Recombinant Human coronavirus HKU1 Spike glycoprotein (S) is produced in E. coli and consists of a partial length from amino acids 310 to 622. The protein includes a C-terminal 6xHis-tag for ease of purification and detection. Purity reaches greater than 90% as determined by SDS-PAGE, which appears to make it suitable for various research applications. This product is intended for research use only, with no endotoxin level specified.
The Spike glycoprotein (S) of Human coronavirus HKU1 seems integral to the virus's ability to attach and enter host cells. It likely plays a crucial role in viral entry through interactions with host cell receptors, making it a key focus in studies of viral infection mechanisms and immune response. Understanding its structure and function may be essential for developing therapeutic strategies and vaccines against coronaviruses.
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 Antibody Development and Characterization
This recombinant spike protein fragment (amino acids 310-622) can serve as an antigen for generating monoclonal or polyclonal antibodies specific to Human coronavirus HKU1. The C-terminal His-tag streamlines purification and immobilization for immunization protocols or screening assays. Researchers might use this protein to develop antibodies that recognize specific epitopes within this region of the HKU1 spike protein. High purity (>90%) suggests consistent immunogenic presentation for antibody production workflows.
2. Protein-Protein Interaction Studies
Pull-down assays could benefit from this His-tagged spike protein fragment to identify and characterize potential cellular receptors or binding partners for Human coronavirus HKU1. The C-terminal His-tag allows for immobilization on nickel-based affinity matrices. This enables researchers to capture interacting proteins from cell lysates or purified protein libraries. Such an approach may help elucidate the molecular mechanisms of HKU1 cellular entry and tropism within the amino acid region 310-622.
3. Structural and Biochemical Characterization
This purified spike protein fragment provides material for biophysical and structural studies to understand the molecular properties of the HKU1 spike protein. Techniques such as circular dichroism spectroscopy, dynamic light scattering, or analytical ultracentrifugation might be performed to characterize protein folding, stability, and oligomerization states. The defined amino acid boundaries (310-622) appear to make this fragment suitable for domain-specific structural analysis and comparison with other coronavirus spike proteins.
4. ELISA-Based Binding and Competition Assays
Immobilization of the His-tagged protein in ELISA plates allows for quantitative binding studies and competitive inhibition assays. This system could be used to screen small molecules, peptides, or other proteins for their ability to interact with this specific region of the HKU1 spike protein. High purity and consistent tag orientation likely support reproducible coating and detection in plate-based assay formats for medium-throughput screening applications.
