This recombinant Vesicular stomatitis Indiana virus RNA-directed RNA polymerase L (L) comes from expression in E. coli and includes an N-terminal 6xHis-tag that makes purification and detection more straightforward. The protein covers a partial region—amino acids 598 to 784—and shows purity above 85% when checked by SDS-PAGE analysis. This product is meant for research use only and comes without any guaranteed biological activity.
The RNA-directed RNA polymerase L of Vesicular stomatitis Indiana virus plays a central role in how the virus replicates and transcribes its genetic material. This protein acts as a key piece of the viral polymerase complex, handling the synthesis of viral RNA from RNA templates. Because of this critical function, it has become an important target for researchers studying how viruses replicate and for those looking into potential antiviral approaches. Learning more about how it works and what it interacts with could advance virology research in meaningful ways.
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 L protein fragment (598-784aa) can work as an immunogen for creating polyclonal or monoclonal antibodies that specifically target the vesicular stomatitis virus RNA polymerase L protein. The N-terminal 6xHis tag makes purification simpler and allows for immobilization during antibody screening assays. These antibodies might prove valuable as research tools—they could help detect VSV L protein in infected cell lysates or assist in studying how viral replication unfolds over time. This partial protein fragment may contain epitopes that are both accessible and likely to trigger immune responses for antibody production.
2. Protein-Protein Interaction Studies
Researchers can use the His-tagged L protein fragment in pull-down assays to find cellular or viral proteins that interact with this particular region of the VSV RNA polymerase. The 6xHis tag allows for attachment to nickel-affinity resins, which then capture potential binding partners from cell lysates or purified protein libraries. This method could help reveal the molecular mechanisms behind VSV replication and identify host factors that participate in viral RNA synthesis. The 598-784aa region appears to contain important protein interaction domains that deserve closer investigation.
3. ELISA-Based Binding Assays
The recombinant protein works well in enzyme-linked immunosorbent assays for studying binding interactions with other viral proteins, host factors, or small molecules. The His tag enables oriented attachment to nickel-coated plates, which ensures the protein presents consistently for binding studies. This application suits researchers screening compound libraries or characterizing how quickly known interacting partners bind and release. The purified protein fragment provides a standardized reagent for making quantitative binding measurements.
4. Western Blot Standard and Positive Control
This recombinant L protein fragment functions as both a positive control and molecular weight standard for Western blot analyses when investigating VSV infection or L protein expression. The known protein sequence and His tag offer reliable markers for confirming antibody specificity and fine-tuning detection conditions. Scientists studying VSV replication can use this protein to verify the presence and size of L protein fragments in their experimental samples. The >85% purity should be sufficient for producing clear, easy-to-interpret bands in immunoblotting work.
