| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPX8 |
| Uniprot No | Q8TED1 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-209aa |
| 氨基酸序列 | MEPLAAYPLKCSGPRAKVFAVLLSIVLCTVTLFLLQLKFLKPKINSFYAFEVKDAKGRTVSLEKYKGKVSLVVNVASDCQLTDRNYLGLKELHKEFGPSHFSVLAFPCNQFGESEPRPSKEVESFARKNYGVTFPIFHKIKILGSEGEPAFRFLVDSSKKEPRWNFWKYLVNPEGQVVKFWRPEEPIEVIRPDIAALVRQVIIKKKEDL |
| 分子量 | 50.3 kDa |
| 蛋白标签 | GST-tag at N-terminal |
| 缓冲液 | 0 |
| 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篇关于重组人GPX8蛋白的参考文献(模拟公开信息，部分文献细节可能需通过学术数据库验证)：
1. **标题**: "Recombinant human GPX8 protects against oxidative stress-induced cell death by modulating ER-mitochondria interactions"
**作者**: Smith J. et al. (2021)
**摘要**: 研究报道人源重组GPX8蛋白在HEK293细胞中表达后，通过调节内质网-线粒体接触点，减少氧化应激诱导线粒体凋亡的分子机制，并证明其保护细胞的功能依赖于其硫氧还蛋白结构域。
2. **标题**: "Structural characterization of human GPX8 reveals a novel selenocysteine-independent catalytic mechanism"
**作者**: Zhang L. et al. (2019)
**摘要**: 通过X射线晶体学解析重组人GPX8蛋白的三维结构，发现其活性位点以半胱氨酸取代传统硒代半胱氨酸，提出了一种非典型谷胱甘肽过氧化物酶催化机制，拓展了对GPX家族酶功能多样性的理解。
3. **标题**: "GPX8 overexpression in cancer cells confers resistance to ferroptosis via suppressing lipid peroxidation"
**作者**: Chen R. et al. (2022)
**摘要**: 通过体外重组GPX8蛋白功能实验，证明其通过清除脂质过氧化物抑制铁死亡(ferroptosis)，为靶向GPX8的癌症治疗策略提供了实验依据。
注：以上为文献模拟描述，实际引用需通过PubMed/Google Scholar检索关键词"recombinant human GPX8"或联系作者获取全文。建议通过Web of Science等平台筛选近5年高被引论文。
Recombinant human GPX8 (glutathione peroxidase 8) is a selenium-independent antioxidant enzyme belonging to the glutathione peroxidase family. Unlike other GPX members, GPX8 primarily localizes to the endoplasmic reticulum (ER), where it plays a critical role in mitigating oxidative stress by reducing reactive oxygen species (ROS) and lipid peroxides. This enzyme is intricately involved in ER stress responses and the unfolded protein response (UPR), mechanisms essential for maintaining cellular homeostasis under stress conditions. GPX8 contains a conserved catalytic motif and utilizes redox-active cysteine residues for its enzymatic activity instead of the selenocysteine found in classical GPXs. Its unique ER-specific function has linked it to pathologies such as cancer, neurodegenerative disorders, and metabolic diseases. Studies suggest GPX8 overexpression may promote tumor progression by enhancing cancer cell survival under oxidative stress, while its downregulation correlates with increased ER stress-induced apoptosis. Recombinant GPX8 protein, typically produced via mammalian or bacterial expression systems, is widely used to investigate ER stress pathways, screen antioxidant therapeutics, and explore redox signaling mechanisms. Ongoing research aims to elucidate its structure-function relationships and validate its potential as a diagnostic biomarker or therapeutic target for ER-related diseases.
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