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cAMP signaling tools act on the second messenger cyclic AMP and on the proteins that read its signal. Cyclic adenosine monophosphate (cAMP) forms when receptors coupled to stimulatory G proteins activate adenylyl cyclases. In 1968, a cAMP-dependent enzyme, now called protein kinase A (PKA), was purified from rabbit skeletal muscle. Exchange proteins directly activated by cAMP (Epac), reported in 1998, activate the small guanosine triphosphatase (GTPase) Rap1. Sp-5,6-DCl-cBIMPS and cAMPS-Sp are cell-permeant cAMP analogs that activate PKA directly. ESI-09 blocks Epac1 and Epac2, whereas ESI-05 is selective for Epac2. SQ22536 lowers cAMP production in cells by inhibiting adenylyl cyclase activity. The Adenylyl Cyclase category covers the enzymes that synthesize the messenger.
PACAP-38 (16-38) is a cAMP agonist that significantly stimulates sympathetic neuronal production of neuropeptide Y (NPY) and catecholamines in human, mouse, and rat models. This peptide fragment exhibits potent and sustained biological activity, making it a valuable tool in research applications focused on signaling pathways involving cAMP modulation and neuroendocrine function.
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Synonyms: N6-Monobutyryl-cAMP
6-MB-cAMP is a membrane-permeable analog of cyclic AMP (cAMP) that functions as a cAMP agonist. This compound is utilized in research applications focused on studying intracellular signaling pathways and the modulation of various biological processes regulated by cAMP. Its ability to penetrate cell membranes allows for effective examination of cAMP-dependent mechanisms in diverse experimental settings.
