| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NDUFS8 |
| Uniprot No | O00217 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 35-210 aa |
| 活性数据 | TYKYVN MQDPEMDMKS VTDRAARTLL WTELFRGLGM TLSYLFREPA TINYPFEKGP LSPRFRGEHA LRRYPSGEER CIACKLCEAI CPAQAITIEA EPRADGSRRT TRYDIDMTKC IYCGFCQEAC PVDAIVEGPN FEFSTETHEE LLYNKEKLLN NGDKWEAEIA ANIQADYLYR |
| 分子量 | 23.7 kDa |
| 蛋白标签 | His tag N-Terminus |
| 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. |
1. **"Structural insights into the role of human NDUFS8 in mitochondrial complex I assembly"**
- Author: Johnson, A. et al.
- 摘要：研究利用重组表达的人NDUFS8蛋白，通过冷冻电镜分析其在复合物I组装中的结构作用，揭示其与辅助蛋白的互作机制及突变导致的复合物I功能障碍。
2. **"Recombinant human NDUFS8 rescues cellular respiration defects in Leigh syndrome patient fibroblasts"**
- Author: Martinez-Ruiz, C. & Fernández-Vizarra, E.
- 摘要：通过在大肠杆菌中重组表达NDUFS8蛋白，验证其功能活性，并证明其可恢复复合物I缺陷细胞模型的线粒体呼吸功能，为基因治疗提供实验依据。
3. **"Characterization of recombinant human NDUFS8 mutations linked to mitochondrial encephalopathy"**
- Author: Gopalakrishnan, S. et al.
- 摘要：对与脑肌病相关的NDUFS8突变体进行重组表达和酶活分析，发现特定突变(如p.Arg102His)导致复合物I组装障碍和氧化磷酸化能力丧失。
4. **"Expression and purification of human NDUFS8 for functional studies of mitochondrial complex I"**
- Author: Lee, J. et al.
- 摘要：优化重组人NDUFS8蛋白在原核系统的表达与纯化流程，并证明其在体外重建复合物I活性中的必要性，为药物筛选提供工具。
(注：上述文献为示例，实际引用需以真实论文信息为准。)
NDUFS8 (NADH:ubiquinone oxidoreductase core subunit S8) is a critical nuclear-encoded component of mitochondrial Complex I (NADH dehydrogenase), the largest enzyme in the electron transport chain responsible for oxidizing NADH and transferring electrons to ubiquinone. As part of the iron-sulfur (Fe-S) cluster-binding module, the NDUFS8 protein plays an essential role in electron transfer and structural stability of Complex I. It localizes to the mitochondrial matrix and interacts with other subunits like NDUFV1 and NDUFS1 to form the catalytic core.
Mutations in the NDUFS8 gene (11q13.1) are linked to mitochondrial disorders, particularly Leigh syndrome, characterized by neurodegeneration, muscle weakness, and lactic acidosis due to defective oxidative phosphorylation. Recombinant human NDUFS8 protein, produced via heterologous expression systems (e.g., *E. coli* or mammalian cells), enables functional studies to dissect Complex I assembly, electron transport mechanisms, and pathogenic variants' effects. Researchers use it to restore Complex I activity in cellular models, screen therapeutic candidates, and analyze structural interactions through techniques like cryo-EM. Its recombinant form is also pivotal for developing biomarkers and gene therapies targeting mitochondrial diseases. Understanding NDUFS8's role provides insights into cellular energy metabolism and the pathobiology of mitochondrial dysfunction.
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