Recombinant Rabies virus Glycoprotein (G) is expressed in E. coli, covering the amino acid region 20-459. The protein carries an N-terminal 6xHis-SUMO tag, which helps with purification and detection. It appears to reach a purity level of over 90%, as confirmed by SDS-PAGE analysis. This product is intended for research use only, potentially providing reliable results for scientific investigations involving the Rabies virus.
Rabies virus Glycoprotein (G) represents a critical component of the viral envelope. It plays a vital role in virus attachment and entry into host cells. The protein seems essential for inducing virus-neutralizing antibodies, which makes it a key target in vaccine research and development. Its involvement in host-pathogen interactions and immune response modulation may underscore its significance in 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 rabies virus glycoprotein fragment can serve as an immunogen for generating monoclonal or polyclonal antibodies against rabies virus G protein. The N-terminal His-SUMO tag helps with purification and immobilization for immunization protocols and subsequent antibody screening assays. Researchers might use this protein in ELISA-based screening to identify antibodies with specific binding properties to the G protein region spanning amino acids 20-459. The high purity (>90%) likely ensures minimal contamination that could interfere with immune responses or antibody specificity.
2. Protein-Protein Interaction Studies
Pull-down assays using this His-SUMO tagged recombinant G protein could help identify cellular proteins that interact with rabies virus glycoprotein. The His tag allows immobilization on nickel-based affinity matrices, while the expressed region (20-459aa) appears to contain potential binding domains for host cell receptors or other viral proteins. This approach may prove valuable for mapping the rabies virus interactome and understanding molecular mechanisms of viral entry and pathogenesis at the protein level.
3. Structural and Biochemical Analysis
This recombinant protein fragment provides material for biophysical characterization studies. These might include circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation. Specific proteases can remove the SUMO tag if native protein structure analysis is required. Researchers could investigate the folding properties, stability, and conformational changes of this glycoprotein region under various buffer conditions and temperatures.
4. Vaccine Research and Immunogenicity Studies
Preclinical vaccine development studies might benefit from using this recombinant G protein fragment to evaluate immune responses in animal models. The protein could serve as a subunit vaccine candidate or as a control antigen in comparative immunogenicity studies. Researchers may assess antibody titers, cellular immune responses, and protective efficacy using this well-defined protein fragment with known purity and composition.
5. Diagnostic Assay Development
This recombinant protein appears suitable as a capture or detection antigen in developing research-grade immunoassays for rabies virus detection. The His tag allows oriented immobilization on assay surfaces, which could potentially improve binding efficiency and assay sensitivity. The protein might serve as a positive control or standard in ELISA, Western blot, or other immunoassay formats used in research laboratories studying rabies virus.
