| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | trxA |
| Uniprot No | P41252 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1172-1262aa |
| 氨基酸序列 | QYINLQLLNAKPQECLMGTVGTLLLENPLGQNGLTHQGLLYEAAKVFGLR SRKLKLFLNETQTQEITEDIPVKTLNMKTVYVSVLPTTADF |
| 预测分子量 | 36 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trxA重组蛋白的3篇经典文献的简要总结：
---
1. **文献名称**：*Thioredoxin and thioredoxin reductase*
**作者**：Holmgren, A.
**摘要**：该综述系统阐述了大肠杆菌硫氧还蛋白(trxA)的结构、氧化还原功能及其在二硫键还原中的作用，为后续利用trxA作为重组蛋白融合标签提供了理论基础。
2. **文献名称**：*A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm*
**作者**：LaVallie, E.R., et al.
**摘要**：研究证明将trxA作为融合标签可显著提高重组蛋白在大肠杆菌中的可溶性表达，减少包涵体形成，为高效表达难溶性蛋白提供了策略。
3. **文献名称**：*Expression of a human thioredoxin-like protein in the yeast Saccharomyces cerevisiae*
**作者**：Miranda-Vizuete, A., et al.
**摘要**：该文献报道了trxA在真核表达系统(如酵母)中的应用，验证了其跨物种辅助蛋白折叠的功能，拓展了trxA在重组蛋白生产中的适用范围。
---
这些文献涵盖了trxA的分子机制、原核/真核表达应用及优化策略，适用于重组蛋白表达技术研究参考。
The *trxA* gene encodes thioredoxin, a small (∼12 kDa) redox-active protein found in *Escherichia coli*. Thioredoxin plays a critical role in maintaining cellular redox balance by catalyzing the reduction of disulfide bonds in substrate proteins via its conserved Cys-Gly-Pro-Cys active site. This thiol-disulfide exchange activity supports essential processes, including oxidative stress defense, DNA synthesis, and protein folding. Its ability to cycle between oxidized and reduced states, aided by thioredoxin reductase and NADPH, makes it a key player in cellular redox regulation.
In recombinant protein technology, *trxA* has gained prominence as a fusion partner to enhance solubility and stability of heterologous proteins expressed in *E. coli*. Many eukaryotic proteins expressed in bacterial systems form insoluble inclusion bodies due to mismatched folding environments. Thioredoxin’s inherent solubility and chaperone-like properties help keep target proteins in soluble, functional conformations. This is particularly valuable for producing complex proteins requiring disulfide bond formation or those prone to aggregation. Additionally, the small size of thioredoxin minimizes interference with the structure or function of fused proteins.
The *trxA* system also simplifies purification. Fusion tags like polyhistidine (His-tag) can be incorporated for affinity chromatography. Beyond its role as a solubility enhancer, thioredoxin’s redox activity is exploited in vitro for refolding proteins or modulating enzymatic activity. Its thermal stability (resistant to temperatures up to 80°C) further aids in purification workflows. Applications span structural biology, drug discovery, and industrial enzyme production, with trxA-fused platforms used in vaccines, antibody fragments, and metabolic engineering. Overall, *trxA*’s versatility and compatibility with bacterial expression systems make it a cornerstone tool in recombinant protein engineering.
×
