PACAP-38 (31-38), human, mouse, rat demonstrates potent, efficacious, and sustained stimulatory effects on sympathetic neuronal NPY and catecholamine production. PACAP is a potent activator of cAMP formation.
CAT No: R1596
CAS No:138764-85-9
Synonyms/Alias:138764-85-9;H-TYR-LYS-GLN-ARG-VAL-LYS-ASN-LYS-NH2;N-[1-[[1-[[6-amino-1-[[4-amino-1-[(1,6-diamino-1-oxohexan-2-yl)amino]-1,4-dioxobutan-2-yl]amino]-1-oxohexan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]-2-[[6-amino-2-[[2-amino-3-(4-hydroxyphenyl)propanoyl]amino]hexanoyl]amino]pentanediamide;PACAP-38 (31-38) (human, chicken, mouse, ovine, porcine, rat);FP109526;DS-017407;G12286;H-Tyr-Lys-Gln-Arg-Val-Lys-Asn-Lys-NH2; H-YKQRVKNK-NH2;PACAP-38 (31-38) (human, chicken, mouse, ovine, porcine, rat) trifluoroacetate salt;
PACAP-38 (31-38), human, mouse, rat is a peptide fragment corresponding to the C-terminal octapeptide of the pituitary adenylate cyclase-activating polypeptide (PACAP-38) sequence, conserved across human, mouse, and rat species. As a synthetic peptide, it represents residues 31 to 38 of the full-length PACAP-38, a neuropeptide known for its roles in neurotransmission, neuroprotection, and modulation of adenylate cyclase activity. This fragment is of significant interest in biochemical and pharmacological research, particularly for exploring structure-activity relationships and the functional domains of PACAP-38. Its defined sequence and species cross-reactivity make it a valuable tool for dissecting the specific contributions of the C-terminal region in PACAP-mediated signaling pathways.
Peptide structure-function analysis: Researchers utilize the 31-38 fragment of PACAP-38 to investigate the role of the C-terminal region in receptor binding and downstream signaling. By comparing the biological activity of this octapeptide with that of full-length PACAP-38 and other truncated analogs, scientists can delineate which peptide domains are essential for receptor interaction, activation, and specificity. Such studies are instrumental in mapping the minimal active sequence necessary for eliciting PACAP-related effects and can inform the rational design of novel peptide ligands or inhibitors.
Receptor binding studies: The defined sequence of PACAP-38 (31-38) enables its use in competitive binding assays to evaluate affinity for PAC1, VPAC1, and VPAC2 receptors. By employing this fragment in radioligand displacement or fluorescence-based binding experiments, researchers can characterize the contribution of the C-terminal residues to receptor subtype selectivity and binding kinetics. These insights are critical for understanding the molecular determinants of PACAP-receptor interactions and for developing selective modulators for neuropeptide signaling pathways.
Peptide synthesis and analytical standards: As a well-characterized peptide fragment, PACAP-38 (31-38) serves as a reference standard in peptide synthesis, quality control, and analytical method development. It is commonly used to validate chromatographic separation techniques, mass spectrometry protocols, and peptide quantification methods. The availability of this defined sequence supports the accurate calibration of analytical instruments and the benchmarking of synthetic peptide production processes, ensuring reproducibility and reliability in peptide research laboratories.
Functional assays in neurobiology: The octapeptide fragment is employed in in vitro and ex vivo assays to probe the contribution of the C-terminal domain to neuropeptide function. It can be applied to neuronal cultures, brain slices, or receptor-expressing cell lines to assess its ability to modulate cyclic AMP production, neurotransmitter release, or other downstream signaling events. These experiments facilitate the dissection of domain-specific activities within the PACAP-38 molecule, advancing the understanding of neuropeptide signaling mechanisms in the central and peripheral nervous systems.
Species-specific comparative studies: Given its sequence conservation among human, mouse, and rat, this peptide fragment enables cross-species investigations of PACAP-38 function and receptor pharmacology. Comparative studies using the 31-38 fragment help elucidate evolutionary conservation and divergence in neuropeptide signaling, providing insights into species-specific differences in receptor recognition and biological activity. Such research is valuable for translational studies, model organism validation, and the development of species-appropriate reagents for neuroscience and endocrinology research.
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