Recombinant TMPRSS2 (Transmembrane Protease Serine Subtype 2), His-tagged (NP_001128571), 50µg

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). Hoffman and colleagues showed that receptor-mediated virus entry is dependent on a serine protease, transmembrane serine protease 2 (TMPRSS2). This protease cleave the viral receptor, the carboxypeptidase angiotensin-converting enzyme 2 (ACE2). Of note, clinically approved inhibitors of TMPRSS2 can prevent cell entry by SARS-CoV-2. Because alveolar type 2 cells highly express both ACE2 and TMPRSS2 in the steady state, these cells might be the primary entry cells for SARS-CoV-2 in the lung. 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. Expression of TMPRSS2 increased cellular uptake of soluble SARS-S, suggesting that protease-dependent augmentation of viral entry might be due to increased uptake of virions into target cells. Finally, TMPRSS2 was found to compete with the metalloprotease ADAM17 for ACE2 processing, but only cleavage by TMPRSS2 resulted in augmented SARS-S-driven entry. All these 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.

Recombinant TMPRSS2 is a type II transmembrane serine protease that can cleave and activate the spike protein (S) of the severe acute respiratory syndrome coronavirus (SARS-CoV) for membrane fusion. It is a recombinant protein, expressed in E.coli cells. The protein consists of 386 aa (106-492) amino acids and a C-terminal His6-tag.

The calculated Mr of the His-tagged protein is 43.8 kDa. The protein is solubilized in 50 mM Tris, 6.8, 150 mM NaCl, 250 mM Arginin, 10% Glycerin.

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