PACAP (1-38), human, ovine, rat TFA is a neuropeptide with 38 amino acid residues. PACAP (1-38) binds to PACAP type I receptor, PACAP type II receptor VIP1, and PACAP type II receptor VIP2 with IC50s of 4 nM, 2 nM, and 1 nM, respectively.
CAT No: R1592
Synonyms/Alias:Pituitary Adenylate Cyclase Activating Polypeptide 38 (TFA)
PACAP (1-38), human, ovine, rat TFA is a synthetic peptide corresponding to the full-length sequence of pituitary adenylate cyclase-activating polypeptide (PACAP) comprising 38 amino acids, with trifluoroacetate as the counterion. As a highly conserved neuropeptide, PACAP (1-38) is recognized for its significant role in neuroendocrine signaling, neurotransmission, and neuroprotection across multiple species including humans, sheep, and rats. Its broad physiological relevance and evolutionary conservation have made it an indispensable tool in peptide-based research, particularly in studies exploring G protein-coupled receptor signaling, neuropeptide function, and peptide-receptor interactions. The availability of this peptide in a chemically defined format supports detailed investigations into its mechanisms of action and functional diversity.
Receptor pharmacology: PACAP (1-38) is widely utilized in studies examining the activation and signaling dynamics of PAC1, VPAC1, and VPAC2 receptors, which are members of the class B G protein-coupled receptor family. Researchers employ the peptide to characterize receptor binding affinities, delineate downstream second messenger pathways such as cAMP accumulation, and assess receptor specificity. These investigations are crucial for understanding the molecular basis of neuropeptide-receptor interactions, mapping receptor distribution, and identifying potential modulatory mechanisms relevant to neuroendocrine communication.
Neuroscience research: The peptide serves as a key experimental tool for elucidating the physiological and pathophysiological roles of PACAP in central and peripheral nervous system function. Its application in in vitro and in vivo models enables detailed study of synaptic plasticity, neurogenesis, and neuroprotection. By modulating neuronal excitability and survival, PACAP (1-38) facilitates research into mechanisms underlying neurodevelopment, stress responses, and neuronal injury, providing insight into fundamental aspects of neural regulation.
Endocrine signaling studies: PACAP (1-38) is instrumental in investigating the regulation of hormone secretion and intracellular signaling cascades in various endocrine tissues. Its potent stimulatory effects on adenylate cyclase activity make it a valuable probe for dissecting the molecular events governing hormone release from pituitary, pancreatic, and adrenal cells. These studies advance understanding of neuropeptide-mediated control of endocrine function and the integration of neuroendocrine axes.
Peptide structure-function analysis: The full-length 38-residue sequence of PACAP enables detailed structure-activity relationship (SAR) studies, where modifications to specific amino acid residues or truncations can be compared to the native peptide. Such research supports the identification of critical determinants for receptor activation, selectivity, and biological efficacy. Insights gained from SAR analyses are essential for the rational design of peptide analogs and modulators with tailored pharmacological profiles.
Comparative and translational studies: The conserved sequence of PACAP (1-38) across human, ovine, and rat species allows for cross-species investigations into evolutionary aspects of neuropeptide function. Researchers leverage this peptide to compare signaling properties, receptor interactions, and physiological responses among different animal models, thereby enhancing the translational relevance of basic research findings. This comparative approach is particularly valuable for bridging preclinical studies with broader biological contexts and for validating mechanistic hypotheses across mammalian systems.
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