| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NDUFS5 |
| Uniprot No | O43920 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-106aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMPFLDIQKRFGLNIDRWLTIQSGEQPY KMAGRCHAFEKEWIECAHGIGYTRAEKECKIEYDDFVECLLRQKTMRRAG TIRKQRDKLIKEGKYTPPPHHIGKGEPRP |
| 预测分子量 | 15 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篇关于NDUFS5重组蛋白的参考文献摘要(模拟学术文献，部分信息为示例性整合)：
---
1. **文献名称**: "Functional characterization of recombinant human NDUFS5 subunit of mitochondrial complex I"
**作者**: Smith J, et al.
**摘要**: 本研究成功在大肠杆菌中表达并纯化了重组人源NDUFS5蛋白，验证其与线粒体复合物I其他亚基的相互作用。通过体外重组实验，证实NDUFS5对复合物I的组装及NADH脱氢酶活性具有关键调控作用。
---
2. **文献名称**: "NDUFS5 mutations impair mitochondrial complex I assembly: Insights from yeast complementation assays"
**作者**: Tanaka K, et al.
**摘要**: 通过构建NDUFS5基因敲除酵母模型，表达重组人NDUFS5蛋白进行功能回补。研究发现，NDUFS5的C端结构域对复合物I的稳定性至关重要，其突变导致活性氧(ROS)水平显著升高，提示与线粒体疾病的相关性。
---
3. **文献名称**: "Crystallographic analysis of the NDUFS5-NDUFS7 subcomplex in human respiratory chain"
**作者**: Lee S, et al.
**摘要**: 利用重组表达技术获得NDUFS5与NDUFS7的异源二聚体，并通过X射线晶体学解析其3D结构。发现两个亚基通过疏水相互作用形成稳定界面，为设计靶向复合物I的抑制剂提供结构基础。
---
注：以上文献信息为基于领域知识的示例性模拟，实际引用需以真实发表论文为准。建议通过PubMed或Web of Science以关键词“NDUFS5 recombinant”或“NDUFS5 complex I”检索最新文献。
NDUFS5 (NADH:ubiquinone oxidoreductase subunit S5) is a critical component of mitochondrial complex I, the largest enzyme complex in the electron transport chain (ETC). Complex I facilitates the transfer of electrons from NADH to ubiquinone, coupled with proton translocation across the mitochondrial inner membrane, driving ATP synthesis. As a nuclear-encoded subunit, NDUFS5 is essential for the structural stability and catalytic activity of complex I. It forms part of the core hydrophobic subunit cluster, contributing to the coordination of iron-sulfur clusters necessary for electron transfer.
Mutations or deficiencies in NDUFS5 are linked to mitochondrial disorders, particularly Leigh syndrome, a severe neurodegenerative condition characterized by developmental regression, motor dysfunction, and lactic acidosis. These pathologies stem from impaired oxidative phosphorylation (OXPHOS), leading to cellular energy deficits and ROS accumulation. Studies using animal models and patient-derived cells have highlighted NDUFS5's role in maintaining complex I assembly and metabolic homeostasis.
Recombinant NDUFS5 protein is engineered using heterologous expression systems (e.g., *E. coli* or mammalian cell lines) to study its biochemical properties, interactions with other complex I subunits, and the functional impact of disease-associated mutations. This tool enables researchers to dissect molecular mechanisms underlying complex I dysfunction and explore therapeutic strategies, such as gene therapy or small-molecule chaperones, to restore OXPHOS activity. Its applications extend to drug screening platforms and structural biology, aiding in the design of targeted therapies for mitochondrial diseases.
In summary, NDUFS5 recombinant protein serves as a vital resource for advancing our understanding of mitochondrial biology and addressing the unmet medical needs in complex I-related disorders.
×
