Angiotensin Converting Enzyme 1 Recombinant Rabbit mAb, PBS Only (SDT-2662-122)

Angiotensin-Converting Enzyme 1 (ACE1) is a zinc-dependent dipeptidyl carboxypeptidase expressed as a 1,306-amino-acid type-I transmembrane glycoprotein, with the bulk of its structure (residues 1–1230) projecting into the extracellular space and containing two homologous catalytic N- and C-terminal domains, each bearing the characteristic HEXXH zinc-binding motif; by cleaving the decapeptide angiotensin I into the potent vasoconstrictor octapeptide angiotensin II, degrading the vasodilator bradykinin, and modulating additional vasoactive peptides, ACE1 sits at the apex of the renin–angiotensin–aldosterone system, thereby governing systemic blood pressure, extracellular fluid volume, and cardiovascular remodeling, while its genetic polymorphisms—most notably the Alu insertion/deletion (I/D) variant in intron 16—have been linked to inter-individual differences in circulating enzyme levels and risk for hypertension, myocardial infarction, diabetic nephropathy, and COVID-19 severity, making ACE1 a cornerstone target for therapeutic inhibitors such as captopril, enalapril, and lisinopril that are now mainstays in treating hypertension and heart failure.