|Detection of Mouse ACE/CD143 by Western Blot. Western blot shows lysates of mouse lung tissue. PVDF membrane was probed with 0.05 µg/mL of Goat Anti-Mouse ACE/CD143 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1513) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). 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.|
|ACE/CD143 in Mouse Kidney. ACE/CD143 was detected in perfusion fixed frozen sections of mouse kidney using 15 µg/mL Goat Anti-Mouse ACE/CD143 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1513) overnight at 4 °C. Tissue was stained (red). View our protocol for Fluorescent IHC Staining of Frozen Tissue Sections.|
|Detection of Mouse ACE/CD143 by Simple WesternTM. Simple Western lane view shows lysates of mouse lung tissue, loaded at 0.2 mg/mL. A specific band was detected for ACE/CD143 at approximately 218 kDa (as indicated) using 10 µg/mL of Goat Anti-Mouse ACE/CD143 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1513) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the 66-440 kDa separation system.|
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).
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