Rekombinante Proteine - SARS-CoV-2 (2019-nCoV)


The spike (S) glycoprotein of coronaviruses is essential for binding of the virus to the host cell at the beginning of the infection process. The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein is responsible for membrane fusion and is therefore required for virus entry and cell fusion. The target protein is also a major immunogen and a possible target for entry inhibitors.
The SARS-CoV-2 spike (S) protein is a large type I transmembrane protein composed of two subunits, S1 and S2. The S1 subunit contains a receptor-binding domain (RCB) responsible for binding to the host cell receptor angiotensin-converting enzyme 2 (ACE2). The S2 subunit mediates fusion between the viral and host cell membranes. The S1 RBD protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

The spike (S) glycoprotein of coronaviruses is essential for binding of the virus to the host cell at the beginning of the infection process. The severe acute respiratory syndrome-coronavirus... mehr erfahren »
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Rekombinante Proteine - SARS-CoV-2 (2019-nCoV)


The spike (S) glycoprotein of coronaviruses is essential for binding of the virus to the host cell at the beginning of the infection process. The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein is responsible for membrane fusion and is therefore required for virus entry and cell fusion. The target protein is also a major immunogen and a possible target for entry inhibitors.
The SARS-CoV-2 spike (S) protein is a large type I transmembrane protein composed of two subunits, S1 and S2. The S1 subunit contains a receptor-binding domain (RCB) responsible for binding to the host cell receptor angiotensin-converting enzyme 2 (ACE2). The S2 subunit mediates fusion between the viral and host cell membranes. The S1 RBD protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

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