Recombinant Severe acute respiratory syndrome coronavirus 2 Nucleoprotein (N) (D103Y) (Active)

Recombinant Severe acute respiratory syndrome coronavirus 2 Nucleoprotein (N) (D103Y) is produced in E. coli with an N-terminal 6xHis-tag, covering the complete protein sequence (1-419aa). The product shows purity levels above 94% as confirmed by SDS-PAGE. Functional ELISA assays indicate the protein retains biological activity, with specific binding to both N Mouse Monoclonal Antibody and N Recombinant Antibody showing EC50 values in the nanogram range.

SARS-CoV-2's Nucleoprotein (N) appears central to viral replication, playing important roles in RNA packaging and ribonucleoprotein complex assembly. As a key structural element of the virus, it's involved in regulating both replication and transcription processes. Researchers often target this protein when developing antiviral drugs or studying immune responses, given its essential functions throughout the viral life cycle.

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

The nucleoprotein's confirmed biological activity via ELISA and its full-length nature strongly support its use as a capture antigen for detecting anti-nucleoprotein antibodies. The N-terminal 6xHis tag facilitates immobilization. The D103Y mutation allows for investigating its specific impact on antibody binding characteristics, which is a valid application given the confirmed activity.

2. Protein-Protein Interaction Studies

While the high purity and confirmed activity make the protein suitable for studying interactions, the D103Y mutation is a key factor. This mutation, located in the N-terminal domain, could potentially alter interactions with viral RNA or host proteins compared to the wild-type protein. Therefore, any findings are specific to this variant and may not represent the wild-type protein's behavior. Studies should be designed as comparative analyses against the wild-type protein.

3. Structural and Biochemical Characterization

The high purity and full-length sequence make this protein suitable for biophysical studies (e.g., circular dichroism, dynamic light scattering) to analyze its folding, stability, and oligomerization state. The confirmed biological activity increases confidence that the protein is correctly folded for such analyses. The D103Y mutation specifically allows researchers to investigate how this substitution affects the protein's structural properties and oligomerization compared to the wild-type protein.

4. Immunoassay Development and Validation

The nucleoprotein's primary and best-supported application is in immunoassay development. The combination of being full-length, having >94% purity, and, most importantly, confirmed specific binding activity (e.g., with defined EC50 values) makes it an excellent candidate for use as a standard or capture antigen in developing and validating quantitative immunoassays, such as ELISA, for research purposes.

5. Comparative Mutational Analysis

The core value of this reagent lies in its defined point mutation (D103Y). It is ideally suited for direct, side-by-side comparative studies with the wild-type nucleoprotein to elucidate the specific effects of the D103Y mutation on antibody binding, protein stability, oligomerization, and interactions with other molecules. The confirmed biological activity provides a solid baseline for such comparative functional studies.

Final Recommendation & Action Plan:

Based on the provided specifications, this recombinant SARS-CoV-2 nucleoprotein (D103Y) is a high-quality reagent with validated binding activity, making it highly reliable for the proposed applications, particularly those related to immunoassay development and comparative mutational analysis. The primary recommendation is to leverage this protein specifically for studying the functional and structural consequences of the D103Y mutation by always including appropriate wild-type nucleoprotein controls in experiments. For all applications, it should be clearly communicated that the data generated is specific to the D103Y variant.