Recombinant Severe acute respiratory syndrome coronavirus 2 Envelope small membrane protein & Membrane protein (E & M) is expressed in E. coli with an N-terminal 6xHis-SUMO tag. This partial protein covers the expression region from 1-42 amino acids and achieves a purity level of over 90% as verified by SDS-PAGE. This product is intended for research use only and does not contain endotoxin levels suitable for clinical applications.
The Envelope (E) and Membrane (M) proteins of Severe acute respiratory syndrome coronavirus 2 appear to play crucial roles in the virus's structure and life cycle. The E protein seems to be involved in virus assembly and release, while the M protein is likely integral to maintaining the virus's shape and size. Both proteins may prove essential for studying viral pathogenesis and developing potential 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 Screening
This recombinant SARS-CoV-2 E&M protein fragment can serve as an immunogen or screening antigen for developing antibodies targeting the envelope and membrane proteins. The N-terminal 6xHis-SUMO tag makes purification and immobilization straightforward for ELISA-based antibody screening assays. The high purity (>90%) suggests reliable and reproducible results in antibody binding studies are achievable. This application could be particularly valuable for generating research tools to study coronavirus envelope and membrane protein interactions.
2. Protein-Protein Interaction Studies
The His-SUMO tagged protein can be used in pull-down assays to identify and characterize protein interactions involving the E and M protein domains. The His tag allows efficient immobilization on nickel-based resins for affinity purification experiments. Researchers might investigate how this partial protein fragment interacts with host cell proteins or other viral components in controlled in vitro conditions. The SUMO tag may also help with proper protein folding and solubility during interaction studies, though this remains to be validated experimentally.
3. Structural and Biochemical Characterization
This purified protein fragment provides material for biophysical and structural studies of the SARS-CoV-2 envelope and membrane protein regions. The high purity level suggests it could work well for techniques such as circular dichroism spectroscopy, dynamic light scattering, or NMR analysis to understand the protein's conformational properties. The defined expression region (1-42aa) allows for focused analysis of this specific domain's structural characteristics. Such studies might contribute to understanding the molecular basis of coronavirus envelope protein function.
4. ELISA-Based Binding Assays
The dual tag system (His-SUMO) enables versatile immobilization strategies for developing ELISA-based research assays. The protein can be used to study binding interactions with potential research compounds, other viral proteins, or cellular receptors in a controlled plate-based format. The high purity appears to ensure consistent coating and reliable quantitative measurements in binding studies. This application supports screening efforts for research tools targeting coronavirus envelope and membrane proteins.
