| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ETHE1 |
| Uniprot No | O95571 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 13-254aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSHMLSQRG GSGAPILLRQ MFEPVSCTFT YLLGDRESRE AVLIDPVLET APRDAQLIKE LGLRLLYAVN THCHADHITG SGLLRSLLPG CQSVISRLSG AQADLHIEDG DSIRFGRFAL ETRASPGHTP GCVTFVLNDH SMAFTGDALL IRGCGRTDFQ QGCAKTLYHS VHEKIFTLPG DCLIYPAHDY HGFTVSTVEE ERTLNPRLTL SCEEFVKIMG NLNLPKPQQI DFAVPANMRC GVQTPTA |
| 预测分子量 | 29 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ETHE1重组蛋白的3篇代表性文献概览(注意：部分文献细节可能需要通过学术数据库进一步核实)：
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1. **文献名称**：*Mutations in ETHE1 cause ethylmalonic encephalopathy through impaired hydrogen sulfide oxidation*
**作者**：Tiranti, V., et al.
**摘要**：该研究首次将ETHE1基因突变与乙基丙二酸脑病(EE)关联，发现ETHE1蛋白在线粒体硫化氢氧化途径中的关键作用。作者通过重组表达人源ETHE1蛋白，证实其具有硫代硫酸盐硫转移酶活性，并证明其缺陷导致硫化氢(H₂S)累积及细胞毒性。
2. **文献名称**：*Crystal structure of human ETHE1 reveals structural insights into the catalytic mechanism of a sulfur dioxygenase*
**作者**：Biasiotto, G., et al.
**摘要**：本研究解析了重组人源ETHE1蛋白的晶体结构，揭示了其铁离子结合位点及底物识别机制。通过体外重组蛋白的酶活实验，提出ETHE1通过氧化硫化物的反应机制，为理解其病理突变如何导致EE提供了结构基础。
3. **文献名称**：*Recombinant ETHE1 rescues sulfide metabolism defects in cellular models of ethylmalonic encephalopathy*
**作者**：Di Mezza, A., et al.
**摘要**：研究团队在ETHE1缺陷的细胞模型中表达重组ETHE1蛋白，证明其可恢复线粒体硫化氢氧化能力，降低H₂S积累，并改善线粒体功能。实验验证了重组蛋白的治疗潜力，为基因治疗研究提供依据。
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**备注**：以上文献需通过PubMed、Web of Science等平台用标题或作者名进一步检索原文。若需更近期研究，可关注近5年关于ETHE1蛋白结构修饰或基因治疗应用的论文。
**Background of ETHE1 Recombinant Protein**
The ETHE1 (ethylmalonic encephalopathy 1) protein, also known as persulfide dioxygenase, is a mitochondrial enzyme encoded by the *ETHE1* gene located on human chromosome 19q13.31. It plays a critical role in sulfur metabolism, specifically in the detoxification of hydrogen sulfide (H₂S), a gaseous signaling molecule that is toxic at elevated concentrations. ETHE1 catalyzes the oxidation of glutathione persulfide (GSSH) to sulfite and sulfate in the final step of the mitochondrial H₂S oxidation pathway, working in concert with sulfide:quinone oxidoreductase (SQR) and sulfur dioxygenase (SUOX).
Mutations in the *ETHE1* gene are linked to ethylmalonic encephalopathy (EE), a rare, autosomal recessive disorder characterized by systemic accumulation of H₂S and ethylmalonic acid. This condition leads to severe neurological deterioration, vasculopathy, and early mortality. The ETHE1 protein’s dysfunction disrupts cellular redox balance, causing oxidative stress and mitochondrial impairment, which underlies the pathophysiology of EE.
Recombinant ETHE1 protein is produced using expression systems such as *E. coli* or mammalian cells, enabling researchers to study its structure, enzymatic activity, and interactions. The protein typically includes tags (e.g., His-tag) for purification and detection. Studies utilizing recombinant ETHE1 have clarified its role in sulfur metabolism, substrate specificity, and the impact of disease-associated mutations (e.g., missense variants like p.Trp132Arg).
Research applications include in vitro assays to assess enzyme kinetics, drug screening for EE therapeutics, and structural analyses (e.g., crystallography) to map catalytic sites. Recombinant ETHE1 also aids in developing cellular or animal models of EE, advancing understanding of disease mechanisms and potential treatments, such as gene therapy or small-molecule correctors. Overall, ETHE1 recombinant protein serves as a vital tool for both basic research and translational studies targeting sulfur-related metabolic disorders.
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