Recombinant Influenza A virus Nucleoprotein (NP) is expressed in E. coli and spans the full length of the protein, covering amino acids 1 to 498. The protein carries an N-terminal 6xHis-SUMO tag to aid purification and improve solubility. SDS-PAGE analysis confirms a purity level greater than 90%, which appears suitable for various research applications. This product is designated for research use only.
The nucleoprotein (NP) of the Influenza A virus represents a critical component in the viral replication cycle. It wraps around the viral RNA genome and plays a vital role in assembling ribonucleoprotein complexes. This protein is essential for transcription, replication, and packaging of viral RNA—making it a key target for influenza research and antiviral strategies. Understanding NP functions may help scientists study viral pathogenesis and immune responses.
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 Characterization
This full-length recombinant influenza A nucleoprotein can serve as an immunogen for generating monoclonal or polyclonal antibodies specific to the H3N2 strain. The N-terminal 6xHis-SUMO tag aids purification and immobilization for antibody screening assays. The >90% purity level appears sufficient for immunization protocols and subsequent antibody validation experiments. These antibodies could potentially be used in research applications such as Western blotting, immunofluorescence, or flow cytometry studies of influenza-infected cells.
2. Protein-Protein Interaction Studies
The 6xHis-SUMO tag enables pull-down assays to identify cellular proteins that interact with influenza A nucleoprotein during viral replication. This tag allows for efficient immobilization on nickel-affinity resins, which may help with co-immunoprecipitation experiments using cell lysates or purified protein libraries. Such approaches could help elucidate the molecular mechanisms of viral ribonucleoprotein complex assembly and host-pathogen interactions. The full-length protein ensures that all potential interaction domains are preserved for comprehensive binding studies.
3. ELISA-Based Binding Assays
The tagged recombinant nucleoprotein can be used to develop enzyme-linked immunosorbent assays for research purposes, with the 6xHis tag providing oriented immobilization on nickel-coated plates. This setup enables screening of antibody libraries, testing cross-reactivity with other influenza strains, or evaluating binding kinetics of potential research compounds. The >90% purity level provides sufficient quality for quantitative binding measurements and likely reduces background interference in immunoassays.
4. Biochemical Characterization Studies
This recombinant nucleoprotein can be used for in vitro biochemical analyses including thermal stability studies, pH tolerance assays, and buffer optimization experiments. The SUMO tag may be removed by SUMO protease treatment if native protein properties need to be studied. Researchers can investigate the protein's oligomerization behavior and RNA-binding properties through gel shift assays. Studies of susceptibility to various proteases are also possible. These investigations provide fundamental insights into nucleoprotein structure-function relationships and viral replication mechanisms.
