PACAP (1-27), human, ovine, rat, the N-terminal fragment of PACAP-38, is a potent PACAP receptor antagonist with IC50s of 3, 2, and 5 nM, respectively, for rat PAC1, rat VPAC1, and human VPAC2.
CAT No: R1590
CAS No:127317-03-7
Synonyms/Alias:PACAP 1-27, Pituitary Adenylate Cyclase Activating Polypeptide,
PACAP (1-27), human, ovine, rat, is a synthetic peptide corresponding to the biologically active N-terminal fragment of Pituitary Adenylate Cyclase-Activating Polypeptide (PACAP). This neuropeptide, highly conserved across species such as humans, sheep, and rats, is recognized for its potent regulatory roles in neuroendocrine signaling and as a key modulator within the central and peripheral nervous systems. Its structure enables selective interaction with PAC1, VPAC1, and VPAC2 receptors, making it a valuable molecular tool for the investigation of peptide-receptor dynamics, intracellular signaling pathways, and physiological processes influenced by PACAP family peptides. Researchers utilize this compound to elucidate mechanisms underlying neuronal communication, hormone secretion, and related cellular responses in both basic and translational studies.
Receptor Pharmacology Studies: PACAP (1-27) is widely employed to characterize the pharmacological properties of PACAP-specific and related G protein-coupled receptors. By serving as a reference ligand in binding and activation assays, it enables the dissection of receptor subtype selectivity, affinity profiles, and downstream signaling events. This supports the identification and validation of novel receptor modulators, aids in mapping functional domains, and provides foundational data for the development of new peptide analogs or small-molecule ligands targeting these neuropeptide receptors.
Neurobiology and Signal Transduction Research: The peptide is instrumental in exploring intracellular signaling cascades activated by PACAP receptor engagement, such as cAMP accumulation, calcium mobilization, and MAP kinase pathway modulation. Its use in neuronal and glial cell models facilitates the study of synaptic plasticity, neuroprotection, and cell survival mechanisms. By precisely mimicking endogenous PACAP activity, it enables researchers to delineate the molecular basis of neuropeptide-driven signal transduction and to investigate the interplay between peptide hormones and neuronal function.
Endocrine Regulation Investigations: PACAP (1-27) has proven essential for studying the regulation of hormone secretion from pituitary and peripheral endocrine tissues. In vitro and ex vivo systems utilize the peptide to probe the stimulus-secretion coupling mechanisms governing the release of growth hormone, prolactin, and other pituitary-derived hormones. This supports the elucidation of neuroendocrine feedback loops, the identification of regulatory checkpoints, and the understanding of species-specific differences in hormone control, informed by its cross-species sequence conservation.
Peptide Structure-Activity Relationship (SAR) Analysis: The compound's defined sequence and functional activity make it a benchmark molecule for structure-activity relationship studies within the PACAP family. Researchers employ it as a template to evaluate the impact of site-directed mutations, truncations, or chemical modifications on receptor binding and biological efficacy. Such SAR studies are crucial for advancing the rational design of peptide mimetics, antagonists, or stabilized analogs with tailored pharmacodynamic profiles for research applications.
Comparative Physiology and Evolutionary Biology: The availability of PACAP (1-27) in forms corresponding to human, ovine, and rat sequences enables comparative investigations into the evolutionary conservation and functional divergence of neuropeptide systems. It is used to assess interspecies differences in receptor activation, signaling efficiency, and physiological outcomes, providing insights into the adaptive significance of PACAP signaling pathways across vertebrate lineages. These studies contribute to a broader understanding of peptide hormone evolution and the molecular underpinnings of species-specific neuroendocrine regulation.
2. High fat diet and GLP-1 drugs induce pancreatic injury in mice
4. The spatiotemporal control of signalling and trafficking of the GLP-1R
5. Adipose tissue is a key organ for the beneficial effects of GLP-2 metabolic function
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