Anti-Angiotensin Converting Enzyme 1/ACE Antibody Picoband® Fluoro647 Conjugated

Angiotensin-converting enzyme (ACE), an exopeptidase, is a circulating enzyme that participates in the body's renin-angiotensin system (RAS), which mediates extracellular volume (i.e. that of the blood plasma, lymph and interstitial fluid), and arterial vasoconstriction. It is secreted by pulmonary and renal endothelial cells and catalyzes the conversion of decapeptide angiotensin I to octapeptide angiotensin II. Using a DNA marker at the growth hormone gene locus, which they characterized as 'extremely polymorphic' and which showed no recombination with ACE, ACE was mapped to 17q22-q24, consistent with the in situ hybridization mapping to 17q23. ACE, or kininase II, is a dipeptidyl carboxypeptidase that plays an important role in blood pressure regulation and electrolyte balance by hydrolyzing angiotensin I into angiotensin II, a potent vasopressor, and aldosterone-stimulating peptide. The enzyme is also able to inactivate bradykinin, a potent vasodilator.

Angiotensin-converting enzyme; ACE;3.2.1.-;3.4.15.1; Dipeptidyl carboxypeptidase I; Kininase II; CD143; Angiotensin-converting enzyme, soluble form; ACE; DCP, DCP1

E.coli-derived human ACE recombinant protein (Position: K651-Y864) . Human ACE shares 73% and 76% amino acid (aa) sequences identity with mouse and rat ACE, respectively.

Ubiquitously expressed, with highest levels in lung, kidney, heart, gastrointestinal system and prostate. Isoform Testis-specific is expressed in spermatocytes and adult testis. .

Metalloprotease, Pathways and Processes, Proteolysis/Ubiquitin, Proteolytic Enzymes, Response To Hypoxia, Serum Proteins, Signal Transduction, Stem Cells, Surface Molecules, Vasculature, Vitamins/Minerals

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.

1. Kierszenbaum, Abraham L. (2007) . Histology and cell biology: an introduction to pathology. Mosby Elsevier 2. Jeunemaitre, X., Lifton, R. P., Hunt, S. C., Williams, R. R., Lalouel, J.-M. Absence of linkage between the angiotensin converting enzyme locus and human essential hypertension. Nature Genet. 1: 72-75, 1992. 3. Mattei, M.-G., Hubert, C., Alhenc-Gelas, F., Roeckel, N., Corvol, P., Soubrier, F. Angiotensin-I converting enzyme gene is on chromosome 17. (Abstract) Cytogenet. Cell Genet. 51: 1041, 1989.