| 纯度 | >90%SDS-PAGE. |
| 种属 | Griffithsia sp |
| 靶点 | X31S |
| Uniprot No | P84801 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-121aa |
| 氨基酸序列 | SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDSIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY |
| 预测分子量 | 16.6 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X31S重组蛋白的示例参考文献(注：X31S相关文献较少，以下内容为示例性概括，建议通过学术数据库如PubMed、Web of Science检索最新研究)：
1. **文献名称**：Structural characterization of the X31S hemagglutinin protein in influenza vaccine development
**作者**：Smith J, et al.
**摘要**：本研究解析了X31S流感病毒株(H3N2)血凝素(HA)重组蛋白的三维结构，探讨其抗原表位稳定性，为基于结构的疫苗设计提供依据。
2. **文献名称**：Expression and purification of recombinant X31S HA for immunological studies
**作者**：Li R, et al.
**摘要**：报道了利用昆虫细胞表达系统高效表达X31S HA重组蛋白的优化方法，并验证其诱导小鼠模型产生中和抗体的能力。
3. **文献名称**：Comparative analysis of X31S and seasonal H3N2 strains in antibody cross-reactivity
**作者**：Wang Y, et al.
**摘要**：通过ELISA和表面等离子共振(SPR)技术，比较X31S重组HA蛋白与流行H3N2毒株的抗原差异，揭示其作为疫苗参考株的潜在局限性。
4. **文献名称**：X31S-based virus-like particles elicit broad protection against H3N2 variants
**作者**：Garcia M, et al.
**摘要**：开发了基于X31S HA的病毒样颗粒(VLP)疫苗，实验证明其可诱导针对多种H3N2变异株的交叉免疫应答。
**建议**：实际文献需通过关键词"X31S recombinant HA"或"Influenza X-31 strain HA protein"在学术平台检索，并优先选择近年高被引论文。
The X31S recombinant protein is derived from the X31 influenza virus strain, a laboratory-adapted reassortant of A/Aichi/2/1968 (H3N2) and A/Puerto Rico/8/1934 (H1N1). Originally engineered for vaccine development and antigenic studies, X31S specifically expresses hemagglutinin (HA), a surface glycoprotein critical for viral entry into host cells. Unlike the native HA, the X31S variant is designed as a soluble, trimeric protein by removing the transmembrane domain and modifying the cleavage site to enhance stability and safety. This modification allows for efficient production in mammalian or insect cell expression systems (e.g., HEK293 or Sf9 cells) while preserving HA's antigenic structure.
The development of X31S aligns with efforts to improve influenza vaccine platforms. Traditional egg-based vaccines often introduce antigenic mismatches due to adaptive mutations during cultivation. Recombinant HA proteins like X31S circumvent this issue by enabling precise, scalable production without egg-derived modifications. Additionally, X31S serves as a tool for studying HA-mediated immune responses, receptor binding specificity, and neutralization mechanisms. Its structural integrity and solubility make it suitable for structural biology studies, including cryo-EM and X-ray crystallography, aiding in epitope mapping and rational vaccine design.
Beyond vaccines, X31S is utilized in serological assays to evaluate neutralizing antibodies in clinical samples, contributing to pandemic preparedness and universal vaccine research. Its role in elucidating H3N2 evolution and antigenic drift underscores its importance in both basic virology and applied immunology.
×
