纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | Cor |
Uniprot No | O75376 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 全长 |
氨基酸序列 | full |
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. |
以下是关于冠状病毒(Cor)重组蛋白研究的3篇模拟参考文献示例,供参考:
1. **《SARS-CoV-2刺突蛋白的重组表达与免疫原性分析》**
- 作者:Smith, J. et al.
- 摘要:研究利用哺乳动物表达系统成功重组表达了SARS-CoV-2刺突蛋白(S蛋白),并验证其在动物模型中诱导中和抗体的能力,为疫苗开发提供了实验依据。
2. **《重组冠状病毒核衣壳蛋白(N蛋白)在血清学诊断中的应用》**
- 作者:Li, X. & Chen, H.
- 摘要:通过大肠杆菌系统表达SARS-CoV-2 N蛋白,开发基于该重组蛋白的ELISA检测方法,证实其在COVID-19患者血清抗体检测中的高灵敏度和特异性。
3. **《MERS-CoV重组受体结合域(RBD)的结构与功能研究》**
- 作者:Zhang, Y. et al.
- 摘要:解析了MERS-CoV刺突蛋白受体结合域(RBD)的晶体结构,阐明其与宿主细胞受体DPP4的相互作用机制,为抗病毒药物设计提供结构基础。
注:以上文献为模拟示例,实际研究中请通过学术数据库(如PubMed、Web of Science)检索真实发表的论文。
Cor recombinant proteins, primarily derived from coronaviruses (CoVs), have gained significant attention following global outbreaks caused by pathogens like SARS-CoV-1. MERS-CoV, and SARS-CoV-2. These proteins are engineered using genetic recombination techniques to express specific viral structural or non-structural components, such as the spike (S) protein, nucleocapsid (N) protein, or envelope (E) protein. The spike protein, particularly its receptor-binding domain (RBD), is a key focus due to its role in viral entry and host immune recognition.
The development of Cor recombinant proteins is driven by their utility in diagnostics, therapeutics, and vaccine research. For instance, recombinant S proteins serve as critical antigens in serological assays to detect anti-CoV antibodies, aiding in epidemiological surveillance. In vaccine design, platforms like mRNA and subunit vaccines rely on recombinant S proteins to elicit neutralizing antibodies. Structural studies using these proteins, often resolved via cryo-EM, have clarified mechanisms of viral fusion and antibody neutralization, informing drug development.
Production typically involves heterologous expression systems (e.g., mammalian, insect, or bacterial cells), with glycosylation patterns tailored to mimic native viral proteins. Challenges include maintaining protein stability and conformational integrity, which influence immunogenicity. Recent advances in protein engineering, such as stabilizing mutations (e.g., proline substitutions in SARS-CoV-2 S protein), have enhanced their application in preclinical models and clinical trials.
Beyond biomedical applications, Cor recombinant proteins are tools for basic virology, enabling studies on host-pathogen interactions and evolutionary adaptations. Their modular design also supports rapid responses to emerging variants, underscoring their importance in pandemic preparedness. Overall, these proteins represent a versatile cornerstone in combating coronavirus-related health crises. (297 words)
×