| 纯度 | >90%SDS-PAGE. |
| 种属 | Salmonella |
| 靶点 | phoQ |
| Uniprot No | P0DM80 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 215-487aa |
| 氨基酸序列 | WWSLRPIEALAREVRELEDHHREMLNPETTRELTSLVRNLNQLLKSERERYNKYRTTLTDLTHSLKTPLAVLQSTLRSLRNEKMSVSKAEPVMLEQISRISQQIGYYLHRASMRGSGVLLSRELHPVAPLLDNLISALNKVYQRKGVNISMDISPEISFVGEQNDFVEVMGNVLDNACKYCLEFVEISARQTDDHLHIFVEDDGPGIPHSKRSLVFDRGQRADTLRPGQGVGLAVAREITEQYAGQIIASDSLLGGARMEVVFGRQHPTQKEE |
| 预测分子量 | 38.5 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. |
以下是基于公开研究整理的3篇与PhoQ重组蛋白相关的模拟参考文献示例(非真实文献，供参考)：
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1. **文献名称**: *Structural insights into PhoQ histidine kinase activation by divalent cations*
**作者**: Cho, U.S. et al.
**摘要**: 通过冷冻电镜解析了沙门氏菌PhoQ胞外结构域在镁离子结合状态下的构象变化，揭示了金属离子诱导的二聚体界面重排如何触发跨膜信号传导，为PhoQ感知宿主低镁环境的分子机制提供结构依据。
2. **文献名称**: *PhoQ/PhoP-regulated genes mediate Salmonella virulence in low magnesium conditions*
**作者**: Miller, S.I. et al.
**摘要**: 研究证明PhoQ重组蛋白通过感知宿主细胞内低镁浓度激活PhoP转录因子，进而调控沙门氏菌毒力基因(如pmrD)的表达，揭示该双组分系统在细菌适应宿主免疫中的关键作用。
3. **文献名称**: *Engineering PhoQ-based biosensors for heavy metal detection*
**作者**: Jung, H. et al.
**摘要**: 利用重组PhoQ蛋白构建合成生物学传感器，通过改造其金属离子结合域实现对镉离子的特异性响应，并耦合报告基因系统开发出高灵敏度的环境重金属检测工具。
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*注：以上文献信息为模拟生成，实际引用时请以真实学术数据库检索结果为准。如需查找真实文献，可通过PubMed或Google Scholar搜索关键词“PhoQ recombinant protein”“PhoQ/PhoP signaling”等。*
PhoQ is a histidine kinase sensor protein that plays a central role in bacterial signal transduction pathways, particularly in Gram-negative bacteria like *Salmonella enterica* and *Escherichia coli*. It forms a two-component regulatory system with its cognate response regulator, PhoP, to mediate adaptive responses to environmental stresses. PhoQ is activated by extracellular signals such as low magnesium (Mg²⁺) concentrations, acidic pH, and antimicrobial peptides (AMPs) produced by host organisms during infection. Upon activation, it autophosphorylates and transfers the phosphate group to PhoP, which subsequently regulates the expression of genes involved in virulence, membrane remodeling, and resistance to host defense mechanisms.
Structurally, PhoQ consists of a periplasmic sensor domain connected via transmembrane helices to cytoplasmic kinase and regulatory domains. The periplasmic domain detects environmental cues, while the cytoplasmic region orchestrates phosphorylation-dependent signaling. Its ability to sense host-derived AMPs links PhoQ to bacterial pathogenesis, enabling pathogens to modulate their outer membrane composition (e.g., lipid A modifications) to evade immune detection.
Recombinant PhoQ proteins are produced via heterologous expression systems (e.g., *E. coli*) for biochemical and structural studies. These engineered variants allow researchers to dissect PhoQ’s signaling mechanisms, ligand interactions, and regulatory roles. Studies on PhoQ have implications for understanding antibiotic resistance and developing antimicrobial strategies, as disrupting PhoQ/PhoP signaling could attenuate bacterial virulence. Additionally, PhoQ homologs in other pathogens highlight its evolutionary conservation as a key mediator of host-microbe interactions. Research continues to explore its potential as a therapeutic target and a tool for synthetic biology applications.
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