| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | NDUFA12 |
| Uniprot No | Q9UI09 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-145aa |
| 氨基酸序列 | MELVQVLKRGLQQITGHGGLRGYLRVFFRTNDAKVGTLVGEDKYGNKYYEDNKQFFGRHRWVVYTTEMNGKNTFWDVDGSMVPPEWHRWLHSMTDDPPTTKPLTARKFIWTNHKFNVTGTPEQYVPYSTTRKKIQEWIPPSTPYK |
| 预测分子量 | 44.1 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NDUFA12重组蛋白的3篇代表性文献概览(内容基于学术背景模拟生成，非真实文献)：
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1. **文献名称**：*Recombinant expression and functional characterization of human NDUFA12 in mitochondrial complex I assembly*
**作者**：Smith A, et al.
**摘要**：本研究通过在大肠杆菌系统中重组表达人源NDUFA12蛋白，并利用体外复性技术将其与线粒体复合物I其他亚基重组，证实NDUFA12对复合物I的结构稳定性及NADH脱氢酶活性具有关键作用，为相关遗传性线粒体疾病的机制研究提供基础。
2. **文献名称**：*NDUFA12 mutations impair oxidative phosphorylation: Insights from yeast complementation assays using recombinant protein*
**作者**：Chen L, et al.
**摘要**：作者构建了携带人类NDUFA12致病突变的酵母重组蛋白模型，通过表型互补实验发现，特定突变导致NDUFA12无法整合至复合物I中，显著降低细胞呼吸效率，揭示了NDUFA12缺陷引发能量代谢障碍的分子机制。
3. **文献名称**：*Structural analysis of NDUFA12 within mammalian complex I by cryo-EM*
**作者**：Wang Y, et al.
**摘要**：利用冷冻电镜技术解析了包含重组NDUFA12蛋白的哺乳动物线粒体复合物I高分辨率结构，明确了NDUFA12在跨膜结构域与辅酶Q结合位点间的空间定位，为靶向复合物I的药物设计提供结构依据。
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**注**：以上文献为示例性内容，实际研究中请通过PubMed、Google Scholar等平台检索真实发表的论文。如需具体文献指引，建议结合研究主题(如疾病关联、蛋白互作等)进一步筛选。
NDUFA12 (NADH:ubiquinone oxidoreductase subunit A12) is a nuclear-encoded component of mitochondrial Complex I, the largest enzyme in the electron transport chain (ETC). As part of the NADH dehydrogenase complex, it contributes to oxidative phosphorylation by facilitating electron transfer from NADH to ubiquinone, coupled with proton translocation across the mitochondrial inner membrane. The NDUFA12 protein is anchored to the membrane domain of Complex I and plays a structural role in maintaining the enzyme’s stability and activity.
Mutations in the NDUFA12 gene (located on chromosome 12q13.2) are linked to mitochondrial disorders, particularly Leigh syndrome, a severe neurodegenerative condition characterized by developmental regression and metabolic acidosis. Such mutations impair Complex I assembly or function, leading to reduced ATP production, oxidative stress, and neuronal degeneration. Studying NDUFA12 helps elucidate mechanisms of mitochondrial dysfunction and associated pathologies.
Recombinant NDUFA12 protein is produced via heterologous expression systems (e.g., E. coli or mammalian cells) for functional studies. Its recombinant form enables in vitro analysis of protein-protein interactions, enzymatic activity, and structural contributions to Complex I. Researchers also use it to investigate disease-causing mutations, screen therapeutic compounds, or develop gene therapies. Purification typically involves affinity tagging (e.g., His-tag) and chromatographic techniques. As mitochondrial diseases lack curative treatments, recombinant NDUFA12 serves as a critical tool for advancing diagnostic and therapeutic strategies targeting ETC deficiencies.
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