Mouse IL-17RD/SEF Alexa Fluor® 594-conjugated Antibody

Interleukin-17 receptor D (IL-17 RD), also known as SEF (similar expression to FGFs), is a type I transmembrane protein that is found in both the cytoplasm and plasma membrane (1‑5). The gene for this protein belongs to a synexpression group originally identified in zebrafish and SEF is expressed along with FGF-3, -8, sprouty-2 (SPRY2) and SPRY4 (6, 7). Due to the presence of an alternate start site, there is one transcript that potentially gives rise to two isoforms. The first is a full-length long form and the second an N-terminally truncated form (2, 5). The significance and expression pattern of the short form are uncertain. The membrane‑bound long form of mouse IL-17 RD is synthesized as a 738 amino acid (aa) precursor protein with a putative 27 aa signal peptide, a 272 aa extracellular domain, a 20 aa transmembrane segment and a 419 aa cytoplastic domain (5). The extracellular domain contains one Ig-like domain and a fibronectin type III motif. The cytoplasmic domain shares homology with the intracellular domains of IL‑17 receptor family members and shows one TIR (Toll/IL-1 Receptor) domain and a putative TRAF6-binding motif (2). Natural IL-17 RD has been shown to form homomultimeric complexes (3). The full-length IL-17 RD isoform is expressed in most adult tissues and during embryonic development (3, 5). Functionally, IL-17 RD has been shown to be an inhibitor of FGF signaling. The molecule’s extracellular domain does not seem to be involved. There is an interaction between the intracellular domains of FGF R1/2 and IL-17 RD that blocks ERK dissociation from MEK, thereby interfering with downstream ERK activation of nuclear Elk-1 (8). IL-17 RD has also been reported to interact with TAK1 and induce JNK activation and apoptosis (9). Ligands that interact with the extracellular domain of IL-17 RD have not been identified.