| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | grxB |
| Uniprot No | P0AC59 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-215aa |
| 氨基酸序列 | MGSSHHHHHHSSGLVPRGSHMKLYIYDHCPYCLKARMIFGLKNIPVELHVLLNDDAETPTRMVGQKQVPILQKDDSRYMPESMDIVHYVDKLDGKPLLTGKRSPAIEEWLRKVNGYANKLLLPRFAKSAFDEFSTPAARKYFVDKKEASAGNFADLLAHSDGLIKNISDDLRALDKLIVKPNAVNGELSEDDIQLFPLLRNLTLVAGINWPSRVADYRDNMAKQTQINLLSSMAI |
| 分子量 | 26.5 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. |
以下是关于大肠杆菌GrxB重组蛋白的3条参考文献示例(文献为虚拟示例，供参考)：
---
1. **文献名称**：*"Cloning, Expression, and Functional Analysis of Glutaredoxin B (grxB) in Escherichia coli"*
**作者**：Müller A, et al.
**摘要**：该研究报道了大肠杆菌grxB基因的重组表达与纯化，证实GrxB蛋白在体外具有硫氧还酶活性，能够有效还原谷胱甘肽化底物，并参与氧化应激中二硫键的修复机制。
2. **文献名称**：*"Structural and Functional Insights into Escherichia coli GrxB as a Redox Regulator"*
**作者**：Chen L, et al.
**摘要**：通过X射线晶体学解析了GrxB的三维结构，揭示了其活性位点Cys-Pro-Tyr-Cys的构象特征，并证明GrxB在维持胞内氧化还原平衡中与硫氧还蛋白互补作用。
3. **文献名称**：*"Role of Recombinant GrxB in Bacterial Antibiotic Resistance Pathways"*
**作者**：Kim S, et al.
**摘要**：研究表明，重组GrxB通过调节硫醇-二硫键稳态，增强了细菌对β-内酰胺类抗生素的耐受性，缺失grxB的菌株表现出更高的氧化损伤敏感性。
---
以上示例总结了GrxB重组蛋白在氧化还原功能、结构解析及耐药性中的作用，可供相关研究参考。如需真实文献，建议通过PubMed或Web of Science以关键词“E. coli GrxB recombinant protein”检索。
Glutaredoxin B (GrxB) is a small redox protein in *Escherichia coli* belonging to the glutaredoxin family, which plays a critical role in maintaining cellular redox homeostasis. It functions primarily as a disulfide reductase, facilitating the reduction of protein disulfide bonds via glutathione-dependent pathways. GrxB is part of the thioredoxin superfamily and shares structural features such as a conserved CXXC active-site motif, enabling electron transfer during redox reactions. Unlike its paralog GrxA, GrxB exhibits unique substrate specificity and interacts preferentially with certain target proteins, including ribonucleotide reductase and methionine sulfoxide reductases, supporting DNA synthesis and oxidative damage repair.
Recombinant GrxB is commonly produced by cloning the *grxB* gene into expression vectors (e.g., pET plasmids) under inducible promoters (e.g., T7), followed by overexpression in *E. coli* hosts like BL21(DE3). Purification typically involves affinity chromatography (e.g., His-tag systems) and buffer optimization to stabilize its redox-sensitive structure. The recombinant protein retains enzymatic activity, making it valuable for studying redox-regulated processes, enzymatic kinetics, and protein-protein interactions *in vitro*. Its applications extend to biotechnology, such as optimizing disulfide bond shuffling in industrial enzyme production, and biomedical research, including exploring bacterial stress responses or developing redox-targeted therapeutics. GrxB’s simplicity, stability, and functional versatility underscore its significance as a model protein in redox biology.
×
