• 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

• Immunogen

  Mouse myeloma cell line NS0-derived recombinant human ACE/CD143    
  aa 30-1261

• Formulation

  Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.

• Label

  Alexa Fluor 594

Applications

• 
  

  Recommended    
  Concentration

  Sample

• Flow Cytometry

  0.25-1 µg/10    ⁶ cells

  Human mature dendritic cells

• 
  

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

Preparation and Storage

• Shipping

  The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

• Stability & Storage

  Store the unopened product at 2 - 8 °C. Do not use past expiration date.

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