纯度 | >90%SDS-PAGE. |
种属 | E.col |
靶点 | oprF |
Uniprot No | P13794 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 25-350aa |
氨基酸序列 | QGQNSVEIEAFGKRYFTDSVRNMKNADLYGGSIGYFLTDDVELALSYGEYHDVRGTYETGNKKVHGNLTSLDAIYHFGTPGVGLRPYVSAGLAHQNITNINSDSQGRQQMTMANIGAGLKYYFTENFFAKASLDGQYGLEKRDNGHQGEWMAGLGVGFNFGGSKAAPAPEPVADVCSDSDNDGVCDNVDKCPDTPANVTVDANGCPAVAEVVRVQLDVKFDFDKSKVKENSYADIKNLADFMKQYPSTSTTVEGHTDSVGTDAYNQKLSERRANAVRDVLVNEYGVEGGRVNAVGYGESRPVADNATAEGRAINRRVEAEVEAEAK |
预测分子量 | 44.1 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oprF重组蛋白的3篇参考文献示例(注:文献信息为模拟示例,实际引用请核对真实数据库):
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1. **标题**:Cloning, expression, and immunogenicity of recombinant OprF protein from *Pseudomonas aeruginosa*
**作者**:Smith A, et al.
**摘要**:研究通过克隆铜绿假单胞菌的oprF基因,在大肠杆菌中表达重组蛋白,并证明其在小鼠模型中诱导保护性免疫应答的能力,提示其作为疫苗候选的潜力。
2. **标题**:Structural and functional analysis of the recombinant OprF porin in bacterial membrane permeability
**作者**:Zhang L, Wang H.
**摘要**:利用重组OprF蛋白分析其结构特征,揭示该蛋白在调控细菌外膜通透性中的作用,并探讨其与抗生素敏感性的关联。
3. **标题**:Development of an ELISA based on recombinant OprF for serodiagnosis of *Pseudomonas aeruginosa* infections
**作者**:Chen R, et al.
**摘要**:构建基于重组OprF蛋白的ELISA检测方法,验证其在临床样本中检测铜绿假单胞菌感染的特异性和敏感性,为快速诊断提供新策略。
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如需具体文献,建议通过PubMed、Web of Science等平台检索关键词“recombinant OprF protein”获取最新研究。
**Background of OprF Recombinant Protein**
OprF is a major outer membrane protein (OMP) in *Pseudomonas aeruginosa*, a Gram-negative opportunistic pathogen notorious for causing severe infections in immunocompromised individuals and cystic fibrosis patients. As a key structural component, OprF contributes to bacterial membrane integrity, osmotic regulation, and selective permeability. It also plays roles in host-pathogen interactions, including immune evasion and adhesion to host cells. Structurally, OprF exhibits a dual-domain architecture: an N-terminal β-barrel transmembrane domain and a C-terminal globular domain that extends into the periplasm. This unique conformation allows it to function as a porin and a structural scaffold.
Recombinant OprF (rOprF) is produced through genetic engineering, typically by cloning the *oprF* gene into expression vectors (e.g., *E. coli*), followed by purification via affinity chromatography. The recombinant protein retains the immunogenic and functional properties of native OprF, making it a valuable tool for studying *P. aeruginosa* pathogenesis. Researchers leverage rOprF to investigate its role in antibiotic resistance, biofilm formation, and interactions with host immune cells.
Additionally, rOprF is a candidate for vaccine development due to its surface exposure and ability to elicit protective immune responses. Studies have explored its use in combination with other antigens (e.g., OprI) to enhance vaccine efficacy. Beyond therapeutics, rOprF serves as a diagnostic antigen for detecting *P. aeruginosa* infections. Despite progress, challenges remain in optimizing its stability and conformational fidelity *in vitro*, which are critical for functional studies and clinical applications. Overall, rOprF remains a focal point in combating *P. aeruginosa*-related diseases.
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