Recombinant Human herpesvirus 6A Envelope glycoprotein B (gB) gets produced in an E. coli expression system and spans amino acids 23-188. The partial protein carries an N-terminal 10xHis-tag plus a C-terminal Myc-tag, which helps with purification and detection. SDS-PAGE analysis confirms purity levels above 85%, suggesting reliable performance in experimental work.
Envelope glycoprotein B (gB) from Human herpesvirus 6A appears to play a crucial role in how the virus infects host cells. It mainly contributes to viral entry by promoting membrane fusion. This protein sits within the viral envelope and represents a key target for researchers trying to understand viral pathogenesis and immune response interactions. That makes it potentially valuable for virology studies.
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 HHV-6A gB fragment (aa 23-188) could work as an immunogen or screening antigen when developing monoclonal or polyclonal antibodies against HHV-6A envelope glycoprotein B. The dual His and Myc tags allow for purification and detection across different immunoassay formats. Scientists might use this protein to create antibodies for studying HHV-6A infection mechanisms or viral entry processes. It could also help develop research tools for detecting HHV-6A in lab settings. The partial gB sequence may harbor important epitopes that are relevant for antibody binding studies.
2. Protein-Protein Interaction Studies
Both the N-terminal His tag and C-terminal Myc tag make this protein suitable for pull-down assays aimed at identifying cellular proteins that interact with HHV-6A glycoprotein B. Scientists can attach the protein to nickel-affinity resins or anti-Myc antibody-coated surfaces to capture potential binding partners from cell lysates. These interaction studies might offer insights into HHV-6A entry mechanisms and help identify host cell receptors. The expressed region (aa 23-188) could contain functionally important domains involved in protein-protein interactions.
3. ELISA-Based Binding Assays
The dual-tagged recombinant gB protein appears useful in enzyme-linked immunosorbent assays for studying binding interactions with potential cellular receptors or other viral proteins. His and Myc tags make protein capture and detection straightforward in plate-based assay formats. Scientists can explore binding kinetics, specificity, and competitive binding using this protein as either a capture antigen or detection reagent. Such assays may contribute to understanding HHV-6A tropism and entry mechanisms at the molecular level.
4. Structural and Biochemical Characterization
This recombinant gB fragment works well for biophysical studies aimed at characterizing the structural properties of the HHV-6A envelope glycoprotein B N-terminal region. High purity (>85%) makes it suitable for techniques like circular dichroism spectroscopy, dynamic light scattering, or analytical ultracentrifugation to assess protein folding and oligomerization states. The defined expression region (aa 23-188) allows focused analysis of this specific domain's biochemical properties. These studies could provide fundamental insights into gB structure-function relationships.
