Detects mouse IL-17 RD/SEF in direct ELISAs and Western blots. In direct ELISAs, approximately 40% cross-reactivity with recombinant human IL-17 RD is observed and less than 1% cross-reactivity with recombinant mouse (rm) IL-17 RC and rmIL-17B R is observed.
Detection of IL‑17 RD/SEF in bEnd.3 Mouse Cell Line by Flow Cytometry. bEnd.3 mouse endothelioma cell line was stained with Goat Anti-Mouse IL‑17 RD/SEF Antigen Affinity‑purified Polyclonal Antibody (Catalog # AF2276, filled histogram) or isotype control antibody (Catalog # AB‑108‑C, open histogram), followed by Phycoerythrin-conjugated Anti-Goat IgG Secondary Antibody (Catalog # F0107).
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
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 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 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). Ligands that interact with the extracellular domain of IL-17 RD have not been identified.
Furthauer, M. et al. (2002) Nat. Cell Biol. 4:170.
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.
R&D Systems personnel manually curate a database that contains references using R&D Systems products.
The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.