Human IL-17 RD/SEF Fluorescein-conjugated Antibody
Human IL-17 RD/SEF Fluorescein-conjugated Antibody Summary
Accession # AAM77571
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of IL‑17 RD/SEF in K562 Human Cell Line by Flow Cytometry. K562 human chronic myelogenous leukemia cell line was stained with Goat Anti-Human IL-17 RD/SEF Fluorescein-conjugated Anti-gen Affinity-purified Polyclonal Anti-body (Catalog # FAB2275F, filled histogram) or isotype control antibody (Catalog # IC108F, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
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, -8, sprouty-2 (SPRY2) and SPRY4 (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-17RD 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 homomultimeric 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). Ligands that interact with the extracellular domain of IL-17 RD have not been identified.
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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.
- Torii, S. et al. (2004) Dev. Cell 7:33.
- Yang, X. et al. (2004) J. Biol. Chem. 279:38099.
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