Recombinant Human coronavirus 229E Nucleoprotein (N) is produced using a baculovirus expression system, which appears to ensure high-quality protein production. The full-length protein spans 1-389 amino acids and comes with an N-terminal 10xHis-tag and a C-terminal Myc-tag for easier purification and detection. SDS-PAGE analysis shows the purity exceeds 85%, making this recombinant protein suitable for various research applications that demand high-quality reagents.
Human coronavirus 229E's Nucleoprotein (N) plays a critical role in the viral replication cycle. It participates in packaging viral RNA and forming the ribonucleoprotein complex—both essential for efficient viral transcription and replication. Studying this protein may be crucial for understanding coronavirus biology mechanisms and could potentially lead to 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 Validation Studies
This full-length recombinant HCoV-229E nucleoprotein can work as an immunogen for generating monoclonal or polyclonal antibodies specific to coronavirus 229E. The dual His and Myc tags help with purification and detection during antibody screening. Researchers might use this protein in ELISA-based assays to characterize antibody binding specificity, affinity, and cross-reactivity with other coronavirus nucleoproteins. The high purity (>85%) likely ensures reliable and reproducible results in immunization protocols and subsequent antibody validation experiments.
2. Protein-Protein Interaction Studies
Both the N-terminal His tag and C-terminal Myc tag make this nucleoprotein suitable for pull-down assays designed to identify cellular proteins that interact with HCoV-229E nucleoprotein during infection. Researchers can immobilize the protein on nickel-affinity resins or use anti-Myc antibodies for immunoprecipitation experiments with cell lysates. These studies may help clarify the molecular mechanisms by which coronavirus nucleoproteins interact with host cell machinery. The baculovirus expression system probably provides proper protein folding, which seems important for maintaining native protein-protein interaction capabilities.
3. Structural and Biochemical Characterization
This recombinant nucleoprotein works well in biophysical studies investigating the structural properties and stability of HCoV-229E nucleoprotein. The full-length construct (1-389aa) lets researchers study the complete protein structure using techniques like circular dichroism spectroscopy, dynamic light scattering, or analytical ultracentrifugation. The dual tagging system makes protein detection and quantification easier during purification and analysis procedures. Such studies could provide insights into nucleoprotein folding, oligomerization states, and thermal stability under various buffer conditions.
4. Comparative Coronavirus Research
This HCoV-229E nucleoprotein can serve as a reference standard in comparative studies examining nucleoprotein sequences, structures, and properties across different coronavirus species. Researchers might use this protein alongside nucleoproteins from other coronaviruses to study evolutionary relationships and identify conserved functional domains. The standardized expression system and purification tags create consistent experimental conditions when comparing multiple coronavirus nucleoproteins. Comparative analyses like these may contribute to understanding common mechanisms of coronavirus replication and pathogenesis.
5. Assay Development and Optimization
The dual-tagged nucleoprotein provides a valuable tool for developing and optimizing various biochemical assays related to coronavirus research. The His tag creates consistent purification protocols, while the Myc tag allows for standardized detection methods using commercially available anti-Myc antibodies. Researchers can use this protein to establish standard curves, validate assay sensitivity and specificity, and optimize experimental conditions for nucleoprotein-based studies. The defined purity level (>85%) offers a reliable standard for quantitative assay development and quality control procedures.
