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(Rp)-cAMPS is a synthetic, cell-permeable analog of cyclic adenosine monophosphate (cAMP) in which the equatorial exocyclic oxygen atom in the cyclic phosphate moiety is replaced by sulfur. It acts as a potent and specific competitive antagonist of cAMP-induced activation of cAMP-dependent protein kinase A (PKA) types I and II. By binding to the regulatory subunits of PKA, it prevents cAMP from activating the kinase, thereby inhibiting downstream signaling pathways mediated by PKA. Unlike natural cAMP, (Rp)-cAMPS is resistant to hydrolysis by phosphodiesterases and exhibits increased lipophilicity, enhancing its membrane permeability in biological systems[2][3][4][6]. It is primarily used as a research tool for studying cAMP/PKA signaling mechanisms.
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