Recombinant Avian infectious bronchitis virus Non-structural protein 3b (3b) is produced in yeast, covering the full-length expression region from 1 to 64 amino acids. The protein carries a C-terminal 6xHis-tag, which helps with purification and detection. SDS-PAGE analysis shows it achieves a purity level exceeding 90%, which should ensure high-quality results for research applications. This product is intended strictly for research use and not for clinical applications.
Non-structural protein 3b from the Avian infectious bronchitis virus appears to play a role in the virus's replication and assembly processes. As part of the viral machinery, it may be crucial for understanding the lifecycle and pathogenicity of IBV. Research on this protein could provide insights into viral replication mechanisms, potentially offering valuable information for virology research and 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 IBV non-structural protein 3b can work as an immunogen for generating polyclonal or monoclonal antibodies specific to this viral protein. The C-terminal 6xHis tag makes purification and immobilization easier for antibody screening assays. Researchers might use this protein in ELISA-based assays to characterize antibody specificity, affinity, and cross-reactivity. The high purity (>90%) should minimize contamination that could interfere with antibody development protocols.
2. Protein-Protein Interaction Studies
The 6xHis-tagged protein works well in pull-down assays to identify potential cellular or viral protein partners that interact with IBV non-structural protein 3b. The tag allows efficient immobilization on nickel-affinity matrices for capturing interacting proteins from cell lysates or viral protein preparations. This approach may help reveal the functional networks involving this non-structural protein during viral replication or host cell interaction studies.
3. Biochemical Characterization and Structural Studies
This purified recombinant protein provides material for basic biochemical analyses including molecular weight confirmation, protein stability studies, and preliminary structural characterization. Researchers can perform techniques such as dynamic light scattering, circular dichroism spectroscopy, or analytical ultracentrifugation to understand the protein's biophysical properties. The yeast expression system might provide proper protein folding for meaningful structural investigations, though results can vary.
4. Viral Protein Detection Assay Development
The recombinant protein works as a positive control and standard in research assays designed to detect IBV non-structural protein 3b in experimental samples. The defined concentration and high purity make it suitable for establishing detection limits and validating assay performance in research applications. This standardized protein preparation enables consistent results across different laboratory experiments studying IBV infection or replication.
