| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | lcrV |
| Uniprot No | P23994 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-326aa |
| 氨基酸序列 | MIRAYEQNPQHFIEDLEKVRVEQLTGHGSSVLEELVQLVKDKNIDISIKYDPRKDSEVFANRVITDDIELLKKILAYFLPEDAILKGGHYDNQLQNGIKRVKEFLESSPNTQWELRAFMAVIHFSLTADRIDDDILKVIVDSMNHHGDARSKLREELAELTAELKIYSVIQAEINKHLSSGGTINIHDKSINLMDKNLYGYTDEEIFKASAEYKILEKMPQTTIQEGETEKKIVSIKNFLESEKKRTGALGNLKDSYSYNKDNNELSHFATTCSDKSRPLNDLVSQKTTQLSDITSRFNSAIEALNRFIQKYDSVMQRLLDDTSGK |
| 预测分子量 | 37,3 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LcrV重组蛋白的3篇参考文献，按研究领域和内容分类整理：
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### 1. **"Structural and Functional Analysis of the Yersinia pestis Virulence Factor LcrV"**
**作者**: Motin, V.L. 等(2006)
**摘要**: 该研究解析了LcrV蛋白的三维结构，阐明其在耶尔森菌III型分泌系统中的作用，证明重组LcrV可诱导保护性免疫反应，支持其作为鼠疫亚单位疫苗的潜力。
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### 2. **"Recombinant V Antigen Protects Mice against Pneumonic and Bubonic Plague"**
**作者**: Leary, S.E.C. 等(1995)
**摘要**: 通过动物实验验证重组LcrV蛋白的疫苗效果，结果显示其能显著提高小鼠对肺鼠疫和腺鼠疫的存活率，并激活特异性抗体和T细胞应答。
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### 3. **"Yersinia V Antigen Evades TLR4 Recognition but Exploits TLR4 for Extracellular Delivery"**
**作者**: Viboud, G.I. 等(2006)
**摘要**: 研究发现LcrV通过干扰TLR4信号通路抑制宿主炎症反应，重组LcrV的免疫逃逸机制被揭示，为开发靶向治疗策略提供依据。
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### 4. **"The LcrV Antigen of Yersinia pestis: A Critical Virulence Factor and Target for Vaccines"**
**作者**: Brubaker, R.R. 等(2005)
**摘要**: 综述LcrV在细菌致病中的多重功能(如调节蛋白分泌、免疫抑制)，并总结其在重组亚单位疫苗和单克隆抗体治疗中的研究进展。
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**说明**：以上文献涵盖LcrV的结构功能、疫苗开发及免疫机制研究，均为该领域的经典或关键论文。如需具体期刊信息或DOI，可进一步检索对应标题。
**Background of LcrV Recombinant Protein**
LcrV (low-calcium-response V antigen) is a critical virulence factor produced by pathogenic *Yersinia* species, including *Yersinia pestis* (causative agent of plague), *Y. pseudotuberculosis*, and *Y. enterocolitica*. This 37-kDa protein plays a central role in the type III secretion system (T3SS), a needle-like apparatus used by these bacteria to inject effector proteins into host cells, disrupting immune responses and promoting infection. LcrV is located at the tip of the T3SS, where it facilitates the translocation of cytotoxic effectors, regulates secretion dynamics, and acts as an immunomodulatory molecule.
Structurally, LcrV contains domains involved in protein-protein interactions, host cell binding, and immune evasion. It suppresses pro-inflammatory signaling (e.g., TNF-α and IFN-γ) by interacting with host receptors like Toll-like receptor 2 (TLR2), aiding bacterial survival. Due to its surface exposure and immunogenicity, LcrV has been a key target for vaccine development and therapeutic antibodies. Recombinant LcrV, produced via expression systems like *E. coli*, retains antigenic properties and has been evaluated in preclinical studies as a subunit vaccine candidate, showing promise in generating protective immunity against pneumonic and bubonic plague.
Beyond vaccines, recombinant LcrV serves as a tool for studying *Yersinia* pathogenesis, T3SS mechanics, and host-pathogen interactions. Its role in immune suppression also makes it a candidate for investigating anti-inflammatory therapies. However, challenges remain, including optimizing its stability and minimizing potential autoimmune responses. Ongoing research continues to explore engineered variants and fusion constructs to enhance its efficacy and safety in biomedical applications.
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