The Recombinant SARS-CoV-2 Nucleoprotein (R203M, D377Y) gets expressed in E. coli and contains the complete 1-419 amino acid sequence with an N-terminal 6xHis-tag for streamlined purification. SDS-PAGE analysis confirms the protein reaches greater than 90% purity. Functional ELISA testing verifies its biological activity, showing specific binding with both mouse monoclonal and recombinant antibodies, along with established EC50 values.
SARS-CoV-2's Nucleoprotein (N) appears to play a critical role in viral replication and assembly. This key structural component wraps around the viral RNA genome and seems central to the virus's ability to spread. Researchers focus heavily on this protein because of its involvement in viral pathogenesis and its potential as a diagnostic and therapeutic target.
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
The full-length protein with validated binding activity via ELISA supports its use as an immunogen or screening antigen. The key application for this specific variant (R203M, D377Y) is to develop antibodies that can specifically distinguish Delta variant-specific epitopes from the wild-type nucleoprotein. The N-terminal 6xHis tag facilitates purification and immobilization. However, antibodies generated using this protein may have differential affinity for the wild-type protein, which must be characterized.
2. Functional ELISA Development and Optimization
The combination of full-length sequence, confirmed binding activity in ELISA, and defined EC50 values makes it an excellent candidate as a reference standard or capture antigen for developing quantitative immunoassays specifically designed to detect antibodies targeting the Delta variant (R203M, D377Y) nucleoprotein.
3. Protein-Protein Interaction Studies
The protein can be used in pull-down assays. However, it is critical to note that the R203M and D377Y mutations are not just neutral markers; they functionally enhance the protein's RNA-binding affinity and alter its interaction with host immune signaling components, particularly RIG-I. Therefore, interaction studies should be explicitly designed as comparative analyses against the wild-type protein to investigate how these mutations impact binding to viral RNA or host proteins like RIG-I, rather than for general interaction mapping.
4. Structural and Biochemical Analysis of Variant Effects
The core value lies in its defined point mutations. It is highly suitable for comparative biophysical studies (e.g., circular dichroism, thermal stability assays) to directly investigate how the R203M and D377Y substitutions affect the protein's oligomerization state, stability, and RNA-binding affinity compared to the wild-type protein. The confirmed binding activity provides a functional correlate for structural findings.
5. Quality Control Standard for Variant Detection Assays
The defined mutations (R203M, D377Y), high purity, and consistent production make this protein an ideal positive control or calibration standard for optimizing and validating immunological assays (e.g., ELISA, lateral flow tests) aimed at specifically detecting SARS-CoV-2 variants carrying these mutations, such as the Delta lineage.
Final Recommendation & Action Plan:
This recombinant SARS-CoV-2 nucleoprotein (R203M, D377Y) is a high-quality reagent with validated utility in immunoassay development and comparative functional studies. Its primary value lies in its defined Delta variant mutations. The most recommended applications are its use as a standard in variant-specific antibody detection assays and for comparative biochemical studies to understand the functional impact of the R203M/D377Y mutations on protein properties and host interactions. For any experimental use, researchers should explicitly frame their work around the Delta variant context and always include wild-type nucleoprotein controls for comparative purposes to draw meaningful conclusions about the mutation-specific effects.
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