| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | SARS |
| Uniprot No | P49591 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-514aa |
| 氨基酸序列 | MVLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPVGDDESVPENVLSFDDLTADALANLKVSQIKKVRLLIDEAILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDVDNKVERIWGDCTVRKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEVMQEVAQLSQFDEELYKVIGKGSEKSDDNSYDEKYLIATSEQPIAALHRDEWLRPEDLPIKYAGLSTCFRQEVGSHGRDTRGIFRVHQFEKIEQFVYSSPHDNKSWEMFEEMITTAEEFYQSLGIPYHIVNIVSGSLNHAASKKLDLEAWFPGSGAFRELVSCSNCTDYQARRLRIRYGQTKKMMDKVEFVHMLNATMCATTRTICAILENYQTEKGITVPEKLKEFMPPGLQELIPFVKPAPIEQEPSKKQKKQHEGSKKKAAARDVTLENRLQNMEVTDA |
| 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篇关于SARS重组蛋白研究的参考文献示例(内容基于真实研究整理，具体作者与标题可能存在调整)：
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1. **标题**：Expression and characterization of recombinant SARS coronavirus spike protein
**作者**：He Y. et al.
**摘要**：研究利用哺乳动物细胞系统表达SARS-CoV的S蛋白重组片段，证实其可诱导中和抗体，为亚单位疫苗开发提供依据。
2. **标题**：Crystal structure of SARS-CoV spike receptor-binding domain bound to ACE2
**作者**：Li F. et al.
**摘要**：通过X射线晶体学解析SARS病毒S蛋白受体结合域(RBD)与宿主ACE2的复合物结构，揭示病毒入侵的分子机制。
3. **标题**：Potent inhibition of SARS-CoV infection by heptad repeat-derived peptides
**作者**：Jiang S. et al.
**摘要**：基于S蛋白HR区域设计重组多肽，实验证明其可有效阻断病毒膜融合，提出新型抗病毒药物开发策略。
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注：建议通过PubMed或Google Scholar以关键词 "SARS recombinant protein"+"spike"+"vaccine" 等组合查询最新文献，并核实具体发表信息。
**Background of SARS Recombinant Proteins**
The Severe Acute Respiratory Syndrome (SARS) outbreak in 2002–2003. caused by the SARS-associated coronavirus (SARS-CoV), highlighted the urgent need for diagnostic tools, therapeutics, and vaccines. A key focus of research involved studying viral structural proteins, particularly the spike (S) glycoprotein, which mediates viral entry into host cells by binding to the angiotensin-converting enzyme 2 (ACE2) receptor. Recombinant protein technology emerged as a critical tool to produce these viral antigens in vitro for functional and immunological studies.
Recombinant SARS proteins are generated by cloning viral gene sequences into expression systems (e.g., bacteria, yeast, or mammalian cells), enabling large-scale production of purified proteins. The S protein, composed of two subunits (S1 and S2), has been a primary target due to its role in eliciting neutralizing antibodies. Recombinant S proteins or their receptor-binding domain (RBD) have been used to develop subunit vaccines and evaluate immune responses. Similarly, nucleocapsid (N) and membrane (M) proteins, though less immunogenic, have been explored for diagnostics and understanding viral assembly.
These recombinant proteins also facilitated the study of SARS-CoV pathogenesis, host interactions, and cross-reactivity with other coronaviruses. During the COVID-19 pandemic, insights from SARS recombinant protein research accelerated the development of SARS-CoV-2 countermeasures, as both viruses share structural and mechanistic similarities.
Overall, recombinant SARS proteins remain essential for advancing coronavirus research, offering a safe and scalable platform for dissecting viral biology and designing targeted interventions. Their utility underscores the importance of recombinant technology in pandemic preparedness and response.
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