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: (IN) SARS-CoV-2 Spike peptide

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

Description: SARS-CoV-2 Spike S1 receptor binding domain (RBD), also known as SARS-CoV-2 Spike 1 RBD, novel coronavirus Spike 1 RBD and nCoV Spike 1 RBD, GenBank Accession No. QHD43416.1, a.a. 319-541 with G476S mutation and with a C-terminal Avi-His-tag, expressed in a HEK293 cell expression system. MW= 28 kDa. This protein runs at a higher M.W. by SDS-PAGE due to glycosylation.

Description: SARS-CoV-2 Spike protein S1 subunit, receptor binding domain (RBD), also known as SARS-CoV-2 spike RBD, novel coronavirus spike RBD and nCoV spike RBD, GenBank Accession No. MN_908947.1, a.a. 319-541, fused at the C-terminus of the Fc portion of human IgG1, with a C-terminal Avi-tag™, expressed in a HEK293 cell expression system. MW=54 kDa. This protein runs at a higher MW by SDS-PAGE due to glycosylation.

Description: SARS-CoV-2 Spike protein S1 subunit, receptor binding domain (RBD), also known as SARS-CoV-2 spike RBD, novel coronavirus spike RBD and nCoV spike RBD, GenBank Accession No. MN_908947.1, a.a. 319-541, fused at the C-terminus of the Fc portion of human IgG1, with a C-terminal Avi-tag™, expressed in a HEK293 cell expression system. MW=54 kDa. This protein runs at a higher MW by SDS-PAGE due to glycosylation.

Description: SARS-CoV-2 Spike S1 receptor binding domain (RBD), also known as SARS-CoV-2 Spike 1 RBD, novel coronavirus Spike 1 RBD and nCoV Spike 1 RBD, GenBank Accession No. QHD43416.1, a.a. 319-541 with a V367F mutation and a with C-terminal Avi-His-tag, expressed in a HEK293 cell expression system. MW= 28 kDa. This protein runs at a higher M.W. by SDS-PAGE due to glycosylation.

Description: SARS-CoV-2 Spike S1 receptor binding domain (RBD), also known as SARS-CoV-2 Spike 1 RBD, novel coronavirus Spike 1 RBD and nCoV Spike 1 RBD, GenBank Accession No. QHD43416.1, a.a. 319-541 with a V367F mutation and a with C-terminal Avi-His-tag, expressed in a HEK293 cell expression system. MW= 28 kDa. This protein runs at a higher M.W. by SDS-PAGE due to glycosylation.

Description: SARS-CoV-2 shares 79.5% sequence identity with SARS-CoV and is 96.2% identical at the genome level to the bat coronavirus BatCoV RaTG133, suggesting it had originated in bats. The coronaviral genome encodes four major structural proteins: the Spike (S) protein, Nucleocapsid (N) protein, Membrane/Matrix (M) protein and the Envelope (E) protein. The SARS Envelope (E) protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. The SARS Membrane/Matrix (M) protein is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with SARS Spike (S) protein and the Nucleocapsid (N) protein. The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms.The CoV Spike (S) protein assembles as trimer and plays the most important role in viral attachment, fusion and entry. It is composed of a short intracellular tail, a transmembrane anchor and a large ectodomain that consists of a receptor binding S1 subunit (RBD domain) and a membrane-fusing S2 subunit. The S1 subunit contains a receptor binding domain (RBD), which binds to the cell surface receptor angiotensin-converting enzyme 2 (ACE2) present at the surface of epithelial cells. Recently, a new variant of SARS-CoV-2, called B.1.351, was detected in South Africa. This variant carries three mutations in the RBD at the positions 417, 484 and 501 (K417N, E484K, N501Y) and is associated with a higher viral load, which may suggest potential for increased transmissibility.

Description: SARS-CoV-2 shares 79.5% sequence identity with SARS-CoV and is 96.2% identical at the genome level to the bat coronavirus BatCoV RaTG133, suggesting it had originated in bats. The coronaviral genome encodes four major structural proteins: the Spike (S) protein, Nucleocapsid (N) protein, Membrane/Matrix (M) protein and the Envelope (E) protein. The SARS Envelope (E) protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. The SARS Membrane/Matrix (M) protein is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with SARS Spike (S) protein and the Nucleocapsid (N) protein. The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms.The CoV Spike (S) protein assembles as trimer and plays the most important role in viral attachment, fusion and entry. It is composed of a short intracellular tail, a transmembrane anchor and a large ectodomain that consists of a receptor binding S1 subunit (RBD domain) and a membrane-fusing S2 subunit. The S1 subunit contains a receptor binding domain (RBD), which binds to the cell surface receptor angiotensin-converting enzyme 2 (ACE2) present at the surface of epithelial cells. Recently, a new variant of SARS-CoV-2, called B.1.351, was detected in South Africa. This variant carries three mutations in the RBD at the positions 417, 484 and 501 (K417N, E484K, N501Y) and is associated with a higher viral load, which may suggest potential for increased transmissibility.The SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) (B.1.351 Variant, SA) can be used as antigen in Serological ELISA Kits to detect anti-SARS-CoV-2 Spike (RBD) antibodies in serum or plasma.

Description: This is a set of capture antibody and HRP-conjugated antbody for quantitative detection of SARS-CoV-2 Spike RBD protein for through solid phase sandwich ELISA.

Description: SARS-CoV-2 shares 79.5% sequence identity with SARS-CoV and is 96.2% identical at the genome level to the bat coronavirus BatCoV RaTG133, suggesting it had originated in bats. The coronaviral genome encodes four major structural proteins: the Spike (S) protein, Nucleocapsid (N) protein, Membrane/Matrix (M) protein and the Envelope (E) protein. The SARS Envelope (E) protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. The SARS Membrane/Matrix (M) protein is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with SARS Spike (S) protein and the Nucleocapsid (N) protein. The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms.The CoV Spike (S) protein assembles as trimer and plays the most important role in viral attachment, fusion and entry. It is composed of a short intracellular tail, a transmembrane anchor and a large ectodomain that consists of a receptor binding S1 subunit (RBD domain) and a membrane-fusing S2 subunit. The S1 subunit contains a receptor binding domain (RBD), which binds to the cell surface receptor angiotensin-converting enzyme 2 (ACE2) present at the surface of epithelial cells. Recently, a more transmissible variant of SARS-CoV-2, called B.1.1.7, was detected in the south of England. This variant carries a mutation in the RBD at the position 501 (N501Y).

Description: SARS-CoV-2 shares 79.5% sequence identity with SARS-CoV and is 96.2% identical at the genome level to the bat coronavirus BatCoV RaTG133, suggesting it had originated in bats. The coronaviral genome encodes four major structural proteins: the Spike (S) protein, Nucleocapsid (N) protein, Membrane/Matrix (M) protein and the Envelope (E) protein. The SARS Envelope (E) protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. The SARS Membrane/Matrix (M) protein is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with SARS Spike (S) protein and the Nucleocapsid (N) protein. The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms.The CoV Spike (S) protein assembles as trimer and plays the most important role in viral attachment, fusion and entry. It is composed of a short intracellular tail, a transmembrane anchor and a large ectodomain that consists of a receptor binding S1 subunit (RBD domain) and a membrane-fusing S2 subunit. The S1 subunit contains a receptor binding domain (RBD), which binds to the cell surface receptor angiotensin-converting enzyme 2 (ACE2) present at the surface of epithelial cells. Recently, a more transmissible variant of SARS-CoV-2, called B.1.1.7, was detected in the south of England. This variant carries a mutation in the RBD at the position 501 (N501Y).The SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) (B.1.1.7 Variant, UK) can be used as antigen in Serological ELISA Kits to detect anti-SARS-CoV-2 Spike (RBD) antibodies in serum or plasma.

Description: Recombinant SARS-CoV-2 Spike protein, RBD (Receptor Binding Domain) encompassing amino acids 319-541. This protein corresponds to SARS-CoV-2 Variant B.1.617 originally identified in India, and contains mutations L452R and E484K. The construct contains a C-terminal Avi-Tag™ followed by a His-tag (6xHis). The protein was affinity purified. HiP™ indicates a high purity protein (≥90% pure) and less than 10% aggregation as measured by gel filtration.