Human ACE/CD143 PE-conjugated Antibody

Catalog # Availability Size / Price Qty
FAB929P
Detection of ACE/CD143 in Human monocyte-derived dendritic cells by Flow Cytometry.
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Citations (2)
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Human ACE/CD143 PE-conjugated Antibody Summary

Species Reactivity
Human
Specificity
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.
Source
Monoclonal Mouse IgG1 Clone # 171417
Purification
Protein A or G purified from hybridoma culture supernatant
Immunogen
Mouse myeloma cell line NS0-derived recombinant human ACE/CD143
aa 30-1261
Formulation
Supplied in a saline solution containing BSA and Sodium Azide.
Label
Phycoerythrin (Excitation= 488 nm, Emission= 565-605 nm)

Applications

Recommended Concentration
Sample
Flow Cytometry
10 µL/106 cells
See below

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Scientific Data

Flow Cytometry Detection of ACE/CD143 antibody in Human monocyte-derived dendritic cells antibody by Flow Cytometry. View Larger

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 Mono-clonal Antibody (Catalog # FAB929P, filled histogram) or isotype control antibody (Catalog # IC002P, open histogram). View our protocol for Staining Membrane-associated Proteins.

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Preparation and Storage

Shipping
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.

Background: ACE/CD143

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).

References
  1. Soubrier, et al. (1988) Proc. Natl. Acad. Sci. USA 85:9386.
  2. Corvol, P. and T.A. Williams (1998) in Handbook of Proteolytic Enzymes. Barrett, A.J. et al. (eds): San Diego, Academic Press, p. 1066.
  3. Hu, et al. (2001) J. Biol. Chem. 276:47863.
  4. Kessler, et al. (2000) J. Biol. Chem. 275:26259.
  5. Eyries, et al. (2001) J. Biol. Chem. 276:5525.
  6. Alfalah, et al. (2001) J. Biol. Chem. 276:21105.
Long Name
Angiotensin I Converting Enzyme
Entrez Gene IDs
1636 (Human); 11421 (Mouse)
Alternate Names
ACE; ACE1angiotensin converting enzyme, somatic isoform; angiotensin I converting enzyme (peptidyl-dipeptidase A) 1; carboxycathepsin; CD143 antigen; CD143; DCP; DCP1; DCP1angiotensin-converting enzyme; dipeptidyl carboxypeptidase 1; Dipeptidyl carboxypeptidase I; EC 3.2.1.-; EC 3.4.15.1; Kininase II; MGC26566; MVCD3; peptidase P; testicular ECA

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Citations for Human ACE/CD143 PE-conjugated Antibody

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

2 Citations: Showing 1 - 2
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  1. Bovine Organospecific Microvascular Endothelial Cell Lines as New and Relevant In Vitro Models to Study Viral Infections
    Authors: Anne-Claire Lagrée, Fabienne Fasani, Clotilde Rouxel, Marine Pivet, Marie Pourcelot, Aurore Fablet et al.
    International Journal of Molecular Sciences
  2. Human haemato-endothelial precursors: cord blood CD34+ cells produce haemogenic endothelium.
    Authors: Pelosi E, Castelli G, Martin-Padura I, Bordoni V, Santoro S, Conigliaro A, Cerio A, De Santis Puzzonia M, Marighetti P, Biffoni M, Alonzi T, Amicone L, Alcalay M, Bertolini F, Testa U, Tripodi M
    PLoS ONE, 2012-12-04;7(12):e51109.
    Species: Human
    Sample Types: Whole Cells
    Applications: Flow Cytometry

FAQs

  1. Is ACE-1 the same as ACE?

    • Yes. ACE-1 is used as an alternative name, but not as commonly as ACE and CD143.

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