Detects mouse IL-17 R in direct ELISAs and Western blots. In Western blots, approximately 5% cross-reactivity with recombinant human IL‑17 R is observed and less than 1% cross-reactivity with recombinant mouse (rm) IL-17 RC and rmIL-17 RD is observed.
Polyclonal Goat IgG
S. frugiperda insect ovarian cell line Sf 21-derived recombinant mouse IL-17 R Extracellular domain
Supplied in a saline solution containing BSA and Sodium Azide.
10 µL/106 cells
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 RA/IL‑17 R in EL‑4 Mouse Cell Line by Flow Cytometry. EL‑4 mouse lymphoblast cell line was stained with Goat Anti-Mouse IL‑17 RA/IL‑17 R Fluorescein‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB448F, filled histogram) or isotype control antibody (Catalog # IC108F, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
Background: IL-17 RA/IL-17 R
IL-17 R, also known as IL-17 RA, is a 120 kDa type I transmembrane glycoprotein protein that plays a central role in inflammatory responses (1-3). Mature mouse IL‑17 R consists of a 291 amino acid (aa) extracellular domain, a 21 aa transmembrane segment, and a 521 aa cytoplasmic domain (4). The cytoplasmic domain contains a region homologous to the TIR domain of the TLR/IL-1 R family (5). Mouse IL-17 R shares 84% and 72% aa sequence identity with rat and human IL-17 R, respectively. Within the extracellular domain, it shares 18-25% sequence identity with mouse IL-17 RB, C, D, and E. While the expression of IL-17 is restricted to activated T cells, IL-17 R exhibits a broad tissue distribution (4). Even in the absence of ligand, IL-17 R exists on the cell surface as a multimer (6). IL-17 R can bind IL-17 but must associate with IL-17 RC to transduce signals (7, 8). Interestingly, human IL-17 R does not appear to form productive complexes with mouse IL-17 RC (8). The IL-17 R can also signal in response to IL-17F (9). IL-17 R ligation promotes T cell activation and the production of IL-6, G-CSF, SCF, and multiple pro-inflammatory chemokines (4, 7, 9, 10). IL-17A and IL-17F synergize with TNF-alpha in the induction of CXCL1, G-CSF, and IL-6 (9, 11). This effect requires the presence of both TNF RI and TNF RII (9). IL-17 interactions with IL-17 R also inhibit the TNF-alpha induced upregulation of fibroblast CCL5 and VCAM-1 (11). CCL5 and VCAM-1 induced effects are differentially sensitive to blockade with IL-17 R specific antibodies, suggesting that IL-17 R triggers divergent intracellular signals (11). In vivo, IL‑17 R activity is important for increased generation of neutrophils and their recruitment to sites of inflammation (10, 12, 13). IL-17 R is required for host defense against microbial infection and for the progression of arthritis from inflammation to destructive joint erosion (10, 13).
Iwakura, Y. and H. Ishigame (2006) J. Clin. Invest. 116:1218.
Moseley, T.A. et al. (2003) Cytokine Growth Factor Rev. 14:155.
Kawaguchi, M. et al. (2004) J. Allergy Clin. Immunol. 114:1265.
Yao, Z. et al. (1995) Immunity 3:811.
Novatchkova, M. et al. (2003) Trends Biochem. Sci. 28:226.
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