Recombinant Severe acute respiratory syndrome coronavirus 2 Nucleoprotein (N) (Q384H) (Active)

Recombinant Severe acute respiratory syndrome coronavirus 2 Nucleoprotein (N) (Q384H) is expressed in E. coli, covering the full-length sequence from 1-419 amino acids with a Q384H mutation. This protein features an N-terminal 6xHis-tag, which makes purification straightforward. It achieves a purity greater than 84% as verified by SDS-PAGE. Functional ELISA confirms its biological activity, showing strong binding capabilities with specific antibodies—this suggests it's well-suited for research applications.

SARS-CoV-2's nucleoprotein (N) appears to play a critical role in the viral replication cycle and seems essential for ribonucleoprotein formation. It's involved in packaging the viral RNA genome and modulating host cellular processes. This makes it a key target for research into viral pathogenesis and potential therapeutic interventions. The protein's significance in coronavirus biology studies and vaccine development may underscore its importance in ongoing scientific investigations.

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. ELISA-Based Antibody Screening and Characterization

This recombinant SARS-CoV-2 nucleoprotein can serve as a capture antigen in ELISA platforms for screening and characterizing anti-nucleoprotein antibodies. The demonstrated binding activity with both monoclonal and recombinant antibodies, with defined EC50 values, establishes its reliability as an antigen for antibody binding assays. The N-terminal 6xHis tag makes oriented immobilization on nickel-coated plates possible, which might improve antibody binding consistency. Researchers evaluating the binding kinetics and specificity of newly developed anti-N protein antibodies could find this particularly valuable.

2. Protein-Protein Interaction Studies

The biologically active nucleoprotein can help investigate its interactions with other viral or host proteins through pull-down assays and co-immunoprecipitation experiments. Its N-terminal 6xHis tag allows for efficient purification and immobilization on nickel-based affinity matrices, capturing potential binding partners from cell lysates or purified protein preparations. These studies may provide insights into the molecular mechanisms of SARS-CoV-2 replication and host cell interactions. Using the full-length protein (1-419aa) with the Q384H variant likely ensures that interaction studies reflect the complete protein structure and any variant-specific binding properties.

3. Biochemical and Biophysical Characterization

This purified nucleoprotein preparation works well for detailed biochemical analysis—structural studies, thermal stability assays, and protein folding investigations. The >84% purity level makes it suitable for techniques such as dynamic light scattering, circular dichroism spectroscopy, and analytical ultracentrifugation to characterize the protein's biophysical properties. The Q384H variant enables comparative studies with wild-type nucleoprotein, helping researchers understand how this specific mutation affects protein stability and conformation. Such characterization work contributes to fundamental understanding of SARS-CoV-2 nucleoprotein structure-function relationships.

4. Immunoassay Development and Validation

The recombinant nucleoprotein can serve as a reference standard and positive control when developing new immunoassays for research applications. Its demonstrated binding activity with defined EC50 values provides quantitative benchmarks for assay optimization and validation. Consistent expression in E. coli and His-tag purification appears to ensure reproducible protein preparations for standardizing assay conditions. This supports the development of research tools for studying immune responses and antibody production in preclinical models.

5. Antigen Presentation and Immunological Studies

This biologically active nucleoprotein proves useful in in vitro immunological studies investigating antigen processing and presentation pathways. Antigen-presenting cells in culture systems can process the full-length protein, allowing researchers to study MHC class I and II presentation of nucleoprotein-derived peptides. The Q384H variant lets researchers examine how specific mutations might affect antigen processing and immune recognition patterns. Such studies may contribute to understanding the immunological properties of SARS-CoV-2 nucleoprotein variants in controlled research environments.