angiotensin i

Angiotensin I/II (1-5) is a peptide (ASP-ARG-VAL-TYR-ILE) that contains the amino acids 1-5 and is converted from Angiotensin I/II.

Angiotensin I/II (1-6) is a peptide (ASP-ARG-VAL-TYR-ILE-HIS) that contains the amino acids 1-6 and is converted from Angiotensin I/II peptide.

Angiotensin I (human, mouse, rat) is the precursor to the vasoconstrictor peptide angiotensin II, cleaved by the angiotensin-converting enzyme (ACE). This peptide hormone causes vasoconstriction and increases blood pressure as part of the renin–angiotensin system, also stimulating aldosterone release from the adrenal cortex to promote sodium retention by the kidneys.

Angiotensin I, asn(1)-val(5)-gly(9)- is isolated from the plasma of American eel, Anquilla rostrata.

Angiotensin I II (1-6) TFA is a chemical compound comprising amino acids 1-6, derived from the Angiotensin I II peptide. This peptide is formed by the cleavage of angiotensinogen by renin, with Angiotensin I subsequently hydrolyzed by angiotensin-converting enzyme (ACE) to produce biologically active Angiotensin II. Angiotensin II has been extensively studied for its potential applications in the treatment of Hypertension, Renin Angiotensin System, and Idiopathic Membranous Nephropathy[1][2][3].

Abz-FR-K(Dnp)-P-OH acetate is an excellent angiotensin I-converting enzyme (ACE) substrate with a Km value of 4.0 μM and a kcat value of 210s-1.

Angiotensin 1/2 (1-9)TFA is containing the amino acids 1-9 that are converted from Angiotensin I/II peptide.

Nitrosoglutathione (GSNO) is an endogenous transnitrosation donor involved in S-nitrosation of a variety of cellular proteins. GSNO, an exogenous NO donor and substrate of rat alcohol dehydrogenase class III isoenzyme, inhibits cerebral angiotensin II-dependent and -independent AT1 receptor responses.

H-Val-Pro-Pro-OH is an inhibitor of Angiotensin I converting enzyme (ACE)( IC50 : 9 μM).

N-Hippuryl-His-Leu hydrate (N-Benzoyl-Gly-His-Leu hydrate) is a peptide compound that is an angiotensin-converting enzyme (ACE) substrate and can be used as a model peptide for measuring ACE-I inhibitory activity.

Angiotensinogen is a serum globulin formed by the liver that is cleaved by renin to form angiotensin I. Angiotensinogen is also called angiotensin precursor.

Excellent angiotensin I-converting enzyme (ACE) substrate with a Km value of 4.0 μM and a kcat value of 210s-1.

Angiotensin 1 2 (1-9) is containing the amino acids 1-9 that are converted from Angiotensin I II peptide.

Hippuryl-His-Leu-OH serves as a substrate to measure angiotensin I converting enzyme activity. Upon its cleavage, the resultant His-Leu moiety reacts with o-phthaldialdehyde or Fluorescamine, facilitating fluorescence detection [1] [2] [3].

Angiotensin II human TFA, a potent vasoconstrictor within the renin/angiotensin system, plays a pivotal role in human blood pressure regulation primarily through interactions with the G-protein-coupled receptors Angiotensin II type 1 receptor (AT1R) and Angiotensin II type 2 receptor (AT2R). It not only prompts sympathetic nervous stimulation, aldosterone biosynthesis, and renal effects but also fosters growth in vascular smooth muscle cells and boosts collagen type I and III synthesis in fibroblasts. This action results in the thickening of the vascular wall and myocardium, alongside fibrosis. Additionally, Angiotensin II human TFA triggers apoptosis and encourages capillary formation from endothelial cells through the LOX-1 dependent redox-sensitive pathway [1] [2] [3] [4].

NH2-AKK-COOH, a synthetic tripeptide, acts as an ACE inhibitor with IC50 values of 0.090 μM, 0.178 μM, and 420.89 μM against substrates FAPGG, HHL, and angiotensin-I, respectively [1].

Saralasin TFA ([Sar1,Ala8] Angiotensin II) is a synthetic octapeptide analog of angiotensin II, functioning as a competitive antagonist at angiotensin II receptors with a K i value of 0.32 nM for 74% of its binding sites, while also exhibiting partial agonist activity. It is utilized in the study of renovascular and renin-dependent (angiotensinogenic) hypertension [1] [3] [6].