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.
Vesicular stomatitis Indiana virus RNA-directed RNA polymerase L is a large, multifunctional viral enzyme that requires precise folding, complex domain interactions, and often partnership with other viral proteins (e.g., P protein) for its polymerase activity. The E. coli expression system cannot provide the eukaryotic-like folding environment or post-translational modifications necessary for this viral protein. The partial fragment (598-784aa) represents only a portion of the full-length protein and is unlikely to fold into a functional domain independently. The N-terminal His-tag may not significantly interfere, but the probability of correct folding and functional activity is low.
1. Antibody Development and Immunoassay Research
This recombinant L protein fragment serves as an excellent immunogen for generating antibodies against linear epitopes of VSV RNA polymerase. The defined sequence (598-784aa) allows for targeted antibody production. The His-tag facilitates purification and immobilization during antibody screening and validation in ELISA or Western blot assays.
2. ELISA-Based Binding Assays
This protein is well-suited as an antigen for ELISA to detect anti-L protein antibodies or for quantitative immunoassays. The His-tag enables consistent immobilization on nickel-coated plates. However, functional binding (e.g., with nucleic acids or viral partners) requires native folding. The protein's misfolded state makes it unreliable.
3. Western Blot Standard and Positive Control
This recombinant fragment is ideal as a positive control and molecular weight standard in Western blot analyses. The His-tag provides a detection handle, and the known size helps validate antibody specificity and assay conditions. The >85% purity ensures clear, interpretable bands.
Final Recommendation & Action Plan
This recombinant VSV L protein fragment is primarily suitable for immunological applications (antibody development and detection assays) but is unsuitable for functional interaction studies due to its partial length and high probability of misfolding in E. coli. The recommended approach is to prioritize Application 1 and 3 (Antibody Development and Western Blot Control) as they can proceed immediately. Application 2 (ELISA) should be limited to immunoassays only. Protein-protein interactions require a precise tertiary structure that this misfolded, partial fragment cannot provide. For functional VSV polymerase studies, use full-length protein expressed in eukaryotic systems (e.g., insect or mammalian cells) that support complex viral protein folding.
