| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | ompA |
| Uniprot No | P45996 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-359aa |
| 氨基酸序列 | APQENTFYAGVKAGQGSFHDGINNNGAIKKGLSSSNYGYRRNTFTYGVFG GYQILNQDNFGLAAELGYDDFGRAKLREAGKPKAKHTNHGAYLSLKGSYE VLDGLDVYGKAGVALVRSDYKFYEDANGTRDHKKGRHTARASGLFAVGAE YAVLPELAVRLEYQWLTRVGKYRPQDKPNTAINYNPWIGCINAGISYRFG QGEAPVVAAPEMVSKTFSLNSDVTFAFGKANLKPQAQATLDSVYGEISQV KSRKVAVAGYTNRIGSDAFNVKLSQERADSVANYFVAKGVAADAISATGY GEANPVTGATCDQVKGRKALIACLAPDRRVEIAVNGTK |
| 预测分子量 | 56 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 **ompA重组蛋白** 的3篇示例参考文献(内容为虚构，供参考格式)：
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1. **文献名称**：*Expression and Purification of Recombinant OmpA Fusion Protein in E. coli for Enhanced Solubility*
**作者**：Smith, J. et al.
**摘要**：本研究利用大肠杆菌表达系统，将目标蛋白与ompA融合表达，显著提高了重组蛋白的可溶性和稳定性。通过优化诱导条件和纯化步骤，获得了高纯度蛋白，为后续功能研究奠定基础。
2. **文献名称**：*OmpA as a Versatile Carrier for Vaccine Development: Delivery of Viral Antigens*
**作者**：Johnson, R. et al.
**摘要**：探索ompA作为疫苗载体的潜力，通过重组技术将病毒抗原表位与ompA结构域融合，在小鼠模型中诱导强烈的体液和细胞免疫应答，证明其在亚单位疫苗开发中的应用价值。
3. **文献名称**：*Structural Insights into OmpA-mediated Bacterial Adhesion via X-ray Crystallography*
**作者**：Lee, S. et al.
**摘要**：解析了重组ompA蛋白的晶体结构，揭示了其与宿主细胞表面受体相互作用的关键区域，为设计针对细菌感染的抑制剂提供了结构基础。
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**提示**：实际文献需通过 **PubMed/Google Scholar** 检索关键词如 *"recombinant OmpA protein"* 或 *"OmpA fusion application"* 获取。
The ompA gene encodes the outer membrane protein A (OmpA), a highly conserved and multifunctional protein found in Gram-negative bacteria, including *Escherichia coli* and several pathogenic *Enterobacteriaceae*. OmpA is a structural component of the bacterial outer membrane, contributing to membrane integrity, solute transport, and host-pathogen interactions. Its N-terminal domain forms an eight-stranded β-barrel embedded in the outer membrane, while the C-terminal domain interacts with the peptidoglycan layer, stabilizing the cell envelope. OmpA also plays roles in bacterial adhesion, immune evasion, and biofilm formation, making it a virulence factor in infections such as urinary tract infections, meningitis, and sepsis.
Recombinant OmpA (rOmpA) is produced through genetic engineering, typically by cloning the ompA gene into expression vectors (e.g., plasmid systems) and purifying the protein from host organisms like *E. coli*. This approach allows large-scale production of OmpA for research and applications. rOmpA retains functional epitopes and structural features, enabling its use in immunological studies, diagnostics, and vaccine development. For instance, it serves as an antigen in serological assays to detect pathogen-specific antibodies or as a subunit vaccine candidate to elicit protective immunity. Additionally, OmpA’s ability to stimulate innate immune responses via Toll-like receptor signaling has sparked interest in its adjuvant potential.
Beyond biomedical applications, recombinant OmpA is a valuable tool in structural biology for studying membrane protein folding and β-barrel assembly mechanisms. Its well-characterized structure and stability also make it a model protein for developing protein purification techniques or fusion tags to enhance soluble expression of recombinant proteins. Overall, OmpA’s versatility underscores its significance in both basic research and biotechnological innovations.
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