Angiotensin 1 (Human) is the precursor to the vasoconstrictor peptide angiotensin II, cleaved by the angiotensin-converting enzyme (ACE).
CAT No: R1197
CAS No:484-42-4
Synonyms/Alias:ANGIOTENSIN I;484-42-4;Proangiotensin;Pepsitensin;Angiotensin I (human);Angiotensin I (human, mouse, rat);Human angiotensin I;Angiotensin I, ile(5)-;5-Ile-angiotensin I;Angiotensin I (rat);Angiotensin I (mouse);9041-90-1;CHEBI:2718;Angiotensin 1 Human;Asp-Arg-Val-Tyr-Ile-His-Pro-Phe-His-Leu;L-aspartyl-L-arginyl-L-valyl-L-tyrosyl-L-isoleucyl-L-histidyl-L-prolyl-L-phenylalanyl-L-histidyl-L-leucine;Angiotensin 1 (Human);Angiotensins; Angiotonin;AC1MIWSO;(Ile5)-Angiotensin I;(Ile5)-Ang I;5-Isoleucine-angiotensin I;Angiotensin I 5-isoleucine;UNII-9C880YQG7C;5-L-Isoleucine-angiotensin I;Angiotensin I, isoleucine(5)-;MFCD00167405;DRVYIHPFHL;Angiotensin I (Callithrix jacchus gene angt);9C880YQG7C;CHEMBL262670;Angiotensin I, 5-L-isoleucine-;DTXSID80866222;D-R-V-Y-I-H-P-F-H-L;HY-P1032;AKOS024456668;CS-7599;FA73185;NCGC00167129-01;L-Leucine, N-(N-(N-(1-(N-(N-(N-(N-(N2-L-alpha-aspartyl-L-arginyl)-L-valyl)-L-tyrosyl)-L-isoleucyl)-L-histidyl)-L-prolyl)-L-phenylalanyl)-L-histidyl)-;NS00074072;C00873;G12434;Q32039285;L-Asp-L-Arg-L-Val-L-Tyr-L-Ile-L-His-L-Pro-L-Phe-L-His-L-Leu;(2S)-2-[(2S)-2-[(2S)-2-{[(2S)-1-[(2S)-2-[(2S,3S)-2-[(2S)-2-[(2S)-2-[(2S)-2-[(2S)-2-AMINO-3-CARBOXYPROPANAMIDO]-5-CARBAMIMIDAMIDOPENTANAMIDO]-3-METHYLBUTANAMIDO]-3-(4-HYDROXYPHENYL)PROPANAMIDO]-3-METHYLPENTANAMIDO]-3-(1H-IMIDAZOL-4-YL)PROPANOYL]PYRROLIDIN-2-YL]FORMAMIDO}-3-PHENYLPROPANAMIDO]-3-(1H-IMIDAZOL-4-YL)PROPANAMIDO]-4-METHYLPENTANOIC ACID;L-alpha-aspartyl-L-arginyl-L-valyl-L-tyrosyl-L-isoleucyl-L-histidyl-L-prolyl-L-phenylalanyl-L-histidyl-L-leucine;Leucine, N-(N-(N-(1-(N-(N-(N-(N-(N2-L-alpha-aspartyl-L-arginyl)-L-valyl)-L-tyrosyl)-L-isoleucyl)-L-histidyl)-L-prolyl)-3-phenylalanyl)-L-histidyl)-, L-;
Angiotensin 1 Human is a synthetic peptide corresponding to the naturally occurring decapeptide fragment generated from the enzymatic cleavage of angiotensinogen by renin in the renin-angiotensin system (RAS). As a key intermediate in the RAS pathway, it plays a pivotal role in the regulation of blood pressure, fluid balance, and electrolyte homeostasis. The unique sequence and biochemical properties of this peptide make it highly relevant for researchers investigating cardiovascular physiology, peptide signaling cascades, and the molecular mechanisms underlying hypertension and related disorders. Its defined structure and activity profile provide a valuable tool for dissecting the complex interplay between peptide hormones, their receptors, and downstream effectors within mammalian systems.
Peptide signaling research: Angiotensin I serves as a crucial substrate for angiotensin-converting enzyme (ACE), which processes it into the potent vasoconstrictor angiotensin II. Researchers utilize this peptide to study the enzymatic kinetics and substrate specificity of ACE and related peptidases. By examining the conversion of angiotensin I in controlled in vitro systems, investigators gain critical insights into the regulation of peptide hormone activation, the modulation of vascular tone, and the development of pharmacological inhibitors targeting the RAS pathway.
Receptor interaction studies: While angiotensin I itself does not directly activate classical angiotensin receptors, it provides an essential starting point for generating downstream bioactive peptides. Experimental use of this decapeptide allows for the assessment of receptor binding, signaling selectivity, and the functional consequences of peptide processing. Through such studies, scientists can explore the impact of precursor-product relationships on receptor activation profiles and elucidate the molecular determinants governing peptide-receptor interactions in cardiovascular and renal tissues.
Peptide synthesis and analytical validation: Angiotensin I Human is widely employed as a reference standard and positive control in peptide synthesis, purification, and analytical method development. Its well-characterized sequence enables laboratories to optimize solid-phase peptide synthesis protocols, validate chromatographic separation techniques, and calibrate mass spectrometry instruments. The availability of this peptide in a defined form supports rigorous quality assurance processes and facilitates the development of robust analytical workflows for peptide-based research.
Enzymology and inhibitor screening: The decapeptide is instrumental in assays designed to assess the activity of ACE and other peptidases involved in the RAS. By serving as a substrate in enzymatic assays, it enables precise measurement of enzyme kinetics, substrate affinity, and inhibitor potency. This application is particularly valuable in the early-stage screening and characterization of novel ACE inhibitors, supporting drug discovery efforts and mechanistic studies in cardiovascular research.
Pathway elucidation and mechanistic modeling: The use of angiotensin I in experimental models allows researchers to map the sequence of biochemical events within the RAS cascade. By systematically introducing this peptide into cell culture systems, tissue preparations, or biochemical assays, investigators can track its conversion, monitor downstream metabolite production, and model the dynamic regulation of the angiotensin axis. Such studies provide a foundation for understanding the physiological and pathological roles of peptide intermediates and inform the rational design of interventions targeting the RAS at multiple levels.
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