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

Angiotensin I converting enzyme (ACE), also called DCP or CD143 is a zinc-containing dipeptidyl carboxypeptidase widely distributed in mammalian tissues and is thought to play a critical role in blood pressure regulation. This gene is mapped to 17q23.3. This gene encodes an enzyme involved in catalyzing the conversion of angiotensin I into a physiologically active peptide angiotensin II. Angiotensin II is a potent vasopressor and aldosterone-stimulating peptide that controls blood pressure and fluid-electrolyte balance. This enzyme plays a key role in the renin-angiotensin system. Many studies have associated the presence or absence of a 287 bp Alu repeat element in this gene with the levels of circulating enzyme or cardiovascular pathophysiologies.

A synthetic peptide corresponding to a sequence at the C-terminus of mouse Ace, which shares 70.3% and 91.9% amino acid (aa) sequence identity with human and rat Ace, respectively.

Cancer, Cancer Metabolism, Cardiovascular, Cell Biology, Cofactors, Vitamins/Minerals, Hematopoietic Progenitors, Metabolism, Metabolism Processes, 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. This GPIase activity seems to be crucial for the egg-binding ability of the sperm.

1. Catarsi, P., Ravazzolo, R., Emma, F., Fruci, D., Finos, L., Frau, A., Morreale, G., Carrea, A., Ghiggeri, G. M. Angiotensin-converting enzyme (ACE) haplotypes and cyclosporine A (CsA) response: a model of the complex relationship between ACE quantitative trait locus and pathological phenotypes. Hum. Molec. Genet. 14: 2357-2367, 2005. 2. Hamdi, H. K., Reznik, J., Castellon, R., Atilano, S. R., Ong, J. M., Udar, N., Tavis, J. H., Aoki, A. M., Nesburn, A. B., Boyer, D. S., Small, K. W., Brown, D. J., Kenney, M. C. Alu DNA polymorphism in ACE gene is protective for age-related macular degeneration. Biochem. Biophys. Res. Commun. 295: 668-672, 2002.