| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | aTRX |
| Uniprot No | P46100 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2311-2410aa |
| 氨基酸序列 | FNLGALSAMSNQQLEDLINQGREKVVEATNSVTAVRIQPLEDIISAVWKE NMNLSEAQVQALALSRQASQELDVKRREAIYNDVLTKQQMLISCVQRILM |
| 预测分子量 | 37 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篇与aTRX(重组硫氧还蛋白)相关的文献摘要信息：
1. **《Expression and purification of recombinant human thioredoxin in Escherichia coli》**
- 作者：Holmgren A, et al.
- 摘要：研究报道了人源硫氧还蛋白(TRX)在大肠杆菌中的高效重组表达及纯化方法，验证了其抗氧化活性及作为分子伴侣在蛋白折叠中的应用潜力。
2. **《Structural and functional analysis of aTRX fusion proteins in enhancing solubility of target proteins》**
- 作者：LaVallie ER, et al.
- 摘要：探讨了aTRX作为融合标签提升难溶蛋白可溶性的机制，通过结构分析揭示其作用原理，并应用于多个工业酶的表达优化。
3. **《Application of recombinant thioredoxin in redox-sensitive drug delivery systems》**
- 作者：Yoshida T, et al.
- 摘要：开发了一种基于aTRX的纳米药物载体系统，利用其氧化还原响应特性实现靶向释放，显著提高了抗癌药物的递送效率并降低副作用。
注：以上文献为模拟概括，实际研究中建议通过PubMed或Web of Science检索具体论文。若需真实文献，可提供更详细关键词或研究方向进一步筛选。
**Background of aTRX Recombinant Protein**
Thioredoxin (TRX) is a small, evolutionarily conserved redox protein found in all living organisms, playing a critical role in maintaining cellular redox homeostasis. It functions as a disulfide reductase, facilitating the reduction of oxidized cysteine residues in target proteins via its conserved CXXC active site. This activity is essential for processes such as DNA synthesis, antioxidant defense, and regulation of enzyme activity.
The *archaeal* thioredoxin (aTRX) variant, derived from extremophilic archaea, exhibits unique stability under harsh conditions (e.g., high temperature, extreme pH), making it a robust candidate for biotechnological applications. Recombinant aTRX is produced using genetic engineering techniques, where the gene encoding aTRX is cloned into expression vectors (e.g., *E. coli*) and purified to homogeneity. Its recombinant form retains the native structural and functional properties, including thermostability and efficient redox activity.
aTRX has gained attention in industrial and research settings. It serves as a fusion partner to enhance solubility and stability of recombinant proteins, a tool for studying redox mechanisms, and a component in diagnostic kits or enzyme-based assays. Its resilience also positions it as a potential therapeutic agent for oxidative stress-related diseases. Overall, aTRX exemplifies how extremophile-derived proteins can address challenges in protein engineering, industrial catalysis, and biomedical research.
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