Can't find the products you're looking for? Try to filter in the left sidebar.Filter By Tag
Our customer service representatives are available 24 hours a day, from Monday to Sunday. Contact Us
For Research Use Only. Not For Clinical Use.
CD markers, Disease related genes, Human disease related genes
Membrane, Secreted (different isoforms)
Cell type enhanced (monocytes, Kupffer cells, Macrophages, Granulosa cells)
Immune cell enhanced (neutrophil)
Cell line enhanced (HL-60, NB-4, THP-1)
Forms heterodimers with IL17RC; the heterodimer binds IL17A and IL17F homodimers as well as the heterodimer formed by IL17A and IL17F (PubMed:16785495, PubMed:18684971, PubMed:32187518). Forms complexes with 2:1 binding stoichiometry: two receptor chains for one interleukin molecule (PubMed:32187518). IL17A homodimer preferentially drives the formation of IL17RA-IL17RC heterodimeric receptor complex, whereas IL17F homodimer forms predominantly complexes with IL17RC homodimer (PubMed:32187518). IL17A homodimer adopts an asymmetrical ternary structure with one IL17RA molecule, allowing for high affinity interactions of one IL17A monomer with one IL17RA molecule (via D1 and D2 domains), while disfavoring binding of a second IL17RA molecule on the other IL17A monomer (PubMed:23695682). IL17A-IL17F forms complexes with IL17RA-IL17RC, but with lower affinity when compared to IL17A homodimer (PubMed:32187518). IL17RA chain cannot distinguish between IL17A and IL17F molecules, potentially enabling the formation of topologically distinct complexes (PubMed:28827714). Interacts with TRAF3IP2 (PubMed:24120361). Forms heterodimers with IL17RE; the heterodimer binds IL17C (PubMed:21993848, PubMed:16785495, PubMed:18684971). (Microbial infection) Interacts with SARS coronavirus-2/SARS-CoV-2 virus protein ORF8.
Receptor