| 纯度 | >85%SDS-PAGE. |
| 种属 | Human |
| 靶点 | TRX1 |
| Uniprot No | P52348 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-299aa |
| 氨基酸序列 | MNSKSSARAAIVDTVEAVKKRKYISIDEGTLNNVVEKERKFLKQFLSGRQNLRIAARVFTPCELLAPELENLGMLMYRFETDVDNPKILFVGLFFLCSNAFNVSTCVRTALTAMYTNSMVDNVLSMINTCRYLEDKVSLFGVTSLVSCGSSCLLSCVMQGNVYDVNKENIYGLTVLKEIILEPDWEPRQHSTQYVYVVHVYKEVLAKLQYGIYVVLTSFQNEDLIVDILRQYFEKERFLFLNYLINSNTTLSYFGSVQRIGRCATEDIKSGFLQYRGITLSVIKLENIFVDLSEKKVFV |
| 预测分子量 | 40.2 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TRX1重组蛋白的3篇参考文献示例(注：以下文献为虚构示例，仅用于演示格式)：
---
1. **文献名称**：*Recombinant Human TRX1 Protects Against Oxidative Stress in Alzheimer’s Disease Models*
**作者**：Yamamoto A. et al.
**摘要**：本研究通过体外表达重组TRX1蛋白，探究其对阿尔茨海默病细胞模型中氧化应激的调控作用。实验表明，重组TRX1显著减少神经元活性氧(ROS)水平，抑制tau蛋白过度磷酸化，并改善线粒体功能，提示其潜在神经保护价值。
2. **文献名称**：*Structural and Functional Characterization of Recombinant TRX1 in Cardiovascular Repair*
**作者**：Chen L. et al.
**摘要**：通过大肠杆菌系统表达并纯化重组TRX1.结合小鼠心肌缺血再灌注损伤模型，发现其通过抑制NF-κB通路减轻炎症反应，降低心肌细胞凋亡率，为心血管疾病治疗提供新策略。
3. **文献名称**：*Enhancing Chemotherapy Efficacy via Recombinant TRX1-Mediated Redox Modulation*
**作者**：Zhang R. et al.
**摘要**：研究证实重组TRX1可选择性调节卵巢癌细胞的氧化还原稳态，增强顺铂对癌细胞的毒性，同时保护正常组织免受氧化损伤，为化疗辅助疗法开发奠定基础。
---
**备注**：以上文献及内容均为模拟创作，实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实文献。
TRX1 (Thioredoxin-1) is a small, evolutionarily conserved redox protein belonging to the thioredoxin family, pivotal in regulating cellular redox homeostasis. Initially identified in *E. coli*, human TRX1 is a 12 kDa protein encoded by the *TXN* gene, characterized by a conserved CXXC active site motif (Cys-Gly-Pro-Cys) that facilitates its redox activity. It functions as a potent antioxidant by catalyzing the reduction of disulfide bonds in target proteins, thereby neutralizing reactive oxygen species (ROS) and maintaining cellular redox balance. TRX1 interacts with thioredoxin reductase and NADPH to form a key antioxidant system, critical for DNA synthesis, apoptosis regulation, and defense against oxidative stress.
Beyond its redox role, TRX1 participates in signaling pathways, modulating transcription factors like NF-κB and AP-1. and influencing inflammatory responses, immune regulation, and cell survival. Its overexpression is linked to cancer progression and resistance to chemotherapy, while deficiencies are associated with neurodegenerative, cardiovascular, and metabolic disorders.
Recombinant TRX1 is produced via genetic engineering in systems like *E. coli* or mammalian cells, ensuring high purity and bioactivity. This engineered protein retains native structure and function, making it invaluable for studying redox mechanisms, protein-protein interactions, and oxidative stress-related pathologies. In therapeutic research, recombinant TRX1 is explored for its anti-inflammatory, anti-apoptotic, and cytoprotective properties, with potential applications in treating ischemic injuries, neurodegenerative diseases, and age-related conditions. Its versatility also extends to biotechnology, where it serves as a fusion partner to enhance solubility and stability of recombinant proteins. Overall, TRX1 exemplifies a multifunctional protein bridging redox biology and translational medicine.
×
