| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPHX1 |
| Uniprot No | P07099 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-455aa |
| 氨基酸序列 | MWLEILLTSVLGFAIYWFISRDKEETLPLEDGWWGPGTRSAAREDDSIRP FKVETSDEEIHDLHQRIDKFRFTPPLEDSCFHYGFNSNYLKKVISYWRNE FDWKKQVEILNRYPHFKTKIEGLDIHFIHVKPPQLPAGHTPKPLLMVHGW PGSFYEFYKIIPLLTDPKNHGLSDEHVFEVICPSIPGYGFSEASSKKGFN SVATARIFYKLMLRLGFQEFYIQGGDWGSLICTNMAQLVPSHVKGLHLNM ALVLSNFSTLTLLLGQRFGRFLGLTERDVELLYPVKEKVFYSLMRESGYM HIQCTKPDTVGSALNDSPVGLAAYILEKFSTWTNTEFRYLEDGGLERKFS LDDLLTNVMLYWTTGTIISSQRFYKENLGQGWMTQKHERMKVYVPTGFSA FPFELLHTPEKWVRFKYPKLISYSYMVRGGHFAAFEEPELLAQDIRKFLS VLERQ |
| 预测分子量 | 76 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 **EPHX1重组蛋白** 的3篇参考文献及其摘要内容概要：
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1. **文献名称**：*"Expression and Purification of Human Soluble Epoxide Hydrolase (EPHX1) in Escherichia coli for Biochemical and Structural Studies"*
**作者**：Morisseau C, et al.
**摘要**：该研究描述了利用大肠杆菌表达系统重组表达人源可溶性环氧化物水解酶(EPHX1)的方法，并通过亲和层析技术纯化获得高活性蛋白。作者进一步分析了其酶动力学特性，并探讨了重组蛋白在药物代谢和炎症相关研究中的应用潜力。
2. **文献名称**：*"Functional Characterization of Recombinant EPHX1 Variants: Insights into Substrate Specificity and Genetic Polymorphism Effects"*
**作者**：Przybyla-Zawislak B, et al.
**摘要**：通过构建不同遗传变异体(如Tyr113His和His139Arg)的重组EPHX1蛋白，研究对比了变异体与野生型酶的催化活性和底物选择性，揭示了基因多态性对EPHX1代谢外源化合物(如环氧脂肪酸和环境毒素)功能的影响。
3. **文献名称**：*"Development of a High-Throughput Screening Assay for EPHX1 Inhibition Using Recombinant Protein"*
**作者**：Decker M, et al.
**摘要**：研究基于重组表达的EPHX1蛋白，开发了一种高通量筛选模型，用于快速检测潜在抑制剂。该方法为治疗EPHX1相关疾病(如高血压、糖尿病并发症)的药物开发提供了高效工具。
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以上文献均聚焦于EPHX1重组蛋白的表达策略、功能分析及实际应用，涵盖酶学特性、遗传变异影响和药物筛选等领域。如需具体文献来源，可进一步通过PubMed或SciHub检索标题或作者。
**Background of Recombinant EPHX1 Protein**
Epoxide Hydrolase 1 (EPHX1), also known as microsomal epoxide hydrolase (mEH), is a key enzyme involved in the metabolism of endogenous and exogenous epoxide-containing compounds. It catalyzes the hydrolysis of reactive epoxides into less reactive diols, playing a critical role in detoxification pathways and the processing of xenobiotics, including environmental carcinogens and therapeutic drugs. EPHX1 is primarily expressed in the liver, kidneys, and lungs, where it contributes to Phase I drug metabolism alongside cytochrome P450 enzymes. Its activity influences individual susceptibility to chemical toxicity and diseases linked to environmental exposures, such as cancer and respiratory disorders.
Structurally, EPHX1 is a 455-amino acid protein anchored to the endoplasmic reticulum membrane. Its catalytic triad (Asp226. Glu404. and His431) enables nucleophilic hydrolysis of epoxide substrates. Genetic polymorphisms in *EPHX1* (e.g., Tyr113His and His139Arg) have been associated with altered enzyme activity, impacting disease risk and drug efficacy.
Recombinant EPHX1 protein is produced using heterologous expression systems (e.g., *E. coli*, insect cells) to study its biochemical properties, substrate specificity, and inhibition. Purified recombinant EPHX1 enables high-throughput screening for inhibitors or activators, aiding drug development for conditions like cancer or inflammatory diseases. Additionally, it serves as a tool to investigate enzyme kinetics, structural dynamics, and interactions with metabolic partners.
Research highlights EPHX1's dual role: while detoxifying harmful epoxides, it may also bioactivate certain procarcinogens. Its involvement in steroid and lipid metabolism further links it to cardiovascular and metabolic disorders. Recombinant EPHX1 thus provides a versatile platform for mechanistic studies and therapeutic exploration, bridging gaps between genetic variability, environmental factors, and disease outcomes.
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