Description: The monoclonal antibody PAJ-17R recognizes mouse IL-17 receptor A (IL-17RA) also known as CD217. This single transmembrane domain-containing receptor can homo- or heterodimerize with IL-17RC or IL-17RB. IL-17RA binds to IL-17A, IL-17F(cytokines of the Th 17 lineage), or IL-17E (IL-25). Ligand binding to the single subunit of IL-17RA has been shown to induce homo- or heterodimerization of the receptor complex that in turn recruits Act-1 via the SEFIR domains leading to recruitment of TRAF6 and signaling through the NFκB and MAPK pathways.
Initial reports suggested ubiquitous expression of IL-17RA based on binding studies with IL-17-Fc and expression of mRNA. Interestingly, despite this, not all cells expressing the receptor respond to IL-17A. In particular, resting T cells do not respond. It is not known if the expression level of IL-17RA protein varies or if some cells express the receptor but are not able to activate downstream signaling events. Recent evidence suggests a more limited expression profile based on IL-17RA knock-out mice which display decreased numbers of neutrophils with impaired function in response to challenge with K. pneumonia or Candida albicans. This suggests IL-17RA plays a more dominant and critical role in neutrophil development and function. Our studies suggest that expression can be found on abundantly on Gr-1dim population and many of the Gr-1bright bone marrow cells, as well as some F4/80 positive cells. This staining with PAJ-17R is not detected in IL-17RA knock-out mice.
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