The Recombinant Lassa virus Pre-glycoprotein polyprotein GP complex (GPC) is produced using an in vitro E.coli expression system, covering the amino acid region 259-490. This partial protein is N-terminally tagged with 10xHis, which appears to make purification and detection more straightforward. The product achieves a purity level greater than 85% as determined by SDS-PAGE, ensuring reliable use in research applications. This product is intended for research use only.
The Lassa virus Pre-glycoprotein polyprotein GP complex (GPC) seems to play a crucial role in the viral life cycle. It's involved in the maturation and function of the viral envelope glycoproteins - proteins that are essential for virus entry into host cells. This makes the GPC a potentially important target for understanding viral pathogenesis and investigating therapeutic interventions.
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 Epitope Mapping Studies
This recombinant GPC fragment (259-490aa) may work well as an immunogen for generating monoclonal or polyclonal antibodies against Lassa virus glycoprotein complex. The N-terminal 10xHis tag allows for purification and immobilization when screening hybridoma supernatants or serum samples. Researchers might use this protein fragment to map linear epitopes within the 259-490 amino acid region of the glycoprotein complex. The high purity (>85%) suggests minimal cross-reactivity is likely during antibody characterization studies.
2. Protein-Protein Interaction Studies
The His-tagged GPC fragment can be used in pull-down assays to identify host cell proteins that interact with this specific region of the Lassa virus glycoprotein complex. The 10xHis tag makes immobilization on nickel-affinity matrices possible, potentially capturing binding partners from cell lysates. This application could help reveal molecular mechanisms of viral entry or host cell responses, though results would need careful validation. Co-immunoprecipitation experiments using anti-His antibodies might further confirm identified interactions.
3. ELISA-Based Binding Assays
The recombinant protein can be coated onto ELISA plates to develop binding assays for studying interactions with potential receptor proteins or other viral components. The His tag may help with oriented immobilization using anti-His antibodies or nickel-coated plates, which should provide more consistent protein presentation. Researchers could use this system to screen compound libraries for molecules that disrupt protein interactions or to characterize binding kinetics with known partners. The defined amino acid region (259-490) allows for structure-activity relationship studies within this specific domain.
4. Biochemical Characterization and Structural Studies
This purified GPC fragment appears suitable for biochemical analyses including mass spectrometry, circular dichroism spectroscopy, and limited proteolysis studies. The high purity level should enable accurate determination of protein stability, folding characteristics, and post-translational modifications within the 259-490 amino acid region. Researchers can perform thermal stability assays and analyze secondary structure content of this specific glycoprotein domain. The His tag provides a convenient anchor point for protein immobilization during various analytical procedures.
