Recombinant Human herpesvirus 6B Protein U22 is produced through an in vitro E.coli expression system. This full-length protein spans amino acids 1-202 and includes an N-terminal 10xHis-tag that helps with purification. The protein reaches purity levels above 85%, verified through SDS-PAGE analysis. It's designed for research use only, with no tested activity or specified endotoxin level.
Protein U22 from Human herpesvirus 6B appears to play a role in the viral lifecycle, though its specific functions remain largely unclear. Scientists study this protein to better understand virus-host interactions and the possible ways the virus persists and evades immune responses. Research on U22 seems crucial for grasping the biology of Human herpesvirus 6B and how it affects human health.
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. Viral Protein Interaction Studies
This recombinant HHV-6B U22 protein can work as bait or target protein in protein-protein interaction assays to find cellular or viral binding partners. The N-terminal His-tag makes it easier to attach the protein to nickel-coated surfaces for pull-down experiments with cell lysates or purified protein libraries. These studies might help reveal the molecular mechanisms by which U22 contributes to HHV-6B disease development and host cell manipulation.
2. Antibody Development and Validation
The full-length recombinant U22 protein offers an ideal antigen for creating monoclonal or polyclonal antibodies specific to HHV-6B U22. Researchers can use the purified protein for immunization protocols and antibody screening via ELISA using the His-tag for capture. They can then validate antibody specificity. These antibodies would likely become valuable research tools for studying U22 expression, where it localizes in cells, and how it functions in infected cells.
3. Structural and Biochemical Characterization
This recombinant protein allows for detailed biochemical analysis of U22 properties. This includes confirming molecular weight, assessing protein folding, and studying stability under different conditions. The high purity level makes it suitable for biophysical techniques such as circular dichroism spectroscopy, dynamic light scattering, or analytical ultracentrifugation. These methods can characterize the protein's secondary structure and oligomerization state.
4. Enzyme-Linked Immunosorbent Assays (ELISA)
The His-tagged U22 protein can serve as a capture antigen in research-grade ELISA platforms to detect and measure anti-U22 antibodies in experimental samples. The tag enables oriented attachment to nickel-coated plates, which may improve assay sensitivity and reproducibility. This application would be particularly useful for studying immune responses to HHV-6B infection in research models or characterizing antibody responses in laboratory studies.
