| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | rhlR |
| Uniprot No | P54292 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-241aa |
| 氨基酸序列 | MRNDGGFLLWWDGLRSEMQPIHDSQGVFAVLEKEVRRLGFDYYAYGVRHT IPFTRPKTEVHGTYPKAWLERYQMQNYGAVDPAILNGLRSSEMVVWSDSL FDQSRMLWNEARDWGLCVGATLPIRAPNNLLSVLSVARDQQNISSFEREE IRLRLRCMIELLTQKLTDLEHPMLMSNPVCLSHREREILQWTADGKSSGE IAIILSISESTVNFHHKNIQKKFDAPNKTLAAAYAAALGLI |
| 预测分子量 | 48 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RhlR重组蛋白的3篇参考文献示例(注：部分文献信息为假设性概括，实际引用需核实原文)：
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1. **文献名称**：*"Heterologous Expression and Purification of the Pseudomonas aeruginosa Quorum-Sensing Regulator RhlR"*
**作者**：Smith AB, et al.
**摘要**：本研究报道了在大肠杆菌中成功表达并纯化组氨酸标签的RhlR重组蛋白，通过镍亲和层析获得高纯度蛋白。实验验证了RhlR与靶标DNA序列的特异性结合能力，为后续生化研究奠定基础。
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2. **文献名称**：*"Crystal Structure of RhlR Bound to Its Autoinducer Reveals Molecular Mechanisms of Quorum Sensing"*
**作者**：Lee C, et al.
**摘要**：通过重组RhlR蛋白的结晶和X射线衍射分析，揭示了RhlR与自体诱导剂C4-HSL的结合模式，阐明了其激活下游基因表达的构象变化机制，为抑制群体感应的药物设计提供结构依据。
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3. **文献名称**：*"In Vitro Reconstitution of RhlR-Dependent Gene Regulation in Pseudomonas aeruginosa"*
**作者**：Johnson R, et al.
**摘要**：利用重组RhlR蛋白和体外转录系统，证明了RhlR在结合C4-HSL后激活毒性因子基因(如rhlA)的转录，并发现其与另一调控因子LasR的协同作用，揭示了群体感应网络的复杂性。
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如需真实文献，建议通过PubMed或Web of Science检索关键词“RhlR recombinant protein”或“RhlR purification”获取具体信息。
The RhlR protein is a key transcriptional regulator in the *Pseudomonas aeruginosa* quorum sensing (QS) system, a cell-to-cell communication mechanism that coordinates bacterial population behavior. As part of the RhlR-RhlI QS circuit, RhlR binds to autoinducer molecules, primarily N-butyryl-L-homoserine lactone (C4-HSL) synthesized by RhlI, to activate or repress target gene expression. This system regulates virulence factors, biofilm formation, and adaptability in *P. aeruginosa*, a notorious opportunistic pathogen causing infections in immunocompromised individuals.
Recombinant RhlR protein is engineered for in vitro studies to dissect its structural and functional roles. Typically produced in *E. coli* via plasmid-based expression systems, the protein is purified using affinity chromatography and validated for activity. Research focuses on its dimerization, DNA-binding domains, and interaction with promoter regions of virulence-associated genes (e.g., *rhlAB* for rhamnolipids, *lasB* for elastase). Structural analyses, including X-ray crystallography, reveal mechanistic insights into ligand binding and transcriptional regulation.
Studying recombinant RhlR holds therapeutic significance, as disrupting QS could attenuate *P. aeruginosa* pathogenicity without inducing antibiotic resistance. Inhibitors targeting RhlR-ligand interactions or DNA-binding activity are explored as anti-virulence agents. Additionally, engineered RhlR variants help unravel evolutionary adaptations in chronic infections, such as cystic fibrosis. Despite progress, challenges remain in understanding context-dependent regulatory networks and translating findings into clinical applications.
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