Recombinant Variola virus A27L protein gets expressed in a mammalian cell system, which helps ensure proper folding and post-translational modifications. The protein covers the full length—amino acids 1 to 194—and includes an N-terminal 6xHis-Myc tag to make purification and detection simpler. SDS-PAGE analysis shows purity levels above 85%, suggesting this product should work well for different research applications.
A27L appears to be a structural component of the Variola virus. Research indicates it plays a role in mediating viral entry and cell-to-cell transmission. The protein seems to interact with other viral proteins to help with virus assembly and egress. Given its apparently critical function in the viral life cycle, A27L has become an important target for studies looking into viral pathogenesis and antiviral strategy development.
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 A27L protein may serve as an immunogen for creating polyclonal or monoclonal antibodies specific to the variola virus A27L protein. The mammalian expression system likely preserves native epitopes through proper protein folding and post-translational modifications. That N-terminal His-Myc tag makes purification and detection more straightforward during antibody screening. These antibodies could prove valuable as research tools for studying poxvirus biology and developing detection methods for variola virus research in authorized laboratories.
2. Protein-Protein Interaction Studies
Researchers can use the His-tagged A27L protein in pull-down assays to identify potential cellular or viral binding partners. The His tag allows immobilization on nickel-affinity matrices, which helps capture interacting proteins from cell lysates or purified protein libraries. That 85% purity level appears sufficient for interaction studies. The mammalian expression system likely helps maintain native protein conformation—something that's necessary for physiologically relevant binding interactions. Such studies might provide insights into the molecular mechanisms behind variola virus pathogenesis and host-pathogen interactions.
3. ELISA-Based Binding Assays
The dual His-Myc tagging system makes this protein well-suited for sandwich ELISA formats or direct binding assays. Scientists can immobilize the protein via the His tag or detect it using anti-Myc antibodies, which provides flexibility in assay design. The mammalian expression system and adequate purity level should support reliable and reproducible binding measurements. These assays could help screen for small molecule inhibitors, study protein stability under various conditions, or investigate binding kinetics with potential interaction partners.
4. Biochemical Characterization Studies
This recombinant A27L protein works well for basic biochemical analyses—thermal stability studies, pH tolerance assays, and buffer optimization experiments. The protein's purity level of greater than 85% appears adequate for spectroscopic analyses like circular dichroism to study secondary structure or dynamic light scattering for oligomerization studies. The mammalian expression system likely provides a more native-like protein compared to bacterial systems. This makes it valuable for understanding the biophysical properties of the A27L protein under various experimental conditions.
