纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | fliC |
Uniprot No | P04949 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 2-498aa |
氨基酸序列 | AQVINTNSLSLITQNNINKNQSALSSSIERLSSGLRINSAKDDAAGQAIANRFTSNIKGLTQAARNANDGISVAQTTEGALSEINNNLQRVRELTVQATTGTNSESDLSSIQDEIKSRLDEIDRVSGQTQFNGVNVLAKNGSMKIQVGANDNQTITIDLKQIDAKTLGLDGFSVKNNDTVTTSAPVTAFGATTTNNIKLTGITLSTEAATDTGGTNPASIEGVYTDNGNDYYAKITGGDNDGKYYAVTVANDGTVTMATGATANATVTDANTTKATTITSGGTPVQIDNTAGSATANLGAVSLVKLQDSKGNDTDTYALKDTNGNLYAADVNETTGAVSVKTITYTDSSGAASSPTAVKLGGDDGKTEVVDIDGKTYDSADLNGGNLQTGLTAGGEALTAVANGKTTDPLKALDDAIASVDKFRSSLGAVQNRLDSAVTNLNNTTTNLSEAQSRIQDADYATEVSNMSKAQIIQQAGNSVLAKANQVPQQVLSLLQG |
预测分子量 | 67.2 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 **fliC重组蛋白** 的示例参考文献(内容为虚构,供参考):
---
1. **《Expression and Purification of Recombinant Salmonella Typhimurium FliC Protein in E. coli》**
- **作者**: Zhang et al.
- **摘要**: 本研究在大肠杆菌中成功表达并纯化了沙门氏菌鞭毛蛋白FliC,通过优化诱导条件(如IPTG浓度和温度)提高了可溶性表达水平,并利用His标签亲和层析获得高纯度蛋白,为后续免疫研究奠定基础。
2. **《FliC Recombinant Protein as a TLR5 Agonist Enhances Innate Immune Response》**
- **作者**: Smith et al.
- **摘要**: 通过体外实验证明,重组FliC蛋白通过激活TLR5信号通路,显著促进巨噬细胞释放促炎因子(如IL-8和TNF-α),提示其在疫苗佐剂或免疫调节剂开发中的潜力。
3. **《Structural and Functional Analysis of Cloned Pseudomonas aeruginosa FliC Protein》**
- **作者**: Johnson et al.
- **摘要**: 利用基因克隆技术获得铜绿假单胞菌FliC重组蛋白,结合圆二色谱和分子动力学模拟分析其二级结构,发现其N端结构域对TLR5结合至关重要,为抗菌药物设计提供依据。
4. **《Application of Recombinant FliC in Serodiagnosis of Bacterial Infections》**
- **作者**: Lee et al.
- **摘要**: 将纯化的重组FliC蛋白作为抗原,建立ELISA检测方法,高效识别患者血清中针对鞭毛蛋白的抗体,证明其在快速诊断沙门氏菌感染中的临床应用价值。
---
如需真实文献,建议通过 **PubMed** 或 **Google Scholar** 搜索关键词“recombinant fliC protein”或“flagellin expression”。
The fliC gene encodes flagellin, the primary structural protein of bacterial flagella, which is critical for bacterial motility and virulence in various pathogenic species, including *Salmonella* and *Escherichia coli*. Flagellin monomers polymerize to form the filamentous propeller structure of flagella, enabling bacterial movement. Beyond its mechanical role, fliC is a key pathogen-associated molecular pattern (PAMP) recognized by the host innate immune system via Toll-like receptor 5 (TLR5), triggering inflammatory responses. This interaction underscores its importance in host-pathogen dynamics and immune evasion strategies.
Recombinant fliC protein is produced by cloning the fliC gene into expression vectors (e.g., *E. coli* plasmids) and purifying the expressed protein. Its conserved N-terminal and C-terminal domains (D1 and D2) are essential for TLR5 activation, while the hypervariable central domain varies across bacterial species. Recombinant fliC retains these immunogenic properties, making it a valuable tool in immunological research, vaccine development, and diagnostics. For instance, it is used to study TLR5 signaling pathways, design flagellin-based vaccines, or develop antibody-based detection assays for bacterial infections.
Additionally, recombinant fliC has been explored as a vaccine adjuvant due to its ability to enhance immune responses. However, its application is species-specific; for example, *Salmonella* fliC is a potent TLR5 agonist in mammals but not in chickens, reflecting evolutionary adaptations. Challenges in its use include potential cross-reactivity in diagnostic settings and the need for precise purification to avoid endotoxin contamination. Ongoing research continues to refine its applications in biotechnology and therapeutics, leveraging its dual role as a virulence factor and immune modulator.
×