| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | CYP2C9 |
| Uniprot No | P11712 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-162aa |
| 氨基酸序列 | MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKVYGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKWKEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKGG |
| 预测分子量 | 25.4 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3条关于CYP2C9重组蛋白研究的模拟参考文献(内容基于领域内典型研究方向构建)：
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1. **文献名称**：*"Heterologous Expression of CYP2C9 in Saccharomyces cerevisiae: Characterization of Warfarin Metabolism"*
**作者**：Smith J.R., Williams P.A.
**摘要**：本研究利用酿酒酵母系统成功表达了人源CYP2C9重组蛋白，并优化了其与还原酶共表达条件。通过体外代谢实验证实重组CYP2C9对华法林的羟基化活性与天然酶相似，为药物代谢研究提供了高效工具。
2. **文献名称**：*"Structural Insights into CYP2C9 Polymorphism via Recombinant Protein Crystallography"*
**作者**：Lee H., Johnson E.F.
**摘要**：作者通过杆状病毒-昆虫细胞系统表达并纯化了CYP2C9*2和*3突变体蛋白，利用X射线晶体学解析其三维结构，揭示了基因多态性导致的活性位点构象变化，阐明了代谢能力差异的分子机制。
3. **文献名称**：*"Functional Reconstitution of CYP2C9 with Cytochrome P450 Reductase in Nanodiscs for Drug Interaction Studies"*
**作者**：Zhang Y., Guengerich F.P.
**摘要**：将重组CYP2C9与细胞色素P450还原酶共嵌入纳米脂盘(Nanodiscs)，构建了膜模拟环境下的酶功能体系。实验证明，该系统能有效评估药物(如苯妥英)与CYP2C9的相互作用及抑制动力学。
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**注**：以上文献为示例性内容，实际引用时建议通过PubMed或Web of Science等平台检索真实论文(关键词：CYP2C9 recombinant protein, heterologous expression, purification, enzymatic activity)。
CYP2C9 is a member of the cytochrome P450 superfamily, primarily expressed in the liver, and plays a critical role in the oxidative metabolism of numerous clinically important drugs, including anticoagulants (e.g., warfarin), antidiabetic agents (e.g., tolbutamide), and nonsteroidal anti-inflammatory drugs (NSAIDs). It accounts for approximately 20% of hepatic CYP450 content and is highly polymorphic, with genetic variants (e.g., *2. *3 alleles) significantly influencing enzyme activity. These polymorphisms contribute to interindividual variability in drug clearance, necessitating dose adjustments to avoid toxicity or therapeutic failure, particularly for narrow therapeutic index drugs.
Recombinant CYP2C9 protein is engineered using heterologous expression systems, such as Escherichia coli, yeast, or baculovirus-infected insect cells, to produce functional enzyme for in vitro studies. The recombinant form retains catalytic activity, enabling researchers to investigate substrate specificity, enzyme kinetics, and drug-drug interactions without interference from other hepatic enzymes. Its production typically involves codon optimization, N-terminal modifications (e.g., truncation or fusion tags), and co-expression with cytochrome P450 reductase to enhance stability and solubility. Purification methods often employ affinity chromatography for high-purity yields.
This recombinant tool is indispensable for preclinical drug development, allowing precise evaluation of metabolic pathways and inhibition potential. It also aids in characterizing the impact of genetic variants on drug metabolism, supporting personalized medicine initiatives. Compared to human liver microsomes, recombinant CYP2C9 offers a controlled system to isolate specific enzyme contributions, improving data reproducibility in toxicity screening and mechanistic studies. However, its utility may be limited by the absence of physiological enzyme complexes or tissue-specific post-translational modifications, underscoring the need for complementary models in comprehensive metabolic profiling.
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