IL-17RD/SEF Antibody [Alexa Fluor™ Plus 555] Summary
| Specificity |
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. |
| Isotype |
IgG |
| Clonality |
Polyclonal |
| Host |
Goat |
| Innovator's Reward |
Test in a species/application not listed above to receive a full credit towards a future purchase. |
Packaging, Storage & Formulations
| Storage |
Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied |
| Buffer |
Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for IL-17RD/SEF Antibody [Alexa Fluor™ Plus 555]
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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