| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NDUFB10 |
| Uniprot No | O96000 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-172aa |
| 氨基酸序列 | MPDSWDKDVYPEPPRRTPVQPNPIVYMMKAFDLIVDRPVTLVREFIERQHAKNRYYYYHRQYRRVPDITECKEEDIMCMYEAEMQWKRDYKVDQEIINIMQDRLKACQQREGQNYQQNCIKEVEQFTQVAKAYQDRYQDLGAYSSARKCLAKQRQRMLQERKAAKEAAAATS |
| 预测分子量 | 47.8 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NDUFB10重组蛋白的3篇参考文献示例(文献信息为模拟虚构，仅供参考)：
1. **《重组NDUFB10蛋白在线粒体复合物I组装中的功能研究》**
- 作者：Smith J, et al.
- 摘要：本研究通过大肠杆菌表达系统成功重组了人源NDUFB10蛋白，并证明其在体外能促进线粒体复合物I的组装。实验表明，NDUFB10缺失会导致复合物I活性下降，重组蛋白的补充可部分恢复功能。
2. **《NDUFB10重组蛋白的晶体结构及其在氧化应激中的作用》**
- 作者：Zhang L, et al.
- 摘要：作者解析了NDUFB10重组蛋白的晶体结构，发现其通过C端结构域与复合物I其他亚基相互作用。进一步功能实验显示，NDUFB10的过表达可降低细胞活性氧(ROS)水平，提示其在氧化应激调控中的关键作用。
3. **《靶向NDUFB10重组蛋白的基因治疗在心肌病模型中的应用》**
- 作者：Kim H, et al.
- 摘要：利用腺病毒载体递送重组NDUFB10蛋白至NDUFB10缺陷的小鼠模型，显著改善了心肌细胞线粒体呼吸链功能，并缓解了心衰表型，为相关线粒体疾病的治疗提供了潜在策略。
4. **《NDUFB10的磷酸化修饰对其重组蛋白功能的影响》**
- 作者：Wang R, et al.
- 摘要：通过体外磷酸化实验，发现NDUFB10在Ser-56位点的磷酸化可增强其与复合物I核心亚基的结合能力。重组磷酸化突变体蛋白的活性分析揭示了该修饰对电子传递链效率的调控机制。
(注：以上文献为示例，实际研究中请通过学术数据库验证具体信息。)
NDUFB10 (NADH:ubiquinone oxidoreductase subunit B10) is a critical component of mitochondrial Complex I, the largest enzyme complex in the electron transport chain (ETC). As part of the nuclear DNA-encoded subunits of Complex I, NDUFB10 plays an essential role in maintaining the structural integrity and catalytic function of the enzyme. This protein localizes to the inner mitochondrial membrane, where it contributes to NADH oxidation, ubiquinone reduction, and proton translocation, processes vital for ATP synthesis. Mutations or dysregulation of NDUFB10 have been linked to mitochondrial disorders, neurodegenerative diseases, and cancer, highlighting its importance in cellular energy metabolism and homeostasis.
Recombinant NDUFB10 protein is produced using heterologous expression systems (e.g., E. coli or mammalian cell cultures) to enable functional and structural studies. Its recombinant form allows researchers to investigate Complex I assembly mechanisms, enzyme kinetics, and interactions with other ETC components under controlled conditions. This tool has become particularly valuable in modeling mitochondrial dysfunction, screening potential therapeutic compounds for metabolic diseases, and studying oxidative stress responses. Recent studies also explore its non-canonical roles, including potential involvement in hypoxia signaling and apoptosis regulation. However, challenges persist in maintaining the protein’s native conformation during recombinant production due to its hydrophobic nature and dependence on mitochondrial chaperones for proper folding. Ongoing optimization of expression and purification protocols aims to enhance its utility in both basic research and drug development pipelines targeting energy metabolism pathways.
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