| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPX1 |
| Uniprot No | P07203 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-203aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMCAARLAAAAAAAQSVYAFSARPLAGGEPV SLGSLRGKVLLIENVASLCGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQ FGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGAHPLFAFLR EALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYS RRFQTIDIEPDIEALLSQGPSCA |
| 预测分子量 | 24 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GPX1重组蛋白的3篇代表性文献摘要(文献信息为模拟示例)：
1. **文献名称**: *Expression and Purification of Recombinant Human GPX1 in E. coli for Antioxidant Activity Studies*
**作者**: Zhang Y, et al.
**摘要**: 该研究报道了利用大肠杆菌表达系统高效表达人源GPX1重组蛋白，并通过亲和层析纯化获得高纯度产物。实验验证了重组GPX1的酶活性，证明其可有效清除过氧化氢，为后续抗氧化机制研究奠定基础。
2. **文献名称**: *Structural Insights into the Catalytic Mechanism of Recombinant GPX1 by Site-Directed Mutagenesis*
**作者**: Smith JL, et al.
**摘要**: 通过定点突变技术分析GPX1活性位点(硒代半胱氨酸)的结构与功能，发现其催化效率与硒原子的特异性结合有关，揭示了重组GPX1在抗氧化防御中的关键分子机制。
3. **文献名称**: *Protective Role of Recombinant GPX1 in Ischemia-Reperfusion-Induced Cardiac Injury*
**作者**: Chen H, et al.
**摘要**: 研究利用重组GPX1蛋白处理心肌缺血再灌注损伤模型，结果显示其显著降低组织氧化应激水平并改善心功能，提示GPX1重组蛋白在治疗氧化损伤相关疾病中的潜在应用价值。
(注：以上文献为示例，实际引用需根据具体研究检索PubMed、Web of Science等数据库获取。)
**Background of GPX1 Recombinant Protein**
Glutathione peroxidase 1 (GPX1) is a critical antioxidant enzyme in the glutathione peroxidase family, primarily responsible for neutralizing reactive oxygen species (ROS) to mitigate oxidative stress in cells. It catalyzes the reduction of hydrogen peroxide (H₂O₂) and lipid hydroperoxides into water or corresponding alcohols using reduced glutathione (GSH) as a co-substrate. This selenoprotein contains a selenocysteine (Sec) residue at its active site, encoded by a TGA codon, which is essential for its catalytic activity. GPX1 is ubiquitously expressed, with high levels in the liver, erythrocytes, and kidney, playing a vital role in cellular defense against oxidative damage linked to aging, neurodegeneration, and chronic diseases.
Recombinant GPX1 protein is produced using biotechnological platforms, such as *E. coli*, yeast, or mammalian expression systems, to enable large-scale studies and therapeutic applications. However, expressing functional GPX1 poses challenges due to the atypical incorporation of Sec, which requires specialized translation machinery absent in prokaryotic systems. To overcome this, researchers often substitute Sec with cysteine (Cys) or employ engineered cell lines with Sec insertion sequences. The recombinant protein is purified via affinity tags (e.g., His-tag) and validated for enzymatic activity using assays like NADPH-coupled oxidation.
GPX1 recombinant protein is widely utilized in biomedical research to explore oxidative stress mechanisms, screen antioxidants, and develop therapies for conditions like diabetes, cardiovascular diseases, and cancer. It also serves as a reference standard in diagnostic kits and a potential therapeutic agent in preclinical studies. Advances in protein engineering and expression systems continue to enhance its stability and catalytic efficiency, broadening its applicability in both research and clinical settings.
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