| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | H3 |
| Uniprot No | P68431 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-136aa |
| 氨基酸序列 | MMHHHHHHARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYR PGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMAL QEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA |
| 预测分子量 | 15 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篇与H3重组蛋白相关的文献示例(注：文献为模拟虚构，仅用于示例，实际引用请以真实文献为准)：
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1. **文献名称**: *"Expression and Purification of Recombinant Histone H3 for Epigenetic Studies"*
**作者**: Smith J. et al.
**摘要**: 研究报道了通过大肠杆菌系统高效表达和纯化重组组蛋白H3的方法，并验证其在体外核小体组装及组蛋白修饰酶活性分析中的应用，为表观遗传机制研究提供工具。
2. **文献名称**: *"Structural Characterization of H3 Hemagglutinin from Influenza A Virus"*
**作者**: Li X. et al.
**摘要**: 利用昆虫细胞表达系统获得重组流感病毒H3血凝素蛋白，通过冷冻电镜解析其三维结构，揭示其与宿主细胞受体的结合机制，为广谱疫苗设计提供依据。
3. **文献名称**: *"Recombinant H3-Based Vaccine Induces Cross-Protective Immunity in Mice"*
**作者**: Wang Y. et al.
**摘要**: 开发基于H3重组蛋白的亚单位疫苗，在小鼠模型中证明其对多种H3N2流感病毒株的交叉保护效果，提示其作为候选疫苗的潜力。
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如需真实文献，建议在PubMed或Web of Science中检索关键词：**"recombinant H3 protein"** 或 **"H3 histone recombinant"**，并筛选近五年高被引论文。
The H3 recombinant protein is a key component derived from the hemagglutinin (HA) glycoprotein of influenza A viruses, specifically the H3 subtype. Hemagglutinin, a surface protein, facilitates viral entry into host cells by binding to sialic acid receptors and mediating membrane fusion. The H3 subtype gained prominence after the 1968 Hong Kong flu pandemic (H3N2) and remains a major circulating strain in seasonal influenza. Its high genetic variability due to antigenic drift necessitates continuous vaccine updates, driving interest in recombinant H3 protein production for research and therapeutic applications.
Recombinant H3 proteins are typically generated using expression systems like baculovirus/insect cells or mammalian cell cultures, ensuring proper post-translational modifications (e.g., glycosylation) for structural and functional authenticity. These proteins retain critical epitopes for neutralizing antibodies, making them valuable tools for studying viral pathogenesis, host immune responses, and antigenic evolution. In vaccine development, recombinant H3 serves as a standardized antigen for potency testing and a candidate for next-generation vaccines, including virus-like particles (VLPs) and subunit vaccines. Its use circumvents biosafety concerns associated with live virus handling.
Additionally, H3 recombinant proteins are employed in serological assays to evaluate population immunity and monitor vaccine effectiveness. Recent advances in structural biology utilize these proteins to map antigenic sites and design broad-spectrum inhibitors. Challenges persist in mimicking the conformational dynamics of native HA trimers and addressing the subtype's diversity. However, progress in protein engineering, such as stabilizing mutations and nanoparticle display, enhances their immunogenicity and thermal stability. As a versatile reagent, recombinant H3 protein bridges basic virology and applied biomedical research, contributing to pandemic preparedness and universal influenza vaccine initiatives.
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