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Recombinant Human ACE-2 His-tag Alexa Fluor® 488 Protein

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Streptavidin beads conjugated to Biotinylated Recombinant SARS-CoV-2 Spike RBD Fc Chimera Avi-tag (AVI10499) were stained with Recombinant Human ACE-2 His-tag Alexa Fluor® 488 Protein (Catalog # AFG933, filled histogram) or unstained (open histogram).
Streptavidin beads conjugated to Biotinylated Recombinant SARS-CoV-2 Spike RBD Fc Chimera Avi-tag (AVI10499) were stained with Recombinant Human ACE-2 His-tag Alexa Fluor® 488 Protein (Catalog # AFG933, filled ...read more
2 μg/lane of Recombinant Human ACE‑2 His-tag Alexa Fluor® 488 Protein (Catalog # AFG933) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human ACE-2 His-tag Alexa Fluor® 488 Protein Summary

Details of Functionality
Measured by flow cytometry for its ability to bind Biotinylated Recombinant SARS-CoV-2 Spike RBD Fc Chimera Avi-tag (Catalog # AVI10499) conjugated streptavidin beads at 0.37-3.33 µg/mL (100 µL/well).

Please Note: Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived human ACE-2 protein
Gln18-Ser740, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
No results obtained: Gln18 predicted
Structure / Form
Recombinant Human ACE‑2 is prone to proteolytic cleavage at C-terminus. The predominant form of the purified protein lacks the His tag.
Labeled with Alexa Fluor® 488 via amines
Excitation Wavelength: 488 nm  
Emission Wavelength: 515­-545 nm
Protein/Peptide Type
Recombinant Enzymes
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
85 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
101-111 kDa, reducing conditions.

Packaging, Storage & Formulations

Storage
Protect from light. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in Tris, NaCl, ZnCl2 and Glycerol with BSA as a carrier protein.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Notes

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.

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human ACE-2 His-tag Alexa Fluor® 488 Protein

  • 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 3.4.17.23
  • Metalloprotease MPROT15

Background

Angiotensin I Converting Enzyme (ACE-2), also called ACEH (ACE homologue), is a dimeric, zinc-dependent metalloprotease of the ACE family that also includes somatic and germinal ACE (1, 2). ACE-2 mRNA is found at high levels in heart, testis, and kidney and at lower levels in a wide variety of tissues (1, 3). ACE-2 is the SARS-CoV and SARS-CoV2 Spike protein receptor in vivo (4-6), functions catalytically as a carboxypeptidase to cleave several substrates including angiotensins I and II, and acts as a partner for B0AT1-family amino acid transporters (1, 2). Through these functions, ACE-2 has been shown to be involved in several diseases including SARS, COVID19, acute lung injury (4, 7), heart disease (8), liver and lung fibrosis (9), inflammatory lung disease (10), and cardiopulmonary disease (11). Full length ACE-2 protein includes an extracellular region composed of a single N-terminal peptidase domain and C-terminal collectrin-like domain (CLD), a transmembrane domain, and a short cytoplasmic tail (12). The N-terminal peptidase region is required for binding to SARS-CoV and SARSCoV2 spike proteins, while the CLD contains a region that promotes dimerization and association with amino acid transporters (2). The peptidase domain contains a long deep cleft that undergoes a large hinge-bending movement at substrate and inhibitor binding (12).  Classical ACE inhibitors such as captopril and lisinopril do not inhibit ACE-2 activity and inhibitors of ACE-2 do not inhibit ACE activity (13).

  1. Kuba, K. et al. (2010) Pharmacol. Ther. 128:119.
  2. Yan, et al. (2020) Science 367:1444.
  3. Tipnis, S.R. et al. (2000) J. Biol. Chem. 275:33238.
  4. Kuba, K. et al. (2005) Nature Med. 11:875.
  5. Hoffmann, M. et al. (2020) Cell.181:1.
  6. Wrapp, et al. (2020) Science 367:1260.
  7. Imai, Y. et al. (2005) Nature 436:112.
  8. Huang, L. et al. (2003) J. Biol. Chem. 278:15532.
  9. Schrom, E. et al. (2017) Mol. Therapy Nuc. Acid 7:350.
  10. Jia, H. et al. (2016) Shock. 46:239.
  11. Cole-Jeffrey, C.T. et al. (2015) J. Cadiovasc. Pharmacol. 66:540.
  12. Towler, P. et al. (2004) J. Biol. Chem. 279:17996.
  13. Crackower, M.A. et al. (2002) Nature 417:822.

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