| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | porB |
| Uniprot No | E6MZM0 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 20-331aa |
| 氨基酸序列 | DVTLYGTIKAGVETSRSVFHQNGQVTEVTTATGIVDLGSKIGFKGQEDLG NGLKAIWQVEQKASIAGTDSGWGNRQSFIGLKGGFGKLRVGRLNSVLKDT GDINPWDSKSDYLGVNKIAEPEARLISVRYDSPEFAGLSGSVQYALNDNA GRHNSESYHAGFNYKNGGFFVQYGGAYKRHHQVQEGLNIEKYQIHRLVSG YDNDALYASVAVQQQDAKLTDASNSHNSQTEVAATLAYRFGNVTPRVSYA HGFKGLVDDADIGNEYDQVVVGAEYDFSKRTSALVSAGWLQEGKGENKFV ATAGGVGLRHKF |
| 预测分子量 | 50 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porB重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**：*"Recombinant PorB from Neisseria gonorrhoeae induces protective immunity in a murine infection model"*
**作者**：Zhu W, Thomas CE, Sparling PF
**摘要**：该研究在大肠杆菌中成功表达并纯化了淋球菌PorB重组蛋白，发现其在小鼠模型中能诱导强烈的体液和细胞免疫反应，显著降低细菌载量，表明其作为疫苗候选的潜力。
2. **文献名称**：*"Structural basis for the interaction of Neisseria meningitidis PorB with Toll-like receptors"*
**作者**：Liu X, Wetzler LM, Massari P
**摘要**：通过X射线晶体学解析了脑膜炎球菌PorB重组蛋白的结构，揭示了其与宿主Toll样受体(TLR2/TLR1)的相互作用机制，阐明PorB在激活先天免疫中的关键作用。
3. **文献名称**：*"PorB recombinant protein from Neisseria enhances antigen delivery and dendritic cell activation in vitro"*
**作者**：Smith H, Tang CM, Pollard AJ
**摘要**：研究发现重组PorB蛋白可作为佐剂，促进树突状细胞对抗原的摄取和加工，并上调共刺激分子表达，增强适应性免疫应答，提示其在疫苗开发中的应用价值。
如需更多文献或特定研究方向，可进一步调整关键词检索。
PorB is a major outer membrane porin protein found in various Gram-negative bacterial pathogens, most notably in the *Neisseria* genus, including *Neisseria meningitidis* (meningococcus) and *Neisseria gonorrhoeae* (gonococcus). As a porin, PorB forms trimeric β-barrel channels in the bacterial outer membrane, facilitating the passive transport of small molecules, ions, and nutrients. It plays a critical role in bacterial survival, virulence, and host-pathogen interactions. For instance, PorB in pathogenic *Neisseria* species contributes to immune evasion by modulating host cell signaling pathways, such as inhibiting phagolysosomal maturation or suppressing apoptosis in infected cells. Its surface exposure and immunogenicity also make it a key target for host immune responses.
Recombinant PorB (rPorB) is produced through genetic engineering, typically by cloning the *porB* gene into expression vectors (e.g., *E. coli*), followed by protein purification. This approach allows large-scale production of PorB for research and therapeutic applications. Studies on rPorB have advanced understanding of its structural dynamics, including conformational changes during membrane integration and ion selectivity. Additionally, rPorB serves as a tool for investigating host immune activation, as it can act as both an antigen and a pathogen-associated molecular pattern (PAMP). It binds to Toll-like receptors (TLRs) or interacts with mitochondrial membranes, triggering pro-inflammatory cytokine production or apoptosis.
In vaccinology, rPorB is explored as a vaccine candidate or adjuvant due to its ability to stimulate robust B-cell and T-cell responses. Efforts to optimize its stability, antigenicity, or delivery systems (e.g., nanoparticle formulations) aim to enhance its efficacy against infections like meningitis or gonorrhea. Research also focuses on its potential in cancer immunotherapy, leveraging its immune-stimulating properties. Overall, PorB recombinant protein bridges microbiological research and translational applications, offering insights into bacterial pathogenesis and novel therapeutic strategies.
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