| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NDUFAF4 |
| Uniprot No | Q9P032 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-175aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMGALVIR GIRNFNLENR AEREISKMKP SVAPRHPSTN SLLREQISLY PEVKGEIARK DEKLLSFLKD VYVDSKDPVS SLQVKAAETC QEPKEFRLPK DHHFDMINIK SIPKGKISIV EALTLLNNHK LFPETWTAEK IMQEYQLEQK DVNSLLKYFV TFEVEIFPPE DKKAIRSK |
| 预测分子量 | 23 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NDUFAF4重组蛋白的参考文献示例(注：文献信息为虚构示例，仅供格式参考)：
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1. **文献名称**: *NDUFAF4重组蛋白在复合物I组装中的功能研究*
**作者**: Zhang Y, et al.
**摘要**: 本研究通过在大肠杆菌中表达并纯化NDUFAF4重组蛋白，揭示其与线粒体复合物I亚基NDUFS1的相互作用，证明其在复合物I早期组装阶段的关键作用，并发现其缺失导致呼吸链功能缺陷。
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2. **文献名称**: *NDUFAF4突变体的重组表达与线粒体疾病机制分析*
**作者**: Wang L, et al.
**摘要**: 通过构建NDUFAF4致病突变体(如p.Arg72Trp)的重组蛋白模型，发现突变导致蛋白稳定性下降及复合物I组装受阻，为儿童线粒体脑肌病的分子机制提供了实验依据。
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3. **文献名称**: *NDUFAF4重组蛋白的晶体结构解析及其功能域研究*
**作者**: Tanaka K, et al.
**摘要**: 利用X射线晶体学解析了NDUFAF4重组蛋白的三维结构，确定了其C端结构域对复合物I辅助因子NDUFAF5的结合能力，为开发靶向药物提供了结构基础。
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4. **文献名称**: *重组NDUFAF4蛋白修复线粒体功能障碍的体外验证*
**作者**: Smith J, et al.
**摘要**: 在NDUFAF4缺陷的细胞模型中，外源性重组NDUFAF4蛋白成功恢复了复合物I活性和ATP合成能力，表明其在基因治疗中的潜在应用价值。
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**注意**：以上文献为示例，实际引用需根据具体研究通过学术数据库(如PubMed、Web of Science)检索真实文献。如需进一步协助定位真实文献，请提供更多研究背景或关键词。
NDUFAF4. also known as NADH:ubiquinone oxidoreductase complex assembly factor 4. is a nuclear-encoded mitochondrial protein critical for the assembly and stability of Complex I (NADH dehydrogenase) in the mitochondrial electron transport chain (ETC). This protein plays a chaperone-like role during the early stages of Complex I biogenesis, interacting with other assembly factors like NDUFAF3 to ensure proper subunit integration. Mutations in the NDUFAF4 gene are linked to mitochondrial disorders, particularly Leigh syndrome and other forms of mitochondrial Complex I deficiency, which manifest as severe neurological and metabolic dysfunction due to impaired cellular energy production.
Recombinant NDUFAF4 protein is engineered using heterologous expression systems (e.g., E. coli or mammalian cells) to study its structural and functional properties. Its production enables researchers to investigate molecular mechanisms underlying Complex I assembly defects, screen therapeutic candidates, or develop diagnostic tools for mitochondrial diseases. The recombinant form typically retains conserved domains essential for interactions with Complex I subunits, such as the LYR motif (a tripeptide sequence involved in iron-sulfur cluster binding), allowing in vitro reconstitution assays to mimic mitochondrial processes.
Studies using recombinant NDUFAF4 have highlighted its role in stabilizing subcomplexes during ETC maturation. Additionally, it serves as a tool to explore post-translational modifications or mutations affecting protein stability, providing insights into genotype-phenotype correlations in mitochondrial disorders. Despite challenges like protein solubility or proper folding in non-native systems, recombinant NDUFAF4 remains pivotal for advancing therapeutic strategies, including gene therapy or small-molecule chaperones targeting Complex I deficiencies.
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