This recombinant Bovine coronavirus Non-structural protein 2a gets expressed in a baculovirus system and contains the complete protein sequence spanning amino acids 1 to 278. The protein comes with a C-terminal 6xHis-tag, which makes purification and detection more straightforward. SDS-PAGE analysis confirms the protein reaches over 85% purity, which should deliver reliable results for research work.
Non-structural protein 2a appears to be crucial for how Bovine coronavirus handles replication and transcription. The protein seems to have a significant role in the viral life cycle, positioning it as an important target for researchers trying to understand coronavirus biology. Scientists studying viral pathogenesis and exploring potential therapeutic approaches may find this protein particularly valuable.
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 Immunological Studies
This recombinant bovine coronavirus non-structural protein 2a could work as an antigen for creating specific antibodies against BCoV-ENT. The C-terminal 6xHis tag makes purification easier and helps with immobilization during immunization protocols or ELISA-based antibody screening. Research teams might develop monoclonal or polyclonal antibodies using this protein to study bovine coronavirus infections in lab settings. Since the expression covers the full-length region (1-278aa), it likely provides thorough epitope coverage for antibody recognition studies.
2. Protein-Protein Interaction Studies
Pull-down assays could benefit from this His-tagged recombinant protein to find cellular proteins that interact with bovine coronavirus non-structural protein 2a during viral replication. The His tag's metal affinity purification properties allow efficient capture of both the protein and its binding partners from cell lysates. This method may help researchers piece together the molecular mechanisms behind how this non-structural protein operates within the viral lifecycle. Co-immunoprecipitation experiments using anti-His tag antibodies can provide additional validation for any interactions discovered.
3. Biochemical Characterization and Enzymatic Assays
Research teams can examine the biochemical properties and potential enzymatic activities of bovine coronavirus non-structural protein 2a using this recombinant protein as a substrate. Scientists might conduct structural studies, stability analyses, and screen for enzymatic functions that could be linked to this viral protein. The baculovirus expression system typically produces properly folded proteins, making it well-suited for functional studies. With purity levels exceeding 85%, the protein should generate dependable results in biochemical assays while minimizing interference from contaminating proteins.
4. Viral Protein Localization and Trafficking Studies
Cell-based assays could incorporate this His-tagged protein to investigate the subcellular localization and trafficking patterns of bovine coronavirus non-structural protein 2a. Scientists might transfect cells with expression constructs or introduce the purified protein directly to observe its cellular distribution through immunofluorescence microscopy using anti-His antibodies. Such studies may reveal details about the protein's contribution to viral replication complex formation and how it interacts with cellular organelles. Using the full-length protein preserves all potential localization signals, which appears important for accurate trafficking studies.
