| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TXN |
| Uniprot No | P10599 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-105aa |
| 氨基酸序列 | VKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV |
| 预测分子量 | 38.6 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TXN(硫氧还蛋白)重组蛋白的参考文献示例(内容为模拟概括，仅供参考)：
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1. **文献名称**: *Recombinant human thioredoxin-1 ameliorates experimental sepsis by modulating inflammation and oxidative stress*
**作者**: Masutani H, et al.
**摘要**: 研究重组人TXN蛋白在小鼠败血症模型中的治疗作用，发现其通过抑制NF-κB通路减少炎症因子释放，同时清除活性氧(ROS)，改善器官损伤。
2. **文献名称**: *Engineering a stable mutant of thioredoxin for enhanced antioxidant activity*
**作者**: Nakamura H, et al.
**摘要**: 通过定点突变技术改造TXN重组蛋白，提高其热稳定性和抗氧化能力，体外实验表明突变体在氧化应激细胞模型中保护效果优于野生型。
3. **文献名称**: *Thioredoxin suppresses cisplatin-induced apoptosis via regulating ASK1 signaling in cancer cells*
**作者**: Saitoh M, et al.
**摘要**: 探讨重组TXN蛋白在化疗药物顺铂诱导的癌细胞凋亡中的作用，发现其通过抑制ASK1-JNK通路减少细胞死亡，提示其在化疗副作用防护中的潜在价值。
4. **文献名称**: *Targeted delivery of recombinant thioredoxin fusion protein for cancer therapy*
**作者**: Kato Y, et al.
**摘要**: 开发了一种TXN与肿瘤靶向肽融合的重组蛋白，证明其能选择性递送至肿瘤组织，通过调节肿瘤微环境中的氧化还原状态抑制肿瘤生长。
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**注**：以上文献信息为示例性虚构，实际文献需通过PubMed、Web of Science等数据库检索确认。如需真实文献，建议以“recombinant thioredoxin”为关键词进行学术检索。
Thioredoxin (TXN) is a small, evolutionarily conserved redox-active protein (~12 kDa) central to cellular redox regulation. It features a conserved Cys-Gly-Pro-Cys catalytic motif that enables its primary function: catalyzing disulfide bond reduction in target proteins via thiol-disulfide exchange. This activity is critical for maintaining cellular redox homeostasis, DNA synthesis (by reducing ribonucleotide reductase), and antioxidant defense. TXN is regenerated by thioredoxin reductase (TrxR) using NADPH as an electron donor, forming the TXN/TrxR redox system.
Recombinant TXN proteins are engineered using expression systems like *E. coli* or yeast, allowing large-scale production with high purity and stability. They retain native structural and functional properties, including interactions with partners like peroxiredoxins and transcription factors (e.g., NF-κB, Ref-1). Recombinant TXN is widely utilized as a solubility-enhancing fusion tag for difficult-to-express proteins, leveraging its stable, soluble nature. In research, it serves as a tool to study oxidative stress-related diseases (cancer, neurodegeneration) and viral infections (e.g., HIV, where TXN interacts with viral proteins).
Pharmaceutically, TXN overexpression is linked to cancer chemoresistance, making it a therapeutic target. Inhibitors like PX-12 and recombinant TXN itself are explored for modulating redox signaling in pathologies. Its role in mitigating ROS damage and regulating apoptosis also positions it as a candidate for anti-aging and anti-inflammatory therapies. Advances in protein engineering, including site-specific mutations (e.g., C35S for substrate trapping) and tagged variants (His-tag, FLAG), have expanded its experimental versatility. Overall, recombinant TXN bridges fundamental redox biology and translational applications, from biotechnology to drug development.
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