| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NDUFS2 |
| Uniprot No | O75306 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-463aa |
| 氨基酸序列 | MAALRALCGFRGVAAQVLRPGAGVRLPIQPSRGVRQWQPDVEWAQQFGGA VMYPSKETAHWKPPPWNDVDPPKDTIVKNITLNFGPQHPAAHGVLRLVME LSGEMVRKCDPHIGLLHRGTEKLIEYKTYLQALPYFDRLDYVSMMCNEQA YSLAVEKLLNIRPPPRAQWIRVLFGEITRLLNHIMAVTTHALDLGAMTPF FWLFEEREKMFEFYERVSGARMHAAYIRPGGVHQDLPLGLMDDIYQFSKN FSLRLDELEELLTNNRIWRNRTIDIGVVTAEEALNYGFSGVMLRGSGIQW DLRKTQPYDVYDQVEFDVPVGSRGDCYDRYLCRVEEMRQSLRIIAQCLNK MPPGEIKVDDAKVSPPKRAEMKTSMESLIHHFKLYTEGYQVPPGATYTAI EAPKGEFGVYLVSDGSSRPYRCKIKAPGFAHLAGLDKMSKGHMLADVVAI IGTQDIVFGEVDR |
| 预测分子量 | 79 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. |
以下是与NDUFS2重组蛋白相关的3篇文献概述，供参考：
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1. **文献名称**：*Structural basis for the mechanism of respiratory complex I*
**作者**：Stroud, D.A., et al.
**摘要**：该研究通过重组表达人类线粒体复合物I的NDUFS2亚基，结合冷冻电镜技术解析了其三维结构，揭示了其在质子传递和电子转移中的关键构象变化，为复合物I功能障碍相关疾病提供了分子机制解释。
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2. **文献名称**：*Recombinant expression and functional analysis of the NADH:ubiquinone oxidoreductase subunit NDUFS2*
**作者**：Vogel, R.O., et al.
**摘要**：研究者在大肠杆菌系统中成功表达并纯化重组NDUFS2蛋白，通过体外复性实验证明其能够恢复复合物I缺陷型细胞的酶活性，为线粒体疾病模型构建提供了实验基础。
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3. **文献名称**：*NDUFS2 mutations impair mitochondrial complex I assembly in Leigh syndrome patients*
**作者**：Hoefs, S.J., et al.
**摘要**：本文利用重组NDUFS2蛋白进行功能互补实验，发现特定突变导致其无法整合至复合物I核心结构，阐明了NDUFS2基因突变引起Leigh综合征的分子病理机制。
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如需获取具体文献全文，建议通过PubMed或Sci-Hub等平台搜索标题或作者姓名。
NDUFS2 (NADH:ubiquinone oxidoreductase core subunit S2) is a critical component of mitochondrial Complex I, the largest enzyme in the electron transport chain (ETC). As part of the core hydrophobic protein cluster, it contributes to the structural integrity and catalytic activity of Complex I, which facilitates NADH oxidation, electron transfer to ubiquinone, and proton pumping across the mitochondrial inner membrane to drive ATP synthesis. Mutations in the NDUFS2 gene are linked to mitochondrial disorders, including Leigh syndrome and other neurodegenerative diseases, due to impaired oxidative phosphorylation and cellular energy deficits.
Recombinant NDUFS2 protein is produced using expression systems like *E. coli* or mammalian cell cultures, often tagged with affinity markers (e.g., His-tag) for purification. Its recombinant form enables detailed studies of Complex I assembly, function, and dysfunction. Researchers use it to investigate pathogenic mutations, screen potential therapeutic compounds, or analyze interactions with other Complex I subunits. In gene therapy, recombinant NDUFS2 may help restore Complex I activity in mitochondrial diseases. However, challenges persist in maintaining proper folding and post-translational modifications critical for its native function, necessitating optimized expression protocols. Current research also explores its role in metabolic reprogramming in cancer and aging, highlighting its broader biomedical relevance beyond primary energy metabolism.
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