Secretin (33-59), rat is a 27-aa peptide, acts on secretin receptor, enhances the secretion of bicarbonate, enzymes, and K+ from the pancreas.
CAT No: R1670
CAS No:121028-49-7
Synonyms/Alias:Secretin (rat);121028-49-7;MFCD00167924;Secretin(rat)(9ci);AKOS024456856;DA-57775;TS-10275;
Secretin (33-59), rat is a synthetic peptide fragment corresponding to amino acid residues 33 through 59 of the rat secretin precursor. As a defined segment of the prosecretin sequence, this peptide is of significant interest in the study of peptide hormone biosynthesis, processing, and function within the gastrointestinal and neuroendocrine systems. Its unique sequence and origin from a well-characterized prohormone make it a valuable molecular tool for dissecting the roles of intermediate peptide fragments, mapping receptor interactions, and elucidating the mechanisms of peptide maturation and signaling in rodent models.
Peptide processing research: The 33-59 fragment of rat secretin is frequently utilized to investigate the enzymatic cleavage events that generate active secretin from its prohormone. By employing this peptide in in vitro systems or enzymatic assays, researchers can characterize the specificity and kinetics of prohormone convertases and other proteolytic enzymes involved in neuropeptide maturation. Such studies are crucial for understanding the regulation of peptide hormone biosynthesis at the molecular level and for identifying potential modulators of prosecretin processing.
Receptor binding and signaling studies: The structural features of this peptide fragment enable detailed analysis of its interactions with secretin receptors or related G protein-coupled receptors (GPCRs). By applying radiolabeled or fluorescently tagged versions of the 33-59 fragment, scientists can assess binding affinities, receptor selectivity, and downstream signaling pathways. These experiments provide valuable insights into the determinants of receptor recognition and the functional consequences of partial or truncated peptide ligands, supporting both fundamental receptor biology and pharmacological research.
Neuroendocrine pathway mapping: Given its origin within the secretin prohormone, the peptide serves as a useful tool for tracing the distribution and fate of precursor-derived fragments in neuroendocrine tissues. Immunochemical detection or mass spectrometry-based quantification of the 33-59 fragment in tissue extracts can help delineate the processing, transport, and storage of secretin-related peptides in the brain, pancreas, and gastrointestinal tract. Such mapping studies advance the understanding of peptide hormone trafficking and compartmentalization in both physiological and experimental contexts.
Antibody production and assay development: The defined epitope structure of the rat secretin (33-59) fragment makes it suitable as an immunogen for generating sequence-specific antibodies. These antibodies are instrumental in developing sensitive and selective immunoassays, such as ELISA or Western blot protocols, for detecting prosecretin intermediates. Employing this peptide as a standard or calibrator enhances the accuracy and reproducibility of quantitative peptide hormone analyses in complex biological samples.
Peptide structure-function analysis: The sequence and conformation of the 33-59 region provide a model system for exploring the relationship between primary structure and biological activity among neuropeptide fragments. By synthesizing analogs or introducing targeted modifications, researchers can systematically dissect the contributions of specific residues to peptide stability, receptor interaction, and bioactivity. These structure-function studies inform the rational design of novel peptide probes and support the broader field of peptide-based research tools in neurobiology and endocrinology.
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