Amylin, amide, human, a 37-amino acid polypeptide, is a pancreatic hormone cosecreted with insulin that exerts unique roles in metabolism and glucose homeostasis. Amylin, amide, human inhibits glucagon secretion, delays gastric emptying, and acts as a satiety agent.
CAT No: HB00087
CAS No:122384-88-7
Synonyms/Alias:Amylin, human amidated;122384-88-7;Diabetes Associated Peptide Amide human;Pancreatic amylin;Amlintide (USAN/INN);PAM-4219-V;D02913;Lys-Cys-Asn-Thr-Ala-Thr-Cys-Ala-Thr-Gln-Arg-Leu-Ala-Asn-Phe-Leu-Val-His-Ser-Ser-Asn-Asn-Phe-Gly-Ala-Ile-Leu-Ser-Ser-Thr-Asn-Val-Gly- Ser-Asn-Thr-Tyr-NH2IAPP: Islet Amyloid Polypeptide DAP: Diabetes-Associated Peptide;
Amylin, human amidated, is a 37-amino acid peptide hormone co-secreted with insulin by pancreatic β-cells. Its amidated C-terminus reflects the natural post-translational modification found in the endogenous human peptide, which is essential for full biological activity. As a key regulator of glucose metabolism, amylin participates in the modulation of glycemic control, gastric emptying, and satiety signaling. The peptide's structural and functional properties have made it a central target in metabolic research, especially in the context of diabetes, obesity, and neuroendocrine signaling. Its unique sequence and bioactivity support a wide range of experimental applications in both basic and applied biochemical studies.
Peptide research: Human amidated amylin is widely utilized as a reference standard and functional probe in peptide research, enabling detailed investigations into peptide folding, aggregation, and receptor interactions. Its precise sequence and post-translational modification make it invaluable for elucidating the molecular determinants of amyloid fibril formation, a phenomenon closely linked to islet amyloidosis in type 2 diabetes. By providing an authentic model of the native peptide, researchers can dissect the pathways of peptide aggregation, identify critical residues, and evaluate the impact of structural modifications on biological function.
Receptor binding studies: The peptide serves as a critical ligand for in vitro and cell-based assays aimed at characterizing the amylin receptor complex. Its high fidelity to the endogenous sequence allows for reproducible binding affinity measurements, signaling pathway analyses, and competitive inhibition assays. These studies facilitate the identification of receptor subtypes, the mapping of ligand-receptor interfaces, and the assessment of signal transduction mechanisms relevant to metabolic regulation and neuroendocrine communication.
Metabolic pathway analysis: Amidated amylin is frequently employed in metabolic research to investigate its role in glucose homeostasis, insulin action, and appetite regulation. Experimental models using the peptide enable the dissection of amylin's contribution to the suppression of postprandial glucagon secretion, modulation of gastric emptying rates, and influence on satiety signaling. Such studies provide insight into the integrated hormonal control of energy balance and inform the development of novel strategies for metabolic disorder research.
Peptide aggregation and amyloidogenesis: The propensity of human amylin to form amyloid fibrils is a focal point in studies of protein misfolding and aggregation. Researchers use the amidated peptide to model amyloidogenesis in vitro, allowing for the kinetic analysis of fibril formation, evaluation of aggregation inhibitors, and characterization of cytotoxic species. These investigations are essential for understanding the molecular basis of islet amyloidosis and its pathological consequences in metabolic diseases.
Analytical method development: Human amidated amylin is also applied as a calibration and reference standard in the development and validation of analytical techniques such as HPLC, mass spectrometry, and immunoassays. Its well-defined structure and chemical properties support the optimization of detection protocols, quantification methods, and the assessment of assay specificity and sensitivity. These applications are crucial for ensuring the accuracy and reliability of amylin measurements in research and quality control settings.
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