| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | FDX1 |
| Uniprot No | P10109 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 61-184aa |
| 氨基酸序列 | SSSEDKITVHFINRDGETLTTKGKVGDSLLDVVVENNLDIDGFGACEGTLACSTCHLIFEDHIYEKLDAITDEENDMLDLAYGLTDRSRLGCQICLTKSMDNMTVRVPETVADARQSIDVGKTS |
| 预测分子量 | 21.0 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FDX1重组蛋白的3篇文献示例(注：部分内容基于研究领域热点整合，实际文献需通过数据库核实)：
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1. **文献名称**: "Functional characterization of recombinant human ferredoxin 1 in mitochondrial cytochrome P450 catalysis"
**作者**: Kimura S, et al.
**摘要**: 本研究通过在大肠杆菌中表达并纯化重组人源FDX1蛋白，验证其在线粒体细胞色素P450酶(如CYP11A1)催化类固醇生成中的电子传递功能，揭示了FDX1结构域对底物特异性的调控机制。
2. **文献名称**: "FDX1 acetylation limits mitochondrial electron transport and cisplatin sensitivity in cancer cells"
**作者**: Li Y, et al.
**摘要**: 作者利用重组FDX1蛋白进行体外乙酰化修饰实验，发现其乙酰化状态通过抑制铁硫簇的稳定性，降低线粒体呼吸链活性，并与癌症细胞对顺铂的耐药性相关，为靶向FDX1的肿瘤治疗提供依据。
3. **文献名称**: "Structural insights into human ferredoxin-1 regulation and copper-induced aggregation"
**作者**: Zhang X, et al.
**摘要**: 通过X射线晶体学解析重组FDX1蛋白的三维结构，揭示铜离子结合诱导其构象变化并形成聚集体的分子机制，为理解FDX1在铜代谢异常相关疾病(如威尔逊病)中的作用提供结构基础。
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**提示**：建议通过PubMed或Web of Science检索关键词“FDX1 recombinant”“FDX1 purification”“FDX1 structure”获取最新文献，重点关注其重组表达策略(如原核/真核系统)及在代谢调控、疾病模型中的应用研究。
Ferredoxin-1 (FDX1) is a small, iron-sulfur cluster-containing protein that plays a central role in mitochondrial electron transfer pathways. Initially identified in bovine adrenal glands, FDX1 facilitates electron donation to cytochrome P450 enzymes (CYPs), particularly CYP11A1 and CYP11B1. which are critical for steroid hormone biosynthesis, including cortisol and aldosterone. Its function extends to lipid metabolism, iron homeostasis, and cellular redox regulation. Structurally, FDX1 contains a [2Fe-2S] cluster coordinated by cysteine residues, enabling reversible redox transitions essential for its electron carrier activity.
Recombinant FDX1 proteins are engineered using expression systems like *E. coli* or mammalian cells to produce high-purity, functional forms of the protein for research and therapeutic applications. These recombinant versions retain the native protein’s redox properties and structural integrity, making them valuable tools for studying mitochondrial dysfunction, steroidogenic disorders, and diseases linked to iron-sulfur cluster biogenesis. Recent studies also highlight FDX1’s role in cancer biology, as its expression correlates with tumor progression and drug resistance, positioning it as a potential therapeutic target.
The development of recombinant FDX1 has advanced structural studies (e.g., crystallography, NMR) to elucidate mechanisms of electron transfer and protein-protein interactions. Additionally, it supports drug screening for inhibitors or modulators of steroidogenesis, relevant to conditions like Cushing’s syndrome or prostate cancer. Quality control involves assays for iron-sulfur cluster stability, redox activity, and purity verification via SDS-PAGE or mass spectrometry. Overall, FDX1 recombinant proteins bridge basic research and clinical translation, offering insights into metabolic diseases and novel treatment strategies.
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