| 纯度 | >90%SDS-PAGE. |
| 种属 | Mycoplasma |
| 靶点 | vlpF |
| Uniprot No | Q49538 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 30-67aa |
| 氨基酸序列 | CGQTNTDQSQQPGSGSGSGSGTSNGSGSTPTPEQGNNQ |
| 预测分子量 | 18.9 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VlpF重组蛋白的参考文献，信息基于模拟数据整理：
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1. **文献名称**: *"Functional Characterization of VlpF in Vibrio cholerae Flagellar Assembly"*
**作者**: Smith A, et al.
**摘要**: 研究报道了霍乱弧菌VlpF蛋白在鞭毛组装中的关键作用，通过重组蛋白表达证实其与鞭毛基座的相互作用，并揭示其调控细菌运动性的分子机制。
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2. **文献名称**: *"Recombinant VlpF Production and Its Role in Biofilm Formation"*
**作者**: Lee JH, Kim B.
**摘要**: 文章描述了重组VlpF蛋白在大肠杆菌中的高效表达与纯化，并通过体外实验证明其通过调控胞外多糖合成促进细菌生物膜形成。
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3. **文献名称**: *"Structural Analysis of VlpF Recombinant Protein in Pseudomonas aeruginosa"*
**作者**: Zhang Y, et al.
**摘要**: 本研究解析了铜绿假单胞菌VlpF重组蛋白的晶体结构，结合功能实验阐明其通过稳定鞭毛马达结构来维持细菌趋化性，为抗感染靶点开发提供依据。
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(注：以上文献为模拟生成，实际研究中建议通过PubMed/Google Scholar以“VlpF recombinant protein”等关键词检索具体文献。)
**Background of VlpF Recombinant Protein**
VlpF is a surface-exposed lipoprotein identified in *Campylobacter jejuni*, a leading bacterial cause of gastroenteritis worldwide. This protein belongs to the variable lipoprotein (Vlp) family, characterized by their role in bacterial adhesion, colonization, and immune evasion. VlpF exhibits phase-variable expression, a mechanism mediated by slippage-like repeats in its coding sequence, allowing *C. jejuni* to adapt to diverse host environments and evade host immune responses.
The recombinant VlpF protein is produced via genetic engineering, typically by cloning the *vlpF* gene into expression vectors (e.g., *E. coli* systems) to enable large-scale purification. Its recombinant form retains key functional domains, including regions implicated in host cell binding and modulation of Toll-like receptor (TLR) signaling pathways. Studies suggest VlpF interacts with host epithelial cells, facilitating bacterial persistence and pathogenesis.
Research on recombinant VlpF focuses on elucidating its role in *C. jejuni* virulence and host-pathogen interactions. It is also explored as a diagnostic antigen or vaccine candidate due to its immunogenicity and surface accessibility. However, challenges remain in understanding its structural variability and precise mechanisms in infection. Recent advances in structural biology and immunoproteomics have accelerated its characterization, highlighting its potential as a target for therapeutic or preventive strategies against campylobacteriosis.
In summary, VlpF recombinant protein serves as a critical tool for studying *C. jejuni* biology and developing interventions against this globally significant pathogen.
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