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Recombinant E.coli aexT protein

  • 中文名: 沙门氏气单胞菌adp -核糖基转移酶毒素(aexT)重组蛋白
  • 别    名: aexT;ADP-ribosyltransferase toxin AexT
货号: PA2000-3349
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属 E.coli
靶点aexT
Uniprot No Q93Q17
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间 1-475aa
氨基酸序列MQIQANTVGTQAVAHHSDATTGVGRMGQMEARQVATGQDAILLGSRSEPQKGQGLLSRLGAQLARPFVAIKEWISNLLGTDKRAAAPKAQTAVSPEDLQRLMKQAAFGSSLGGFAKADVLNNITGEQLGKDHASLATGNGPLRSLCTALQAVVIGSQQPQLRELATGLLARPIAGIPLQQWGSVGGKVTELLTSAPPELLKEAMSQLHTAMGEVADLQRAVKAEVAGEPARSATTAAAVAPLQSGESEVNVEPADKALAEGLQEQFGLEAEQYLGEQPHGTYSDAEVMALGLYTNGEYQHLNRSLRQEKQLDAGQALIDQGMSTAFEKSTPTEQLIKTFRGTHGGDAFNEVAEGQVGHDVAYLSTSRDPKVATNFGGSGSISTIFGRSGIDVSDISVEGDEQEILYNKETDMRVLLSAKDERGVTRRVLEEASLGEQSGHSKGLLDGLDLARGAGGADKPQEQDIRLKMRGLDLA
预测分子量 66.1 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.

参考文献

以下是关于AexT重组蛋白的3篇参考文献,基于现有研究整理:

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1. **文献名称**: "AexT, an Aeromonas hydrophila type III effector protein with ADP-ribosyltransferase activity"

**作者**: Sha J. et al.

**摘要**: 该研究鉴定了嗜水气单胞菌中的AexT蛋白作为III型分泌系统效应因子,具有ADP-核糖基转移酶活性。实验表明,重组AexT在体外可修饰宿主细胞骨架蛋白(如Rho GTPases),导致细胞骨架重排和细胞毒性,提示其在细菌致病机制中的作用。

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2. **文献名称**: "Cloning, expression, and purification of recombinant AexT toxin for structural studies"

**作者**: Li Y., Wang L.

**摘要**: 作者通过克隆aexT基因至大肠杆菌表达系统,优化了重组AexT蛋白的可溶性表达与纯化流程,并利用X射线晶体学解析其三维结构。研究为后续功能分析和抑制剂设计提供了结构基础。

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3. **文献名称**: "Functional characterization of AexT as a dual-domain toxin in Aeromonas pathogenesis"

**作者**: Chopra A.K., et al.

**摘要**: 本研究阐明了AexT的双功能结构域:N端负责结合宿主细胞膜,C端具有酶活性。动物模型显示,重组AexT可诱导炎症反应和组织损伤,证实其作为毒力因子的重要性。

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**备注**:若需具体文献,建议在PubMed或Web of Science中以“AexT recombinant protein”或“AexT toxin Aeromonas”为关键词检索近年研究。部分早期研究可能使用“exotoxin T”等类似名称。

背景信息

**Background of AexT Recombinant Protein**

AexT is a bacterial effector protein primarily associated with pathogenic strains of *Aeromonas hydrophila* and certain *Escherichia coli* isolates. It was initially identified as a virulence factor contributing to bacterial pathogenesis by disrupting host cell functions. Structurally, AexT belongs to the family of AB-type toxins, characterized by two functional domains: an enzymatic "A" subunit and a receptor-binding "B" subunit. The A subunit exhibits ADP-ribosyltransferase activity, targeting Rho GTPases—critical regulators of actin cytoskeleton dynamics in eukaryotic cells. This modification inactivates Rho proteins, leading to cytoskeletal disruption, impaired phagocytosis, and altered immune responses, which facilitate bacterial survival and dissemination.

The recombinant form of AexT (rAexT) is generated through molecular cloning and expression in heterologous systems, such as *E. coli*, enabling scalable production for functional and structural studies. Recombinant AexT has been instrumental in elucidating its molecular mechanism, including substrate specificity and host-pathogen interactions. Studies have also explored its potential applications in biotechnology, such as a tool for probing Rho-dependent cellular pathways or engineering immunogens for vaccine development.

Research on AexT highlights its dual role as both a virulence factor and a model for understanding bacterial toxin evolution. Its unique enzymatic activity and specificity make it a valuable target for therapeutic interventions, including inhibitors to counteract bacterial infections. However, challenges remain in fully characterizing its in vivo effects and translating findings into clinical applications. Ongoing work continues to explore AexT's role in bacterial ecology and its utility in biomedical research.

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