This recombinant avian infectious bronchitis virus nucleoprotein (N) is produced in an E. coli expression system and spans the full length of the protein, from amino acids 1 to 409. It features a C-terminal 6xHis-tag for easy purification and detection. The protein achieves a purity greater than 85% as verified by SDS-PAGE, ensuring reliable results for research applications.
The nucleoprotein (N) of the avian infectious bronchitis virus appears to play a crucial role in the virus's replication and assembly processes. It's a structural protein that binds to the viral RNA, forming the ribonucleoprotein complex. This protein seems integral to the study of viral pathogenesis and immune responses, making it an important focus in virology research.
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. Antigen for IBV-specific Antibody Development
This full-length recombinant IBV nucleoprotein can serve as an immunogen for generating polyclonal or monoclonal antibodies specific to avian infectious bronchitis virus. The C-terminal 6xHis tag makes purification and immobilization easier for immunization protocols and subsequent antibody screening assays. While the >85% purity level should be sufficient for antibody production, researchers may want to consider additional purification steps to minimize cross-reactive antibodies against E. coli contaminants. These antibodies could prove valuable as research tools for IBV detection and characterization studies.
2. Protein-Protein Interaction Studies Using His-Tag Affinity
The C-terminal 6xHis tag enables nickel-affinity based pull-down assays to identify potential cellular or viral protein partners that interact with IBV nucleoprotein. Scientists can immobilize the recombinant protein on nickel-coated surfaces or beads and incubate it with cell lysates or purified protein libraries to capture interacting partners. This approach is particularly useful for studying the role of nucleoprotein in viral replication complexes or host-pathogen interactions. The full-length nature of the protein (1-409aa) ensures that all potential interaction domains are preserved.
3. Biochemical Characterization and Functional Assays
This recombinant nucleoprotein can be used for in vitro biochemical studies to characterize its basic properties such as oligomerization state, RNA-binding capacity, and thermal stability. Expressing the protein in E. coli and subsequent purification via the His-tag provides sufficient material for spectroscopic analyses, gel filtration chromatography, and other biophysical techniques. Researchers can investigate the protein's behavior under different buffer conditions, pH ranges, and salt concentrations to understand its biochemical properties relevant to viral replication.
4. ELISA-Based Research Assays
The His-tagged IBV nucleoprotein can be used in enzyme-linked immunosorbent assays for research applications, including antibody characterization, epitope mapping studies, and comparative immunogenicity assessments. The protein can be directly coated onto ELISA plates or captured via anti-His antibodies for more oriented presentation. The >85% purity appears adequate for these applications, and the full-length protein ensures representation of all potential antigenic epitopes present in the native viral nucleoprotein.
