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Recombinant Hamster ACE-2 His-tag Protein, CF

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Recombinant Hamster ACE-2 His-tag (Catalog # 10578-ZN) binds Recombinant SARS-CoV-2 Spike RBD Fc Chimera Protein (10499-CV) in a functional ELISA.
Recombinant Hamster ACE-2 His-tag (Catalog # 10578-ZN) is measured by its ability to cleave a fluorogenic peptide substrate, Mca-YVADAPK(Dnp)-OH (ES007).
2 μg/lane of Recombinant Hamster ACE-2 His-tag Protein (Catalog # 10578-ZN) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands ...read more

Product Details

Summary
Reactivity HaSpecies Glossary
Applications Bioactivity, Enzyme Activity
Format
Carrier-Free

Order Details

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Recombinant Hamster ACE-2 His-tag Protein, CF Summary

Details of Functionality
Recombinant Hamster ACE-2 His-tag (Catalog # 10578-ZN) binds Recombinant Viral SARS-CoV-2 S Protein RBD Fc Chimera (Catalog # 10499-CV) in a functional ELISA. Measured by its ability to cleave a fluorogenic peptide substrate, Mca-YVADAPK(Dnp)-OH (Catalog # ES007). The specific activity is >700 pmol/min/μg, as measured under the described conditions.
Source
Human embryonic kidney cell, HEK293-derived hamster ACE-2 protein
Gln18-Thr740
with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Protein identity confirmed by mass spectrometry.
Protein/Peptide Type
Recombinant Enzymes
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
  • Enzyme Activity
Theoretical MW
84 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
89-109 kDa, under reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 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.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.

Notes

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

Alternate Names for Recombinant Hamster ACE-2 His-tag Protein, CF

  • 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, R. 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. Hoffman, M. et al. (2020) Cell. 181:1.
  6. Wrapp, D. 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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