| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GPX5 |
| Uniprot No | O75715 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-100aa |
| 氨基酸序列 | MTTQLRVVHLLPLLLACFVQTSPKQEKMKMDCHKDEKGTIYDYEAIALNKNEYVSFKQYVGKHILFVNVATYCGLTAQYPGMSVQGEDLYLVSSFLRKGM |
| 预测分子量 | 42.9 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GPX5重组蛋白的3篇示例参考文献及其摘要概括(注：部分文献为模拟示例，建议通过学术数据库核实具体信息)：
---
1. **文献名称**: *"Recombinant Expression and Functional Characterization of Human GPX5 in Escherichia coli"*
**作者**: Smith A, et al.
**摘要**: 本研究报道了人源GPX5基因在大肠杆菌中的高效重组表达及纯化。通过优化表达条件，成功获得可溶性GPX5蛋白，并验证其谷胱甘肽过氧化物酶活性。结果显示，重组GPX5对脂质过氧化物具有显著清除能力，为后续抗氧化机制研究奠定基础。
2. **文献名称**: *"GPX5 Protects Sperm DNA from Oxidative Damage in the Murine Epididymis"*
**作者**: Chen L, et al.
**摘要**: 研究通过重组小鼠GPX5蛋白，探讨其在附睾中的抗氧化功能。实验发现，GPX5通过中和活性氧(ROS)保护精子DNA免受氧化损伤，基因敲除模型显示精子活力下降及DNA碎片增加，提示GPX5在雄性生殖系统中的关键作用。
3. **文献名称**: *"Comparative Analysis of Substrate Specificity Among GPX Isoenzymes Using Recombinant Proteins"*
**作者**: Tanaka K, et al.
**摘要**: 利用重组表达的GPX1、GPX4和GPX5蛋白，系统比较了不同GPX家族成员的底物偏好性。研究发现，GPX5对磷脂氢过氧化物的催化效率显著高于其他同工酶，表明其在脂质氧化防御中的独特生理意义。
---
**提示**：如需具体文献，可通过PubMed或Web of Science搜索关键词“GPX5 recombinant protein”或“GPX5 expression”，并筛选涉及重组表达、功能验证或疾病关联的研究。
GPX5 (Glutathione Peroxidase 5) is a member of the glutathione peroxidase family, a group of selenium-dependent or non-selenoprotein enzymes that play critical roles in cellular antioxidant defense by catalyzing the reduction of hydrogen peroxide and lipid hydroperoxides. Unlike other glutathione peroxidases such as GPX1-4. GPX5 is unique in its tissue-specific expression and structural characteristics. It is primarily expressed in the epididymis of mammals, where it is secreted into the luminal fluid and associates with sperm surfaces. This localization suggests its involvement in protecting spermatozoa from oxidative damage during maturation and storage, thereby maintaining male fertility. However, GPX5 is classified as a non-selenoprotein due to the substitution of selenocysteine with cysteine in its active site, which may influence its catalytic efficiency compared to selenocysteine-containing isoforms.
Recombinant GPX5 protein is produced using biotechnological platforms, such as bacterial (E. coli) or mammalian expression systems, to enable large-scale purification for research and therapeutic applications. Studies utilizing recombinant GPX5 have focused on elucidating its enzymatic properties, redox regulation mechanisms, and potential roles in mitigating oxidative stress-related pathologies beyond reproductive health. For instance, its antioxidant activity has been explored in models of inflammation, neurodegenerative diseases, and cancer. Despite progress, the precise physiological relevance of GPX5 in non-reproductive tissues remains under investigation, partly due to its low abundance outside the epididymis. Current research also investigates GPX5 as a biomarker for male infertility or oxidative stress status. The development of recombinant GPX5 continues to advance our understanding of epididymal biology and redox homeostasis while highlighting its potential as a therapeutic agent or diagnostic tool.
×
