Atrial Natriuretic Peptide (ANP) (1-28), rat is a major circulating form of ANP in rats, potently inhibits Angiotensin II (Ang II)-stimulated endothelin-1 secretion in a concentration-dependent manner.
CAT No: R1223
CAS No:88898-17-3
Synonyms/Alias:Cardiodilatin;Cardiodilatin-126;88898-17-3;CDD-ANP-99-126;Atrial Natriuretic Peptide rat;Cardiodilation-atrial natriuretic peptide;92047-08-0;Atrial Natriuretic Factor (1-28) (mouse, rabbit, rat) H-Ser-Leu-Arg-Arg-Ser-Ser-Cys-Phe-Gly-Gly-Arg-Ile-Asp-Arg-Ile-Gly-Ala-Gln-Ser-Gly-Leu-Gly-Cys-Asn-Ser-Phe-Arg-Tyr-OH (Disulfide bond);AKOS024456849;Atrial natriuretic factor(1-28)(rat);FA73200;Atrial Natriuretic Peptide (1-28), rat;DA-61305;PD076374;Atrial Natriuretic Peptide rat, >=97% (HPLC);Atrial Natriuretic Factor (1-28) (mouse, rabbit, rat) trifluoroacetate salt;
Atrial Natriuretic Peptide (ANP) (1-28), rat is a synthetic peptide corresponding to the biologically active 28-amino acid sequence of the endogenous rat atrial natriuretic peptide. As a key regulator of cardiovascular homeostasis, ANP exerts its effects through binding to natriuretic peptide receptors, leading to cyclic GMP production and subsequent modulation of vascular tone, renal function, and fluid balance. Its molecular structure and conserved sequence make it an essential tool for dissecting the physiological and pathophysiological roles of natriuretic peptides in preclinical research. The availability of the rat-specific sequence enables translational studies that bridge basic biochemical investigation with animal model research, facilitating a deeper understanding of peptide signaling pathways.
Receptor pharmacology: ANP (1-28) is widely employed in studies characterizing the binding kinetics, selectivity, and downstream signaling of natriuretic peptide receptors, particularly NPR-A and NPR-C. By providing a defined ligand, researchers can elucidate receptor affinities, investigate receptor-ligand interaction dynamics, and map signaling cascades involving cyclic GMP in various cell types. This approach supports the development of receptor subtype-selective modulators and enhances the understanding of natriuretic peptide receptor biology in cardiovascular and renal tissues.
Signal transduction analysis: The peptide is instrumental in probing intracellular signaling pathways activated by natriuretic peptides, especially those involving guanylyl cyclase activity and cGMP-mediated responses. Application of ANP (1-28) in cultured cells or tissue preparations allows for the quantification of second messenger generation, kinase activation, and downstream effector modulation. Such studies are critical for delineating the molecular mechanisms by which natriuretic peptides exert vasodilatory and natriuretic effects, and for identifying novel regulatory checkpoints within these pathways.
Cardiovascular physiology research: In animal models, the rat-derived ANP (1-28) peptide serves as a tool for investigating the regulation of blood pressure, cardiac hypertrophy, and volume homeostasis. By administering the peptide in vivo or ex vivo, researchers can assess hemodynamic changes, renal excretory function, and neurohormonal interactions under physiological and experimental conditions. These studies contribute to the broader understanding of cardiovascular adaptation and maladaptation, and provide insight into the interplay between natriuretic peptides and other hormonal systems.
Renal function studies: ANP (1-28) is frequently utilized to examine its direct and indirect effects on renal hemodynamics, glomerular filtration, and tubular sodium handling. By modulating peptide concentrations in isolated kidney preparations, perfused organs, or animal models, investigators can dissect the mechanisms underlying natriuresis, diuresis, and renal vasodilation. This application is particularly valuable for clarifying the role of natriuretic peptides in fluid and electrolyte balance, as well as their interaction with the renin-angiotensin-aldosterone system.
Peptide structure-activity relationship (SAR) analysis: The defined sequence of ANP (1-28) enables its use in structure-activity studies aimed at identifying functional domains responsible for receptor binding and biological activity. Through site-directed mutagenesis, peptide analog synthesis, or comparative assays with truncated or modified forms, researchers can map critical residues and conformational features that govern peptide-receptor interactions. Insights gained from SAR investigations support the rational design of novel peptide analogs and contribute to the advancement of peptide-based research tools.
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