Amylin (8-37), rat is a truncated analog of native Amylin that selectively inhibits insulin-related glucose uptake and glycogen deposition in muscle tissue. Amylin (8-37), rat is a weak amylin receptor (AMY) antagonist.
CAT No: R1187
CAS No:138398-61-5
Synonyms/Alias:138398-61-5;Amylin (8-37) (mouse, rat);Amylin (8-37) (rat);MFCD00214573;Amylin(8-37)(rat);DA-61036;G12499;
Amylin (8-37), rat is a synthetic peptide fragment corresponding to residues 8 through 37 of the rat amylin protein, also known as islet amyloid polypeptide (IAPP). As a truncated form lacking the N-terminal segment, this peptide acts as a well-characterized antagonist of amylin receptors. Amylin is a hormone co-secreted with insulin by pancreatic β-cells and is implicated in glucose metabolism, satiety, and the pathophysiology of type 2 diabetes, particularly in the formation of islet amyloid deposits. The (8-37) fragment retains receptor-binding capacity but lacks agonist activity, enabling selective modulation of amylin-mediated signaling pathways. Researchers utilize this peptide to dissect the physiological and pathological roles of amylin in metabolic regulation and amyloidogenesis, making it a valuable tool in endocrinology, neurobiology, and diabetes research.
Receptor antagonism studies: Amylin (8-37), rat is widely employed as a competitive antagonist in investigations of amylin receptor function. By selectively blocking amylin receptors, the peptide allows researchers to distinguish between amylin-dependent and independent signaling events in target tissues such as the pancreas, hypothalamus, and central nervous system. This application is critical for elucidating the physiological actions of endogenous amylin, including its influence on satiety, gastric emptying, and glucose homeostasis, as well as for identifying downstream signaling cascades that are specifically triggered by amylin-receptor activation.
Metabolic and endocrine research: The peptide serves as a key experimental tool for probing the role of amylin in metabolic regulation. By inhibiting endogenous amylin activity, it enables the assessment of amylin's contribution to glucose uptake, insulin secretion, and energy balance in both in vitro and in vivo models. Studies utilizing this antagonist help clarify the interplay between amylin and other metabolic hormones, providing insights into the mechanisms underlying β-cell function and dysfunction in metabolic disorders such as obesity and diabetes.
Amyloidogenesis and protein aggregation assays: Amylin (8-37), rat is frequently used in studies examining the aggregation and amyloidogenic properties of full-length amylin. The truncated peptide can modulate or compete with native amylin for fibril formation, serving as an investigative tool in biophysical assays that monitor amyloid assembly kinetics, oligomerization, and cytotoxicity. These applications are instrumental in understanding the molecular basis of islet amyloid deposition and its pathological consequences in pancreatic tissue.
Neurobiological investigations: Researchers utilize the antagonist properties of this peptide to explore the central effects of amylin signaling, particularly in the regulation of appetite, feeding behavior, and energy expenditure. By blocking amylin receptors in neural tissues, the peptide enables dissection of the neural circuits and neurotransmitter systems modulated by amylin, supporting studies in neuroendocrinology and behavioral neuroscience. Such applications contribute to a deeper understanding of how peripheral metabolic signals are integrated within the central nervous system.
Peptide-receptor interaction studies: The defined sequence and high specificity of Amylin (8-37), rat make it a valuable model for characterizing peptide-receptor binding interactions. It is commonly used in binding affinity assays, structure-activity relationship analyses, and receptor mapping experiments to delineate the molecular determinants of amylin receptor recognition. These studies inform the rational design of novel amylin analogs, receptor modulators, and peptide-based probes, advancing both basic science and translational research in peptide hormone biology.
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