Trimeric Sars Spike Protein

Description: SARS-CoV Spike Antibody: A novel coronavirus has been identified as the causative agent of SARS (Severe Acute Respiratory Syndrome). Coronaviruses are a major cause of upper respiratory diseases in humans. The genomes of these viruses are positive-stranded RNA approximately 27-31kb in length. SARS infection can be mediated by the binding of the viral spike protein, a glycosylated 139 kDa protein and the major surface antigen of the virus, to the angiotensin-converting enzyme 2 (ACE2) on target cells. This binding can be blocked by a soluble form of ACE2.

Description: SARS-CoV Spike Antibody: A novel coronavirus has been identified as the causative agent of SARS (Severe Acute Respiratory Syndrome). Coronaviruses are a major cause of upper respiratory diseases in humans. The genomes of these viruses are positive-stranded RNA approximately 27-31kb in length. SARS infection can be mediated by the binding of the viral spike protein, a glycosylated 139 kDa protein and the major surface antigen of the virus, to the angiotensin-converting enzyme 2 (ACE2) on target cells. This binding can be blocked by a soluble form of ACE2.

Description: SARS-CoV Spike Antibody: A novel coronavirus has recently been identified as the causative agent of SARS (Severe Acute Respiratory Syndrome). Coronaviruses are a major cause of upper respiratory diseases in humans. The genomes of these viruses are positive-stranded RNA approximately 27-31kb in length. SARS infection can be mediated by the binding of the viral spike protein, a glycosylated 139 kDa protein and the major surface antigen of the virus, to the angiotensin-converting enzyme 2 (ACE2) on target cells. This binding can be blocked by a soluble form of ACE2.

Description: SARS-CoV-2 full-length Trimeric Spike Antigen (UK/Nigerian Variant, 100ug)

Description: SARS-CoV-2 full-length Trimeric Spike Antigen (UK/Nigerian Variant, 1mg)

Description: SARS-CoV-2 full-length Trimeric Spike Antigen (UK/Nigerian Variant, 10mg)

Description: SARS-CoV-2 full-length Trimeric Spike Recombinant Protein (South African Variant, 100ug)

Description: SARS-CoV-2 full-length Trimeric Spike Recombinant Protein (South African Variant, >1mg)

Description: SARS-CoV-2 full-length Trimeric Spike Antigen (South African Variant, 10mg)

Description: SARS-CoV-2 full-length Trimeric Spike Antigen MultiPack (7 Variants & Wild 1mg each_)

Description: The spike protein (S) of coronavirus (CoV) attaches the virus to its cellular receptor, angiotensin-converting enzyme 2 (ACE2). A defined receptor-binding domain (RBD) on S mediates this interaction. The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.

Description: Severe acute respiratory Coronavirus SARS Coronavirus Spike trimer (S1+S2) (SARS-CoV S protein), Genbank Accession No. AAP13567, a.a. 1-1195(full length), with a C-terminal His-tag, expressed in a HEK293 expression system. MW=136 kDa. This protein runs at a higher M.W. by SDS-PAGE due to glycosylation.

Description: Severe acute respiratory Coronavirus SARS Coronavirus Spike trimer (S1+S2) (SARS-CoV S protein), Genbank Accession No. AAP13567, a.a. 1-1195(full length), with a C-terminal His-tag, expressed in a HEK293 expression system. MW=136 kDa. This protein runs at a higher M.W. by SDS-PAGE due to glycosylation.

Description: Severe acute respiratory Coronavirus Spike trimer (S1+S2), with 682RRAR685>A, K986P, and V987P mutations, Genbank Accession No. MN908947, a.a. 1-1213, with a C-terminal His-tag, expressed in a HEK293 expression system. MW=139 kDa.

Description: Severe acute respiratory Coronavirus Spike trimer (S1+S2), with 682RRAR685>A, K986P, and V987P mutations, Genbank Accession No. MN908947, a.a. 1-1213, with a C-terminal His-tag, expressed in a HEK293 expression system. MW=139 kDa.

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-CoV-2 Variant B.1.351, also known as variant Beta originally discovered in South Africa, and contains the nine known mutations listed below, in addition to deletion 242-244. It also contains mutations 682RRAR685>A, K986P and V987P. The construct has a C-terminal His-tag (6xHis). Note that the expected MW of the S1+S2 monomer is 137kDa but migrates at a higher MW in SDS-PAGE due to glycosylation. The recombinant protein was affinity purified.

*Deletion 242-244 is known as 241-243 in some databases and on the CDC website. This is the same deletion. As stated by Tegally et al., Nature 2021: "We also observe a deletion of three amino acids at positions 242 to 244, which was seen in samples extracted and generated in different laboratories across the NGS-SA. This region is difficult to align; the deletion could potentially also be located at positions 241 to 243, but the resulting sequence would be exactly the same. "

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 original Wuhan strain of the virus has become quickly replaced by its more transmissible variant, mainly determined by a single amino acid point mutation D614G. 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. It has been demonstrated that certain mutations and the inclusion of trimerization motif can stabilize recombinant Spike protein trimers.The recombinant protein SARS-CoV-2 Spike Protein (D614G) (Stable Trimer) (rec.) (His) could be useful for structural biology research, vaccine development, serological diagnostic kit development or neutralizing antibody screening.

Description: Severe acute respiratory Coronavirus Spike trimer (S1+S2), with 682-685>A, K986P, V987P, and D614G mutations, Genbank Accession No. MN908947, a.a. 1-1213, with a C-terminal His-tag, expressed in a HEK293 expression system. MW=137 kDa. This protein runs at a higher M.W. by SDS-PAGE due to glycosylation.

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-CoV-2 Variant B.1.617 originally discovered in India, and contains mutations L452R, E484Q, D614G and P681R. The construct also contains mutations 682RRAR685>A, K986P and V987P, and a T4 trimerization domain followed by a His-tag (6xHis) in C-terminal. The recombinant protein was affinity purified._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-CoV-2 Variant B.1.618, originally identified in India, and contains deletion 145/146YH as well as mutations E484K and D614G.  The construct also contains mutations 682RRAR685>A, K986P and V987P, and a T4 trimerization domain followed by a His-tag (6xHis) in C-terminal. The recombinant protein was affinity purified.