| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | toxR |
| Uniprot No | P09852 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-259aa |
| 氨基酸序列 | MTATDRTPPPLKWLCLGNRDANDGFELFAHGIYARNGALVGSKLSLRERRQRVDLSAFLSGAPPLLAEAAVKHLLARLLCVHRHNTDLELLGKNFIPLHASSLGNAGVCERILASARQLQQHQVELCLLLAIDEQEPASAEYLTSLARLRDSGVRIALHPQRIDTDARQCFAEVDAGLCDYLGLDARLLAPGPLTRNLRQRKSIEYLNRLLVAQDIQMLCLNVDNEELHQQANALPFAFRHGRHYSEPFQAWPFSSPAC |
| 预测分子量 | 32.9 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ToxR重组蛋白的3篇代表性文献及其摘要概括：
1. **"ToxR protein activates the promoters of virulence genes in Vibrio cholerae"**
- 作者：Miller, V. L., & Mekalanos, J. J.
- 摘要：该研究首次证实ToxR作为转录调控因子，直接结合并激活霍乱弧菌中毒力基因(如霍乱毒素基因ctxA和菌毛基因tcpA)的启动子，揭示了其在病原菌致病性调控中的核心作用。
2. **"Control of the ToxR virulence regulon in Vibrio cholerae by environmental stimuli"**
- 作者：DiRita, V. J., & Mekalanos, J. J.
- 摘要：本文探讨环境信号(如温度、pH和渗透压)如何通过ToxR蛋白调控霍乱弧菌的毒力基因表达，揭示了ToxR作为环境感应器协调宿主适应与毒力表达的分子机制。
3. **"Transmembrane transcription activation by ToxR protein in Vibrio cholerae"**
- 作者：Ottemann, K. M., & Mekalanos, J. J.
- 摘要：通过分析ToxR的跨膜结构域，研究发现其通过二聚化作用激活下游基因，提出了跨膜信号传导模型，为理解细菌膜结合转录因子的功能提供了新视角。
4. **"Engineering and functional analysis of recombinant ToxR proteins in E. coli"**
- 作者：Pfau, J. D., & Taylor, R. K.
- 摘要：该研究在大肠杆菌中重组表达并纯化ToxR蛋白，通过定点突变验证其DNA结合域和跨膜结构域的功能，为后续结构解析和工程化应用奠定基础。
以上文献聚焦于ToxR的调控机制、环境响应、结构功能及重组表达研究，涵盖基础生物学和生物技术应用方向。
ToxR is a transmembrane transcriptional regulatory protein first identified in *Vibrio cholerae*, the bacterium responsible for cholera. It plays a central role in coordinating virulence gene expression, particularly under environmental conditions encountered in the human host. ToxR activates the expression of critical virulence factors, including the toxin-coregulated pilus (TCP) and cholera toxin (CT), by binding to specific promoter regions of target genes. Its activity is modulated through interactions with ToxS, a periplasmic protein that stabilizes ToxR and enhances its function. Environmental signals such as temperature, pH, and bile salts influence ToxR activity, enabling *V. cholerae* to adapt to host niches.
Recombinant ToxR protein refers to the genetically engineered version produced in heterologous expression systems (e.g., *E. coli*) for functional and structural studies. Researchers clone the *toxR* gene into expression vectors, allowing controlled production and purification of the protein. Recombinant ToxR has been instrumental in elucidating its DNA-binding mechanisms, dimerization properties, and interaction partners. Studies using purified ToxR have revealed its unique dual-domain structure: an N-terminal cytoplasmic DNA-binding domain and a C-terminal transmembrane domain that senses environmental cues.
This protein is also used to investigate regulatory networks linking virulence to stress responses, such as osmolarity and membrane integrity. Additionally, recombinant ToxR serves as a tool for developing anti-virulence strategies, as disrupting its function could attenuate *V. cholerae* pathogenicity. Its application extends to structural biology (e.g., crystallography) and high-throughput screening for inhibitors. Despite its significance, questions remain about its precise signaling cascade and cross-talk with other regulators like ToxT. Overall, recombinant ToxR remains a key model for understanding bacterial pathogenesis and host-pathogen interactions.
×
