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Recombinant inlA protein

  • 中文名: 钙黏蛋白-1(inlA)重组蛋白
  • 别    名: inlA;CDHE;UVO;;Cadherin-1
货号: PA2000-5126
Price: ¥询价
数量:
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产品详情

纯度>90%SDS-PAGE.
种属Human
靶点inlA
Uniprot No P0DJM0
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间32-414aa(S192N,Y369S)
氨基酸序列NAQAATITQDTPINQIFTDTALAEKMKTVLGKTNVTDTVSQTDLDQVTTLQADRLGIKSIDGVEYLNNLTQINFSNNQLTDITPLKNLTKLVDILMNNNQIADITPLANLTNLTGLTLFNNQITDIDPLKNLTNLNRLELSSNTISDISALSGLTSLQQLNFGNQVTDLKPLANLTTLERLDISSNKVSDISVLAKLTNLESLIATNNQISDITPLGILTNLDELSLNGNQLKDIGTLASLTNLTDLDLANNQISNLAPLSGLTKLTELKLGANQISNISPLAGLTALTNLELNENQLEDISPISNLKNLTYLTLYFNNISDISPVSSLTKLQRLFFSNNKVSDVSSLANLTNINWLSAGHNQISDLTPLANLTRITQLGLND
预测分子量48.9 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 **inlA重组蛋白** 的3篇参考文献示例(文献信息为模拟概括,仅供参考):

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1. **文献名称**:*"Heterologous Expression and Functional Characterization of Listeria monocytogenes InlA in Escherichia coli"*

**作者**:Mengaud J. et al.

**摘要**:研究通过在大肠杆菌中异源表达重组InlA蛋白,证实其与宿主细胞E-cadherin的特异性结合能力,揭示了InlA在介导单核细胞增生李斯特菌入侵肠道上皮细胞中的关键作用。

2. **文献名称**:*"Structural Basis for the Interaction of Listeria InlA with E-cadherin"*

**作者**:Lecuit M. et al.

**摘要**:利用重组InlA蛋白进行X射线晶体学分析,解析了InlA与人类E-cadherin结合的分子机制,发现其N端结构域是宿主特异性的决定因素,为开发阻断李斯特菌感染的疗法提供依据。

3. **文献名称**:*"Recombinant InlA as a Vaccine Candidate Against Listeriosis in Mice"*

**作者**:Bierne H. et al.

**摘要**:评估重组InlA蛋白作为疫苗的免疫原性,实验表明接种后的小鼠对李斯特菌感染的保护力显著增强,提示InlA可能成为抗李斯特菌病的新型亚单位疫苗。

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**备注**:以上文献为示例,实际研究中建议通过PubMed或Web of Science等平台以关键词“inlA recombinant protein”“Listeria InlA”检索最新论文。

背景信息

**Background of InlA Recombinant Protein**

InlA (Internalin A) is a critical virulence factor produced by *Listeria monocytogenes*, a Gram-positive bacterial pathogen responsible for listeriosis. This surface protein facilitates bacterial invasion into host cells by binding to E-cadherin, a receptor on epithelial cells, enabling the pathogen to cross intestinal, placental, and blood-brain barriers. InlA’s role in host-pathogen interactions has made it a key focus in understanding *Listeria* pathogenesis and developing targeted interventions.

Recombinant InlA refers to the protein produced through genetic engineering, typically by cloning the *inlA* gene into expression systems like *E. coli* or mammalian cells. This approach allows large-scale production of purified InlA for research and therapeutic applications. Unlike native InlA, recombinant variants can be modified to enhance stability, solubility, or receptor-binding specificity, enabling tailored studies.

Research on recombinant InlA has advanced multiple areas:

1. **Pathogenesis Studies**: It helps dissect molecular mechanisms of bacterial invasion and host immune evasion.

2. **Vaccine Development**: InlA-based vaccines aim to induce protective immunity by targeting this critical virulence factor.

3. **Diagnostic Tools**: Recombinant InlA serves as an antigen in immunoassays to detect *Listeria*-specific antibodies.

4. **Therapeutic Strategies**: Engineered InlA variants are explored as decoy receptors to block bacterial adhesion.

Structural analyses of recombinant InlA have revealed domains critical for E-cadherin binding, guiding the design of inhibitors. Additionally, its use in cell culture and animal models has improved understanding of barrier tropism in listeriosis.

Despite progress, challenges remain, such as ensuring proper post-translational modifications in heterologous expression systems. Ongoing efforts focus on optimizing production and leveraging recombinant InlA for novel antimicrobials or delivery systems. Its versatility underscores its importance in both basic research and translational applications against *Listeria* infections.

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