| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | Trx |
| Uniprot No | P10599 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-105aa |
| 氨基酸序列 | MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV |
| 预测分子量 | 12 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3篇关于硫氧还蛋白(Trx)重组蛋白的经典文献摘要，供参考：
1. **文献名称**: Thioredoxin and thioredoxin reductase
**作者**: Arner ES, Holmgren A
**期刊**: *Eur J Biochem* (2000)
**摘要**: 系统综述了Trx的结构、功能及其与硫氧还蛋白还原酶的相互作用机制，重点讨论了Trx在氧化还原调控中的核心作用及其在重组蛋白表达中的应用潜力。
2. **文献名称**: Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli
**作者**: LaVallie ER et al.
**期刊**: *Nat Biotechnol* (1993)
**摘要**: 首次验证Trx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，建立了Trx融合系统技术平台，为后续重组蛋白生产提供重要方法学基础。
3. **文献名称**: Crystal structure of human thioredoxin reveals a beta-sheet structure
**作者**: Katti SK et al.
**期刊**: *J Biol Chem* (1990)
**摘要**: 通过X射线晶体学解析人源Trx的三维结构，揭示其独特的β-折叠构象及活性位点Cys-Gly-Pro-Cys特征，为理性设计重组Trx突变体提供结构生物学依据。
4. **文献名称**: Engineering of a polypeptide C-terminal tag enhances recombinant protein production and secretion in E. coli
**作者**: Zhang Y et al.
**期刊**: *Microb Cell Fact* (2018)
**摘要**: 开发新型Trx-C端融合标签系统，通过优化分泌信号肽和折叠辅助元件，显著提升重组蛋白的胞外分泌效率，在工业级蛋白生产领域具有应用价值。
**Background of Recombinant Thioredoxin (Trx) Protein**
Thioredoxin (Trx) is a small, highly conserved redox protein (~12 kDa) originally identified in *Escherichia coli*. It plays a critical role in maintaining cellular redox homeostasis through its active site motif (Cys-X-X-Cys), which enables reversible oxidation-reduction reactions. Trx facilitates the reduction of disulfide bonds in target proteins, supporting processes like DNA synthesis, antioxidant defense, and regulation of transcription factors. Its stability, solubility, and simple structure make it an attractive tool for recombinant protein production.
Recombinant Trx is widely engineered using bacterial expression systems (e.g., *E. coli*) due to its high yield and ease of purification. It is often employed as a fusion partner to enhance the solubility and proper folding of heterologous proteins that are prone to aggregation, such as antibodies or viral antigens. For example, the Trx fusion system (e.g., pET-32a vector) is routinely used in structural biology to improve protein crystallizability.
Beyond biotechnology applications, Trx has therapeutic relevance. Human Trx (hTrx) is implicated in modulating oxidative stress, inflammation, and apoptosis, linking it to diseases like cancer, neurodegeneration, and cardiovascular disorders. Recombinant hTrx has been explored as a therapeutic agent or drug target. Additionally, plant Trx systems are studied for improving stress tolerance in crops.
Research on Trx continues to expand, driven by its versatility in industrial protein production, its role in redox signaling, and its potential in medical and agricultural innovations. Advances in protein engineering and synthetic biology are further optimizing Trx-based platforms for tailored applications.
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