| 纯度 | >90%SDS-PAGE. |
| 种属 | Mycoplasma |
| 靶点 | vlpE |
| Uniprot No | Q49537 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-243aa |
| 氨基酸序列 | CGQTTDNLSQSQQPGSGTGSGSGTNTENGSNNGSGSGTTNSSGGTNQSGSASGNGSSNSSVSTPDGQHSNPSNPTTSDPKESNPSNPTTSDPKESNPSNPTTSDGQHSNPSNPTTSDPKESNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQHSNPSNPTTSDGQNQNK |
| 预测分子量 | 28.7 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3-4条关于 **vlpE重组蛋白** 的参考文献示例(内容基于模拟文献信息整理)：
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1. **文献名称**: *"Functional characterization of recombinant VlpE protein in Mycoplasma motility"*
**作者**: Hassanpour, S. et al.
**摘要**: 研究通过在大肠杆菌中重组表达丝状支原体的VlpE蛋白，证实其在支原体滑动运动中的关键作用。实验表明，VlpE缺失突变体运动能力显著下降，重组蛋白可部分恢复功能，提示其作为运动相关结构组分的潜力。
2. **文献名称**: *"Immunogenicity evaluation of a novel VlpE-based subunit vaccine against Mycoplasma infections"*
**作者**: Nakane, T. & Shirai, M.
**摘要**: 利用重组VlpE蛋白开发亚单位疫苗，并在小鼠模型中评估免疫效果。结果显示，重组VlpE能诱导高水平抗体和Th1型免疫反应，显著降低病原体载量，为抗支原体感染疫苗设计提供依据。
3. **文献名称**: *"Crystallographic analysis of recombinant VlpE reveals a conserved structural motif in bacterial adhesins"*
**作者**: Tulum, I. et al.
**摘要**: 通过X射线晶体学解析重组VlpE蛋白的三维结构，发现其N端含有保守的β-折叠结构域，可能与宿主细胞黏附相关。研究为靶向VlpE的抗菌药物设计提供了结构基础。
4. **文献名称**: *"Heterologous expression and purification of VlpE protein for diagnostic antigen development"*
**作者**: Zhang, Y. et al.
**摘要**: 报道了一种高效纯化重组VlpE蛋白的方法，并验证其作为诊断抗原的灵敏度与特异性。该蛋白在ELISA检测中可区分自然感染与疫苗接种动物，具有临床应用潜力。
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注：以上文献信息为模拟生成，实际研究中建议通过 **PubMed/Google Scholar** 等数据库检索真实文献。
**Background of VlpE Recombinant Protein**
VlpE (variable lipoprotein E) is a surface-exposed lipoprotein predominantly studied in *Mycoplasma hyopneumoniae*, a pathogenic bacterium responsible for porcine enzootic pneumonia. As a member of the variable lipoproteins family, VlpE exhibits antigenic variation, a survival strategy enabling the pathogen to evade host immune responses by altering surface protein epitopes. This adaptability complicates vaccine development and diagnostic targeting, making VlpE a critical focus in understanding mycoplasma pathogenicity.
Structurally, VlpE contains conserved N-terminal domains for membrane anchoring and variable C-terminal regions that drive antigenic diversity. Its role in bacterial adhesion to host respiratory epithelium highlights its importance in colonization and infection. Recombinant VlpE (rVlpE) is produced via genetic engineering, typically through cloning the *vlpE* gene into expression systems like *Escherichia coli*, followed by purification. This approach allows large-scale production of the protein while retaining immunogenic properties.
Research on rVlpE centers on its application in diagnostics and subunit vaccines. It serves as an antigen in serological assays to detect *M. hyopneumoniae* antibodies, improving disease surveillance. Vaccine studies explore its potential to elicit protective immune responses, though challenges persist due to antigenic variability. Additionally, rVlpE aids in studying host-pathogen interactions, such as immune evasion mechanisms and lipoprotein-mediated inflammation.
Despite progress, gaps remain in understanding how VlpE variation impacts cross-strain immunity or influences vaccine efficacy. Ongoing work aims to characterize conserved epitopes for broad-spectrum solutions, emphasizing rVlpE’s dual role as a research tool and therapeutic candidate in combating mycoplasma infections.
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