This Recombinant Bovine coronavirus Protein I (N) is expressed in E. coli and includes the full-length sequence from amino acids 1 to 207. The protein carries a C-terminal 6xHis-tag, which helps with purification and detection. SDS-PAGE analysis shows the protein reaches a purity level greater than 85%, making it suitable for various research applications. This product is for research use only—not for diagnostic or therapeutic purposes.
Protein I (N) of Bovine coronavirus (BCoV) appears to play a central role in the viral life cycle. The protein is primarily involved in viral replication and assembly processes. As the nucleocapsid protein, it's essential for packaging the viral RNA genome and likely contributes to maintaining the virus's structural integrity. Studying this protein may be crucial for understanding coronavirus biology and could help in developing antiviral strategies.
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 recombinant bovine coronavirus nucleocapsid protein can work as an immunogen for creating polyclonal or monoclonal antibodies specific to BCoV. The C-terminal 6xHis tag makes purification and immobilization easier for antibody screening assays. Since the full-length expression region (1-207aa) is present, antibodies produced should recognize native epitopes found in the complete nucleocapsid protein. These antibodies might prove valuable as research tools for studying BCoV infection mechanisms and tracking viral protein localization.
2. Protein-Protein Interaction Studies
The His-tagged nucleocapsid protein works well in pull-down assays to identify host cell proteins that interact with the BCoV nucleocapsid during infection. The 6xHis tag allows efficient immobilization on nickel-based affinity matrices for capturing potential binding partners from cell lysates. Studies like these could reveal cellular pathways involved in viral replication, assembly, or how host cells respond to BCoV infection.
3. ELISA-Based Detection Assays
The recombinant protein can function as a coating antigen or standard in enzyme-linked immunosorbent assays for research applications. The His tag allows for oriented immobilization on nickel-coated plates, which may improve assay consistency. Researchers could use this protein to develop assays for measuring anti-BCoV antibody responses in experimental animal studies or for quantifying viral protein levels in infected cell culture systems.
4. Structural and Biochemical Characterization
The purified nucleocapsid protein can undergo biophysical analyses to examine its structural properties. These might include circular dichroism spectroscopy, dynamic light scattering, or analytical ultracentrifugation. The high purity (>85%) and His tag make these analyses more straightforward by allowing consistent protein preparation and concentration determination. Such studies could provide insights into the protein's folding, oligomerization state, and stability under different buffer conditions.
