Angiotensin II Acetate is a potent research peptide regulating blood pressure and vascular tone. Purchase this synthetic peptide to support cardiovascular and renal studies.
CAT No: 10-101-03
CAS No:4474-91-3 (net)
Synonyms/Alias:68521-88-0;Angiotensin II acetate;Angiotensin II human acetate;Human angiotensin II acetate salt;ASP-ARG-VAL-TYR-ILE-HIS-PRO-PHE ACETATE SALT;Angiotensin II human (acetate);32044-01-2;Angiotensin II acetate salt;Angiotensin II acetate (USAN);Angiotensin II acetate [USAN];Angiotensin II acetate human;UNII-31L3HS630A;(Ile5)-Angiotensin II acetate;Giapreza (TN);Angiotensin ii triacetate;Angiotensin II monoacetate;Angiotensin II, 5-L-isoleucine-, acetate (salt);Angiotensin II, 5-L-isoleucine-, monoacetate (salt);SCHEMBL1585377;CHEMBL3989932;31L3HS630A;Angiotensin II (human) (acetate);DTXSID501027705;Angiotensin II, human acetate salt;H-Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-OH; H-DRVYIHPF-OH;HY-13948A;MFCD00133092;AKOS040759453;CCG-270639;DA-70863;FA108510;MS-31969;CS-0102935;D11142;G12348;Q27256060;Angiotensin II acetate;Ang II acetate;DRVYIHPF acetate;(3S)-3-amino-3-{[(1S)-4-carbamimidamido-1-{[(1S)-1-{[(1S)-1-{[(1S,2S)-1-{[(2S)-1-[(2S)-2-{[(1S)-1-carboxy-2-phenylethyl]carbamoyl}pyrrolidin-1-yl]-3-(1H-imidazol-4-yl)-1-oxopropan-2-yl]carbamoyl}-2-methylbutyl]carbamoyl}-2-(4-hydroxyphenyl)ethyl]carbamoyl}-2-methylpropyl]carbamoyl}butyl]carbamoyl}propanoic acid; acetic acid;
Chemical Name:acetic acid;(3S)-3-amino-4-[[(2S)-1-[[(2S)-1-[[(2S)-1-[[(2S,3S)-1-[[(2S)-1-[(2S)-2-[[(1S)-1-carboxy-2-phenylethyl]carbamoyl]pyrrolidin-1-yl]-3-(1H-imidazol-5-yl)-1-oxopropan-2-yl]amino]-3-methyl-1-oxopentan-2-yl]amino]-3-(4-hydroxyphenyl)-1-oxopropan-2-yl]amino]-3-methyl-1-oxobutan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-4-oxobutanoic acid
Angiotensin II Acetate is a synthetic peptide corresponding to the naturally occurring octapeptide hormone angiotensin II, presented here as its acetate salt form. As a key effector molecule within the renin-angiotensin system, it plays a central role in the regulation of blood pressure, fluid balance, and electrolyte homeostasis in mammalian physiology. Its potent vasoconstrictive properties and involvement in diverse cellular signaling pathways have made it a critical tool in cardiovascular, renal, and endocrine research. The biochemical relevance of angiotensin II, combined with the stability and solubility advantages provided by the acetate form, makes this compound highly valuable for a wide range of experimental applications in both basic and applied life sciences.
Receptor binding studies: Angiotensin II Acetate is widely employed in the characterization and quantification of angiotensin II receptors, particularly the AT1 and AT2 subtypes, in various tissue preparations and cell lines. By serving as a reference ligand in radioligand binding assays or as a competitor in displacement studies, it enables researchers to elucidate receptor density, affinity, and pharmacological profiles. Such investigations are fundamental for mapping receptor distribution, understanding ligand-receptor interactions, and supporting the development of novel receptor modulators.
Signal transduction research: The peptide is integral to experiments dissecting the downstream signaling events triggered by angiotensin II receptor activation. Its application in cell-based assays allows for the controlled stimulation of pathways such as phospholipase C activation, inositol phosphate turnover, calcium mobilization, and MAP kinase cascades. These studies provide mechanistic insight into how angiotensin II mediates physiological responses, facilitates cross-talk with other signaling networks, and contributes to pathophysiological processes such as hypertrophy, fibrosis, and inflammation.
Vascular function assays: Angiotensin II Acetate is routinely used in ex vivo and in vitro vascular preparations, such as isolated vessel rings or perfused organ systems, to induce vasoconstriction and assess vascular reactivity. By applying defined concentrations of the peptide, researchers can evaluate endothelial function, smooth muscle contractility, and the influence of pharmacological agents on vascular tone. These assays are essential for investigating the molecular basis of blood pressure regulation and for screening potential antihypertensive compounds.
Renal physiology investigations: The compound serves as a critical experimental tool in studies exploring the regulation of renal hemodynamics, sodium transport, and glomerular filtration. Its ability to mimic endogenous angiotensin II actions allows researchers to probe the peptide's effects on renal arteriolar constriction, tubular reabsorption processes, and the modulation of renin secretion. Such applications are central to advancing the understanding of kidney function, fluid balance, and the pathogenesis of hypertension and related disorders.
Peptide signaling modulation: Beyond its primary physiological roles, Angiotensin II Acetate is valuable in studies designed to modulate or inhibit peptide-driven signaling pathways. It is often used to validate the specificity and efficacy of angiotensin receptor antagonists, enzyme inhibitors, or peptide analogs in both biochemical and cellular models. These applications support drug discovery efforts, structure-activity relationship analyses, and the identification of novel modulators targeting the renin-angiotensin system.
Numerous clinical and laboratory data are now available supporting the hypothesis that the renin-angiotensin system is mechanistically relevant in the pathogenesis of atherosclerosis. The traditional role of the renin-angiotensin system in the context of blood pressure regulation has been modified to incorporate the concept that angiotensin II (Ang II) is a potent proinflammatory agent. In vascular cells, Ang II is a potent stimulus for the generation of reactive oxygen species. As a result, Ang II upregulates the expression of many redox-sensitive cytokines, chemokines, and growth factors that have been implicated in the pathogenesis of atherosclerosis. Extensive data now confirm that inhibition of the renin-angiotensin system inhibits atherosclerosis in animal models as well as in humans. These studies provide mechanistic insights into the precise role of Ang II in atherosclerosis and suggest that pharmacologic interventions involving the renin-angiotensin system may be of fundamental importance in the treatment and prevention of atherosclerosis.
Weiss D, Sorescu D, Taylor W R. Angiotensin II and atherosclerosis[J]. The American journal of cardiology, 2001, 87(8): 25-32.
Angiotensin II (Ang II) is a potent effector peptide of the renin-angiotensin system that exerts a wide variety of physiological actions on the cardiovascular, renal, endocrine, and central and peripheral nervous systems. Angiotensin exerts its actions by binding to specific receptors in the plasma membrane of various tissues. Structure-activity relationship studies and competition-binding experiments have identified a potency series of angiotensin analogues. Such studies have demonstrated that target organs display different preferences for Ang II and homologues such as Ang III and des-[Phe8] angiotensin II. Similarly, agents that normally are considered to be pure receptor antagonists for a given response (tissue) are full agonists in other tissues. Indirect evidence obtained from the above studies have led to the speculation that there are multiple angiotensin receptor subtypes among various tissues as well as within single cell types. Multiple mechanisms of signal transduction have been demonstrated for angiotensin. For example, depending on the effector organ, angiotensin stimulates phosphoinositide turnover and release of internal calcium, modulates voltage-dependent calcium channels, directly activates calcium channels, and inhibits adenylate cyclase activity. Recently, the identification of selective, high-affinity peptide and nonpeptide antagonists has resulted in further characterization of angiotensin receptors into distinct subtypes. In addition, dithiothreitol, an agent that reduces disulfide bridges, has been a useful tool in the characterization of angiotensin receptors as the subtypes apparently are not affected equally by this agent. However, further work needs to be performed to characterize angiotensin receptors with respect to heterogeneity, structure, transducing mechanisms, and physiological function.
Peach M J, Dostal D E. The angiotensin II receptor and the actions of angiotensin II[J]. Journal of cardiovascular pharmacology, 1990, 16: S25&hyhen.
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