| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | DME |
| Uniprot No | Q8LK56 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-320aa |
| 氨基酸序列 | MNSRADPGDRYFRVPLENQTQQEFMGSWIPFTPKKPRSSLMVDERVINQDLNGFPGGEFVDRGFCNTGVDHNGVFDHGAHQGVTNLSMMINSLAGSHAQAWSNSERDLLGRSEVTSPLAPVIRNTTGNVEPVNGNFTSDVGMVNGPFTQSGTSQAGYNEFELDDLLNPDQMPFSFTSLLSGGDSLFKVRQYGPPACNKPLYNLNSPIRREAVGSVCESSFQYVPSTPSLFRTGEKTGFLEQIVTTTGHEIPEPKSDKSMQSIMDSSAVNATEATEQNDGSRQDVLEFDLNKTPQQKPSKRKRKFMPKVVVEGKPKRKPRK |
| 预测分子量 | 51.4 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DME(药物代谢酶，Drug Metabolism Enzymes)重组蛋白研究的参考文献示例(内容基于学术文献常见主题虚构，供参考)：
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1. **文献名称**：*Expression and functional characterization of recombinant human CYP2D6 in Saccharomyces cerevisiae*
**作者**：Johnson, R.T., et al.
**摘要**：本研究利用酿酒酵母系统成功表达了重组人源CYP2D6酶，并通过体外代谢实验验证其对右美沙芬的氧化活性。结果显示重组酶与天然肝微粒体中的CYP2D6活性高度一致，表明其在药物代谢研究中的替代潜力。
2. **文献名称**：*Optimization of P450 oxidoreductase expression for enhanced activity of recombinant CYP3A4 in E. coli*
**作者**：Chen, L., & Wang, H.
**摘要**：通过共表达细胞色素P450还原酶(POR)，优化了大肠杆菌中重组CYP3A4的表达条件，显著提高了其对睾酮的6β-羟化酶活性。研究为大规模生产功能性药物代谢酶提供了技术参考。
3. **文献名称**：*Application of recombinant DMEs in high-throughput screening of drug-drug interactions*
**作者**：Martinez, S., et al.
**摘要**：开发了一种基于重组CYP2C9和CYP2C19的多酶体外体系，用于快速评估药物-药物相互作用。实验证明该方法与传统肝微粒体模型结果相关性达90%，可加速临床前药物安全性评估。
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**备注**：若需真实文献，建议通过PubMed或Web of Science检索关键词(如“recombinant drug metabolism enzymes”“CYP expression systems”)，并筛选近五年内发表的论文以确保前沿性。
**Background of DME Recombinant Proteins**
Drug-metabolizing enzymes (DMEs) are critical proteins responsible for the biotransformation of xenobiotics, including pharmaceuticals, environmental toxins, and endogenous compounds. These enzymes, primarily cytochrome P450s (CYPs), UDP-glucuronosyltransferases (UGTs), and flavin-containing monooxygenases (FMOs), play a central role in drug metabolism, influencing pharmacokinetics, toxicity, and therapeutic efficacy. Traditional studies of DMEs relied on tissue-derived enzymes, which posed challenges in scalability, purity, and reproducibility.
The advent of recombinant DNA technology revolutionized DME research by enabling the production of recombinant DME proteins. These proteins are engineered via heterologous expression systems (e.g., *E. coli*, yeast, insect, or mammalian cells*), allowing precise control over enzyme isoforms and post-translational modifications. Mammalian systems (e.g., HEK293 or CHO cells) are preferred for human DMEs due to their ability to replicate native folding and cofactor interactions.
Recombinant DMEs are widely used in *in vitro* drug metabolism assays to predict *in vivo* outcomes. They facilitate high-throughput screening of drug candidates, enzyme kinetic studies, and identification of metabolic pathways, drug-drug interactions, and genetic polymorphisms affecting enzyme activity. Additionally, they support personalized medicine by elucidating interindividual variability in drug responses.
Recent advancements, such as CRISPR-edited cell lines and structural biology tools, have enhanced recombinant DME fidelity and functionality. However, challenges remain, including maintaining enzyme stability and mimicking complex *in vivo* environments. Despite this, recombinant DMEs remain indispensable in drug development, toxicology, and mechanistic studies, bridging the gap between preclinical research and clinical applications. Their continued optimization promises to refine drug safety assessments and therapeutic strategies.
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