Recombinant Influenza A virus Nucleoprotein (NP) is produced in E. coli and includes the full-length sequence from 1 to 498 amino acids, ensuring complete representation of the native protein. It features an N-terminal 6xHis-tag for convenient purification and detection. The protein appears to be highly purified, with a purity exceeding 90% as confirmed by SDS-PAGE analysis, making it suitable for various research applications requiring high-quality protein.
The Nucleoprotein (NP) of the Influenza A virus plays a crucial role in the virus's life cycle, particularly in RNA genome replication and packaging. It's a vital component of the ribonucleoprotein complex and is involved in the nuclear import of viral RNA. Because of its essential function in viral replication, NP has become a significant focus in influenza research, providing insights into viral assembly and potential antiviral targets.
Potential Applications
Note: The applications listed below are based on what we know about this protein's biological functions, published research, and experience from experts in the field. However, we haven't fully tested all of these applications ourselves yet. We'd recommend running some preliminary tests first to make sure they work for your specific research goals.
1. Antibody Development and Validation Studies
This full-length recombinant influenza A nucleoprotein can serve as an immunogen for generating monoclonal or polyclonal antibodies specific to the H3N2 strain. The high purity (>90%) and N-terminal 6xHis tag make it suitable for immunization protocols and subsequent antibody characterization assays. Researchers can use this protein in ELISA-based screening to identify high-affinity antibodies and validate their specificity through Western blot analysis. The His-tag makes purification and immobilization on nickel-coated surfaces straightforward for antibody binding studies.
2. Protein-Protein Interaction Studies
The recombinant NP can be used in pull-down assays to identify and characterize cellular proteins that interact with influenza nucleoprotein during viral replication. The N-terminal His-tag allows efficient immobilization on nickel-affinity matrices for capturing potential binding partners from cell lysates. This approach may help clarify the molecular mechanisms of viral ribonucleoprotein complex assembly and host-pathogen interactions. Co-immunoprecipitation experiments using this protein can validate specific interactions identified through initial screening.
3. Structural and Biophysical Characterization
This E.coli-expressed full-length nucleoprotein provides material for detailed structural studies including X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy analysis. The high purity level should minimize contamination for biophysical techniques such as dynamic light scattering, analytical ultracentrifugation, and thermal stability assays. Researchers can investigate the protein's oligomerization states, conformational changes, and stability under various buffer conditions. The recombinant nature allows for isotopic labeling strategies if produced in minimal media for NMR studies.
4. Vaccine Research and Immunogenicity Studies
The purified nucleoprotein can be used in preclinical vaccine development studies as a potential immunogen or adjuvant component. Researchers can evaluate its immunogenicity in animal models by measuring antibody responses and cellular immune activation following immunization. The protein serves as a control antigen for comparing immune responses against different influenza strains or vaccine formulations. In vitro studies can assess its ability to stimulate dendritic cells or other antigen-presenting cells using cell culture-based assays.
