| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ompC |
| Uniprot No | P06996 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 22-367aa |
| 氨基酸序列 | AEVYNKDGNKLDLYGKVDGLHYFSDNKDVDGDQTYMRLGFKGETQVTDQLTGYGQWEYQIQGNSAENENNSWTRVAFAGLKFQDVGSFDYGRNYGVVYDVTSWTDVLPEFGGDTYGSDNFMQQRGNGFATYRNTDFFGLVDGLNFAVQYQGKNGNPSGEGFTSGVTNNGRDALRQNGDGVGGSITYDYEGFGIGGAISSSKRTDAQNTAAYIGNGDRAETYTGGLKYDANNIYLAAQYTQTYNATRVGSLGWANKAQNFEAVAQYQFDFGLRPSLAYLQSKGKNLGRGYDDEDILKYVDVGATYYFNKNMSTYVDYKINLLDDNQFTRDAGINTDNIVALGLVYQF |
| 预测分子量 | 54.3 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3-4条关于OmpC重组蛋白的参考文献示例(注：以下文献为虚拟示例，实际文献需通过学术数据库检索获取)：
1. **文献名称**: "Heterologous Expression and Functional Characterization of Recombinant OmpC Porin from Salmonella Typhimurium"
**作者**: Zhang Y, Wang L, Li J
**摘要**: 该研究通过在大肠杆菌中异源表达沙门氏菌OmpC蛋白，优化了重组蛋白的可溶性表达条件，并通过脂质体重组实验证实了其形成功能性孔道的能力，为后续疫苗开发提供了基础。
2. **文献名称**: "Structural Insights into Recombinant OmpC: Implications for Antibiotic Permeability"
**作者**: Kumar S, et al.
**摘要**: 利用X射线晶体学解析了重组OmpC蛋白的三维结构，揭示了其跨膜β-桶状构象及关键氨基酸残基对抗生素渗透的调控作用，为针对外膜蛋白的药物设计提供了依据。
3. **文献名称**: "Recombinant OmpC as a Novel Vaccine Candidate Against Enterobacterial Infections"
**作者**: Gupta R, et al.
**摘要**: 评估了重组OmpC蛋白在小鼠模型中的免疫保护效果，结果显示其能诱导高滴度抗体并增强对多种肠杆菌科病原体的清除能力，表明其作为广谱疫苗的潜力。
4. **文献名称**: "Optimization of OmpC Recombinant Protein Production Using a High-Density E. coli Fermentation System"
**作者**: Chen X, et al.
**摘要**: 通过优化发酵条件(如温度、诱导剂浓度)，显著提高了重组OmpC的产量，并开发了高效层析纯化工艺，为大规模工业化生产奠定了基础。
如需真实文献，建议在PubMed、Web of Science等平台检索关键词“recombinant OmpC protein”或结合具体研究方向(如疫苗、结构、表达优化)筛选文献。
**Background of OmpC Recombinant Protein**
OmpC (outer membrane protein C) is a major porin found in the outer membrane of Gram-negative bacteria, such as *Escherichia coli*. As a β-barrel transmembrane protein, OmpC forms trimeric channels that regulate the passive diffusion of small hydrophilic molecules (e.g., nutrients, ions) across the membrane. Its expression is tightly regulated by environmental factors, particularly osmolarity, through the EnvZ/OmpR two-component system. Under high osmotic conditions, OmpC production increases, replacing its homolog OmpF, to limit membrane permeability and enhance bacterial survival.
Recombinant OmpC refers to the protein produced via genetic engineering, where the *ompC* gene is cloned into expression vectors (e.g., plasmids) and expressed in heterologous host systems (e.g., *E. coli*). This approach enables large-scale, cost-effective production while avoiding risks associated with purifying native OmpC from pathogenic strains. Purification typically involves affinity chromatography, leveraging tags like His-tags, followed by refolding steps to restore the protein’s native structure.
OmpC recombinant protein holds significant biomedical and biotechnological value. In vaccinology, it serves as a potential antigen or carrier for conjugate vaccines, leveraging its immunogenicity to trigger host immune responses against bacterial infections. It is also used in diagnostic assays to detect pathogen-specific antibodies. Additionally, OmpC’s stable structure and pore-forming ability make it a candidate for synthetic biology applications, such as nanopore sensors or drug delivery systems. Researchers further employ recombinant OmpC to study bacterial membrane dynamics, antibiotic resistance mechanisms, and host-pathogen interactions.
Overall, OmpC recombinant protein bridges fundamental microbiology with applied sciences, offering tools for therapeutic development, diagnostics, and novel biomaterials. Its study continues to uncover insights into bacterial adaptation and membrane protein engineering.
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