Human ACE-2 Alexa Fluor® 700-conjugated Antibody Summary
Accession # Q9BYF1
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of ACE-2 in HEK293 Human Cell Line Transfected with Human ACE-2 and eGFP by Flow Cytometry. HEK293 human embryonic kidney cell line transfected with (A) human ACE-2 or (B) irrelevant protein, and eGFP was stained with Mouse anti-Human Alexa Fluor® 700-conjugated ACE-2 Monoclonal Antibody (Catalog # FAB9332N). Quadrant markers were set based on Mouse IgG2A Isotype Control (IC003N, data not shown). Staining was performed using our Staining Membrane-Associated Proteins protocol.
Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
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.
Product Specific Notices
This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.
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