This recombinant Human coronavirus HKU1 Protein I (N) comes from E. coli expression and spans the complete sequence from amino acids 1 to 205. The protein carries a C-terminal 6xHis-tag, which makes purification and detection more straightforward. SDS-PAGE analysis confirms the protein reaches over 85% purity. This product is meant strictly for research purposes and appears to offer a dependable resource for coronavirus protein studies.
The N protein from Human coronavirus HKU1 seems to play an essential role in how the virus replicates and transcribes its genetic material. It's involved in wrapping the viral RNA genome into the nucleocapsid and likely contributes to maintaining the virus's structural stability. Given its central position in coronavirus assembly, the N protein has become a major target for research into viral disease mechanisms and immune responses.
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. Antigen for Anti-HCoV-HKU1 Antibody Development
This recombinant nucleocapsid protein may work well as an immunogen or screening antigen when developing monoclonal or polyclonal antibodies against Human coronavirus HKU1. The C-terminal 6xHis tag makes purification easier and allows attachment to solid supports during antibody screening. High purity levels (>85%) should minimize unwanted cross-reactions with bacterial proteins during immunization or screening steps. These antibodies could prove valuable for investigating HCoV-HKU1 infection pathways and tracking where viral proteins end up in cells.
2. Protein-Protein Interaction Studies Using Pull-Down Assays
The C-terminal 6xHis tag opens up possibilities for nickel-affinity pull-down experiments to find cellular proteins that bind to the HCoV-HKU1 nucleocapsid protein. This strategy might help reveal how the viral nucleocapsid protein connects with host cell processes during infection. Researchers can mix cell lysates or purified protein collections with immobilized His-tagged nucleocapsid protein to trap potential binding partners. Mass spectrometry can then identify which proteins get pulled down together.
3. ELISA-Based Binding and Inhibition Assays
The purified nucleocapsid protein appears suitable for creating enzyme-linked immunosorbent assays to study antibody binding patterns or screen for small molecule inhibitors. Researchers can coat the protein directly onto ELISA plates or capture it using anti-His tag antibodies for more consistent positioning. This setup would let scientists measure how tightly experimental antibodies bind or test compounds that might interfere with nucleocapsid protein activity. The standardized approach works well for high-throughput screening in research labs.
4. Structural and Biophysical Characterization Studies
This recombinant protein provides raw material for laboratory-based structural biology work, including circular dichroism spectroscopy, dynamic light scattering, and analytical ultracentrifugation to examine how the HCoV-HKU1 nucleocapsid protein folds and forms complexes with itself. The purified protein can help determine heat stability, pH tolerance, and which buffers work best for storage and experiments. This kind of biophysical characterization is probably necessary for understanding what makes this viral protein tick and planning additional biochemical studies.
