Detection of Mouse ACE/CD143 by Western Blot.
Western blot shows lysate of mouse lung tissue. PVDF membrane was probed with 2 µg/mL of Rat Anti-Mouse ACE/CD143 Monoclonal Antibody (Catalog # MAB1513) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for ACE/CD143 at approximately 180 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
(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
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.
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.
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