| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPHX4 |
| Uniprot No | Q8IUS5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-362aa |
| 氨基酸序列 | MARLRDCLPRLMLTLRSLLFWSLVYCYCGLCASIHLLKLLWSLGKGPAQTFRRPAREHPPACLSDPSLGTHCYVRIKDSGLRFHYVAAGERGKPLMLLLHGFPEFWYSWRYQLREFKSEYRVVALDLRGYGETDAPIHRQNYKLDCLITDIKDILDSLGYSKCVLIGHDWGGMIAWLIAICYPEMVMKLIVINFPHPNVFTEYILRHPAQLLKSSYYYFFQIPWFPEFMFSINDFKVLKHLFTSHSTGIGRKGCQLTTEDLEAYIYVFSQPGALSGPINHYRNIFSCLPLKHHMVTTPTLLLWGENDAFMEVEMAEVTKIYVKNYFRLTILSEASHWLQQDQPDIVNKLIWTFLKEETRKKD |
| 预测分子量 | 45.2 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EPHX4重组蛋白的3篇参考文献的简要信息：
1. **《Functional Characterization of Human Epoxide Hydrolase 4 (EPHX4) in Lipid Metabolism》**
- **作者**: Zhang Y, et al.
- **摘要**: 本研究通过重组表达人源EPHX4蛋白，发现其能够水解特定环氧脂肪酸代谢物，并揭示其在调控细胞氧化应激和炎症反应中的作用。实验表明，重组EPHX4在体外可显著降低促炎脂质信号分子水平。
2. **《Expression and Purification of Recombinant EPHX4 for Structural Studies》**
- **作者**: Thompson R, et al.
- **摘要**: 文章描述了利用大肠杆菌系统高效表达和纯化EPHX4重组蛋白的优化方法，并通过X射线晶体学解析其三维结构。研究为EPHX4的底物结合机制及抑制剂设计提供了结构基础。
3. **《Role of EPHX4 in Drug Metabolism: Insights from Recombinant Enzyme Assays》**
- **作者**: Kumar S, et al.
- **摘要**: 利用重组EPHX4蛋白进行体外代谢实验，发现其对多种临床药物(如抗肿瘤化合物)的环氧代谢产物具有催化活性，提示其在药物代谢和个体化治疗中的潜在应用价值。
注：上述文献为示例，实际研究中建议通过PubMed或Web of Science等平台检索最新论文。若相关研究较少，可扩展至EPHX家族其他成员(如EPHX1/2)的重组蛋白研究作为参考。
**Background of EPHX4 Recombinant Protein**
The EPHX4 (Epoxide Hydrolase 4) gene encodes a member of the epoxide hydrolase family, enzymes critical in metabolizing epoxide-containing lipids and xenobiotics. These enzymes hydrolyze epoxides to corresponding diols, influencing cellular homeostasis, detoxification, and signaling pathways. EPHX4. specifically, is implicated in the regulation of bioactive lipid mediators, such as epoxyeicosatrienoic acids (EETs), which play roles in inflammation, vascular function, and cellular proliferation.
Structurally, EPHX4 shares the conserved α/β-hydrolase fold characteristic of epoxide hydrolases, featuring a catalytic triad (aspartate-histidine-glutamate) essential for its enzymatic activity. Unlike other EPHX isoforms (e.g., EPHX1 and EPHX2), EPHX4 exhibits distinct substrate preferences and tissue expression patterns, with higher abundance in organs like the liver, kidney, and brain. Its precise physiological roles remain under investigation, though studies suggest involvement in lipid metabolism and cellular stress responses.
Recombinant EPHX4 protein is engineered for *in vitro* studies, typically produced via heterologous expression in bacterial or mammalian systems. This protein retains enzymatic activity, enabling researchers to characterize its kinetic properties, substrate specificity, and interactions with inhibitors or modulators. Its recombinant form is often tagged (e.g., His-tag) for purification and detection.
Research on EPHX4 has gained momentum due to its potential links to diseases, including cancer, neurodegenerative disorders, and metabolic syndromes. Polymorphisms or dysregulation of EPHX4 may alter lipid signaling, contributing to pathological states. Additionally, its role in processing environmental epoxides highlights relevance in toxicology and drug metabolism.
Overall, EPHX4 recombinant protein serves as a vital tool for unraveling the enzyme's biological functions and therapeutic potential, bridging gaps in understanding lipid-mediated signaling and disease mechanisms.
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