|Datasheet||Specific References||Reviews||Related Products||Protocols|
|ACE2, ACEH, DKFZp434A014|
|A DNA sequence encoding the extracellular domain (Met 1-Ser 740) of human ACE2 precursor (NP_068576.1) was expressed with the fused Fc region of human IgG1 at the C-terminus.|
|In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.|
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
|> 95 % as determined by SDS-PAGE|
|1. Using the Octet RED System, the affinity constant (Kd) of human AEC2-Fc (Cat: 10108-H02H) bound to Spike (HCoV-EMC/2012) (Cat: 40071-V31B) was 6 nM.|
2. Using the Octet RED System, the affinity constant (Kd) of human AEC2-Fc (Cat: 10108-H02H) bound to Spike (HCoV-EMC/2012) (Cat: 40071-V05B) was 30 nM.
3. Using the Octet RED System, the affinity constant (Kd) of human AEC2-Fc (Cat: 10108-H02H) bound to Spike (HCoV-EMC/2012) (ECD, aa 1-1297) (Cat: 40069-V08B) was 30 nM.
4. Using the Octet RED System, the affinity constant (Kd) of human AEC2-Fc (Cat: 10108-H02H) bound to Spike-His (aa 1-760) (Cat: 40021-V08H) was 10 nM.
|< 1.0 EU per μg of the protein as determined by the LAL method|
|Samples are stable for up to twelve months from date of receipt at -70℃|
|The recombinant human ACE2/Fc is a disulfide-linked homodimeric protein. The reduced monomer consists of 961 amino acids and predicts a molecular mass of 110.3 kDa. As a result of glycosylation, the rhACE2/Fc monomer migrates as approximately 145-150 kDa band in SDS-PAGE under reducing conditions.|
|Lyophilized from sterile 100mM Glycine, 10mM NaCl, 50mM Tris, pH 7.5|
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
|Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.|
|A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.|
Angiotensin-converting enzyme 2 (ACE2), a first homolog of ACE, regulates the renin angiotensin system (RAS) by counterbalancing ACE activity. Accumulating evidence in recent years has demonstrated a physiological and pathological role of ACE2 in the cardiovascular, renal and respiratory systems. ACE2 also has an important role in blood pressure control. This enzyme, an homolog of ACE, hydrolyzes angiotensin (Ang) I to produce Ang-(1-9), which is subsequently converted into Ang-(1-7) by a neutral endopeptidase and ACE. ACE2 releases Ang-(1-7) more efficiently than its catalysis of Ang-(1-9) by cleavage of Pro(7)-Phe(8) bound in Ang II. Thus, the major biologically active product of ACE2 is Ang-(1-7), which is considered to be a beneficial peptide of the RAS cascade in the cardiovascular system. A physiological role for ACE2 has been implicated in hypertension, cardiac function, heart function and diabetes, and as a receptor of the severe acute respiratory syndrome coronavirus. In the acute respiratory distress syndrome (ARDS), ACE, AngII, and AT1R promote the disease pathogenesis, whereas ACE2 and the AT2R protect from ARDS. Importantly, ACE2 has been identified as a key SARS-coronavirus receptor and plays a protective role in severe acute respiratory syndrome (SARS) pathogenesis. Furthermore, the recent explosion of research into the ACE2 homolog, collectrin, has revealed a new physiological function of ACE2 as an amino acid transporter, which explains the pathogenic role of gene mutations in Hartnup disorder. This review summarizes and discusses the recently unveiled roles for ACE2 in disease pathogenesis.