This recombinant Human coronavirus NL63 Membrane protein (M) is produced through an in vitro E.coli expression system, yielding a full-length protein of 226 amino acids. The protein carries an N-terminal 10xHis tag, which helps with purification and detection processes. SDS-PAGE analysis confirms a purity exceeding 85%, making it well-suited for various research applications in viral protein studies.
The Membrane protein (M) of Human coronavirus NL63 appears to be a crucial component of the viral envelope. It likely plays a fundamental role in virus assembly and morphogenesis. As an integral membrane protein, it interacts with other structural proteins and contributes to viral particle formation. Understanding the M protein's structure and function may be essential for advancing coronavirus biology research and developing therapeutic strategies.
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 HCoV-NL63 membrane protein could serve as an immunogen for generating polyclonal or monoclonal antibodies specific to the viral M protein. The N-terminal His-tag streamlines purification and immobilization for immunization protocols and subsequent antibody screening assays. Researchers might use this protein in ELISA-based assays to characterize antibody binding specificity and affinity. The complete protein sequence (1-226aa) offers comprehensive epitope coverage for antibody development targeting various regions of the M protein.
2. Protein-Protein Interaction Studies
The His-tagged M protein can be applied in pull-down assays to identify and characterize potential cellular or viral protein binding partners. The tag allows efficient immobilization on nickel-affinity matrices for capturing interacting proteins from cell lysates or purified protein libraries. This approach may help reveal the molecular mechanisms behind HCoV-NL63 membrane protein function and its role in viral assembly or host cell interactions. The 85% purity level appears sufficient for these interaction studies while reducing interference from contaminating proteins.
3. Biochemical Characterization and Stability Studies
This recombinant protein can be applied for comprehensive biochemical analysis, including molecular weight determination, thermal stability profiling, and chemical cross-linking studies. Researchers might investigate the protein's behavior under different buffer conditions, pH ranges, and temperature gradients to understand its biophysical properties. The His-tag streamlines consistent purification for reproducible biochemical assays and allows tag-specific detection methods. These studies could provide fundamental insights into the structural stability and folding characteristics of the HCoV-NL63 membrane protein.
4. Immunoassay Development and Validation
The recombinant M protein serves as a valuable standard and control reagent for developing coronavirus detection immunoassays. The His-tag allows consistent immobilization on assay plates and provides a reliable detection handle for assay optimization. Researchers can apply this protein to establish standard curves, validate assay specificity, and optimize detection protocols for research applications. The defined protein concentration and purity make it suitable for quantitative immunoassay development and cross-reactivity studies with related coronavirus proteins.
