋白进行高通量药物筛选,发现小分子抑制剂可特异性干扰其与复合物I的结合,为靶向线粒体代谢的癌症治疗策略提供新方向。
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**备注**:以上文献为示例性内容,实际研究中建议通过PubMed、Web of Science等数据库检索具体文献。
**Background of NDUFB5 Recombinant Protein**
NDUFB5 (NADH:ubiquinone oxidoreductase subunit B5) is a nuclear-encoded component of mitochondrial complex I, the largest enzyme in the electron transport chain (ETC). Complex I catalyzes NADH oxidation, transfers electrons to ubiquinone, and contributes to proton gradient formation for ATP synthesis. As part of the ETC, NDUFB5 localizes to the mitochondrial inner membrane and plays a structural or regulatory role in complex I assembly, stability, or electron transfer activity.
Recombinant NDUFB5 protein is produced using expression systems (e.g., *E. coli* or mammalian cells*) to enable functional studies. Its production typically involves cloning the *NDUFB5* gene into expression vectors, followed by purification via affinity tags (e.g., His-tag). This recombinant form allows researchers to investigate NDUFB5's interactions with other complex I subunits, its role in ETC dysfunction, or its contribution to mitochondrial disorders.
Defects in complex I, including mutations in *NDUFB5*, are linked to metabolic and neurodegenerative diseases, such as Leigh syndrome, Parkinson’s disease, and cardiomyopathies. Recombinant NDUFB5 serves as a tool for studying disease mechanisms, screening therapeutic compounds, or developing antibodies. Additionally, structural analyses using recombinant protein help map binding domains and post-translational modifications critical for complex I activity.
In summary, NDUFB5 recombinant protein bridges molecular biology and clinical research, offering insights into mitochondrial energy metabolism and its pathophysiological disruptions.
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