| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | omp38 |
| Uniprot No | Q6RYW5 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-356aa |
| 氨基酸序列 | ANAGVTVTPLLLGYTFQDSQHNNGGKDGNLTNGPELQDDLFVGAALGIELTPWLGFEAEYNQVKGDVDGASAGAEYKQKQINGNFYVTSDLITKNYDSKIKPYVLLGAGHYKYDFDGVNRGTRGTSEEGTLGNAGVGAFWRLNDALSLRTEARATYNADEEFWNYTALAGLNVVLGGHLKPAAPVVEVAPVEPTPVAPQPQELTEDLNMELRVFFDTNKSNIKDQYKPEIAKVAEKLSEYPNATARIEGHTDNTGPRKLNERLSLARANSVKSALVNEYNVDASRLSTQGFAWDQPIADNKTKEGRAMNRRVFATITGSRTVVVQPGQEAAAPAAAQ |
| 预测分子量 | 44.0 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omp38重组蛋白的3篇模拟参考文献示例(注：实际文献需通过学术数据库检索，以下为虚构内容供参考)：
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1. **文献名称**: *Structural and functional characterization of recombinant Omp38 from Acinetobacter baumannii*
**作者**: Zhang L., et al.
**摘要**: 本研究通过大肠杆菌系统表达并纯化了重组Omp38蛋白，解析其β-桶状结构特征，证实其作为外膜通道蛋白的功能，并发现其与碳青霉烯类抗生素耐药性的潜在关联。
2. **文献名称**: *Omp38 recombinant protein as a vaccine candidate against multidrug-resistant Gram-negative bacteria*
**作者**: Lee S., et al.
**摘要**: 在小鼠模型中评估了重组Omp38的免疫原性，结果显示其可诱导高滴度抗体，增强宿主对鲍曼不动杆菌和铜绿假单胞菌感染的清除能力，提示其作为广谱疫苗的潜力。
3. **文献名称**: *Expression optimization and pore-forming activity of Omp38 in lipid bilayer assays*
**作者**: Gupta R., et al.
**摘要**: 通过优化诱导条件和纯化策略提高重组Omp38的产量，并在人工脂质膜实验中证实其形成离子通道的能力，为开发基于Omp38的抗菌药物递送系统提供依据。
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**建议检索关键词**：
- "omp38 recombinant protein Acinetobacter"
- "Omp38 structure function"
- "Omp38 antibiotic resistance"
可使用PubMed、Google Scholar或Web of Science获取真实文献。
Omp38 recombinant protein is a biotechnologically engineered version of the outer membrane protein 38 (Omp38), originally identified in Gram-negative bacteria such as *Acinetobacter baumannii* and related pathogens. As a member of the outer membrane protein family, Omp38 plays a critical role in bacterial survival, facilitating nutrient uptake, ion transport, and interactions with host environments. In pathogenic strains, Omp38 is often implicated in virulence, antibiotic resistance, and immune evasion, making it a target for therapeutic and diagnostic research.
The recombinant form of Omp38 is produced via heterologous expression systems, typically in *Escherichia coli*, followed by purification using affinity chromatography. This approach ensures high yield and purity for experimental applications. Structurally, Omp38 is predicted to form a β-barrel fold, characteristic of porins, with surface-exposed loops that may participate in antigenic recognition or ligand binding. Studies suggest its involvement in carbapenem resistance in *A. baumannii*, possibly by regulating membrane permeability or efflux mechanisms.
Research on Omp38 recombinant protein focuses on its potential as a vaccine candidate, diagnostic antigen, or drug target. Immunization trials in animal models have shown that Omp38 elicits specific antibody responses, indicating its immunogenic properties. Additionally, it serves as a tool for studying host-pathogen interactions, particularly in understanding how bacterial outer membrane proteins modulate immune responses or contribute to persistence in hostile environments. Challenges include optimizing its stability for clinical use and addressing structural heterogeneity observed during recombinant production. Despite these hurdles, Omp38 remains a promising subject for combating multidrug-resistant infections.
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