| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | trxC |
| Uniprot No | P0AGG4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-139aa |
| 氨基酸序列 | MNTVCTHCQAINRIPDDRIEDAAKCGRCGHDLFDGEVINATGETLDKLLKDDLPVVIDFWAPWCGPCRNFAPIFEDVAQERSGKVRFVKVNTEAERELSSRFGIRSIPTIMIFKNGQVVDMLNGAVPKAPFDSWLNESL |
| 预测分子量 | 17.6 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篇与trxC重组蛋白相关的文献及其摘要概述：
1. **文献名称**: "Enhanced solubility of recombinant proteins by fusion with thioredoxin in Escherichia coli"
**作者**: Smith J, et al.
**摘要**: 研究证明将trxC基因作为融合标签与目标蛋白共表达，可显著提高重组蛋白在大肠杆菌中的溶解性，机制与硫氧还蛋白的分子伴侣功能相关。
2. **文献名称**: "Crystallization and functional analysis of TrxC from Bacillus subtilis"
**作者**: Li Y, et al.
**摘要**: 解析了枯草芽孢杆菌TrxC蛋白的晶体结构，揭示其氧化还原活性位点的构象特征，并验证其在体外抗氧化应激中的功能。
3. **文献名称**: "TrxC-based redox system improves disulfide bond formation in eukaryotic proteins expressed in prokaryotes"
**作者**: Chen L, et al.
**摘要**: 提出利用trxC重组蛋白与谷胱甘肽还原酶协同作用，优化原核表达系统中真核蛋白二硫键的正确形成，显著提升蛋白活性。
4. **文献名称**: "Comparative study of thioredoxin family proteins as solubility enhancers in recombinant protein production"
**作者**: Wang H, et al.
**摘要**: 对比多种硫氧还蛋白家族成员(包括trxC)在重组蛋白表达中的效果，发现trxC在高温或高密度培养条件下具有更优的稳定性和促溶解能力。
(注：上述文献信息为模拟生成，实际引用时需根据真实文献核对。)
**Background of TrxC Recombinant Protein**
Thioredoxin (Trx), a small redox protein found ubiquitously in organisms, plays a critical role in maintaining cellular redox homeostasis. The *trxC* gene, encoding thioredoxin in *Escherichia coli*, has been extensively studied for its structural simplicity, stability, and versatile functionality. Recombinant TrxC protein is engineered by cloning and expressing the *trxC* gene in heterologous host systems (e.g., *E. coli* or yeast), enabling large-scale production for research and industrial applications.
TrxC functions as a disulfide reductase, catalyzing dithiol-disulfide exchange reactions via its conserved active-site motif (Cys-Gly-Pro-Cys). This activity supports essential processes like DNA synthesis, antioxidant defense, and proper folding of secreted proteins by reducing incorrect disulfide bonds. Its small size (~12 kDa) and high solubility make it an ideal fusion partner to enhance the stability and solubility of recombinant proteins, particularly in biotechnology workflows.
In research, TrxC recombinant protein is widely utilized as a tool to study redox signaling, oxidative stress, and protein-protein interactions. Industrially, it aids in the production of enzymes, antibodies, and vaccines. Additionally, TrxC's ability to bind and stabilize diverse substrates has spurred interest in drug development, particularly for diseases linked to oxidative damage, such as cancer and neurodegenerative disorders.
The recombinant form retains native-like activity and can be purified efficiently using affinity tags (e.g., His-tag). Its robustness under varying pH and temperature conditions further underscores its practicality. Overall, TrxC recombinant protein exemplifies how a fundamental cellular component can be repurposed into a multifunctional biotechnological asset, bridging basic science and applied innovation.
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