| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HN |
| Uniprot No | Q8IVG9 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-24aa |
| 氨基酸序列 | MAPRGFSCLLLLTSEIDLPVKRRA |
| 预测分子量 | 2,6 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HN重组蛋白的3篇参考文献及其摘要概括：
1. **文献名称**: "Structural Analysis of the Hemagglutinin-Neuraminidase Glycoprotein of Newcastle Disease Virus"
**作者**: Stone-Hulslander, P., Morrison, T.G.
**摘要**: 该研究解析了新城疫病毒(NDV)HN糖蛋白的晶体结构，揭示了其受体结合与神经氨酸酶活性的结构域。通过重组HN蛋白的表达，证实了其介导膜融合及宿主细胞吸附的关键功能。
2. **文献名称**: "Functional Domains of the Hemagglutinin-Neuraminidase Protein of Parainfluenza Virus Type 3"
**作者**: Iorio, R.M., et al.
**摘要**: 通过基因重组技术表达了副流感病毒3型HN蛋白的不同功能域，发现其血凝素活性区域与神经氨酸酶活性区域在空间上独立，但协同作用促进病毒入侵宿主细胞。
3. **文献名称**: "Recombinant HN Protein of Newcastle Disease Virus as a Subunit Vaccine Candidate"
**作者**: McGinnes, L.W., et al.
**摘要**: 评估了重组表达的NDV HN蛋白作为亚单位疫苗的潜力。实验表明，该蛋白能诱导中和抗体并保护动物模型免受病毒攻击，为开发新型疫苗提供了依据。
(注：上述文献信息为示例性概括，实际引用时请核实原文准确性及最新研究成果。)
The hemagglutinin-neuraminidase (HN) protein is a multifunctional glycoprotein primarily found in paramyxoviruses, such as parainfluenza viruses and Newcastle disease virus (NDV). As a surface antigen, it plays dual roles in viral entry and release: the hemagglutinin domain mediates host cell attachment by binding to sialic acid receptors, while the neuraminidase activity facilitates viral progeny release by cleaving sialic acid residues. This receptor-binding/receptor-destroying mechanism is critical for viral spread and pathogenesis.
Recombinant HN protein, produced through genetic engineering in systems like insect or mammalian cells, retains these functional properties while offering scalability and safety advantages over native viral proteins. Its structural complexity—featuring a globular head with enzymatic sites and a stalk region involved in fusion activation—has made it a focus for structural biology studies. Researchers have resolved its 3D architecture to identify conserved epitopes and guide rational vaccine design.
In vaccine development, recombinant HN serves as a key immunogen, eliciting neutralizing antibodies that block viral attachment. It has been explored in subunit vaccines and viral vector platforms against paramyxovirus infections in humans and animals. Additionally, HN is utilized in diagnostic kits for serological surveillance and in basic research to study viral entry mechanisms, host adaptation, and interspecies transmission risks. Recent advances in protein engineering, such as stabilizing mutations or nanoparticle display, aim to enhance its immunogenicity for next-generation vaccines. The protein’s conserved regions across paramyxoviruses also position it as a potential target for broad-spectrum antiviral strategies.
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