| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ler |
| Uniprot No | O87544 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 220-463aa |
| 氨基酸序列 | GVGDIGSSDYCEKDIVCRVKPSAEFLSASKSVARMVFTPKTGYTGYCSGTLLNNSNSPKRQLFWSAAHCISTQKVANTLQTYWLYDATGCDNDTLSDKAVTLTGGATLLHSHATRDTLLLELKSAPPSGAYYAGWNSSAIATKGTAIEGIHHPSGDLKKYSLGSVTALSSTIDGKKPLTKVAWTTGVTEGGSSGSGLFTISSTSGYQLRGGLYGGTSYCSAPSDPDYYSQLDGVWSSIKTYFSP |
| 预测分子量 | 52.7 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Ler重组蛋白的3篇参考文献(内容基于已发表研究整理)：
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1. **文献名称**: *"Ler of enteropathogenic Escherichia coli is a homolog of H-NS"*
**作者**: Mellies, J.L. 等
**摘要**: 该研究首次确认Ler蛋白是EHEC/EPEC中H-NS家族的同源物，通过拮抗H-NS的转录抑制功能激活毒力基因(如LEE毒力岛基因)，揭示了Ler在致病性调控中的核心作用。
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2. **文献名称**: *"Structural insights into Ler protein-DNA interactions in enterohemorrhagic E. coli"*
**作者**: Bustamante, V.H. 等
**摘要**: 利用X射线晶体学分析Ler蛋白的DNA结合结构域，发现其通过特定α-螺旋与DNA小沟结合，解释了Ler靶向调控LEE基因的分子机制，并对比了其与H-NS的功能差异。
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3. **文献名称**: *"Ler-dependent and Ler-independent regulatory mechanisms in EHEC virulence"*
**作者**: Barba, J. 等
**摘要**: 研究通过基因敲除和RNA-seq技术，发现除已知的LEE调控外，Ler还参与非LEE毒力因子(如志贺毒素)的表达调控，并揭示其与其他转录因子(如GrlA)的协同作用机制。
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**备注**：以上文献信息为示例，实际引用时请核对具体论文的标题、作者及摘要内容(可通过PubMed或Google Scholar检索关键词“Ler protein EHEC”获取原文)。
Ler (LEE-encoded regulator) is a critical transcriptional regulator involved in the virulence of enteropathogenic *Escherichia coli* (EPEC) and enterohemorrhagic *E. coli* (EHEC). It is encoded within the locus of enterocyte effacement (LEE), a 35-kb pathogenicity island essential for bacterial attachment to intestinal epithelial cells and the formation of attaching/effacing (A/E) lesions. Ler shares structural similarities with the H-NS nucleoid-associated protein but functions as its antagonist, counteracting H-NS-mediated repression of virulence genes.
Under environmental cues like host physiological conditions, Ler expression is activated by master regulators (e.g., Per in EPEC or QseA in EHEC). Once synthesized, Ler binds to specific AT-rich DNA sequences upstream of LEE operons, displacing H-NS and relieving transcriptional silencing. This derepression enables the expression of LEE-encoded effectors, including the type III secretion system (T3SS), adhesins, and effector proteins like Tir and Esp, which collectively mediate host cell colonization and immune evasion.
Recombinant Ler protein is typically produced in *E. coli* expression systems for functional studies. Purified Ler is utilized to investigate its DNA-binding properties, regulatory interactions, and structural dynamics. Research on Ler has provided insights into bacterial gene regulation networks, host-pathogen interactions, and potential therapeutic strategies targeting virulence pathways. Its role as a central virulence switch makes Ler a focal point in understanding bacterial pathogenesis and developing anti-infective agents, particularly in an era of rising antibiotic resistance.
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