| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | H1 |
| Uniprot No | Q8IZA3 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-346aa |
| 氨基酸序列 | MAPGSVTSDI SPSSTSTAGS SRSPESEKPG PSHGGVPPGG PSHSSLPVGR RHPPVLRMVL EALQAGEQRR GTSVAAIKLY ILHKYPTVDV LRFKYLLKQA LATGMRRGLL ARPLNSKARG ATGSFKLVPK HKKKIQPRKM APATAPRRAG EAKGKGPKKP SEAKEDPPNV GKVKKAAKRP AKVQKPPPKP GAATEKARKQ GGAAKDTRAQ SGEARKVPPK PDKAMRAPSS AGGLSRKAKA KGSRSSQGDA EAYRKTKAES KSSKPTASKV KNGAASPTKK KVVAKAKAPK AGQGPNTKAA APAKGSGSKV VPAHLSRKTE APKGPRKAGL PIKASSSKVS SQRAEA |
| 预测分子量 | 35,8 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H1重组蛋白的3篇代表性文献及其摘要概括：
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1. **文献名称**：*Recombinant H1 histone-based gene delivery system for efficient transfection of mammalian cells*
**作者**：Zhang Y, et al.
**摘要**：研究开发了一种基于重组H1组蛋白的非病毒基因递送载体，通过融合细胞穿透肽增强其跨膜能力，实验证明其在小鼠成纤维细胞中显著提高质粒DNA的转染效率，且细胞毒性低于传统脂质体载体。
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2. **文献名称**：*Engineering H1 parvovirus-like particles for targeted cancer therapy*
**作者**：Wang L, et al.
**摘要**：利用重组H1蛋白自组装形成病毒样颗粒(VLPs)，通过修饰表面靶向分子使其特异性结合肿瘤细胞受体。体内实验表明该颗粒能有效递送化疗药物，抑制小鼠肿瘤生长并降低全身毒性。
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3. **文献名称**：*Functional characterization of recombinant H1 linker histones in chromatin condensation*
**作者**：Thomas JO, et al.
**摘要**：通过大肠杆菌表达系统获得高纯度重组H1组蛋白，体外实验揭示其通过结合核小体连接区DNA调控染色质高级结构，不同亚型H1在染色质凝聚中表现出功能差异，为表观遗传机制研究提供工具。
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注：以上文献为虚拟示例，实际研究中需根据具体方向查阅权威期刊(如*Nature Biotechnology*、*Nucleic Acids Research*等)的论文。
**Background of H1 Recombinant Protein**
The H1 recombinant protein is a genetically engineered version of hemagglutinin (HA), a surface glycoprotein critical to the influenza virus's ability to infect host cells. HA, composed of two subunits (HA1 and HA2), facilitates viral entry by binding to sialic acid receptors on host cells and mediating membrane fusion. The "H1" designation refers to one of 18 HA subtypes, historically associated with seasonal influenza A strains (e.g., H1N1) and pandemics, including the 2009 swine flu outbreak.
Recombinant H1 protein is produced using expression systems such as insect cells (baculovirus) or mammalian cells (e.g., HEK293), which ensure proper post-translational modifications. This technology bypasses the need for live virus handling, enhancing safety and scalability. The purified protein retains key antigenic regions, making it valuable for vaccine development, particularly for eliciting neutralizing antibodies against H1N1 strains.
Applications extend beyond vaccines. Researchers use H1 recombinant protein to study viral entry mechanisms, screen antiviral compounds, and develop diagnostic assays (e.g., ELISA). Its structural fidelity allows for epitope mapping and immune response analysis, aiding in universal vaccine design.
Compared to traditional egg-based influenza vaccines, recombinant HA production offers faster turnaround, reduced allergenicity, and batch-to-batch consistency—critical during pandemics. The 2009 H1N1 crisis underscored its utility, accelerating adoption in both therapeutic and research settings.
In summary, H1 recombinant protein exemplifies advancements in biotech, providing a safer, versatile tool for combating influenza and deepening insights into viral glycoprotein biology.
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