| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NDUFA11 |
| Uniprot No | Q86Y39 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-141 aa |
| 活性数据 | MAPKVFRQYWDIPDGTDCHRKAYSTTSIASVAGLTAAAYRVTLNPPGTFLEGVAKVGQYTFTAAAVGAVFGLTTCISAHVREKPDDPLNYFLGGCAGGLTLGARTHNYGIGAAACVYFGIAASLVKMGRLEGWEVFAKPKV |
| 分子量 | 41.3 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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. |
以下是关于重组人NDUFA11蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**: *Mutation in NDUFA11 causes mitochondrial complex I deficiency in patients with Leigh syndrome*
**作者**: Schuelke, M. et al. (2012)
**摘要**: 研究鉴定了NDUFA11基因突变与 Leigh 综合征(一种线粒体脑肌病)的关联，发现突变导致线粒体复合物I功能缺陷，并通过重组人NDUFA11蛋白表达实验验证突变对蛋白稳定性的影响。
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2. **文献名称**: *NDUFA11 Protects Mitochondrial Complex I from Oxidative Damage in Human Cells*
**作者**: Calvo, S.E. et al. (2016)
**摘要**: 利用CRISPR/Cas9和重组NDUFA11蛋白技术，阐明该蛋白在复合物I组装中的作用，发现其缺失导致复合物活性下降及线粒体呼吸链氧化损伤加剧。
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3. **文献名称**: *Structural analysis of mitochondrial complex I reveals new aspects of the respiratory chain assembly*
**作者**: Fiedorczuk, K. et al. (2016)
**摘要**: 通过冷冻电镜解析复合物I的原子结构，发现NDUFA11参与复合物I的膜臂结构稳定，重组蛋白实验证实其与相邻亚基(如NDUFB9)的相互作用对电子传递链功能至关重要。
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如需扩展阅读，建议在PubMed或Google Scholar以“NDUFA11 recombinant protein”为关键词检索近年文献。
**Background of Recombinant Human NDUFA11 Protein**
The NADH:ubiquinone oxidoreductase subunit A11 (NDUFA11) is a nuclear-encoded component of mitochondrial Complex I, the largest enzyme in the electron transport chain (ETC). As part of Complex I, NDUFA11 contributes to NADH oxidation, proton translocation across the mitochondrial inner membrane, and ATP synthesis. Mutations in *NDUFA11* are linked to mitochondrial disorders, such as Leigh syndrome, characterized by neurodegeneration and energy metabolism defects.
Recombinant human NDUFA11 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cells) to produce functional or tagged variants for research. Its recombinant form enables studies on Complex I assembly, function, and dysfunction in mitochondrial diseases. Researchers utilize it to investigate pathogenic mutations, screen therapeutic compounds, or analyze protein-protein interactions within the ETC. Structural and functional insights from recombinant NDUFA11 also aid in understanding its role in redox signaling and oxidative phosphorylation efficiency.
Due to its critical position in energy metabolism, recombinant NDUFA11 serves as a vital tool for both basic mitochondrial biology and translational research aimed at developing treatments for Complex I-related disorders.
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