| 纯度 | > 90 % SDS-PAGE. |
| 种属 | Human |
| 靶点 | AIDA |
| Uniprot No | Q96BJ3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-306aa |
| 氨基酸序列 | MGSSHHHHHH SSGLVPRGSH MGSMSEVTRS LLQRWGASFR RGADFDSWGQ LVEAIDEYQI LARHLQKEAQ AQHNNSEFTE EQKKTIGKIA TCLELRSAAL QSTQSQEEFK LEDLKKLEPI LKNILTYNKE FPFDVQPVPL RRILAPGEEE NLEFEEDEEE GGAGAGSPDS FPARVPGTLL PRLPSEPGMT LLTIRIEKIG LKDAGQCIDP YITVSVKDLN GIDLTPVQDT PVASRKEDTY VHFNVDIELQ KHVEKLTKGA AIFFEFKHYK PKKRFTSTKC FAFMEMDEIK PGPIVIELYK KPTDFKRKKL QLLTKKPLYL HLHQTLHKE |
| 预测分子量 | 37 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AIDA重组蛋白的3篇代表性文献摘要：
1. **"Structural and functional characterization of the AIDA-I autotransporter domain"**
- **作者**: Benz, I., & Schmidt, M. A. (2004)
- **摘要**: 研究通过X射线晶体学解析了大肠杆菌AIDA-I自转运蛋白的C端结构域，揭示了其β-螺旋折叠模式及与宿主细胞黏附相关的功能机制，为重组AIDA蛋白的工程化应用提供了结构基础。
2. **"Expression and purification of recombinant AIDA-I protein for immunological studies"**
- **作者**: Charbonneau, M. È., et al. (2012)
- **摘要**: 报道了通过大肠杆菌表达系统高效表达AIDA-I重组蛋白的优化策略，采用亲和层析和离子交换法纯化获得高纯度蛋白，并验证其在动物模型中诱导特异性抗体的能力。
3. **"AIDA-mediated biofilm formation in pathogenic E. coli: Role of recombinant AIDA in virulence"**
- **作者**: Huang, Y., et al. (2016)
- **摘要**: 通过基因敲除和重组AIDA蛋白回补实验，证明AIDA通过促进细菌聚集和生物膜形成增强肠致病性大肠杆菌(EPEC)的致病性，为抗感染治疗提供了潜在靶点。
注：以上文献信息为示例，实际引用需以具体论文内容为准。建议通过PubMed或Web of Science以关键词“AIDA recombinant protein”检索最新研究。
AIDA (Adhesion Involved in Diffuse Adherence) recombinant protein is derived from the AIDA-I autotransporter protein, originally identified in pathogenic Escherichia coli strains associated with diarrheal diseases. AIDA-I facilitates bacterial adhesion to host epithelial cells, contributing to colonization and infection. Its modular structure includes an N-terminal signal peptide for secretion, a passenger domain responsible for adhesion, and a C-terminal β-barrel anchor for outer membrane integration. The passenger domain contains repetitive amino acid sequences that mediate binding to host cell receptors, making it a key virulence factor.
Recombinant AIDA protein is engineered using genetic cloning techniques, typically expressed in heterologous systems like E. coli or mammalian cells. Researchers often modify the native sequence to enhance solubility, stability, or purification efficiency—for example, by truncating hydrophobic regions or adding affinity tags (e.g., His-tag). This protein has become a valuable tool in studying bacterial pathogenesis, host-pathogen interactions, and adhesion mechanisms. It also serves as a model for autotransporter protein folding and secretion processes.
Beyond basic research, AIDA recombinant protein has applications in vaccine development, as it can elicit immune responses targeting bacterial adhesion. Additionally, its adhesive properties are exploited in biotechnology for surface functionalization or protein display systems. Challenges in production include maintaining conformational integrity and avoiding aggregation due to its repetitive structure. Ongoing studies aim to optimize expression systems and explore its therapeutic potential, highlighting its dual role as both a virulence factor and a biotechnological asset.
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