| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NDUFB4 |
| Uniprot No | O95168 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-87aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSFPKYK PSSLRTLPET LDPAEYNISP ETRRAQAERL AIRAQLKREY LLQYNDPNRR GLIENPALLR WAYARTINVY PNFRPTPKNS |
| 预测分子量 | 13 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3篇涉及NDUFB4重组蛋白研究的文献概览(注：文献为虚构示例，实际研究中可能存在相关主题的论文)：
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1. **文献名称**：*Recombinant NDUFB4 expression rescues mitochondrial complex I assembly in Leigh syndrome models*
**作者**：Chen L, et al.
**摘要**：本研究利用大肠杆菌表达系统成功制备了重组人源NDUFB4蛋白，并证明其在体外可恢复复合物I缺陷型细胞系的线粒体呼吸功能。通过质谱和免疫共沉淀分析，揭示了NDUFB4在复合物I亚基组装中的关键作用。
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2. **文献名称**：*Structural insights into NDUFB4 mutations linked to Parkinson's disease using recombinant protein crystallography*
**作者**：Gomez-Ruiz S, et al.
**摘要**：作者通过昆虫细胞表达系统获得高纯度NDUFB4重组蛋白，并解析其晶体结构(分辨率2.1Å)。研究发现，帕金森病相关突变位点(如R124L)会破坏NDUFFB4与相邻亚基NDUFA9的相互作用，导致复合物I稳定性下降。
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3. **文献名称**：*NDUFB4 recombinant protein attenuates oxidative stress in diabetic cardiomyopathy via modulating NAD+ metabolism*
**作者**：Wang Y, et al.
**摘要**：通过腺病毒介导的NDUFB4重组蛋白递送，实验证实其在糖尿病小鼠模型中显著改善心肌线粒体功能障碍。机制研究表明，NDUFB4通过维持NAD+/NADH平衡，抑制ROS过度生成，为代谢性疾病治疗提供新靶点。
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**提示**：实际文献可通过PubMed/Google Scholar检索关键词如：
`NDUFB4 recombinant expression`、`mitochondrial complex I assembly`、`NDUFB4 AND structural analysis`
建议结合具体研究领域(如神经退行性疾病、癌症代谢)进一步筛选。
NDUFB4 (NADH:ubiquinone oxidoreductase subunit B4) is a nuclear-encoded component of mitochondrial Complex I, the largest enzyme in the electron transport chain (ETC). As part of the ETC, Complex I facilitates NADH oxidation, proton translocation across the inner mitochondrial membrane, and ATP synthesis. NDUFB4 is classified as an accessory subunit, contributing to Complex I assembly, stability, and regulatory functions rather than direct catalytic activity. Its structure includes a conserved LYR motif, which is associated with iron-sulfur (Fe-S) cluster binding—a critical feature for ETC redox reactions.
Recombinant NDUFB4 protein is engineered using expression systems like *E. coli* or mammalian cell lines to produce purified, biologically active forms for research. This involves cloning the human NDUFB4 gene into expression vectors, followed by protein purification via affinity tags (e.g., His-tag). Recombinant versions enable studies on Complex I dysfunction linked to mitochondrial diseases, neurodegenerative disorders (e.g., Parkinson’s), and cancer. Mutations in Complex I subunits, including NDUFB4. are implicated in Leigh syndrome, cardiomyopathy, and metabolic deficiencies due to disrupted oxidative phosphorylation.
Researchers use recombinant NDUFB4 to investigate its role in mitochondrial dynamics, apoptosis, and reactive oxygen species (ROS) regulation. It also serves as an antigen for antibody development or a tool for drug screening targeting mitochondrial disorders. Structural studies of recombinant NDUFB4 help map interaction sites within Complex I, advancing therapeutic strategies to restore ETC efficiency. Its production supports precision medicine approaches for mitochondrial pathologies, emphasizing its relevance in both basic research and translational applications.
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