This recombinant Avian infectious bronchitis virus Nucleoprotein (N) gets expressed in mammalian cells and contains the complete 409 amino acid sequence. The protein comes with a C-terminal 6xHis-tag that makes purification and detection much simpler. SDS-PAGE analysis confirms the purity exceeds 85%, which appears suitable for most research applications. This product is for research use only.
The Avian infectious bronchitis virus Nucleoprotein seems to play a central role in the viral life cycle. It's primarily involved in RNA binding and genome packaging - processes that are likely essential for forming the viral ribonucleoprotein complex. This complex represents a key component in viral replication and assembly. Researchers studying viral replication mechanisms or developing strategies against infectious bronchitis virus infections may find understanding this protein's function particularly important.
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
This full-length recombinant IBV nucleoprotein could work as an immunogen for creating polyclonal or monoclonal antibodies that target IBV specifically. The C-terminal 6xHis tag makes purification straightforward and helps with immobilization during antibody screening assays. Since it's expressed in mammalian cells, the protein probably maintains proper folding and post-translational modifications. These modifications might be critical for preserving native epitopes. Researchers could then validate the antibodies they generate using this same recombinant protein in ELISA, Western blot, and immunoprecipitation assays.
2. Protein-Protein Interaction Studies
Coronavirus nucleoproteins typically interact with viral RNA and other viral proteins during replication and assembly. This recombinant protein works well in pull-down assays - the C-terminal His tag allows for immobilization on metal affinity resins to identify binding partners. Co-immunoprecipitation experiments and yeast two-hybrid screens could also take advantage of this protein to map interaction networks. Studies like these would likely contribute to our understanding of IBV replication mechanisms and may help identify potential antiviral targets.
3. Structural and Biochemical Characterization
Having the full-length recombinant nucleoprotein provides material for detailed structural studies. This includes X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy. Biochemical assays can examine protein stability, oligomerization states, and how the protein changes shape under different conditions. The His tag makes protein purification easier for these analyses, while the mammalian expression system helps ensure the folding resembles what happens naturally. These studies would advance our basic understanding of how IBV nucleoprotein structure relates to function.
4. Enzyme-Linked Immunosorbent Assays (ELISA) Development
This recombinant protein could work as a coating antigen for developing research-grade ELISA systems that detect IBV-specific antibodies in experimental samples. The high purity (>85%) and His tag allow for consistent immobilization and measurement on ELISA plates. Such assays would be valuable for monitoring immune responses in vaccination studies, tracking viral exposure in research flocks, or screening hybridoma supernatants during antibody development projects.
5. RNA-Binding Studies
Coronavirus nucleoproteins are known to bind viral RNA and appear crucial for genome packaging and replication. This recombinant IBV nucleoprotein can be used in electrophoretic mobility shift assays (EMSA) or filter binding assays to characterize RNA-binding specificity and affinity. The protein could also work in RNA immunoprecipitation experiments - using the His tag for capture helps identify preferred binding sequences or secondary structures in IBV genomic or subgenomic RNAs.
