| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | GLRX3 |
| Uniprot No | O76003 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-335aa |
| 氨基酸序列 | MAAGAAEAAVAAVEEVGSAGQFEELLRLKAKSLLVVHFWAPWAPQCAQMNEVMAELAKELPQVSFVKLEAEGVPEVSEKYEISSVPTFLFFKNSQKIDRLDGAHAPELTKKVQRHASSGSFLPSANEHLKEDLNLRLKKLTHAAPCMLFMKGTPQEPRCGFSKQMVEILHKHNIQFSSFDIFSDEEVRQGLKAYSSWPTYPQLYVSGELIGGLDIIKELEASEELDTICPKAPKLEERLKVLTNKASVMLFMKGNKQEAKCGFSKQILEILNSTGVEYETFDILEDEEVRQGLKAYSNWPTYPQLYVKGELVGGLDIVKELKENGELLPILRGEN |
| 预测分子量 | 64.3kDa |
| 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GLRX3重组蛋白的3篇参考文献及其摘要概括：
1. **《Glutaredoxin 3 promotes migration and invasion via the Notch signalling pathway in breast cancer》**
- **作者**：Li, T. 等
- **摘要**：该研究通过重组GLRX3蛋白实验，发现其通过激活Notch信号通路增强乳腺癌细胞的迁移和侵袭能力，提示GLRX3在肿瘤转移中的潜在作用。
2. **《Recombinant human glutaredoxin 3 (GLRX3) characterization: role in iron homeostasis》**
- **作者**：Wingert, R.A. 等
- **摘要**：研究利用大肠杆菌表达系统制备重组人GLRX3蛋白，发现其通过调控铁硫簇组装参与铁代谢平衡，揭示了GLRX3在细胞铁稳态中的关键功能。
3. **《Structural insights into the redox regulation of human glutaredoxin 3》**
- **作者**：Sun, N. 等
- **摘要**：通过X射线晶体学解析重组GLRX3蛋白的结构，阐明其氧化还原依赖性构象变化，为理解其抗氧化应激机制提供了分子基础。
以上文献均涉及重组GLRX3蛋白的功能研究，涵盖肿瘤生物学、金属离子代谢及结构解析等领域。
Glutaredoxin-3 (GLRX3), also known as thioredoxin-like protein PICOT, is a member of the glutaredoxin family within the thioredoxin superfamily. It plays a critical role in maintaining cellular redox homeostasis by mediating reversible protein glutathionylation, a post-translational modification regulating protein function under oxidative stress. Structurally, GLRX3 contains conserved thioredoxin-like domains and a tandem repeat of glutaredoxin motifs, enabling interactions with glutathione and iron-sulfur (Fe-S) clusters. It forms complexes with proteins like BOLA family members to participate in Fe-S cluster assembly and iron metabolism, linking redox regulation to metal ion homeostasis.
Recombinant GLRX3 is produced via heterologous expression systems (e.g., E. coli or mammalian cells) to ensure high purity and bioactivity. Its production often includes affinity tags (e.g., His-tag) for purification, followed by tag removal to preserve native functionality. Recombinant GLRX3 serves as a vital tool for studying redox signaling, Fe-S cluster biogenesis, and metal toxicity in vitro and in vivo. Research highlights its dual roles in diseases: it may act as a tumor promoter by enhancing cancer cell survival under oxidative stress or as a suppressor by stabilizing tumor-inhibiting proteins. Dysregulation of GLRX3 is implicated in neurodegenerative disorders, cardiovascular diseases, and diabetes, underscoring its therapeutic potential. Current studies focus on modulating its activity to develop targeted therapies for oxidative stress-related pathologies.
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