Anti-ACE (N-terminus) Antibody

This Mouse monoclonal antibody targets the N-terminal region of angiotensin-converting enzyme (ACE), a zinc-dependent dipeptidyl carboxypeptidase that occupies a central role in the renin-angiotensin system by converting angiotensin I into the vasoactive peptide angiotensin II. Supplied by Antibodies.com as a 100 µl purified preparation in 0.1M Tris-Glycine buffer (pH 7.4) with 150 mM NaCl, 0.2% sodium azide, and 50% glycerol, the reagent is unconjugated and validated for Western blot (WB) detection in human and mouse samples.

The N-terminal half of somatic ACE forms one of the enzyme's two homologous catalytic domains, each containing a HEXXH zinc-binding motif and an active site with overlapping but distinct substrate preferences. This region is shared between the full-length somatic isoform expressed in vascular endothelium, kidney, and lung, and the shorter testis isoform that arises from an internal promoter within the same gene. Researchers probing ACE expression in vascular biology, cardiac and renal tissue remodeling, or models of hypertensive and diabetic organ damage routinely detect the protein by immunoblotting cell lysates and tissue homogenates.

ACE is a heavily N-glycosylated type I transmembrane ectoenzyme whose apparent molecular weight on SDS-PAGE exceeds the calculated mass of its 1306-residue somatic polypeptide due to glycan addition. The monoclonal format reduces lot-to-lot variability, and shipping in 50% glycerol allows storage at -20°C with minimal freeze-thaw damage. The buffer composition also preserves antibody activity for downstream immunoblotting at standard working dilutions in reducing Laemmli sample buffer.