| 纯度 | >90%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | ha17 |
| Uniprot No | P14429 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-334aa |
| 氨基酸序列 | MALTMLLLLVAAALTLIETRAGQHSLQYFHTAVSRPGLGEPWFISVGYVDDTQFVRFDSDAENPRMEPRARWMEQEGPEYWERETQIAKGHEQSFRGSLRTAQSYYNQSKGGSHTLQWMYGCDMGSDGRLLRGYLQFAYEGRDYIALNEDLKTWTAVDMAAQITRRKWEQAGIAEKDQAYLEGTCMQSLRRYLQLGKETLLRTDPPKAHVTHHPRSYGAVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCHVNHEGLPEPLTLRWGRWEPPPYTVSNMATIAVVVDLGAVAIIGAVVAFVMNRR |
| 预测分子量 | 37,9 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HA17重组蛋白的3篇模拟参考文献示例(注：部分内容基于真实研究背景，但文献名称及作者为虚构示例，建议通过学术数据库核实真实文献)：
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1. **文献名称**：Structural and functional characterization of bat-derived H17N10 hemagglutinin
**作者**：Tong S, et al.
**摘要**：本研究首次从蝙蝠流感病毒中克隆并表达了重组HA17蛋白，解析了其晶体结构，揭示了其与哺乳动物细胞受体的结合特性差异，为跨物种传播机制提供了依据。
2. **文献名称**：Recombinant HA17 expressed in insect cells elicits neutralizing antibodies in mice
**作者**：Wang LF, et al.
**摘要**：利用杆状病毒-昆虫细胞系统成功表达HA17重组蛋白，纯化后的小鼠免疫实验表明其可诱导特异性抗体反应，提示其作为通用流感疫苗候选抗原的潜力。
3. **文献名称**：Comparative analysis of HA17 glycosylation patterns in mammalian and avian influenza viruses
**作者**：García-Sastre A, et al.
**摘要**：通过重组HA17蛋白的糖基化修饰研究，发现其糖基化位点显著少于传统禽源HA，可能影响病毒免疫逃逸能力和宿主适应性。
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**备注**：HA17相关研究主要集中在蝙蝠流感病毒(如H17N10亚型)，真实文献可参考：
- **Tong et al. (2012)** 在《PNAS》发表的蝙蝠流感病毒H17发现论文;
- 后续研究多聚焦于HA17的结构与进化分析，建议通过PubMed或Google Scholar检索关键词“H17 hemagglutinin recombinant”获取最新进展。
HA17. a subtype of hemagglutinin (HA), is a surface glycoprotein primarily associated with influenza A viruses. As a key viral entry protein, HA mediates receptor binding and membrane fusion. HA17 gained attention due to its identification in bat-origin influenza-like viruses (e.g., H17N10), expanding our understanding of influenza diversity beyond avian and mammalian reservoirs. Its unique receptor-binding properties distinguish it from conventional HA subtypes, showing preferential affinity to MHC class II molecules rather than sialic acid receptors, suggesting alternative infection mechanisms.
Recombinant HA17 protein is produced through genetic engineering, typically using mammalian expression systems (e.g., HEK293 or CHO cells) to ensure proper glycosylation and structural integrity. The protein consists of two subunits (HA1 and HA2) forming trimeric spikes, with conserved structural domains critical for viral entry. Researchers utilize recombinant HA17 to study viral evolution, host adaptation, and interspecies transmission risks, particularly given bats' role as zoonotic reservoirs.
This recombinant protein serves as a vital tool for vaccine development, serological diagnostics, and neutralizing antibody production. Structural studies of HA17 have revealed unique features in its receptor-binding pocket and fusion peptide, providing insights into pH-dependent conformational changes during infection. Recent investigations focus on its antigenic variability and potential cross-reactivity with human-adapted HA subtypes, which could inform pandemic preparedness. Moreover, HA17's distinct characteristics make it a valuable model for exploring alternative antiviral strategies targeting conserved epitopes across influenza subtypes.
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