| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | VF |
| Uniprot No | Q9HCQ7 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 56-92aa |
| 氨基酸序列 | SLNFE ELKDWGPKNV IKMSTPAVNK MPHSFANLPL RF |
| 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3篇与重组蛋白设计、生产及应用相关的参考文献，简要概括供参考：
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1. **文献名称**: "Design of a recombinant protein-based COVID-19 vaccine with enhanced stability and immunogenicity"
**作者**: Zhang, Y. et al.
**摘要**: 该研究利用结构生物学方法优化了新冠病毒刺突蛋白的受体结合域(RBD)重组设计，通过引入二硫键提升蛋白稳定性，并在动物模型中验证其诱导高效中和抗体的能力，为重组亚单位疫苗开发提供新策略。
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2. **文献名称**: "High-yield production of recombinant SARS-CoV-2 spike protein in mammalian cells for vaccine development"
**作者**: Liu, X. et al.
**摘要**: 文章报道了一种基于哺乳动物细胞(HEK293)的高效表达系统，通过优化密码子、启动子及纯化工艺，实现新冠病毒刺突蛋白(S蛋白)的大规模生产，并证实其与天然构象高度一致，适用于疫苗研发。
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3. **文献名称**: "Affinity chromatography platform for rapid purification of engineered viral fusion proteins"
**作者**: Smith, J. et al.
**摘要**: 研究开发了一种新型亲和层析技术，利用金属螯合配体特异性捕获含组氨酸标签的重组病毒融合(VF)蛋白，显著提升纯化效率并保持蛋白生物活性，为病毒蛋白药物规模化生产提供技术支撑。
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4. **文献名称**: "Structural and functional analysis of a recombinant vesicular stomatitis virus fusion glycoprotein"
**作者**: Wang, H. et al.
**摘要**: 通过冷冻电镜解析重组水泡性口炎病毒(VSV)融合糖蛋白(G蛋白)的三维结构，阐明其介导病毒-宿主膜融合的分子机制，为靶向VF蛋白的抗病毒药物设计奠定基础。
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注：以上文献为虚拟示例，实际研究中建议通过PubMed或Web of Science检索具体论文。若需真实文献，可提供更具体的VF蛋白定义(如特定病毒名称或功能)。
**Background of VF Recombinant Proteins**
Recombinant protein technology has revolutionized biomedical research and therapeutic development by enabling the production of specific proteins through genetic engineering. VF recombinant proteins, often associated with viral vector-based platforms, represent a critical advancement in this field. These proteins are typically designed using viral vectors—such as modified vaccinia virus (e.g., VACV strain) or other engineered viruses—to express target antigens or therapeutic proteins. The "VF" designation may refer to specific vector systems or proprietary technologies optimized for high-yield, stable protein expression.
The development of VF recombinant proteins is rooted in the need for scalable, cost-effective methods to produce proteins for vaccines, diagnostics, and treatments. For instance, viral vectors can infect host cells and hijack their machinery to mass-produce proteins encoded by inserted genes. This approach ensures proper post-translational modifications, enhancing protein functionality compared to bacterial expression systems. VF-based platforms gained prominence during the COVID-19 pandemic, where viral vector vaccines (e.g., AstraZeneca’s ChAdOx1) demonstrated rapid, large-scale production of spike proteins to elicit immune responses.
Applications extend beyond vaccines to cancer immunotherapy, gene therapy, and infectious disease research. VF recombinant proteins are valued for their ability to mimic natural protein structures, improving antigenicity and therapeutic efficacy. Challenges include minimizing vector-induced immune reactions and optimizing purification processes. Ongoing innovations focus on vector engineering, such as reducing virulence or enhancing tissue specificity, to expand their utility in precision medicine. Overall, VF recombinant proteins bridge genetic design with practical biomedical solutions, underscoring their pivotal role in modern biotechnology.
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