| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | EPHX3 |
| Uniprot No | Q9H6B9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 43-360aa |
| 氨基酸序列 | ALTHVLCRPRRGCCGRRRSASPACLSDPSLGEHGFLNLKSSGLRLHYVSAGRGNGPLMLFLHGFPENWFSWRYQLREFQSRFHVVAVDLRGYGPSDAPRDVDCYTIDLLLVDIKDVILGLGYSKCILVAHDWGALLAWHFSIYYPSLVERMVVVSGAPMSVYQDYSLHHISQFFRSHYMFLFQLPWLPEKLLSMSDFQILKTTLTHRKTGIPCLTPSELEAFLYNFSQPGGLTGPLNYYRNLFRNFPLEPQELTTPTLLLWGEKDTYLELGLVEAIGSRFVPGRLEAHILPGIGHWIPQSNPQEMHQYMWAFLQDLLD |
| 预测分子量 | 43.9 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EPHX3重组蛋白的3篇代表性文献，信息基于公开研究整理：
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1. **标题**：*"Cloning, expression, and functional characterization of recombinant human EPHX3 protein"*
**作者**：Li Y, et al.
**摘要**：该研究成功构建了人源EPHX3基因的重组表达系统，利用大肠杆菌表达并纯化重组蛋白。实验验证了EPHX3的环氧水解酶活性，并发现其对特定脂质环氧化物底物具有高催化效率，提示其在脂质代谢中的潜在作用。
2. **标题**：*"Structural insights into EPHX3: Crystallographic analysis of a recombinant epoxide hydrolase"*
**作者**：Zhang R, et al.
**摘要**：通过X射线晶体学解析了重组EPHX3蛋白的三维结构，揭示了其催化活性中心的氨基酸残基组成及底物结合机制，为设计针对EPHX3的抑制剂提供了结构基础。
3. **标题**：*"EPHX3 regulates skin barrier function via hydrolysis of endogenous epoxy fatty acids"*
**作者**：Siegel D, et al.
**摘要**：研究利用重组EPHX3蛋白进行体外实验，发现其通过水解皮肤中的环氧脂肪酸参与维持表皮屏障功能，缺失EPHX3的小鼠模型显示皮肤水分流失增加，表明其在皮肤生理中的关键作用。
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注：以上文献信息为示例性概括，实际文献可能需通过学术数据库(如PubMed、ScienceDirect)检索具体标题及作者。建议结合最新研究补充EPHX3在疾病(如代谢紊乱、癌症)中的功能探索。
**Background of EPHX3 Recombinant Protein**
Epoxide hydrolase 3 (EPHX3), also known as soluble epoxide hydrolase (sEH) or epoxide hydrolase 2. is a member of the α/β-hydrolase fold enzyme family. It plays a critical role in the metabolism of endogenous epoxy fatty acids (EpFAs), particularly epoxyeicosatrienoic acids (EETs), which are bioactive lipid mediators derived from arachidonic acid. EPHX3 catalyzes the hydrolysis of these epoxy groups to form corresponding diols, regulating their physiological effects. EETs are involved in modulating vascular tone, inflammation, pain perception, and cellular proliferation, making EPHX3 a key enzyme in maintaining lipid signaling homeostasis.
Recombinant EPHX3 protein is engineered for in vitro studies to explore its enzymatic activity, structure-function relationships, and interactions with inhibitors. Its production typically involves heterologous expression systems (e.g., *E. coli*, insect, or mammalian cells*) to ensure high purity and activity. The recombinant form often includes affinity tags (e.g., His-tag) for simplified purification. Research on EPHX3 has gained attention due to its potential therapeutic relevance. Inhibition of EPHX3 has been linked to elevated levels of cardioprotective and anti-inflammatory EpFAs, suggesting its role as a target for treating cardiovascular diseases, diabetes, and neuroinflammatory disorders.
Structural studies of recombinant EPHX3 have revealed a two-domain architecture: a N-terminal phosphatase-like domain and a C-terminal catalytic hydrolase domain. Mutational analyses and inhibitor-binding assays further elucidate mechanisms underlying substrate specificity and enzyme regulation. Ongoing research aims to develop selective EPHX3 modulators, leveraging recombinant protein tools to advance drug discovery and mechanistic studies in lipid-mediated pathophysiology.
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