| 纯度 | >85%SDS-PAGE. |
| 种属 | Escherichia coli |
| 靶点 | TRXB |
| Uniprot No | P0A9P4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-321aa |
| 氨基酸序列 | GTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA GTGCMAALDA ERYLDGLADA K |
| 预测分子量 | 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TRXB重组蛋白的3篇示例参考文献(注：内容为虚构，仅用于格式参考)：
1. **标题**: "High-yield expression and purification of recombinant TRXB in Escherichia coli for enzymatic studies"
**作者**: Chen L., et al.
**摘要**: 本研究报道了在大肠杆菌中优化TRXB(硫氧还蛋白还原酶)重组蛋白的表达与纯化策略，通过密码子优化和温度调控显著提高蛋白产量，并验证其催化活性及在体外抗氧化体系中的应用。
2. **标题**: "Structural insights into the redox mechanism of TRXB through X-ray crystallography"
**作者**: Wang Y., et al.
**摘要**: 通过X射线晶体学解析了重组TRXB蛋白的三维结构，揭示了其活性中心的构象变化及与底物结合的关键氨基酸残基，为设计靶向TRXB的药物提供结构基础。
3. **标题**: "Functional characterization of recombinant TRXB in Helicobacter pylori pathogenesis"
**作者**: Gupta S., et al.
**摘要**: 利用重组TRXB蛋白探究其在幽门螺杆菌氧化应激耐受中的作用，证实TRXB通过调节硫氧还蛋白系统维持细菌内环境稳态，是潜在的抗菌治疗靶点。
如需真实文献，建议在PubMed或Web of Science中检索关键词："thioredoxin reductase recombinant expression/production/function"。
**Background of Recombinant TRXB Protein**
Thioredoxin reductase (TRXB), a key enzyme in the thioredoxin system, plays a central role in maintaining cellular redox homeostasis. It catalyzes the reduction of oxidized thioredoxin (Trx) using NADPH as an electron donor, thereby supporting critical processes like DNA synthesis, antioxidant defense, and regulation of apoptosis. TRXB is a flavoprotein, typically containing a conserved FAD-binding domain and a redox-active disulfide motif. In humans, its dysfunction is linked to oxidative stress-related diseases, including cancer, neurodegenerative disorders, and inflammatory conditions.
Recombinant TRXB is engineered through heterologous expression in microbial (e.g., *E. coli*) or eukaryotic systems, enabling scalable production for research and industrial applications. Its recombinant form retains catalytic activity and structural stability, making it valuable for studying redox signaling pathways, protein-folding mechanisms, and enzyme kinetics. Additionally, recombinant TRXB is utilized in biopharmaceutical manufacturing to enhance disulfide bond formation in therapeutic proteins, ensuring proper folding and functionality.
Recent advancements in protein engineering have optimized recombinant TRXB for improved thermostability, substrate specificity, and resistance to oxidative inactivation. These modifications expand its utility in harsh industrial conditions or therapeutic contexts requiring prolonged activity. Furthermore, recombinant TRXB serves as a tool in drug discovery, particularly for screening inhibitors targeting the thioredoxin system in cancer or infectious diseases.
Overall, recombinant TRXB bridges fundamental redox biology with practical applications, offering insights into cellular stress responses while driving innovations in biotechnology and medicine.
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