Recombinant Human herpesvirus 2 Tegument protein VP22 (UL49) gets produced in an E. coli expression system. The construct contains a partial protein segment spanning amino acids 170 to 300. An N-terminal 6xHis-tag has been added to make purification and detection more straightforward. SDS-PAGE analysis indicates the protein achieves over 90% purity, which appears to make it suitable for various research applications.
VP22, a tegument protein found in Human herpesvirus 2, seems to play a critical role in how the virus assembles and exits cells. The protein is involved in moving viral components around inside infected cells, which likely helps with efficient viral particle assembly. VP22 may also be significant for studying how viruses cause disease and modulate immune responses. This makes it an important target for virology research.
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 Immunoassay Research
This recombinant VP22 fragment could work as an immunogen for creating polyclonal or monoclonal antibodies that specifically recognize the HSV-2 tegument protein. The N-terminal 6xHis tag makes purification easier and allows for immobilization during antibody screening assays. Researchers might use this protein in ELISA-based experiments to characterize how well antibodies bind and their binding strength. The >90% purity appears suitable for immunization protocols and as a coating antigen in different immunoassay formats.
2. Protein-Protein Interaction Studies
The 6xHis-tagged VP22 fragment can be used in pull-down assays to find potential cellular or viral binding partners. The tag allows for efficient attachment to nickel-based affinity matrices, which can then capture interacting proteins from cell lysates or purified protein libraries. This strategy may help reveal the molecular interactions that occur during HSV-2 tegument assembly or when the virus interacts with host cells. The partial protein sequence (170-300aa) represents a specific domain that might retain important binding sites for interaction studies.
3. Biochemical Characterization and Biophysical Analysis
This recombinant protein fragment works well for detailed biochemical characterization. Studies could include molecular weight determination, amino acid composition analysis, and stability testing under different buffer conditions. Researchers can run thermal stability assays, pH tolerance experiments, and protein aggregation analyses to understand how this VP22 domain behaves physically. The high purity level supports accurate quantitative biochemical measurements and spectroscopic analyses like UV-Vis absorption and fluorescence spectroscopy.
4. Comparative Viral Protein Studies
The recombinant VP22 fragment works as a reference standard for comparing HSV-1 and HSV-2 tegument proteins. Researchers can use this protein in cross-reactivity studies to examine antigenic differences between herpesvirus strains. The defined expression region (170-300aa) allows for precise domain-specific comparisons with corresponding regions from other herpesvirus species. This application may support evolutionary studies and help identify which regions stay the same versus which ones vary within the VP22 protein family.
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