| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | tsx |
| Uniprot No | P0A928 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 23-294aa |
| 氨基酸序列 | AENDKPQYLSDWWHQSVNVVGSYHTRFGPQIRNDTYLEYEAFAKKDWFDFYGYADAPVFFGGNSDAKGIWNHGSPLFMEIEPRFSIDKLTNTDLSFGPFKEWYFANNYIYDMGRNKDGRQSTWYMGLGTDIDTGLPMSLSMNVYAKYQWQNYGAANENEWDGYRFKIKYFVPITDLWGGQLSYIGFTNFDWGSDLGDDSGNAINGIKTRTNNSIASSHILALNYDHWHYSVVARYWHDGGQWNDDAELNFGNGNFNVRSTGWGGYLVVGYNF |
| 预测分子量 | 35.5 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条与TSX重组蛋白相关的研究文献示例(内容基于常见研究方向构造，非真实文献)：
1. **《Structural analysis of TSX (TolC) protein in Escherichia coli》**
- 作者：Koronakis, V., et al.
- 摘要：解析了大肠杆菌TSX(TolC)蛋白的三维晶体结构，揭示了其作为外膜通道蛋白的β桶状结构域，并探讨其在多重耐药性外排泵中的功能机制。
2. **《Heterologous expression and functional characterization of recombinant TSX in Salmonella typhimurium》**
- 作者：Zhang, L., et al.
- 摘要：通过基因重组技术在大肠杆菌中高效表达沙门氏菌TSX蛋白，验证其参与细菌毒素分泌及宿主细胞侵袭的功能，为疫苗开发提供基础。
3. **《Optimization of TSX recombinant protein production using Pichia pastoris》**
- 作者：Wang, Y., et al.
- 摘要：利用毕赤酵母表达系统优化TSX重组蛋白的分泌表达条件，显著提高产量并保留蛋白抗原性，为大规模制备诊断抗体奠定基础。
注：TSX在不同文献中可能指代不同蛋白(如细菌外膜通道蛋白TolC或特定病原体抗原)，建议根据具体研究方向核对文献。
**Background of TSX Recombinant Protein**
TSX (Toxin-antitoxin system X) recombinant protein is a product of genetic engineering techniques designed to study or exploit bacterial toxin-antitoxin (TA) systems. These systems, widespread in prokaryotes, consist of paired genes encoding a stable toxin and a labile antitoxin. Under stress conditions, the antitoxin is degraded, allowing the toxin to inhibit bacterial growth, promoting survival through dormancy or programmed cell death. TSX, often associated with *E. coli* or other Gram-negative bacteria, exemplifies such systems, where the toxin component disrupts essential cellular processes like DNA replication or translation.
Recombinant TSX proteins are synthesized by cloning the toxin gene into expression vectors, followed by purification using affinity chromatography. This allows researchers to study its structure, mechanism, and interactions in controlled settings. TSX recombinant proteins are particularly valuable in antimicrobial research, as understanding toxin activity could lead to novel strategies to combat bacterial persistence or antibiotic resistance. Additionally, engineered TA systems, including TSX, are explored as tools in biotechnology, such as plasmid stabilization in molecular cloning or controlled cell death in synthetic biology applications.
Recent studies also highlight potential biomedical applications, including targeting TA systems to eradicate bacterial biofilms or sensitizing pathogens to antibiotics. However, challenges remain in ensuring specificity and minimizing off-target effects. The development of TSX recombinant proteins underscores the intersection of molecular biology and therapeutic innovation, offering insights into bacterial behavior and paving the way for next-generation antimicrobials. Further research aims to optimize production methods and expand its utility in both industrial and clinical contexts.
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