| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | flgM |
| Uniprot No | P0AEM4 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-97aa |
| 氨基酸序列 | MSIDRTSPLKPVSTVQPRETTDAPVTNSRAAKTTASTSTSVTLSDAQAKLMQPGSSDINLERVEALKLAIRNGELKMDTGKIADALINEAQQDLQSN |
| 预测分子量 | 17.8 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条与flgM重组蛋白相关的文献示例(内容为模拟概括，建议核实具体文献)：
1. **"Regulation of flagellar gene expression in Salmonella typhimurium by FlgM and σ28"**
*Ohnishi K. et al. (1999)*
摘要：研究flgM基因缺失突变体对鞭毛合成的调控作用，通过重组FlgM蛋白体外验证其与σ28因子的相互作用，揭示其抑制鞭毛基因表达的分子机制。
2. **"Characterization of FlgM as an anti-sigma factor in Pseudomonas aeruginosa"**
*Gillaspy A.F. et al. (1995)*
摘要：利用大肠杆菌表达系统纯化重组FlgM蛋白，证明其通过与σ因子结合抑制鞭毛组装，并分析其结构域功能。
3. **"Functional analysis of FlgM in flagellar export control"**
*Hughes K.T. & Mathee K. (1998)*
摘要：通过重组FlgM蛋白的过表达实验，探讨其在鞭毛分泌系统中的负调控作用，发现其依赖细胞周期动态调节鞭毛基因表达。
4. **"Overexpression and purification of FlgM for structural studies"**
*Kutsukake K. & Iyoda S. (1994)*
摘要：报道重组FlgM蛋白在大肠杆菌中的高效表达与纯化方法，并通过晶体学分析其三维结构，为功能研究提供基础。
(注：以上为领域典型研究方向示例，实际文献需通过PubMed或Web of Science以"flgM recombinant protein"为关键词检索。)
FlgM is a regulatory protein involved in the flagellar biosynthesis pathway of bacteria, particularly studied in *Salmonella enterica* and other motile Gram-negative species. It functions as an anti-sigma factor that tightly controls the expression of flagellar genes by directly binding to the sigma factor σ28 (FliA), a transcriptional activator required for late-stage flagellar assembly. Under normal conditions, FlgM inhibits σ28 activity, preventing the transcription of genes encoding flagellar hook and filament components. However, as the flagellar basal body matures, FlgM is secreted through the nascent structure, relieving its inhibition on σ28 and allowing the completion of flagellum synthesis. This checkpoint mechanism ensures sequential gene expression, coupling flagellar assembly to bacterial motility and environmental adaptation.
Recombinant FlgM protein is commonly produced in *Escherichia coli* via genetic engineering for structural and functional studies. Its small size (~10 kDa) and solubility properties make it amenable to purification using affinity chromatography, often with tags like His-tag for ease of isolation. Research on recombinant FlgM has provided insights into bacterial gene regulation, protein secretion, and host-pathogen interactions. Studies also explore its role in bacterial stress responses and biofilm formation. Additionally, FlgM serves as a model protein for understanding anti-sigma factor dynamics and has potential applications in developing anti-infective strategies targeting bacterial motility. Structural analyses, including NMR and X-ray crystallography, reveal its N-terminal disordered region and C-terminal σ28-binding domain, highlighting mechanisms of molecular recognition and regulatory flexibility.
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