| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | OMP |
| Uniprot No | P47874 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-163aa |
| 氨基酸序列 | MAEDRPQQPQLDMPLVLDQGLTRQMRLRVESLKQRGEKRQDGEKLLQPAESVYRLNFTQQQRLQFERWNVVLDKPGKVTITGTSQNWTPDLTNLMTRQLLDPTAIFWRKEDSDAIDWNEADALEFGERLSDLAKIRKVMYFLVTFGEGVEPANLKASVVFNQL |
| 预测分子量 | 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OMP重组蛋白的3篇参考文献示例(虚构内容，仅供格式参考)：
1. **《高效表达与纯化大肠杆菌OmpA重组蛋白的优化策略》**
*作者：Zhang L, et al. (2020)*
**摘要**：研究通过优化表达载体和大肠杆菌宿主系统，显著提高了OmpA重组蛋白的产量，并建立了高效层析纯化方法，为后续结构研究奠定基础。
2. **《沙门氏菌OmpD重组蛋白的免疫原性及疫苗潜力评估》**
*作者：Wang Y, et al. (2018)*
**摘要**：利用重组OmpD蛋白免疫小鼠，诱导强烈的Th1型免疫应答，证实其作为候选疫苗组分对沙门氏菌感染具有保护作用。
3. **《基于OMP重组蛋白的快速诊断试剂盒开发及应用》**
*作者：Kim S, et al. (2021)*
**摘要**：以重组表达的嗜血杆菌OMP为抗原，开发出高灵敏度ELISA检测方法，显著提升临床样本中病原体抗体检出率。
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注：以上文献为示例性内容，实际研究中请通过PubMed或Web of Science等平台检索真实文献。
**Background of OMP Recombinant Proteins**
Outer Membrane Proteins (OMPs) are essential components of the outer membrane in Gram-negative bacteria, playing critical roles in nutrient uptake, pathogen-host interactions, and maintaining membrane integrity. Structurally, OMPs often adopt β-barrel folds, which stabilize their integration into the lipid bilayer. Due to their surface exposure and involvement in bacterial survival, OMPs are key targets for vaccine development, diagnostic tools, and antimicrobial therapies.
Recombinant OMPs are produced via genetic engineering, where OMP-encoding genes are cloned into expression systems (e.g., *E. coli* or yeast) to enable large-scale protein production. This approach overcomes challenges in isolating native OMPs, such as low abundance or contamination risks. Recombinant technology also allows for modifications, including epitope tagging or structural optimization, to enhance stability or immunogenicity.
In vaccinology, recombinant OMPs have been explored as subunit vaccines against pathogens like *Neisseria meningitidis* and *Haemophilus influenzae*. Their ability to elicit protective immune responses stems from surface-exposed antigenic regions recognized by the host immune system. Additionally, OMPs serve as diagnostic antigens in serological assays to detect bacterial infections. Beyond medical applications, recombinant OMPs are used in biotechnology for nanopore sensors, drug delivery systems, and enzyme immobilization due to their structural versatility.
Challenges persist in recombinant OMP production, including improper folding in heterologous systems and endotoxin contamination. Advances in protein engineering, codon optimization, and purification techniques continue to address these issues, broadening their therapeutic and industrial potential. Overall, recombinant OMPs represent a versatile tool bridging microbiology, immunology, and biotechnology.
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