Detects mouse IL‑17 RD/SEF in Western blots. In Western blots, approximately 40% cross-reactivity with recombinant human (rh) IL-17 RD is observed and less than 1% cross-reactivity with recombinant mouse (rm) IL-17 RC and rmIL-17B R is observed.
Source
N/A
Isotype
IgG
Clonality
Polyclonal
Host
Goat
Gene
IL17RD
Purity Statement
Antigen Affinity-purified
Innovator's Reward
Test in a species/application not listed above to receive a full credit towards a future purchase.
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Preservative
No Preservative
Concentration
LYOPH
Reconstitution Instructions
Reconstitute at 0.2 mg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for IL-17RD/SEF Antibody [Biotin]
FLJ35755
IL-17 RD
IL17RD
IL-17RD
IL-17RDIL-17 receptor D
IL17Rhom
IL17RLM
IL17RLMDKFZp434N1928
interleukin 17 receptor D
interleukin-17 receptor D
Interleukin-17 receptor-like protein
MGC133309
Sef homolog
SEF
SEFhSef
Background
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.
Torii, S. et al. (2004) Dev. Cell 7:33.
Yang, X. et al. (2004) J. Biol. Chem. 279:38099.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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