| 纯度 | >90%SDS-PAGE. |
| 种属 | E.coli |
| 靶点 | A33R |
| Uniprot No | P68616 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 57-185aa |
| 氨基酸序列 | VRLNQCMSANEAAITDAAVAVAAASSTHRKVASSTTQYDHKESCNGLYYQGSCYILHSDYQLFSDAKANCTAESSTLPNKSDVLITWLIDYVEDTWGSDGNPITKTTSDYQDSDVSQEVRKYFCVKTMN |
| 预测分子量 | 17.8 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A33R重组蛋白的模拟参考文献示例(仅供信息参考，实际文献需通过学术数据库查询)：
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1. **"A33R重组痘苗病毒作为疫苗载体的免疫原性研究"**
*作者：Smith J et al. (2010)*
**摘要**：研究A33R重组蛋白在小鼠模型中诱导的体液和细胞免疫反应，证明其作为痘病毒疫苗载体可增强针对异源抗原的保护效果。
2. **"A33R蛋白的晶体结构揭示其抗原表位特征"**
*作者：Jones R et al. (2015)*
**摘要**：通过X射线晶体学解析A33R重组蛋白的三维结构，发现其表面暴露的抗原表位，为靶向疫苗设计提供结构基础。
3. **"A33R在痘病毒宿主细胞入侵中的功能机制"**
*作者：Lee H et al. (2018)*
**摘要**：利用A33R重组蛋白进行体外结合实验，证实其与宿主细胞表面受体相互作用，对病毒包膜融合及细胞入侵至关重要。
4. **"基于A33R重组蛋白的血清学诊断方法开发"**
*作者：Zhang Y et al. (2020)*
**摘要**：构建A33R重组蛋白的ELISA检测体系，验证其在痘病毒感染血清学诊断中的高特异性和灵敏度。
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**注意**：以上为模拟文献，实际研究中请通过PubMed、Google Scholar等平台检索关键词(如"A33R recombinant protein"、"vaccinia virus A33R")获取真实数据。
The A33R recombinant protein is a key antigenic component derived from the vaccinia virus (VACV), a member of the Orthopoxvirus genus. It is a type II transmembrane glycoprotein predominantly expressed on the surface of extracellular enveloped virions (EEVs), which play a critical role in viral dissemination and immune evasion. A33R is highly conserved across poxviruses, including variola virus (the causative agent of smallpox), making it a promising target for broad-spectrum poxvirus vaccine development.
Structurally, A33R contains a C-terminal ectodomain with a conserved C-type lectin-like fold, mediating interactions with host cell receptors or viral proteins (e.g., A34 or A36) to facilitate EEV formation and cell-to-cell spread. Its immunodominant epitopes elicit potent neutralizing antibodies and T-cell responses, contributing to protective immunity. Recombinant A33R is typically produced in eukaryotic expression systems (e.g., mammalian or insect cells) to ensure proper glycosylation and conformational fidelity.
In vaccine research, A33R is often combined with other VACV antigens (e.g., L1. B5) in subunit vaccine formulations to enhance protection against orthopoxviruses. Preclinical studies demonstrate that A33R-based vaccines reduce viral loads and improve survival in challenge models. Its inclusion in modern vaccine platforms (e.g., mRNA, viral vectors) is being explored to address emerging poxvirus threats and improve smallpox preparedness. Additionally, A33R serves as a tool to study poxvirus entry mechanisms and antiviral drug development.
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