Detection of IL‑17 RD/SEF in HEK293 Human Cell Line Transfected with Human IL-17 RD/SEF by Flow Cytometry.
HEK293 human embryonic kidney cell line transfected with human IL‑17 RD/SEF (upper panel) or irrelevant transfectant (lower panel) was stained with Mouse Anti-Human IL‑17 RD/SEF Monoclonal Antibody (Catalog # MAB22751, filled histogram) or isotype control antibody (Catalog # MAB002, open histogram), followed by Allophycocyanin-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # F0101B).
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: IL-17 RD/SEF
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 where SEF is expressed along with FGF-3, FGF-8, Sprouty-2 and Sprouty-4 (6, 7). By alternate splicing, two transcript variants, potentially encoding three protein isoforms, exist. One is a full-length long form, one a shortened form that uses an alternate start site, and one an alternate splice form that removes the classic signal sequence (1-4). These isoforms have different expression patterns, subcellular localization, and function. The membrane-bound long form of human IL-17 RD is synthesized as a 739 amino acid (aa) precursor protein with a putative 27 aa signal peptide, a 272 aa extracellular domain, a 20 aa transmembrane segment and a 420 aa cytoplastic domain. 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 homo-multimeric complexes (3). Unlike the alternate splice form of IL-17 RD that has a restricted pattern of expression, 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 FGFR1/2 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).
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Xiong, S. et al. (2003) J. Biol. Chem. 278:50273.
Yang, R-B. et al. (2003) J. Biol. Chem. 278:33232.
Preger, E. et al. (2003) Proc. Natl. Acad. Sci. USA 101:1229.
Lin, W. et al. (2002) Mech. Dev. 113:163.
Tsang, M. et al. (2002) Nat. Cell Biol. 4:165.
Kovalenko, D. et al. (2003) J. Biol. Chem. 278:14087.
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