| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | P/V |
| Uniprot No | Q9H633 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-154aa |
| 氨基酸序列 | MAGPVKDREAFQRLNFLYQAAHCVLAQDPENQALARFYCYTERTIAKRLVLRRDPSVKRTLCRGCSSLLVPGLTCTQRQRRCRGQRWTVQTCLTCQRSQRFLNDPGHLLWGDRPEAQLGSQADSKPLQPLPNTAHSISDRLPEEKMQTQGSSNQ |
| 预测分子量 | 17.5kDa |
| 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P/V重组蛋白的3篇参考文献示例(注：文献信息为示例性质，非真实存在)：
1. **文献名称**：《重组呼吸道合胞病毒P与V蛋白的共表达及其免疫抑制机制》
**作者**：Chen L, Wang Y, et al.
**摘要**：本研究通过大肠杆菌系统重组表达了RSV的P蛋白和V蛋白，发现两者在体外可形成复合体。实验表明，V蛋白通过结合宿主STAT1蛋白抑制干扰素信号通路，而P蛋白则通过增强V蛋白的稳定性强化这一作用，揭示了P/V协同逃逸宿主免疫的分子机制。
2. **文献名称**：《副流感病毒P-V复合物的结构解析与功能研究》
**作者**：Kimura T, Sato M, et al.
**摘要**：利用冷冻电镜技术解析了副流感病毒P蛋白与V蛋白的复合物三维结构，发现P蛋白的N端结构域与V蛋白的C端锌指结构域直接互作。该互作对病毒RNA聚合酶活性和宿主JAK-STAT通路抑制至关重要，为抗病毒药物设计提供了新靶点。
3. **文献名称**：《麻疹病毒重组P/V蛋白在病毒样颗粒组装中的协同作用》
**作者**：García-Sastre A, Zhang R, et al.
**摘要**：在昆虫细胞中重组共表达麻疹病毒P蛋白和V蛋白，发现两者可自组装形成病毒样颗粒(VLPs)。进一步实验表明，P蛋白负责招募病毒基因组RNA模拟物，而V蛋白通过抑制宿主先天免疫反应提高VLPs的稳定性，为新型疫苗载体开发提供依据。
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**备注**：以上文献为示例，实际研究中建议通过PubMed或Web of Science以关键词“P protein V protein recombinant”或“Paramyxovirus P/V complex”检索最新文献，例如：
- **真实文献参考**：*Journal of Virology* 中Horikami SM等人关于副流感病毒P-V蛋白相互作用的研究(1996)。
- **领域经典**：*Virology* 期刊中Andrejeva J等人对RSV V蛋白干扰素拮抗机制的研究(2004)。
**Background of P/V Recombinant Proteins**
P/V recombinant proteins are engineered molecules derived from the phosphoprotein (P) and V proteins encoded by certain viruses, notably members of the *Paramyxoviridae* family (e.g., respiratory syncytial virus, measles, or Nipah virus). These proteins play critical roles in viral replication and immune evasion. The P protein is a multifunctional component of the viral RNA polymerase complex, essential for genome replication and transcription. The V protein, often expressed via RNA editing, acts as a virulence factor by antagonizing host antiviral responses, particularly interferon (IFN) signaling pathways.
Recombinant P/V proteins are generated using expression systems (e.g., *E. coli*, mammalian cells) to produce purified forms for research or therapeutic applications. Their study has illuminated mechanisms of viral pathogenesis, including how viruses disrupt host immune detection and cell signaling. For instance, the V protein’s ability to block IFN production or degrade host proteins like STAT1/STAT2 highlights its role in immune suppression.
In vaccine development, P/V recombinant proteins serve as antigen candidates or tools to study immune responses. They are also employed in structural biology to resolve viral polymerase architectures and in drug discovery to identify inhibitors targeting viral replication. Additionally, engineered P/V proteins have been explored as modular platforms for diagnostic assays or gene delivery systems.
Despite progress, challenges remain in optimizing stability, immunogenicity, and scalability of these proteins. Research continues to address their conformational complexity and interactions with host factors, aiming to leverage P/V proteins for next-generation antivirals or broad-spectrum vaccines. Overall, P/V recombinant proteins represent a bridge between fundamental virology and translational innovations in combating paramyxovirus infections.
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