| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | fliA |
| Uniprot No | P0AEM6 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-239aa |
| 氨基酸序列 | MNSLYTAEGVMDKHSLWQRYVPLVRHEALRLQVRLPASVELDDLLQAGGIGLLNAVERYDALQGTAFTTYAVQRIRGAMLDELRSRDWVPRSVRRNAREVAQAIGQLEQELGRNATETEVAERLGIDIADYRQMLLDTNNSQLFSYDEWREEHGDSIELVTDDHQRENPLQQLLDSNLRQRVMEAIETLPEREKLVLTLYYQEELNLKEIGAVLEVGESRVSQLHSQAIKRLRTKLGKL |
| 预测分子量 | 27.7 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. |
以下是关于fliA重组蛋白的3篇虚构参考文献示例(仅供格式参考，实际文献需通过学术数据库查询)：
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1. **标题**: *Heterologous Expression and Purification of Salmonella FliA Sigma Factor in E. coli*
**作者**: Tanaka, K. et al.
**摘要**: 本研究报道了在大肠杆菌BL21中成功表达并纯化沙门氏菌来源的FliA重组蛋白。通过His标签亲和层析获得高纯度蛋白，并证实其体外结合鞭毛基因启动子的活性，为鞭毛调控机制研究提供工具。
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2. **标题**: *Structural Insights into FliA-RNA Polymerase Interaction Using Recombinant Protein Complexes*
**作者**: Müller, R. & Chen, L.
**摘要**: 通过共表达FliA与大肠杆菌RNA聚合酶核心酶，解析了重组复合物的冷冻电镜结构，揭示了σ28因子介导的启动子识别特异性，阐明了鞭毛基因转录激活的结构基础。
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3. **标题**: *Recombinant FliA as a Potential Vaccine Adjuvant in Anti-Bacterial Immunity*
**作者**: Gupta, S. et al.
**摘要**: 将重组FliA蛋白与霍乱毒素B亚基融合，评估其在小鼠模型中的免疫增强效果。实验显示FliA可显著提高黏膜IgA水平，提示其在鞭毛相关病原体疫苗中的应用潜力。
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**提示**：实际文献建议通过PubMed或Google Scholar检索关键词“fliA recombinant protein”、“σ28 expression”等，重点关注微生物学、蛋白质工程领域的期刊(如*J. Bacteriology*、*Protein Expression and Purification*)。
**Background of FliA Recombinant Protein**
FliA, also known as σ28, is a bacterial transcription factor that functions as a sigma factor regulating the expression of flagellar genes in many Gram-negative bacteria, including *Escherichia coli* and *Salmonella enterica*. As a key component of the flagellar biosynthesis system, FliA directs RNA polymerase to initiate transcription of late-stage flagellar genes, enabling the assembly of the flagellar hook and filament. This process is critical for bacterial motility, chemotaxis, and host-pathogen interactions, making FliA a focal point in studies of bacterial behavior and virulence.
Recombinant FliA protein is engineered using genetic cloning techniques, where the *fliA* gene is inserted into expression vectors (e.g., plasmids) and expressed in heterologous hosts like *E. coli*. This approach allows large-scale production of purified FliA for structural and functional studies. Researchers often employ affinity tags (e.g., His-tag) to facilitate protein purification via chromatography.
The study of recombinant FliA has advanced our understanding of bacterial gene regulation, particularly how sigma factors coordinate developmental cascades. It has also shed light on FliA’s role in bacterial stress responses and biofilm formation. Additionally, FliA is explored as a potential target for antimicrobial strategies, as disrupting flagellar assembly could attenuate bacterial infectivity.
Recent applications include using FliA in synthetic biology to engineer motility-controlled bacterial systems or as an antigen in diagnostic tools for detecting pathogenic strains. Challenges remain in elucidating its post-translational regulation and interactions with anti-sigma factors (e.g., FlgM). Overall, FliA recombinant protein serves as a vital tool for dissecting bacterial motility mechanisms and developing novel biotechnological or therapeutic interventions.
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