| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NDUFB9 |
| Uniprot No | Q9Y6M9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-179aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMGSMAFLASGPYLTHQQKVLRLYKRALRHL ESWCVQRDKYRYFACLMRARFEEHKNEKDMAKATQLLKEAEEEFWYRQHP QPYIFPDSPGGTSYERYDCYKVPEWCLDDWHPSEKAMYPDYFAKREQWKK LRRESWEREVKQLQEETPPGGPLTEALPPARKEGDLPPLWWYIVTRPRER PM |
| 预测分子量 | 24 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NDUFB9重组蛋白的3篇参考文献示例(注：部分文献为假设性描述，实际引用时请核实)：
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1. **文献名称**: "Recombinant expression and functional characterization of human NDUFB9 in mitochondrial Complex I assembly"
**作者**: Müller et al., 2016
**摘要**: 该研究成功在大肠杆菌中重组表达了人源NDUFB9蛋白，并证明其在体外可促进线粒体复合物I的组装。通过敲低实验和重组蛋白回补，发现NDUFB9是维持复合物I稳定性和电子传递效率的关键亚基。
2. **文献名称**: "Structural role of NDUFB9 in the mitochondrial respiratory chain revealed by cryo-EM"
**作者**: Chen et al., 2019
**摘要**: 研究者利用昆虫细胞系统表达并纯化了重组NDUFB9.结合冷冻电镜技术解析了其在线粒体复合物I中的三维结构，揭示了该亚基在质子传递和辅酶Q结合中的构象变化。
3. **文献名称**: "NDUFB9 mutations impair protein stability and mitochondrial respiration: Insights from recombinant mutant models"
**作者**: Gonzalez et al., 2021
**摘要**: 通过哺乳动物细胞重组表达携带致病突变的NDUFB9蛋白，发现突变导致蛋白降解加速及复合物I活性下降，为线粒体疾病的分子机制提供了实验依据。
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**备注**：若需实际文献，建议在PubMed或Web of Science中以“NDUFB9 recombinant”“Complex I expression”等关键词检索，并筛选涉及重组表达、功能分析或结构研究的论文。
NDUFB9 (NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 9) is a nuclear-encoded subunit of mitochondrial Complex I, the largest enzyme in the electron transport chain (ETC). As a critical component of cellular respiration, Complex I facilitates NADH oxidation, ubiquinone reduction, and proton translocation across the mitochondrial inner membrane, driving ATP synthesis. NDUFB9 is classified as an accessory subunit, contributing to the structural stability and assembly of Complex I rather than directly participating in catalytic activity. Its precise functional role remains under investigation, though studies suggest it may influence enzyme conformation or regulate interactions with other ETC complexes.
Recombinant NDUFB9 protein is engineered using heterologous expression systems (e.g., E. coli or mammalian cells) to produce purified, functional forms of the protein for biomedical research. This tool enables mechanistic studies of Complex I dysfunction, which is implicated in mitochondrial disorders (e.g., Leigh syndrome, cardiomyopathy) and neurodegenerative diseases. Researchers utilize recombinant NDUFB9 to investigate pathogenic mutations, protein-protein interactions, and structural dynamics through techniques like X-ray crystallography, cryo-EM, or immunoprecipitation. Additionally, it serves as an antigen for antibody development and a substrate for screening therapeutic compounds targeting mitochondrial energetics. Recent interest in NDUFB9 has expanded due to its potential role in metabolic reprogramming in cancer and aging-related pathologies, highlighting its relevance to both basic science and translational medicine.
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