Amylin (IAPP), feline, a 37-amino acid polypeptide. Amylin (IAPP) is one of the major secretory products of β-cells of the pancreatic islets. Amylin (IAPP) is a regulatory peptide, which inhibits insulin and glucagon secretion.
CAT No: R1188
Amylin (IAPP), feline, is a peptide hormone that plays a crucial role in glucose metabolism and energy homeostasis in cats. Structurally, it is a 37-amino acid peptide co-secreted with insulin by pancreatic β-cells, and it is highly conserved across mammalian species, including felines. In the context of biochemical research, feline amylin is of particular interest due to its involvement in the regulation of blood glucose levels, inhibition of glucagon secretion, and modulation of gastric emptying. The peptide's propensity to aggregate into amyloid fibrils also links it to islet amyloidosis, a pathological hallmark observed in feline diabetes mellitus. Its unique sequence and aggregation properties make it a valuable target for comparative endocrinology, metabolic disease modeling, and amyloid research.
Peptide aggregation studies: Feline amylin is widely utilized in in vitro investigations of amyloidogenesis due to its intrinsic ability to form amyloid fibrils. Researchers employ this peptide to explore the molecular mechanisms underlying amyloid formation in the pancreas, which is a central feature of type 2 diabetes in cats. By examining the kinetics and structural aspects of feline IAPP aggregation, scientists can gain insights into the factors that drive amyloid deposition and identify potential modulators or inhibitors of this process. Such studies are critical for understanding species-specific differences in amyloidogenicity and for developing strategies to mitigate islet amyloidosis.
Comparative endocrinology: The peptide serves as a key tool in comparative studies examining the physiological roles of amylin across different mammalian species. Feline IAPP is particularly valuable for elucidating the similarities and distinctions in amylin function between cats, humans, and other animals. These investigations contribute to a deeper understanding of the evolutionary conservation of peptide hormones, as well as the divergence in their metabolic effects and pathological consequences. Such comparative analyses are essential for interpreting animal models of diabetes and for translating findings across species.
Metabolic pathway research: In metabolic studies, feline amylin provides a model system for dissecting the complex interplay between insulin, glucagon, and amylin in glucose regulation. Researchers use the peptide to probe its effects on glucose uptake, hepatic glucose output, and satiety signaling. By integrating feline IAPP into cell-based assays and ex vivo tissue models, investigators can map its signaling pathways and assess its impact on metabolic homeostasis. These approaches are instrumental in delineating the peptide's physiological roles and in identifying novel targets for metabolic intervention.
Protein interaction assays: The unique sequence and aggregation behavior of feline amylin facilitate its application in protein-protein interaction studies. Scientists employ the peptide to investigate its interactions with cellular chaperones, membrane components, and other regulatory proteins implicated in amyloid formation or β-cell function. Such assays are vital for unraveling the molecular partners that influence amylin's stability, aggregation propensity, and biological activity. These findings inform broader efforts to characterize the molecular environment of the pancreatic islet and to understand the determinants of β-cell health.
Analytical method development: The availability of pure, synthetic feline IAPP supports the development and validation of analytical techniques for peptide quantification, aggregation monitoring, and structural characterization. Researchers utilize this peptide as a standard or reference material in mass spectrometry, high-performance liquid chromatography, and spectroscopic assays. Its defined sequence and predictable aggregation profile make it an ideal candidate for optimizing protocols that require sensitive detection or precise measurement of amylin and related peptides in complex biological samples. Such methodological advances underpin accurate biochemical analysis in both basic and applied research settings.
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