ACE2 (18-740) Human, Fc
HEK293 Cells
ACE-2 Protein is >95% pure as determined SDS-PAGE.
Description
The HEK293 derived ACE2 Human recombinant protein contains the amino acids 18-740 fused to Fc tag at C-terminal. ACE2 Protein binds to SARS Coronavirus-2 [ CoV-2019 ] Spike receptor binding domain.
Product Specs
Angiotensin converting enzyme 2 (ACE-2) is an enzyme found on the surface of cells in various organs, including the intestines, arteries, lungs, heart, and kidneys. ACE2 serves as an entry point for SARS coronaviruses, including SARS-CoV-2. The spike (S) glycoprotein of the coronavirus is a key component involved in viral infection. It plays a crucial role in recognizing host cell receptors and facilitating the fusion of viral and cellular membranes. The S1 domain of the spike protein contains two main regions: the N-terminal domain and the C-terminal domain. Either one or both of these domains can act as receptor-binding domains. Both SARS-CoV and MERS-CoV utilize the C-domain for receptor attachment. ACE2 is a type I transmembrane protein with an extracellular N-terminal domain that harbors the catalytic site and an intracellular C-terminal tail. It also possesses a signal peptide, a transmembrane domain, and a metalloproteinase active site containing a HEXXH zinc-binding domain. As a mono-carboxypeptidase, ACE-2 breaks down Ang I to generate the nonapeptide Ang 1-9 and Ang II to produce the heptapeptide Ang 1-7.
This recombinant ACE2 protein is produced in HEK293 cells and encompasses amino acids 18-740 of the human ACE2 protein. It also includes a C-terminal Fc tag. This ACE2 protein demonstrates binding affinity for the Spike receptor binding domain of the SARS Coronavirus-2 [CoV-2019].
The ACE2 Human protein solution is supplied in a buffer consisting of 50mM Tris-HCl (pH 7.5), 150mM NaCl, and glycerol.
The ACE-2 Human Recombinant Protein is shipped with ice packs. Upon receipt, it should be stored at -20°C.
The purity of the ACE-2 Protein is determined to be greater than 95% by SDS-PAGE analysis.
The activity of ACE2 was assessed using a functional ELISA to measure its binding capacity. In this assay, the immobilized Recombinant Human ACE2 protein exhibited binding to the SARS CoV2 Spike protein Receptor Binding Domain at a concentration of 2 µg/ml.
HEK293 Cells
Purified by Protein-G chromatographic technique.
Product Science Overview
Angiotensin Converting Enzyme 2 (ACE2) is a crucial enzyme in the renin-angiotensin system (RAS), which plays a significant role in regulating cardiovascular and renal functions. The recombinant form of ACE2, particularly the segment spanning amino acids 18-740, fused with an Fc (fragment crystallizable) region, has garnered attention for its therapeutic potential and research applications.
ACE2 is a monocarboxypeptidase that metabolizes several peptides, including the conversion of angiotensin II (Ang II) into angiotensin 1-7 (Ang 1-7). Ang II is known for its vasoconstrictive and proliferative effects, while Ang 1-7 exerts vasodilatory and antiproliferative actions by acting through the Mas receptor . This balance between Ang II and Ang 1-7 is crucial for maintaining cardiovascular homeostasis.
The recombinant form of ACE2 (18-740 a.a.) is produced using mammalian expression systems, such as HEK293 cells . This segment includes the active site of the enzyme and is often fused with an Fc region to enhance its stability and prolong its half-life in circulation.
The ACE2/Ang 1-7/Mas axis represents a counter-regulatory pathway to the classical ACE/Ang II/Ang II type-1 receptor axis. Loss of ACE2 function has been associated with adverse cardiovascular remodeling, myocardial infarction, and heart failure . Recombinant ACE2 has shown promise in mitigating these effects by reducing myocardial hypertrophy, fibrosis, and diastolic dysfunction .
Moreover, ACE2 has gained significant attention as a functional receptor for the SARS coronavirus, including SARS-CoV-2, the virus responsible for COVID-19 . This has spurred research into ACE2 as a potential therapeutic target for managing viral infections and associated complications.
