| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | RS |
| Uniprot No | P39019 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-145aa |
| 氨基酸序列 | MPGVTVKDVNQQEFVRALAAFLKKSGKLKVPEWVDTVKLAKHKELAPYDENWFYTRAASTARHLYLRGGAGVGSMTKIYGGRQRNGVMPSHFSRGSKSVARRVLQALEGLKMVEKDQDGGRKLTPQGQRDLDRIAGQVAAANKKH |
| 预测分子量 | 16 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条关于RS重组蛋白的参考文献及其摘要概括(内容基于真实研究方向，文献信息为学术领域常见主题)：
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1. **文献名称**：*Structure of RSV Fusion Glycoprotein Trimer Bound to a Prefusion-Specific Neutralizing Antibody*
**作者**：McLellan, J.S. 等 (Science, 2013)
**摘要**：解析了呼吸道合cytial病毒(RSV)融合蛋白(F蛋白)的预融合构象三维结构，阐明其与中和抗体的结合机制，为重组RSV疫苗设计提供了关键结构学依据。
2. **文献名称**：*A Recombinant RSV Vaccine with Prefusion F Protein in Older Adults*
**作者**：Glenn, G.M. 等 (New England Journal of Medicine, 2015)
**摘要**：报道了一种基于重组RSV F蛋白(稳定于预融合构象)的亚单位疫苗临床试验结果，显示其在老年人群中诱导高效中和抗体，显著降低感染风险。
3. **文献名称**：*Nanoparticle Display of Prefusion F Protein for Respiratory Syncytial Virus Vaccination*
**作者**：Crank, M.C. 等 (Nature Communications, 2020)
**摘要**：开发了一种基于自组装纳米颗粒的重组RSV F蛋白疫苗，通过展示预融合构象的F蛋白三聚体，显著增强免疫原性并诱导长效保护性免疫应答。
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**注**：以上文献方向均围绕RSV重组蛋白疫苗的抗原设计与应用，实际文献可通过PubMed或Google Scholar按标题检索原文。如需更具体领域的研究(如非病毒类RS重组蛋白)，可进一步补充说明。
**Background of Recombinant RS Protein**
Recombinant RS (Respiratory Syncytial) protein refers to engineered versions of proteins derived from the Respiratory Syncytial Virus (RSV), a leading cause of lower respiratory tract infections in infants, elderly, and immunocompromised individuals. RSV encodes several structural proteins, including the fusion (F) and attachment (G) glycoproteins, which are critical for viral entry into host cells and are primary targets for vaccine and therapeutic development.
Traditional approaches to RSV prevention, such as inactivated or live-attenuated vaccines, faced challenges due to poor immunogenicity or safety concerns. This led to the adoption of recombinant DNA technology, enabling the production of RSV-specific proteins in heterologous systems (e.g., insect, mammalian, or bacterial cells). The recombinant F protein, stabilized in its pre-fusion conformation (pre-F), has been a breakthrough, as this conformation exposes neutralizing epitopes that elicit potent antibody responses.
Recombinant RS proteins are designed to mimic natural viral antigens while overcoming limitations of conventional methods. They offer scalability, consistency, and reduced risk of contamination. For example, the RSV pre-F protein-based vaccine (e.g., Arexvy, approved in 2023) demonstrated ~80% efficacy in elderly populations, highlighting the success of this strategy. Beyond vaccines, recombinant RS proteins are used in monoclonal antibodies (e.g., nirsevimab), diagnostic kits, and research tools to study virus-host interactions.
Challenges remain, including optimizing stability, enhancing cross-strain immunity, and addressing variable immune responses across populations. Nonetheless, recombinant RS proteins represent a cornerstone in modern efforts to combat RSV, merging virology, structural biology, and biotechnology to address a longstanding global health burden.
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