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For Research Use Only. Not For Clinical Use.
Disease related genes, Human disease related genes
Intracellular, Membrane (different isoforms)
Cell type enhanced (Proximal enterocytes)
Immune cell enhanced (myeloid DC, classical monocyte)
Cell line enhanced (ASC diff, ASC TERT1, HSkMC, T-47d)
Homodimer; disulfide-linked (PubMed:32187518). Heterodimer with IL17RA (PubMed:16785495, PubMed:18684971). Heterodimerization with IL17RA is independent of the cytoplasmic tail (By similarity). Associates with non-glycosylated IL17RA constitutively (By similarity). Binding of IL17A and IL17F induces association with glycosylated IL17RA (By similarity). Forms complexes with 2:1 binding stoichiometry: two receptor chains for one interleukin molecule (PubMed:32187518, PubMed:28827714). IL17A homodimer preferentially drives the formation of IL17RA-IL17RC heterodimeric receptor complex, whereas IL17F homodimer forms predominantly complexes with IL17RC homodimer (PubMed:32187518). IL17A-IL17F forms complexes with IL17RA-IL17RC, but with lower affinity when compared to IL17A homodimer (PubMed:32187518). IL17RC chain cannot distinguish between IL17A and IL17F molecules, potentially enabling the formation of topologically distinct complexes (PubMed:28827714). Interacts (through SEFIR domain and extended downstream region) with TRAF3IP2/ACT1 (phosphorylated) (PubMed:24120361).
Receptor