| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLRX |
| Uniprot No | P35754 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-106aa |
| 氨基酸序列 | MAQEFVNCKIQPGKVVVFIKPTCPYCRRAQEILSQLPIKQGLLEFVDITATNHTNEIQDYLQQLTGARTVPRVFIGKDCIGGCSDLVSLQQSGELLTRLKQIGALQ |
| 预测分子量 | 38.8kDa |
| 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GLRX重组蛋白的3篇参考文献及其摘要概括：
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1. **标题**：*Recombinant Glutaredoxin (GLRX) from *E. coli*: Efficient Production and Functional Characterization*
**作者**：Smith J, Brown A, Lee S
**摘要**：研究报道了一种通过大肠杆菌表达系统高效重组表达GLRX的方法，并优化了纯化流程。功能实验证实重组GLRX可有效还原氧化蛋白底物，在体外抗氧化系统中表现出显著活性。
2. **标题**：*Role of Recombinant Human GLRX in Ameliorating Oxidative Stress in Neurodegenerative Models*
**作者**：Zhang Y, Wang L, Chen H
**摘要**：通过细胞实验和小鼠模型，证明重组人源GLRX能够减少β-淀粉样蛋白诱导的神经元氧化损伤，并改善阿尔茨海默病模型中的认知功能，提示其治疗潜力。
3. **标题**：*Structural Insights into Recombinant GLRX2: Implications for Its Catalytic Mechanism*
**作者**：Johnson R, Müller P, García-Sastre A
**摘要**：利用X射线晶体学解析了重组GLRX2的三维结构，揭示了其活性位点的半胱氨酸残基构象，并通过突变实验验证了其在硫醇-二硫键交换反应中的关键作用。
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以上文献涵盖了GLRX重组蛋白的表达优化、疾病治疗应用及结构机制研究，均为假设性示例，实际引用时需根据具体文献调整。
Glutaredoxin (GLRX), a member of the thioredoxin superfamily, is a small, evolutionarily conserved oxidoreductase critical for maintaining cellular redox homeostasis. It functions primarily by catalyzing the reduction of protein disulfide bonds or glutathione (GSH)-mixed disulfides via its conserved CXXC active site, utilizing glutathione as a cofactor. GLRX plays a pivotal role in regulating cellular processes such as DNA synthesis, apoptosis, and iron-sulfur cluster biogenesis, and is implicated in oxidative stress response, inflammation, and metabolic regulation. Dysregulation of GLRX has been linked to various pathologies, including neurodegenerative diseases, cancer, and cardiovascular disorders.
Recombinant GLRX proteins are engineered through molecular cloning techniques, typically expressed in bacterial (e.g., *E. coli*) or eukaryotic systems to ensure proper folding and post-translational modifications. These proteins retain the enzymatic activity of native GLRX and are widely used in biochemical and biomedical research. Applications include studying redox signaling mechanisms, developing assays for oxidative stress biomarkers, and exploring therapeutic strategies for diseases involving redox imbalance. Recombinant GLRX also serves as a tool to investigate protein-protein interactions, substrate specificity, and the role of specific cysteine residues in redox regulation. Its stability and activity under experimental conditions make it valuable for both *in vitro* and *in vivo* studies, bridging basic science and translational research in redox biology.
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