Description: (IN) SARS-CoV-2 Spike peptide

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).

Description: Coronavirus disease 2019 (COVID-19), formerly known as 2019-nCoV acute respiratory disease, is an infectious disease caused by SARS-CoV-2, a virus closely related to the SARS virus (1). The disease is the cause of the 2019–20 coronavirus outbreak (2). The structure of 2019-nCoV consists of the following: a Spike protein (S), hemagglutinin-esterease dimer (HE), a membrane glycoprotein (M), an envelope protein (E) a nucleoclapid protein (N) and RNA. Coronavirus invades cells through Spike (S) glycoproteins, a class I fusion protein. It is the major viral surface protein that coronavirus uses to bind to the human cell surface receptor. It also mediates the fusion of host and viral cell membrane, allowing the virus to enter human cells and begin infection (3). The spike protein is the major target for neutralizing antibodies and vaccine development (4). The protein modeling suggests that there is strong interaction between Spike protein receptor-binding domain and its host receptor angiotensin-converting enzyme 2 (ACE2), which regulate both the cross-species and human-to-human transmissions of COVID-19 (5). The recent study has shown that the SARS-CoV-2 spike protein binds ACE2 with higher affinity than SARS-CoV spike protein (6).

Description: Recombinant SARS-CoV-2 Spike protein in its homotrimeric form, containing S1+S2 subunits and encompassing amino acids 16-1213. This protein corresponds to SARS-CoV2 South African Variant B.1.351 and contains mutations K417N, E484K and N501Y. It also contains a C-terminal His-tag. Note that the expected MW of the S1+S2 monomer is 136kDa. The recombinant protein is ≥90% pure following high affinity Ni-NTA purification._x000D_

Description: Recombinant SARS-CoV-2 Spike protein in its homotrimeric form, containing S1+S2 subunits and encompassing amino acids 16-1213. This protein corresponds to SARS-CoV2 South African Variant B.1.351 and contains mutations K417N, E484K and N501Y. It also contains a C-terminal His-tag. Note that the expected MW of the S1+S2 monomer is 136kDa. The recombinant protein is ≥90% pure following high affinity Ni-NTA purification._x000D_

Description: Recombinant SARS-CoV-2 Spike protein in its homotrimeric form, containing S1+S2 subunits and encompassing amino acids 16-1213. This protein corresponds to SARS-CoV2 United Kingdom Variant B.1.1.7. It contains mutations N501Y, A570D, D614G, P681H, T716I, S982A, D1118; deletions: 21765:6 (69-70HV), 21991:3 (44Y).  This construct also contains a C-terminal His tag. Note that the expected MW of the S1+S2 monomer is 136kDa. The recombinant protein is ≥90% pure following high affinity Ni-NTA purification.

Description: Recombinant SARS-CoV-2 Spike protein in its homotrimeric form, containing S1+S2 subunits and encompassing amino acids 16-1213. This protein corresponds to SARS-CoV2 United Kingdom Variant B.1.1.7. It contains mutations N501Y, A570D, D614G, P681H, T716I, S982A, D1118; deletions: 21765:6 (69-70HV), 21991:3 (44Y).  This construct also contains a C-terminal His tag. Note that the expected MW of the S1+S2 monomer is 136kDa. The recombinant protein is ≥90% pure following high affinity Ni-NTA purification.

Description: Recombinant SARS-CoV-2 Spike protein in its homotrimeric form, containing S1+S2 subunits and encompassing amino acids 16-1213. This protein contains three mutations: K417T, E484K and N501Y that have been found in emerging SARS-CoV-2 Variants of Concern and may lead to higher transmissibility and infectivity. This mutant Spike Trimer will be useful for structure-function studies, testing of neutralizing antibodies, or antibody and drug screening.  The construct also contains a C-terminal His-tag. Note that the expected MW of the S1+S2 monomer is 136kDa but migrates at a higher MW in SDS-PAGE due to glycosylation. The recombinant protein is ?90% pure following affinity purification.

Description: Recombinant SARS-CoV-2 Spike protein in its homotrimeric form, containing S1+S2 subunits and encompassing amino acids 16-1213. This protein contains three mutations: K417T, E484K and N501Y that have been found in emerging SARS-CoV-2 Variants of Concern and may lead to higher transmissibility and infectivity. This mutant Spike Trimer will be useful for structure-function studies, testing of neutralizing antibodies, or antibody and drug screening.  _x000D_The construct also contains a C-terminal His-tag. Note that the expected MW of the S1+S2 monomer is 136kDa but migrates at a higher MW in SDS-PAGE due to glycosylation. The recombinant protein is ?90% pure following affinity purification.

Description: Recombinant COVID-19 (2019 novel coronavirus) Spike protein S1 subunit was fused to His tag at C-terminus and expressed in human cells. The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell: they are essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. Most notable is severe acute respiratory syndrome (SARS). The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein alone can mediate the membrane fusion required for virus entry and cell fusion. It is also a major immunogen and a target for entry inhibitors. The SARS-CoV spike (S) protein is composed of two subunits; the S1 subunit contains a receptor-binding domain that engages with the host cell receptor angiotensin-converting enzyme 2 and the S2 subunit mediates fusion between the viral and host cell membranes. The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity, during infection with SARS-CoV.

Description: Recombinant COVID-19 (2019 novel coronavirus) Spike protein S1 subunit was fused to to Human IgG1 Fc tag at C-terminus and expressed in human cells. The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell: they are essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. Most notable is severe acute respiratory syndrome (SARS). The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein alone can mediate the membrane fusion required for virus entry and cell fusion. It is also a major immunogen and a target for entry inhibitors. The SARS-CoV spike (S) protein is composed of two subunits; the S1 subunit contains a receptor-binding domain that engages with the host cell receptor angiotensin-converting enzyme 2 and the S2 subunit mediates fusion between the viral and host cell membranes. The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity, during infection with SARS-CoV.

Description: Recombinant COVID-19 (2019 novel coronavirus) Spike protein S1 subunit was fused to to Mouse IgG1 Fc tag at C-terminus and expressed in human cells. The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell: they are essential for both host specificity and viral infectivity. The term 'peplomer' is typically used to refer to a grouping of heterologous proteins on the virus surface that function together. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. Most notable is severe acute respiratory syndrome (SARS). The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein alone can mediate the membrane fusion required for virus entry and cell fusion. It is also a major immunogen and a target for entry inhibitors. The SARS-CoV spike (S) protein is composed of two subunits; the S1 subunit contains a receptor-binding domain that engages with the host cell receptor angiotensin-converting enzyme 2 and the S2 subunit mediates fusion between the viral and host cell membranes. The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity, during infection with SARS-CoV.

Description: (IN) SARS-CoV-2 Spike peptide

Description: (CT) SARS-CoV-2 Spike peptide