Pancreatic Polypeptide, human is a C-terminally amidated 36 amino acid peptide, which acts as a neuropeptide Y (NPY) Y4/Y5 receptor agonist.
CAT No: R1600
CAS No:75976-10-2
Synonyms/Alias:75976-10-2;59763-91-6;CHEMBL4540843;CID 24868176;BDBM50528183;AKOS024456422;NCGC00167143-01;DA-66474;DA-76584;Pancreatic Polypeptide (human) trifluoroacetate salt;
Pancreatic Polypeptide, human is a biologically active peptide hormone composed of 36 amino acids, primarily secreted by the pancreatic F cells. It plays a pivotal role in regulating pancreatic secretion activities and gastrointestinal motility, and is recognized for its involvement in the complex interplay of metabolic and neuroendocrine signaling pathways. As a member of the neuropeptide Y (NPY) family, its sequence and structure are highly conserved among mammals, making it a valuable tool for comparative studies in endocrinology and metabolism. Its unique biochemical properties and physiological relevance have established this peptide as an essential reagent for a broad range of research applications in metabolic regulation, peptide receptor studies, and neuroendocrine system investigations.
Metabolic Regulation Research: Pancreatic polypeptide is widely utilized in studies investigating the regulation of food intake, energy homeostasis, and glucose metabolism. Researchers employ this peptide to elucidate its inhibitory effects on pancreatic exocrine secretion and its role in modulating hepatic glucose production. By incorporating it into in vitro and in vivo experimental models, investigators can dissect the signaling mechanisms underlying appetite regulation, insulin sensitivity, and the hormonal cross-talk that governs metabolic balance.
Peptide Receptor Characterization: The peptide serves as a critical ligand for the Y4 and Y5 receptor subtypes within the NPY receptor family. Its application in receptor binding assays and functional studies enables precise characterization of receptor-ligand interactions, downstream signaling pathways, and receptor pharmacology. Such research is instrumental in advancing the understanding of neuropeptide receptor specificity, affinity, and the physiological consequences of receptor activation in various tissues.
Neuroendocrine System Studies: Owing to its role as a neuroendocrine modulator, pancreatic polypeptide is frequently used to probe the functional connectivity between the pancreas, central nervous system, and peripheral organs. Experimental use of the peptide facilitates the exploration of neural circuits involved in appetite control, stress response, and autonomic regulation. These studies contribute to a broader comprehension of how peptide hormones integrate metabolic and behavioral responses at the systemic level.
Peptide Structure-Activity Relationship (SAR) Analysis: The human peptide is an exemplary model for investigating structure-activity relationships within the NPY family. Synthetic analogs and site-directed mutants are often compared to the native sequence to identify key residues responsible for receptor binding and biological activity. Such SAR studies provide valuable insights for the rational design of peptide-based probes, agonists, or antagonists, thereby supporting drug discovery and development efforts targeting peptide hormone systems.
Analytical Method Development: The well-defined sequence and stability of pancreatic polypeptide make it a preferred standard in the development and validation of analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and immunoassays. Its use as a reference compound aids in the accurate quantification and detection of peptide hormones in complex biological matrices, ensuring the reliability and reproducibility of bioanalytical methods in research and diagnostic contexts.
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