Detection of Human ACE‑2 by Western Blot. Western blot shows lysates of NS0 mouse myeloma cell line and human kidney tissue. PVDF membrane was probed with 2 µg/mL of Mouse Anti-Human ACE‑2 Monoclonal Antibody (Catalog # MAB933) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band was detected for ACE‑2 at approximately 110 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.
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.
Angiogensin I Converting Enzyme-2 (ACE-2), also called ACEH (ACE homolog), is a type I transmembrane zinc protease that cleaves angiotensins I and II to produce vasodilatory and anti-proliferative peptides. The balance between ACE-1 and ACE-2 activity is critical for maintaining cardiovascular, renal, and pulmonary function (1). ACE-2 also functions as the cellular uptake receptor for the SARS coronoavirus. Within the extracellular domain, human ACE-2 shares 83% aa sequence identity with mouse and rat ACE-2. Human ACE-2 has about 40% amino acid identity to the N- and C-terminal domains of human somatic ACE. The predicted human ACE-2 protein sequence consists of 805 amino acids, including a N-terminal signal peptide, a single catalytic domain, a C-terminal membrane anchor, and a short cytoplasmic tail. ACE-2 mRNA is found at high levels in testis, kidney and heart and at moderate levels in colon, small intestine and ovary. Classical ACE inhibitors such as captopril and lisinopril do not inhibit ACE-2 activity. Novel peptide inhibitors of ACE-2 do not inhibit ACE activity (2). Genetic data from Drosophila, mice and rats show that ACE-2 is an essential regulator of heart function in vivo (3). ACE-2 isoforms of 75 kDa and 120 kDa are differentially expressed between lung and kidney, respectively, and a shed soluble form is generated by TACE/ADAM17 mediated cleavage.
Tipnis, S.R. et al. (2000) J. Biol. Chem. 275:33238.
Crackower, M.A. et al. (2002) Nature 417:822.
Huang, L. et al. (2003) J. Biol. Chem. 278:15532.
Angiotensin I Converting Enzyme 2
Entrez Gene IDs:
59272 (Human); 70008 (Mouse); 302668 (Rat)
ACE2; ACE-2; ACEH; ACEHangiotensin I converting enzyme 2; ACE-related carboxypeptidase; angiotensin I converting enzyme (peptidyl-dipeptidase A) 2; angiotensin-converting enzyme 2; Angiotensin-converting enzyme homolog; DKFZp434A014; EC 3.4.17; EC 18.104.22.168; Metalloprotease MPROT15
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