Recombinant Human Interleukin-17F (IL17F) is produced in a mammalian expression system and represents a full-length mature protein with a C-terminal 6xHis tag. The product shows purity greater than 95% as determined by SDS-PAGE analysis. Biological activity appears confirmed through binding ability in a functional ELISA. Endotoxin levels remain below 1.0 EU/µg, which likely makes it suitable for research applications.
Interleukin-17F (IL17F) is a cytokine that participates in immune responses, mainly produced by activated T cells. It seems to play an important role in inflammatory responses and belongs to the IL-17 family of cytokines, which may be critical for host defense against pathogens. IL17F appears involved in signaling pathways that contribute to inflammation and represents a key area of interest in research related to immune regulation and inflammatory diseases.
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. IL-17 Receptor Binding Studies and Interaction Analysis
This recombinant IL-17F protein can investigate the binding kinetics and affinity between IL-17F and its receptors, particularly IL-17RA as shown by the functional ELISA activity test. Researchers might use surface plasmon resonance, bio-layer interferometry, or similar biophysical techniques to characterize the binding parameters. Comparisons with other IL-17 family members could prove valuable. The C-terminal His-tag appears to simplify immobilization and detection in these binding assays. Studies like these would likely contribute to understanding the molecular basis of IL-17F receptor recognition and specificity.
2. Antibody Development and Characterization
The high purity and biological activity of this IL-17F protein may make it suitable as an immunogen for generating research antibodies. It could also serve as a standard for characterizing existing anti-IL-17F antibodies. The protein might work well in ELISA-based screening of hybridoma clones or in validating antibody specificity and cross-reactivity. His-tag presence allows for easier purification and immobilization for antibody binding assays. Low endotoxin levels suggest minimal interference in cell-based antibody validation experiments.
3. Competitive Binding Assays for IL-17 Family Studies
This recombinant IL-17F could work in competitive binding experiments to study receptor binding preferences among IL-17 family cytokines. Researchers might investigate whether IL-17F competes with IL-17A or other family members for receptor binding sites. The established IL-17RA binding assay could provide a foundation for such work. The defined ED50 value offers a quantitative reference point for designing competition experiments. Studies of this nature would likely help clarify the relative receptor affinities and potential functional redundancies within the IL-17 cytokine family.
4. Structural and Biochemical Characterization Studies
The mammalian-expressed IL-17F protein with proper folding and biological activity may serve as a substrate for structural biology applications. This includes crystallization trials and NMR studies. The protein's confirmed receptor binding activity suggests proper tertiary structure formation, which could make it suitable for biophysical characterization techniques. Circular dichroism spectroscopy or analytical ultracentrifugation appear to be viable options. The His-tag simplifies purification for these applications while the high purity likely minimizes interference from contaminants in structural analyses.
5. Cell-Free Biochemical Assays and Protein-Protein Interaction Studies
This biologically active IL-17F protein might work in cell-free systems to study downstream signaling pathway components and identify novel IL-17F-interacting proteins. Pull-down experiments using the His-tag could help identify binding partners from cell lysates or purified protein libraries. The low endotoxin content suggests that any observed effects in subsequent cell-based validation experiments are likely due to IL-17F activity rather than contamination. The established binding activity provides confidence that the protein maintains its native conformation for interaction studies.
