Recombinant Human Interleukin-17 receptor A (IL17RA) is produced in a mammalian cell expression system, covering the extracellular region from amino acids 33 to 320. This protein is C-terminally Fc-tagged and exhibits a purity greater than 90%, as determined by SDS-PAGE. It maintains a low endotoxin level of less than 1.0 EU/µg according to the LAL method. Its biological activity is confirmed through functional ELISA, demonstrating a binding affinity with an ED50 of 13.50 ng/ml for Anti-Human IL-17RA monoclonal antibody.
Interleukin-17 receptor A (IL17RA) appears to be a crucial component of the IL-17 receptor complex, playing what seems to be a significant role in mediating immune responses. The receptor is involved in the signaling pathway of interleukin-17, a cytokine that promotes inflammatory responses. IL17RA has become essential in studies focusing on immune regulation and has been implicated in various research areas related to inflammation and immune system function.
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
This recombinant IL17RA extracellular domain can serve as an immunogen for generating monoclonal or polyclonal antibodies against human IL17RA. The Fc-tagged protein provides enhanced immunogenicity and makes purification easier for immunization protocols. The demonstrated binding activity with anti-IL17RA monoclonal antibodies, as shown in the functional ELISA, confirms the protein likely maintains proper folding and epitope presentation. Scientists can use this protein to screen and validate antibody specificity, affinity, and cross-reactivity across various immunoassay formats.
2. Protein-Protein Interaction Studies
The biologically active IL17RA extracellular domain can be used to investigate binding interactions with IL-17 family cytokines and other potential ligands in vitro. The C-terminal Fc tag enables easy immobilization on protein A/G surfaces for surface plasmon resonance, bio-layer interferometry, or ELISA-based binding assays. Scientists can determine binding kinetics, affinity constants, and specificity profiles of IL17RA interactions. The mammalian expression system ensures proper glycosylation and post-translational modifications that may be critical for physiologically relevant binding studies.
3. Competitive Binding and Inhibition Assays
This recombinant protein can serve as a capture reagent in competitive binding assays to screen for small molecule inhibitors or competing proteins that disrupt IL17RA-ligand interactions. The established functional ELISA protocol with known ED50 values provides a validated platform for developing high-throughput screening assays. Scientists can immobilize the IL17RA-Fc protein and measure displacement of known binding partners by test compounds. The high purity and low endotoxin levels make it suitable for sensitive biochemical assays requiring minimal background interference.
4. Structural and Biophysical Characterization
The purified IL17RA extracellular domain can be used for structural biology studies including X-ray crystallography, NMR spectroscopy, or cryo-electron microscopy to elucidate the three-dimensional structure of the receptor. The protein's demonstrated biological activity suggests proper folding, making it suitable for biophysical analyses such as circular dichroism spectroscopy, dynamic light scattering, and thermal stability studies. The Fc tag can be removed enzymatically if needed for structural studies. Alternatively, the fusion protein can be analyzed to understand receptor dimerization and clustering mechanisms.
5. Cell-Based Receptor Binding Studies
This soluble IL17RA-Fc fusion protein can function as a decoy receptor in cell culture experiments to sequester IL-17 family cytokines and study their biological effects on target cells. Scientists can add the recombinant protein to cell culture media to competitively inhibit endogenous IL17RA signaling pathways. The Fc tag allows for easy detection and quantification of protein uptake or binding to cell surfaces using fluorescently labeled anti-Fc antibodies. The mammalian expression system ensures compatibility with human cell culture studies without species-specific glycosylation artifacts.
