Fig 1: Epitope mapping. (a) The binding epitope for the parental mouse anti-human IL-36R antibody and for the rat anti-mouse IL-36R antibody was mapped by hydrogen-deuterium exchange mass spectrometry. Both antibodies show overlapping binding preference to domain-2 on IL-36R. (b) A homology model of IL-36R extracellular domain, highlighting the overlapping binding epitope for mMAB92 and MAB04 on domain-2.
Fig 2: IL-36R signaling. Binding of the proteolytically maturated agonistic IL-36 ligands (α, β and γ) to the IL-36R results in the recruitment of the co-receptor (IL-1RAcP) and lead to activation of the NFκB, MAPK and ERK. Intracellular signaling activates gene transcription of proinflammatory mediators. IL-36Ra competes with IL-36 for IL-36R binding, thereby acting as an IL-36 antagonist. IL-36 can directly or indirectly stimulate various cellular responses and is involved in models of psoriasis and in generalized pustular psoriasis in humans. Binding of MAB92 to huIL-36R would antagonize the IL-36R signaling.
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