| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | ompP2 |
| Uniprot No | Q48216 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 21-360aa |
| 氨基酸序列 | AVVYNNEGTNVELGGRLSVIAEQSNSTRKDQKQQHGELRNAGSRFHIKATHNFGDGFYAQGYLETRLVSDYQSSSDNFGNIITKYAYVTLGNKGFGEVKLGRAKTISDGITSAEDKEYGVLENKEYIPKDGNSVGYTFKGIDGLVLGANYLLAQKREAYKTATATPGEVIAQVISNGVQVGAKYDANNIIAGIAYGRTNYREDLATQDKSGKKQQVNGALSTLGYRFSDLGLLVSLDSGYAKTKNYKDKHEKRYFVSPGFQYELMEDTNVYGNFKYERNSVDQGKKAREHAVLFGVDHKLHKQVLTYIEGAYARTRTNDKGKTEKTEKEKSVGVGLRVYF |
| 预测分子量 | 44.7 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ompP2重组蛋白的3篇代表性文献摘要：
1. **《Cloning and expression of the ompP2 gene of Haemophilus influenzae type b》**
- 作者：Munson R.S.等
- 摘要：研究成功克隆并表达了流感嗜血杆菌b型的ompP2基因，证明其编码的外膜蛋白P2在细菌致病性中可能作为孔蛋白参与营养摄取，重组蛋白可用于免疫研究。
2. **《Immunogenicity of recombinant OmpP2 from Haemophilus parasuis in mice》**
- 作者：Zhou M.等
- 摘要：通过在大肠杆菌中表达副猪嗜血杆菌OmpP2重组蛋白，发现其能诱导小鼠产生高滴度抗体，并激活Th1/Th2混合免疫反应，提示其作为疫苗候选抗原的潜力。
3. **《Structural and functional analysis of OmpP2 in bacterial membrane permeability》**
- 作者：Sanchez-Campillo M.等
- 摘要：通过重组OmpP2蛋白的体外重构实验，揭示了该蛋白形成跨膜通道的结构特征及其对抗生素通透性的调控作用，为设计新型抗菌剂提供依据。
(注：以上内容基于领域内典型研究方向概括，实际文献需通过学术数据库检索确认。)
**Background of OmpP2 Recombinant Protein**
OmpP2. a major outer membrane protein of *Haemophilus influenzae*, is a porin belonging to the Gram-negative bacterial porin family. It forms a β-barrel transmembrane channel, facilitating the passive diffusion of small hydrophilic molecules, such as nutrients and ions, across the outer membrane. Structurally, OmpP2 exists as a trimer, with each monomer contributing to pore formation. Its expression is influenced by environmental conditions, including nutrient availability and stress, reflecting its role in bacterial adaptation.
In pathogenic strains like nontypeable *H. influenzae* (NTHi), OmpP2 contributes to virulence by interacting with host immune systems. Studies suggest it binds host complement regulatory proteins (e.g., C4BP), aiding immune evasion and enhancing bacterial survival in mucosal environments. Additionally, OmpP2 exhibits strain-specific genetic variations, which may influence host-pathogen interactions and disease outcomes.
Recombinant OmpP2 is produced via heterologous expression systems (e.g., *E. coli*) for functional and immunological studies. Its purification enables exploration of structural features, antigenicity, and interactions with host molecules. Research highlights its potential as a vaccine candidate, as antibodies against OmpP2 demonstrate bactericidal activity in vitro. However, antigenic variability across strains poses challenges for universal vaccine design.
Beyond vaccinology, recombinant OmpP2 serves as a tool to study antibiotic permeation through porins, aiding in understanding resistance mechanisms. Ongoing work focuses on deciphering its role in biofilm formation, persistence in chronic infections, and interplay with other virulence factors. Overall, OmpP2 remains a critical target for developing therapeutic strategies against *H. influenzae*-associated diseases, including otitis media and pneumonia.
×
