Code | CSB-YP3324GMY2 |
Abbreviation | Recombinant SARS-CoV-2 S protein, partial |
MSDS | |
Size | $250 |
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The Recombinant Severe acute respiratory syndrome coronavirus 2 Spike glycoprotein (S) is expressed in a yeast system, covering the amino acid region 16-318. It features an N-terminal 6xHis-PDI tag for enhanced purification and detection. The protein is provided at a purity level greater than 90%, as confirmed by SDS-PAGE analysis, ensuring reliable results in research applications.
SARS-CoV-2's Spike glycoprotein (S) appears to be essential for viral entry into host cells, mediating attachment and fusion processes. It likely plays a critical role in the viral life cycle and has become a major target for vaccine development and therapeutic interventions. Understanding its structure and function may be crucial for advancing research on coronavirus pathogenesis and potential treatments.
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 Screening
This recombinant SARS-CoV-2 spike protein fragment (amino acids 16-318) can serve as an antigen for generating monoclonal or polyclonal antibodies targeting the N-terminal domain region of the spike protein. The N-terminal 6xHis-PDI tag makes purification and immobilization easier for immunization protocols and subsequent antibody screening assays. ELISA-based screening with this protein could help researchers identify antibodies with specific binding properties to this particular spike region. The high purity (>90%) suggests consistent immunogenic presentation for reliable antibody production, though some variability in immune responses might still occur.
2. Protein-Protein Interaction Studies
Pull-down assays become possible with the 6xHis-PDI tag, allowing investigation of potential binding partners or host cell receptors that interact with this specific region of the SARS-CoV-2 spike protein. Researchers can immobilize the tagged protein on nickel-affinity matrices and incubate with cell lysates or purified proteins to identify interacting molecules. This approach seems particularly valuable for studying early binding events or conformational changes in the N-terminal region of the spike protein. The yeast expression system provides eukaryotic post-translational modifications that may be relevant for authentic protein interactions, though it's worth noting that yeast modifications don't always mirror human cellular processing.
3. Structural and Biochemical Characterization
Detailed structural studies including X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy may help researchers understand the three-dimensional organization of amino acids 16-318 of the spike protein. The high purity level makes it suitable for biophysical analyses such as dynamic light scattering, circular dichroism spectroscopy, and thermal stability assays. Folding properties, stability parameters, and conformational dynamics of this specific spike protein region can be investigated. The defined expression region allows for focused structural analysis of this particular domain without interference from other spike protein regions, though interpreting results from isolated fragments requires careful consideration of how they might behave differently than in the full-length protein.
4. ELISA-Based Binding Assays
Direct coating or capture-based ELISA formats for quantitative binding studies with various ligands, small molecules, or other proteins become straightforward with the N-terminal tag. Researchers can develop standardized assays to measure binding kinetics, affinity constants, and specificity of interactions involving this spike protein region. Sandwich ELISA configurations are also possible where the protein can be captured via anti-His antibodies while maintaining proper orientation for binding partner access. This application appears particularly useful for screening compound libraries or characterizing the binding properties of this specific spike protein fragment, though researchers should consider that results may not always translate directly to full-length protein behavior.
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