Recombinant ACE2 (angiotensin Converting Enzyme 2), His-tagged (EC 3.4.17.23), 10µg

The novel coronavirus disease 2019 (COVID-19) is rapidly expanding and causing many deaths all over the world with the World Health Organization (WHO) declaring a pandemic in March 2020. Current therapeutic options are limited and there is no registered and/or definite treatment or vaccine for this disease or the causative infection, severe acute respiratory coronavirus 2 syndrome (SARS-CoV-2). Angiotensin-converting enzyme 2 (ACE2), a part of the renin-angiotensin system (RAS), serves as the major entry point into cells for SARS-CoV-2 which attaches to human ACE2, thereby reducing the expression of ACE2 and causing lung injury and pneumonia.
Heurich et al., showed that arginine and lysine residues within ACE2 amino acids 697 to 716 are essential for cleavage by TMPRSS2 and that ACE2 processing is required for augmentation of SARS-S-driven entry by these proteases. In contrast, ACE2 cleavage was dispensable for activation of the viral S protein. A lot of studies indicate that TMPRSS2 and potentially related proteases promote SARS-CoV entry by two separate mechanisms: ACE2 cleavage, which might promote viral uptake, and SARS-S cleavage, which activates the S protein for membrane fusion. These observations have interesting implications for the development of novel therapeutics. In addition, they should spur efforts to determine whether receptor cleavage promotes entry of other coronaviruses, which use peptidases as entry receptors.

Molecular form: Angiotensin Converting Enzyme 2 (ACE2), a zinc-based metallo-carboxypeptidase that was proved as cell entry receptor for SARS-CoV-2. It is a recombinant protein, expressed in E.coli cells. The protein consists of 793 amino acids (12-805) and a C-terminal His6-tag.
The calculated Mr of the His-tagged protein is 93.4 kDa. The protein is solubilized in 20 mM Tris, pH 8, 5 mM CaCl2, 10% Glycerin.

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