| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CYP11A1 |
| Uniprot No | P05108 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-521aa |
| 氨基酸序列 | MLAKGLPPRSVLVKGCQTFLSAPREGLGRLRVPTGEGAGISTRSPRPFNE IPSPGDNGWLNLYHFWRETGTHKVHLHHVQNFQKYGPIYREKLGNVESVY VIDPEDVALLFKSEGPNPERFLIPPWVAYHQYYQRPIGVLLKKSAAWKKD RVALNQEVMAPEATKNFLPLLDAVSRDFVSVLHRRIKKAGSGNYSGDISD DLFRFAFESITNVIFGERQGMLEEVVNPEAQRFIDAIYQMFHTSVPMLNL PPDLFRLFRTKTWKDHVAAWDVIFSKADIYTQNFYWELRQKGSVHHDYRG ILYRLLGDSKMSFEDIKANVTEMLAGGVDTTSMTLQWHLYEMARNLKVQD MLRAEVLAARHQAQGDMATMLQLVPLLKASIKETLRLHPISVTLQRYLVN DLVLRDYMIPAKTLVQVAIYALGREPTFFFDPENFDPTRWLSKDKNITYF RNLGFGWGVRQCLGRRIAELEMTIFLINMLENFRVEIQHLSDVGTTFNLI LMPEKPISFTFWPFNQEATQQ |
| 预测分子量 | 87 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CYP11A1重组蛋白的3篇参考文献示例(内容基于公开研究整理，非真实文献，仅供参考格式)：
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1. **文献名称**: *"Functional expression of human cytochrome P450 CYP11A1 in Saccharomyces cerevisiae"*
**作者**: Lin D. et al.
**摘要**: 研究通过酵母表达系统成功重组表达了人源CYP11A1.验证其催化胆固醇转化为孕烯醇酮的活性，并用于类固醇生成途径的体外分析。
2. **文献名称**: *"Recombinant CYP11A1 characterization: Role of redox partners in catalytic efficiency"*
**作者**: Miller W.L. et al.
**摘要**: 探讨不同电子传递蛋白(如肾上腺皮质铁氧还蛋白)对重组CYP11A1酶活性的影响，揭示其依赖铁氧还蛋白还原酶系统的必要性。
3. **文献名称**: *"Crystal structure of human CYP11A1 bound to substrate cholesterol"*
**作者**: Strushkevich N. et al.
**摘要**: 通过杆状病毒-昆虫细胞系统表达并纯化CYP11A1.解析其与胆固醇结合的晶体结构，阐明底物识别及催化机制。
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如需查找真实文献，建议在PubMed或Google Scholar中搜索关键词 **"CYP11A1 recombinant expression"** 或 **"CYP11A1 purification"**。经典研究多集中于其酶学特性、结构解析及与疾病相关的突变分析。
CYP11A1 (cytochrome P450 family 11 subfamily A member 1), also known as cholesterol side-chain cleavage enzyme (P450scc), is a critical mitochondrial enzyme in steroid hormone biosynthesis. It catalyzes the first and rate-limiting step in steroidogenesis: the conversion of cholesterol to pregnenolone by cleaving its side chain. This reaction occurs in steroidogenic tissues, including the adrenal glands, gonads, and placenta, and is essential for producing glucocorticoids, mineralocorticoids, and sex hormones. The enzyme functions as part of a multi-component electron transport system, relying on interactions with ferredoxin (FDX1) and ferredoxin reductase (FDXR) to facilitate its catalytic activity.
Recombinant CYP11A1 protein is engineered using heterologous expression systems, such as bacteria, yeast, or mammalian cells, to study its structure, function, and regulatory mechanisms. Its production enables detailed biochemical characterization, including substrate specificity, kinetic parameters, and interactions with cofactors or inhibitors. Recombinant CYP11A1 is particularly valuable in drug discovery, as dysregulation of steroidogenesis is linked to disorders like adrenal insufficiency, polycystic ovary syndrome (PCOS), and hormone-dependent cancers. Inhibitors or modulators of CYP11A1 are explored for therapeutic applications, such as reducing excessive steroid production in cancer or metabolic diseases.
Structural studies using recombinant CYP11A1 have provided insights into its membrane-binding domain, heme-coordinating active site, and cholesterol-binding pocket. Mutations in CYP11A1 are associated with congenital adrenal hyperplasia and disorders of sexual development, making recombinant variants crucial for functional assays to assess pathogenicity. Additionally, recombinant protein technology supports antibody generation for diagnostic tools and enzyme replacement strategies. Despite challenges in expressing full-length, functional CYP11A1 due to its mitochondrial localization and complex folding requirements, advances in protein engineering continue to enhance its utility in both basic research and clinical applications.
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