Angiotensin I converting enzyme (ACE1), a dipeptidyl carboxypeptidase, is part of the renin-angiotensin system (RAS) that controls regulation of blood pressure by cleaving the C-terminal dipeptides of angiotensin I and bradykinin.
Fluorescent
Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.
ACE2
Angiotensin-converting enzyme, ACE, Dipeptidyl carboxypeptidase I, Kininase II, DCP1, DCP, ACE
Angiotensin I converting enzyme (ACE1), a dipeptidyl carboxypeptidase, is part of the renin-angiotensin system (RAS) that controls regulation of blood pressure by cleaving the C-terminal dipeptides of angiotensin I and bradykinin.
Fluorescent
Microplate (12 x 8 well strips)
Blue Ice
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Angiotensin I converting enzyme (ACE1), a dipeptidyl carboxypeptidase, is part of the renin-angiotensin system (RAS) that controls regulation of blood pressure by cleaving the C-terminal dipeptides of angiotensin I and bradykinin.
This ACE1 Inhibitor Screening Kit can be used to screen for potent inhibitors of ACE1 activity to regulate hypertension. It utilizes the ability of an active ACE1 to cleave a synthetic o-aminobenzoyl peptide (Abz-based peptide substrate to release a free fluorophore). The released Abz can be easily quantified using a fluorescence microplate reader. In the presence of an ACE1 specific inhibitor, the enzyme loses its peptidase activity which results in decrease of fluorescence intensity. This assay kit is simple and can be used to identify and characterize ACE1 inhibitors in a high-throughput format.
This product is manufactured by BioVision, an Abcam company and was previously called K228 Angiotensin I Converting Enzyme (ACE1) Inhibitor Screening Kit. K228-100 is the same size as the 100 test size of ab283372.
This supplementary information is collated from multiple sources and compiled automatically.
Angiotensin Converting Enzyme 1 also known as ACE1 or ACE is an important enzyme in the renin-angiotensin system. This enzyme exhibits a significant role in blood pressure regulation. ACE1 is a zinc-metallopeptidase with a molecular weight of approximately 130 kDa. It converts angiotensin I into the potent vasoconstrictor angiotensin II a critical function in cardiovascular physiology. ACE1 is widely expressed in endothelial cells particularly in the lungs kidneys and the small intestine.
The enzyme generates angiotensin II by cleaving angiotensin I. Angiotensin II an important effector peptide impacts cardiovascular and renal systems influencing vasoconstriction and fluid balance. While not directly forming a complex ACE1's activity increases the potency of angiotensin II which binds to angiotensin II receptors to exert its effects therefore indirectly forming a functional signaling complex.
ACE1 plays a central role in the renin-angiotensin system and the kallikrein-kinin system. The enzyme's activity boosts angiotensin II production which connects it to the regulation of blood pressure via the renin-angiotensin pathway. ACE1 also indirectly interacts with proteins like bradykinin by degrading them modulating kinin-related functions and influencing inflammation and tension in vascular smooth muscle.
Understanding ACE1 is important for addressing hypertension and congestive heart failure. ACE1's conversion of angiotensin I to angiotensin II means overactivity can cause elevated blood pressure leading to hypertension. This makes ACE inhibitors such as lisinopril and ramipril therapeutic for these conditions. Furthermore its connection with aldosterone production places ACE1 in relevance to heart failure as excessive aldosterone can cause detrimental remodeling of cardiac tissue.
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Inhibition of Angiotensin I Converting Enzyme activity by Angiotensin I Converting Enzyme Inhibitor Captopril. IC50 was 1.46 nM (n = 3).
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