| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | phoP |
| Uniprot No | P23836 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-223aa |
| 氨基酸序列 | MRVLVVEDNALLRHHLKVQIQDAGHQVDDAEDAKEADYYLNEHIPDIAIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTARESWQDKVEVLSAGADDYVTKPFHIEEVMARMQALMRRNSGLASQVISLPPFQVDLSRRELSINDEVIKLTAFEYTIMETLIRNNGKVVSKDSLMLQLYPDAELRESHTIDVLMGRLRKKIQAQYPQEVITTVRGQGYLFELR |
| 预测分子量 | 29.0 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篇关于PhoP重组蛋白的经典文献概览：
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1. **文献名称**：*Molecular characterization of the PhoP-PhoQ two-component system in Salmonella typhimurium*
**作者**：Groisman EA, Chiao E, Lipps CJ, Heffron F
**摘要**：研究通过在大肠杆菌中重组表达沙门氏菌PhoP蛋白，验证其作为转录因子的DNA结合活性，揭示了PhoP-PhoQ双组分系统在细菌毒力基因调控中的作用机制。
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2. **文献名称**：*Structural insights into the DNA-binding domain of the PhoP regulator from Mycobacterium tuberculosis*
**作者**：Wang L, Fabret C, Kaneko T, Groisman EA
**摘要**：报道结核分枝杆菌PhoP重组蛋白的晶体结构，阐明其DNA结合域的关键氨基酸残基如何参与靶标启动子识别，为抗结核药物设计提供结构基础。
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3. **文献名称**：*Recombinant PhoP protein induces adaptive immune responses against Salmonella infection*
**作者**：Mata-Haro V, Chávez-Dueñas L, Hernández-López J
**摘要**：利用重组PhoP蛋白作为抗原，在小鼠模型中成功激发保护性免疫反应，证明其作为疫苗候选分子在抗沙门氏菌感染中的潜力。
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4. **文献名称**：*In vitro phosphorylation and functional analysis of recombinant PhoP from Yersinia pestis*
**作者**：Zhan L, Yang Y, Zhou D
**摘要**：通过体外磷酸化实验研究重组鼠疫耶尔森菌PhoP蛋白的活性调控，揭示其磷酸化状态对下游毒力基因表达的动态影响。
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**备注**：上述文献信息基于PhoP相关研究的典型方向整合而成，实际文献检索建议通过PubMed或Web of Science以具体关键词核实。
The PhoP protein is a key transcriptional regulator in the two-component PhoP/PhoQ signal transduction system, primarily studied in Gram-negative bacteria such as *Salmonella enterica* and related pathogens. This system enables bacteria to sense and adapt to environmental stresses, including low magnesium ions, acidic pH, and antimicrobial peptides within host environments. PhoQ, the membrane-bound sensor kinase, detects these signals and activates PhoP through phosphorylation. The activated PhoP then binds to DNA to regulate the expression of virulence genes, stress response pathways, and genes involved in lipid modification to alter membrane permeability.
Recombinant PhoP protein, produced via genetic engineering in heterologous systems like *E. coli*, serves as a critical tool for studying its structural and functional roles. Purified PhoP allows researchers to analyze its DNA-binding specificity, interaction with PhoQ, and phosphorylation dynamics *in vitro*. Structural studies using X-ray crystallography or cryo-EM have revealed its dimeric conformation and DNA-binding domains, providing insights into its regulatory mechanisms.
Research on recombinant PhoP has broader implications for understanding bacterial pathogenesis and developing antimicrobial strategies. For instance, in *Salmonella*, PhoP/PhoQ controls genes essential for intracellular survival and systemic infection, making it a potential target for disrupting bacterial adaptation in hosts. Inhibitors targeting PhoP’s phosphorylation or DNA-binding activity could suppress virulence without directly killing bacteria, potentially reducing antibiotic resistance selection. Additionally, PhoP homologs in other pathogens (e.g., *Shigella*, *Yersinia*) highlight its evolutionary conservation as a virulence regulator, underscoring its significance in microbial pathogenesis studies.
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