Recombinant Vaccinia virus Protein B5 (PS/HR) gets expressed in yeast and comes with an N-terminal 6xHis-tag, which makes purification and detection much easier. The protein includes amino acids 18-279, creating what appears to be a partial but still functional form. SDS-PAGE analysis shows purity levels above 85%, and this product is intended for research applications where reliable performance matters.
Protein B5 acts as a structural piece of the Vaccinia virus. It plays what seems to be a crucial role in how the virus assembles and exits cells. The protein is involved in forming the viral envelope - something that's essential for releasing mature virions. Getting a better handle on how Protein B5 functions and interacts may provide useful insights into viral life cycles 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 Studies
This recombinant vaccinia virus protein B5 fragment can work as an immunogen for creating polyclonal or monoclonal antibodies that target the B5 protein specifically. That N-terminal 6xHis tag makes purification straightforward and allows for easy immobilization during antibody screening assays. The protein quality appears sufficient for immunization protocols and follow-up antibody characterization, given its greater than 85% purity. Since it's expressed in yeast, the protein likely gets proper eukaryotic folding that may keep native epitopes intact - something that's important for antibody recognition.
2. Protein-Protein Interaction Studies
Researchers can use the His-tagged B5 protein fragment in pull-down assays to hunt for potential cellular binding partners or other viral protein interactions. The 6xHis tag allows researchers to stick the protein onto nickel-based resins, which then captures interacting proteins from cell lysates or purified protein libraries. This method could help clarify how vaccinia virus infection and replication actually work at the molecular level. The partial protein covers amino acids 18-279, retaining substantial sequence content that probably contains important interaction domains.
3. ELISA-Based Binding Assays
The recombinant B5 protein works well as a coating antigen in enzyme-linked immunosorbent assays for studying antibody binding patterns or hunting for B5-specific antibodies in serum samples. The His tag makes oriented immobilization on nickel-coated plates possible, which may improve how consistent the assays are. At 85% purity, this protein preparation should handle quantitative binding studies and dose-response analyses just fine. Basic research into vaccinia virus immunology would benefit from this application, as would vaccine development studies.
4. Biochemical Characterization Studies
This recombinant protein preparation opens the door for detailed biochemical analysis of the B5 protein fragment. Researchers can determine molecular weight, isoelectric point, and stability under different buffer conditions. The yeast expression system might provide post-translational modifications that are relevant to the native protein structure. Scientists can run SDS-PAGE analysis to confirm the protein is intact and check for degradation patterns under various storage conditions. This kind of characterization data would support additional experimental work and give baseline information for comparing with other vaccinia virus proteins.
