|Detection of IL‑17 RC in RAW 264.7 Mouse Cell Line by Flow Cytometry. RAW 264.7 mouse monocyte/macrophage cell line was stained with Goat Anti-Mouse IL‑17 RC APC‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB2270A, filled histogram) or isotype control antibody (Catalog # IC108A, open histogram). View our protocol for Staining Membrane-associated Proteins.|
IL-17 receptor C (IL-17 RC; also known as IL-17 RL) is an 85‑110 kDa member of the IL-17 receptor family. This is one of five families, termed IL-17 RA, B, C, D and E, that comprise the cytokine receptor superfamily (1‑6). Not all receptors appear to bind known members of the IL-17 cytokine family. To date, IL-17 RA is reported to bind IL-17A, while IL-17 RB is reported to bind IL-17B and IL-17E (2, 4). Mouse IL-17 RC is a type I transmembrane glycoprotein that is expressed on a variety of nonhematopoietic cell types. Full-length IL-17 RC is synthesized as a 674 amino acid (aa) precursor. It contains a 21 aa signal sequence, a 419 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 213 aa cytoplasmic region. There are multiple potential N‑linked glycosylation sites in the ECD and potential phosphorylation sites in the cytoplasmic tail. Four mouse variants have been identified that have been designated mIL-17 RC (7). The isoform expressed here as an R&D product is an unusual 567 aa form (8). Its precursor contains a 20 aa signal sequence, a 444 aa extracellular region, a 20 aa transmembrane segment and an 83 aa cytoplasmic tail. When compared to the full length mouse IL-17 RC form, this expressed isoform’s extracellular region shows absolute aa identity, save for an additional 24 aa insert. In the cytoplasmic region, it is highly divergent and shows virtually no aa identity (8‑9). The extracellular region of mouse IL-17 RC shows about 70% aa identity to the equivalent region in human IL-17 RC isoform # 3. IL-17 RC is the cognate receptor for IL-17F (7). In humans, IL-17 RC binds IL-17A with similar affinity, and with IL-17 RA, it forms a definitive receptor for both IL-17A and IL-17F (7). The stoichiometry is unclear; it may form a heterodimer with IL-17 RA, or a heterotrimer with a preexisting IL-17 RA homodimer (4, 7, 10, 11). The heteromeric nature of the receptor may be important given that the predominant form of the IL-17 cytokine is now considered to be an IL-17A:IL-17F heterodimer (4).
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