Detects mouse ACE/CD143 in ELISAs and Western blots. In sandwich immunoassays, less than 0.2% cross‑reactivity with recombinant mouse ACE-2 and recombinant human ACE is observed.
Source
N/A
Isotype
IgG
Clonality
Polyclonal
Host
Goat
Gene
ACE
Purity Statement
Antigen Affinity-purified
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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
Background
ACE (also known as peptidyl-dipetidase A) is a zinc metallopeptidase important for blood pressure control and water and salt metabolism (1). 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 (2).
ACE is a type I membrane protein and exists in two isoforms (1). Somatic ACE, found in endothelial, epithelial and neuronal cells, comprises two highly similar catalytic domains called N- and C-domains. Germinal ACE, found exclusively in the testes, comprises a single catalytic 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 (3). 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 (1). 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 (4, 5).
Corvol, P. et al. (2004) in Handbook of Proteolytic Enzymes (Barrett, A.J. et al., eds.) p. 332, Academic Press, San Diego.
Hu, J. et al. (2001) J. Biol. Chem. 276:47863.
Kessler, S.P. et al. (2000) J. Biol. Chem. 275:26259.
Eyries, M. et al. (2001) J. Biol. Chem. 276:5525.
Alfalah, M. et al. (2001) J. Biol. Chem. 276:21105.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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