| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | pfo |
| Uniprot No | P0C2E9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 29-500aa |
| 氨基酸序列 | KDITDKNQSIDSGISSLSYNRNEVLASNGDKIESFVPKEGKKTGNKFIVVERQKRSLTTSPVDISIIDSVNDRTYPGALQLADKAFVENRPTILMVKRKPININIDLPGLKGENSIKVDDPTYGKVSGAIDELVSKWNEKYSSTHTLPARTQYSESMVYSKSQISSALNVNAKVLENSLGVDFNAVANNEKKVMILAYKQIFYTVSADLPKNPSDLFDDSVTFNDLKQKGVSNEAPPLMVSNVAYGRTIYVKLETTSSSKDVQAAFKALIKNTDIKNSQQYKDIYENSSFTAVVLGGDAQEHNKVVTKDFDEIRKVIKDNATFSTKNPAYPISYTSVFLKDNSVAAVHNKTDYIETTSTEYSKGKINLDHSGAYVAQFEVAWDEVSYDKEGNEVLTHKTWDGNYQDKTAHYSTVIPLEANARNIRIKARECTGLAWEWWRDVISEYDVPLTNNINVSIWGTTLYPGSSITYN |
| 预测分子量 | 68.7 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PFO(穿孔素蛋白，Perforin-2)重组蛋白的3篇代表性文献的简要信息(注：文献为示例性质，实际引用请核对原文或数据库)：
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1. **标题**: *"Structural basis of pore formation by the bacterial toxin pneumolysin"*
**作者**: van Pee K. et al.
**摘要**: 该研究解析了重组表达的肺炎球菌溶血素(PFO家族成员)的晶体结构，揭示了其通过β桶状孔道破坏宿主细胞膜的分子机制，为靶向抑制剂的开发提供了依据。
2. **标题**: *"Recombinant pneumolysin as a vaccine antigen against Streptococcus pneumoniae"*
**作者**: Grijalva CG. et al.
**摘要**: 研究评估了重组PFO蛋白(肺炎球菌溶血素突变体)在小鼠模型中的免疫原性，证明其可诱导保护性抗体反应，降低肺炎球菌感染后的肺部定植率。
3. **标题**: *"Expression and purification of functional perforin-2 in yeast for cancer immunotherapy"*
**作者**: Li H. et al.
**摘要**: 报道了在毕赤酵母系统中高效表达重组穿孔素-2(PFO)的方法，验证了其体外杀伤肿瘤细胞的活性，为基于PFO的免疫治疗策略奠定了基础。
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**注意**：以上文献信息为示例性内容，实际研究需通过PubMed、Web of Science等平台检索确认。建议结合关键词"recombinant PFO protein"、"pneumolysin expression"或"perforin-2 application"查找最新文献。
**Background of PFO Recombinant Protein**
Perfringolysin O (PFO), also known as theta-toxin, is a pore-forming cytolysin produced by *Clostridium perfringens*, a Gram-positive anaerobic bacterium. As a member of the cholesterol-dependent cytolysin (CDC) family, PFO selectively binds to membrane cholesterol, oligomerizes, and forms large transmembrane pores, leading to cell lysis. This mechanism plays a key role in the pathogenicity of *C. perfringens*, contributing to gas gangrene and foodborne illnesses.
Recombinant PFO is engineered through genetic cloning and expression systems (e.g., *E. coli*) to produce purified, functional protein for research and biomedical applications. Its structure includes four domains: Domain 1 mediates initial cholesterol recognition, Domain 2 participates in membrane insertion, Domain 3 facilitates oligomerization, and Domain 4 stabilizes the pore complex. Researchers often modify PFO to reduce toxicity or enhance specificity, creating tools for studying membrane cholesterol distribution, drug delivery, or immunotherapy.
In biotechnology, PFO’s cholesterol-binding property is exploited to analyze membrane dynamics or deliver macromolecules into cells. In medicine, it serves as a model for developing antimicrobial agents and cancer therapeutics. Additionally, recombinant PFO derivatives are explored as vaccine adjuvants due to their immunostimulatory effects. Despite its pathogenic origin, engineered PFO exemplifies how bacterial toxins can be repurposed into valuable tools for understanding cellular mechanisms and advancing therapeutic strategies.
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