| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | HN1 |
| Uniprot No | Q9UK76 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 2-154aa |
| 氨基酸序列 | TTTTTFKGVDPNSRNSSRVLRPPGGGSNFSLGFDEPTEQPVRKNKMASNIFGTPEENQASWAKSAGAKSSGGREDLESSGLQRRNSSEASSGDFLDLKGEGDIHENVDTDLPGSLGQSEEKPVPAAPVPSPVAPAPVPSRRNPPGGKSSLVLG |
| 预测分子量 | 17.9kDa |
| 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HN1重组蛋白的3篇参考文献示例(注：文献为虚构示例，仅供参考格式)：
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1. **文献名称**：Structural Characterization and Functional Analysis of Recombinant HN1 Protein from Influenza Virus
**作者**：J. Smith et al.
**摘要**：本研究成功在大肠杆菌中表达并纯化了HN1重组蛋白，通过X射线晶体学解析其三维结构，揭示了其血凝素和神经氨酸酶活性位点的关键氨基酸残基，为抗病毒药物设计提供了结构基础。
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2. **文献名称**：HN1 Recombinant Protein Enhances Tumor Metastasis via PI3K/AKT Pathway in Breast Cancer
**作者**：L. Chen et al.
**摘要**：通过体外实验验证了重组HN1蛋白在乳腺癌细胞中的促转移作用，发现其通过激活PI3K/AKT信号通路促进上皮-间质转化(EMT)，为靶向HN1的癌症治疗提供了理论依据。
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3. **文献名称**：Expression Optimization and Immunogenicity Evaluation of HN1 Recombinant Protein for Vaccine Development
**作者**：M. Gupta et al.
**摘要**：优化了昆虫细胞系统中HN1重组蛋白的表达条件，证明其在小鼠模型中能诱导高滴度中和抗体，提示其作为候选疫苗的潜力。
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**备注**：实际文献需通过PubMed、Google Scholar等平台以关键词“HN1 recombinant protein”或“HN1 protein structure/function”检索确认。若研究领域为特定疾病(如癌症或病毒感染)，建议结合疾病名称缩小搜索范围。
HN1 recombinant protein is derived from the hemagglutinin-neuraminidase (HN) glycoprotein, a critical surface antigen of paramyxoviruses such as parainfluenza virus type 1 (PIV1) or mumps virus. The HN protein plays dual roles in viral infection: it facilitates host cell attachment by binding to sialic acid receptors (hemagglutinin activity) and promotes viral release by cleaving sialic acid residues (neuraminidase activity). These functions make HN a key target for antiviral therapies and vaccine development.
The recombinant HN1 protein is typically produced using expression systems like mammalian cells, insect cells, or *E. coli*, enabling scalable and controlled production. Structural studies of HN1. often resolved via X-ray crystallography or cryo-EM, reveal a tetrameric architecture with distinct receptor-binding and enzymatic domains. These insights guide rational drug design and epitope mapping for neutralizing antibodies.
In research, HN1 serves as a critical tool for studying viral entry mechanisms, immune responses, and cross-reactivity among paramyxoviruses. It is also employed in diagnostic assays to detect virus-specific antibodies and in subunit vaccine candidates to elicit protective immunity. Recent efforts focus on engineering HN1 variants with enhanced stability or immunogenicity, often through glycosylation optimization or epitope scaffolding. Challenges include balancing antigenicity with safety (e.g., avoiding antibody-dependent enhancement) and addressing genetic variability across viral strains.
Overall, HN1 recombinant protein bridges virology and translational medicine, offering a platform for next-generation antivirals and vaccines against paramyxovirus infections.
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