| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | BFP |
| Uniprot No | Q9ULX5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-631aa |
| 氨基酸序列 | MPRPALSVTSFCHRLGKRERKQSFMGNSGNSWSHTPFPKLELGLGPQPMAPRELPTCSICLERLRDPISLDCGHDFCIRCFSTHRLPGCEPPCCPECRKICKQKRGLRSLGEKMKLLPQRPLPPALQETCPVRAEPLLLVRINASGGLILRMGAINRCLKHPLARDTPVCLLAVLGEQHSGKSFLLNHLLQGLPGLESGEGGRPRGGEASLQGCRWGANGLARGIWMWSHPFLLGKEGKKVAVFLVDTGDAMSPELSRETRIKLCALTTMLSSYQILSTSQELKDTDLDYLEMFVHVAEVMGKHYGMVPIQHLDLLVRDSSHPNKAGQGHVGNIFQRLSGRYPKVQELLQGKRARCCLLPAPGRRRMNQGHASPGDTDDDFRHLLGAYVSDVLSAAPQHAKSRCQGYWNEGRAVARGDRRLLTGQQLAQEIKNLSGWMGRTGPGFTSPDEMAAQLHDLRKVEAAKREFEEYVRQQDVATKRIFSALRVLPDTMRNLLSTQKDAILARHGVALLCKGRDQTLEALEAELQATAKAFMDSYTMRFCGHLAAVGGAVGAGLMGLAGGVVGAGMAAAALAAEAGMVAAGAAVGATGAAVVGGGVGAGLAATVGCMEKEEDERLLEGDREPLLQEE |
| 预测分子量 | 68,2 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BFP(蓝色荧光蛋白)重组蛋白的模拟参考文献示例，供参考(注：部分内容为虚构概括，实际文献需通过学术数据库检索)：
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1. **文献名称**：*"Engineering and Characterization of an Enhanced Blue Fluorescent Protein (EBFP) for Live-Cell Imaging"*
**作者**：Heim, R., Tsien, R.Y.
**摘要**：报道了通过定点突变技术对野生型蓝色荧光蛋白(BFP)进行优化，开发出增强型BFP(EBFP)，显著提高了荧光强度和光稳定性。该研究验证了EBFP在哺乳动物细胞中的重组表达效果，并展示了其在多色标记和动态追踪中的应用潜力。
2. **文献名称**：*"Cloning and Heterologous Expression of BFP in E. coli: A Tool for Protein Localization Studies"*
**作者**：Yang, T.T., et al.
**摘要**：描述了BFP基因的克隆策略及其在大肠杆菌中的高效重组表达。研究通过纯化与光谱分析证实了重组BFP的荧光特性，并利用其与目标蛋白的融合表达实现了细菌细胞内蛋白质定位的可视化。
3. **文献名称**：*"Comparative Analysis of BFP, GFP, and mCherry in Multicolor Super-Resolution Microscopy"*
**作者**：Shaner, N.C., et al.
**摘要**：比较了BFP与其他荧光蛋白(如GFP、mCherry)的光物理性质，验证了BFP在超分辨率显微技术中的兼容性。研究表明，重组BFP可作为多色成像系统中的重要蓝色通道标记物，减少光谱串扰。
4. **文献名称**：*"Improving the Thermostability of BFP through Directed Evolution for Industrial Biosensing"*
**作者**：Wang, L., et al.
**摘要**：通过定向进化技术改造BFP，提高了其热稳定性和pH耐受性。改造后的重组BFP在体外生物传感器开发中表现出更优的性能，拓展了其在高温环境下的应用场景。
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如需真实文献，建议通过PubMed、Web of Science或Google Scholar检索关键词(如"BFP recombinant protein"、"Blue Fluorescent Protein expression")，并筛选近年高被引研究。经典研究可参考Roger Tsien团队或荧光蛋白相关综述。
Bacterial fimbrial protein (BFP) is a key structural component of type IV pili produced by enteropathogenic *Escherichia coli* (EPEC), a major cause of diarrheal diseases in children. Discovered in the 1980s, BFP forms hair-like appendages critical for bacterial adhesion to host intestinal epithelial cells, enabling colonization and pathogenesis. These filaments facilitate microcolony formation, a hallmark of EPEC infection, and participate in interbacterial interactions during biofilm development.
The *bfp* gene cluster, located on the EPEC virulence plasmid, encodes multiple proteins involved in pilus assembly, including the major subunit BfpA. Recombinant BFP technology emerged to study its role in infection without handling live pathogens. By cloning *bfpA* into expression vectors, researchers produce purified BFP in heterologous systems like *E. coli*. This enables structural analysis, antibody development, and adhesion inhibition studies.
Recombinant BFP retains the ability to self-assemble into polymeric structures *in vitro*, mimicking native pili. Its applications span vaccine development (as an immunogen), diagnostics (antigen-based assays), and mechanistic studies of bacterial adherence. However, challenges include maintaining proper post-translational modifications during heterologous expression and replicating the complex assembly machinery required for functional pilus formation.
Recent advances in structural biology using recombinant BFP have revealed details about pilus biogenesis and host receptor interactions, informing therapeutic strategies targeting EPEC adhesion. Ongoing research also explores engineered BFP variants for nanotechnology applications due to their self-assembling properties.
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