Detects human ACE/CD143 in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant human ACE-2 is observed. Detects the surface expression of human ACE on full length ACE transfectants, but not on control transfectants by flow cytometry.
Monoclonal Mouse IgG1 Clone # 171417
Protein A or G purified from hybridoma culture supernatant
Mouse myeloma cell line NS0-derived recombinant human ACE/CD143 aa 30-1261
Supplied in a saline solution containing BSA and Sodium Azide.
Detection of ACE/CD143 in Human monocyte-derived dendritic cells by Flow Cytometry.
Human monocyte-derived dendritic cells were stained with Mouse Anti-Human ACE/CD143 PE‑conjugated Monoclonal Antibody (Catalog # FAB929P, filled histogram) or isotype control antibody (Catalog # IC002P, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
ACE (also known as peptidyl-dipetidase A) is a zinc metallopeptidase important for blood pressure control and water and salt metabolism (2). It cleaves the C-terminal dipeptide from angiotensin I to produce the potent vasopressor octapeptide angiotensin II and inactivates bradykinin by the sequential removal of two C-terminal dipeptides. In addition to the two physiological substrates, ACE cleaves C-terminal dipeptides from various oligopeptides with a free C-terminus. Because of its location and specificity, ACE plays additional roles in immunity, reproduction and neuropeptide regulation. For example, ACE degrades Alzheimer amyloid beta -peptide (A beta ), retards A beta aggregation, deposition, fibril formation, and inhibits cytotoxicity (3).
ACE is a type I membrane protein and exists in two isoforms (2). Somatic ACE, found in endothelial, epithelial and neuronal cells, comprises two highly similar domains called N- and C-domains, each of which contains the HExxH consensus sequence for zinc binding. Germinal ACE, found exclusively in the testes, comprises a single catalytically active domain identical to the C-domain of somatic ACE except for an N-terminal 67 residue germinal ACE-specific sequence. Physiological functions of the two tissue-specific isozymes are not interchangeable (4). For example, sperm-specific expression of the germinal ACE, not the somatic ACE, in ACE knockout male mice restored fertility.
Soluble ACE is present in many biological fluids, such as serum, seminal fluid, amniotic fluid and cerebrospinal fluid (2). The soluble ACE is derived from the membrane forms by actions of secretases or sheddases. The identities of the secretases have not been revealed, although they belong to the family of zinc metallopeptidases (5, 6).
Soubrier, et al. (1988) Proc. Natl. Acad. Sci. USA 85:9386.
Corvol, P. and T.A. Williams (1998) in Handbook of Proteolytic Enzymes. Barrett, A.J. et al. (eds): San Diego, Academic Press, p. 1066.
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