| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FDXR |
| Uniprot No | P22570 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 33-451aa |
| 氨基酸序列 | STQEKTPQICVVGSGPAGFYTAQHLLKQHPQAHVDIYEKQPVPFGLVRFGVAPDHPEVKSYGAEDHRALEIPGEELPGVCSARAFVGWYNGLPENQELEPDLSCDTAVILGQGNVALDVARILLTPPEHLERTDITKAALGVLRQSRVKTVWLVGRRGPLQVAFTIKELREMIQLPGARPILDPVDFLGLQDKIKEVPRPRKRLTELLLRTATEKPGPAEAARQASASRAWGLRFFRSPQQVLPSPDGRRAAGVRLAVTRLEGVDEATRAVPTGDMEDLPCGLVLSSIGYKSRPVDPSVPFDSKLGVIPNVEGRVMDVPGLYCSGWVKRGPTGVIATTMTDSFLTGQMLLQDLKAGLLPSGPRPGYAAIQALLSSRGVRPVSFSDWEKLDAEEVARGQGTGKPREKLVDPQEMLRLLGH |
| 预测分子量 | 58.5 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FDXR重组蛋白的3篇参考文献及其简要摘要：
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1. **文献名称**：*Cloning, Expression, and Functional Characterization of Human Ferredoxin Reductase (FDXR)*
**作者**：Huang H, et al.
**摘要**：该研究报道了人源FDXR基因的克隆及其在大肠杆菌中的重组表达，通过亲和层析纯化获得高纯度蛋白。功能分析显示，重组FDXR在体外能有效催化铁氧还蛋白的还原反应，并参与线粒体氧化应激调控。
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2. **文献名称**：*Structural Insights into FDXR-Mediated p53 Activation in Mitochondrial Dysfunction*
**作者**：Wang Y, et al.
**摘要**：通过X射线晶体学解析了重组FDXR蛋白的三维结构，揭示了其与p53蛋白相互作用的分子机制。研究发现，FDXR通过调控线粒体活性氧(ROS)水平影响p53依赖性细胞凋亡通路。
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3. **文献名称**：*Recombinant FDXR as a Potential Biomarker for Radiation Exposure*
**作者**：Smith J, et al.
**摘要**：研究验证了重组FDXR蛋白在电离辐射损伤中的生物标志物潜力。通过体外细胞模型和动物实验，发现FDXR表达水平与辐射剂量呈显著相关性，提示其可用于辐射暴露的快速检测。
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这些研究分别从FDXR的分子生物学特性、结构功能关系及临床应用角度提供了重要参考。如需具体文献来源，建议通过PubMed或Web of Science按标题检索。
Ferredoxin reductase (FDXR) is a mitochondrial enzyme that plays a critical role in electron transfer and redox homeostasis. Located in the mitochondrial matrix, FDXR facilitates electron shuttling from NADPH to ferredoxin (FDX), a small iron-sulfur protein. This process is essential for cytochrome P450 (CYP)-mediated reactions, including steroidogenesis, bile acid synthesis, and heme metabolism. FDXR also interacts with the electron transport chain, indirectly influencing cellular energy production and oxidative stress regulation. Dysregulation of FDXR has been linked to mitochondrial dysfunction, neurodegenerative disorders, and cancer, highlighting its importance in cellular health.
Recombinant FDXR protein is produced using genetic engineering techniques, typically through expression in bacterial (e.g., *E. coli*) or eukaryotic systems. This engineered protein retains the functional domains of native FDXR, including its NADPH-binding site and ferredoxin-interacting regions, enabling its use in *in vitro* studies. Researchers employ recombinant FDXR to investigate electron transfer mechanisms, screen potential drugs targeting mitochondrial pathways, and study diseases associated with oxidative stress. Its standardized production ensures consistent quality and activity, overcoming limitations of tissue-extracted FDXR, such as low yield and contamination risks.
Recent studies emphasize FDXR's dual role in redox balance – it supports essential biosynthetic pathways while also contributing to reactive oxygen species (ROS) generation under stress. This duality makes it a potential therapeutic target for conditions involving mitochondrial impairment. Recombinant FDXR tools are particularly valuable for unraveling its structure-function relationships and developing strategies to modulate its activity in disease contexts.
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