The Recombinant Bovine coronavirus Spike glycoprotein (S) is produced using a mammalian cell expression system, ensuring proper folding and post-translational modifications. This protein represents a partial sequence from amino acids 314 to 634 and includes a C-terminal 6xHis-tag for simplified purification and detection. The purity level exceeds 85%, as confirmed by SDS-PAGE, which makes it suitable for various research applications.
Bovine coronavirus relies heavily on its Spike glycoprotein (S) to infect host cells. This protein mediates attachment to host cell receptors, playing what appears to be a pivotal role in viral entry and the overall viral life cycle. Research into the structure and function of this protein may be essential for understanding viral pathogenesis and developing therapeutic interventions.
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 recombinant bovine coronavirus spike protein fragment (aa 314-634) can serve as an immunogen for generating polyclonal or monoclonal antibodies specific to this region of the spike protein. The C-terminal 6xHis tag makes purification and immobilization straightforward for antibody screening assays. Researchers might use this protein in ELISA-based screening to identify and characterize antibodies that recognize conformational or linear epitopes within this specific domain. The mammalian expression system likely helps preserve native-like glycosylation patterns, though whether these patterns are critical for antibody recognition remains to be fully determined.
2. Protein-Protein Interaction Studies
The 6xHis tag allows for pull-down assays to investigate potential binding partners or host cell receptors that interact with this specific region of the bovine coronavirus spike protein. Scientists can immobilize the protein on nickel-affinity matrices and incubate with cell lysates or purified proteins to identify interacting molecules. This approach could help reveal the molecular mechanisms underlying viral attachment or entry processes, though the complexity of these interactions may require additional validation methods.
3. Structural and Biochemical Characterization
This purified spike protein fragment proves useful for biophysical studies including circular dichroism spectroscopy, dynamic light scattering, or analytical ultracentrifugation to characterize its folding, stability, and oligomerization properties. The defined amino acid boundaries (314-634) make it well-suited for domain-specific structural analysis. Researchers can also perform glycosylation analysis or limited proteolysis experiments to understand post-translational modifications and protein architecture within this region, though interpreting results from a truncated protein fragment requires some caution.
4. Comparative Coronavirus Research
This bovine coronavirus spike protein fragment can serve as a reference protein for comparative studies with spike proteins from other coronaviruses, including cross-reactivity assays with existing antibodies or sera. The protein works well in competitive binding assays or Western blot analysis to study evolutionary relationships and antigenic similarities between different coronavirus species. Such studies might contribute to understanding coronavirus diversity and cross-species transmission mechanisms, though the relevance of findings from this specific fragment to full-length proteins may need careful consideration.
