Description
Biotinylated SARS-CoV-2 Spike Trimer Protein, His, Avitag™ (XBB/Omicron) (MALS verified) | SPN-C82Ew-25ug| Gentaur Distribution US, UK & Europe
It's been reported that coronavirus can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. The spike protein is a large type I transmembrane protein containing two subunits, S1 and S2. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. S2 contains basic elements needed for the membrane fusion.The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.
Source: Biotinylated SARS-CoV-2 Spike Trimer, His, Avitag (XBB/Omicron) (SPN-C82Ew) is expressed from human 293 cells (HEK293). It contains AA Val 16 - Pro 1213 (Accession # QHD43416.1 (T19I, LPP24-26del, A27S, V83A, G142D, Y144del, H146Q, Q183E, V213E, G339H, R346T, L368I, S371F, S373P, S375F, T376A, D405N, R408S, K417N, N440K, V445P, G446S, N460K, S477N, T478K, E484A, F486S, F490S, Q498R, N501Y, Y505H, D614G, H655Y, N679K, P681H, N764K, D796Y, Q954H, N969K, R683A, R685A, F817P, A892P, A899P, A942P, K986P, V987P). The spike mutations are identified on the SARS-CoV-2 Omicron variant (Pango lineage: XBB). The recombinant protein is expressed from human 293 cells (HEK293) with T4 fibritin trimerization motif and a polyhistidine tag at the C-terminus. Proline substitutions (F817P, A892P, A899P, A942P, K986P, V987P) and alanine substitutions (R683A and R685A) are introduced to stabilize the trimeric prefusion state of SARS-CoV-2 S protein and abolish the furin cleavage site, respectively.
Format: Powder.
Tag: C-10×His & C-Avi.
Expression System: HEK293.
Expression Region: Val 16 - Pro 1213.
Conjugate: Biotin-labeled.
Molecular Weight: 139.5 kDa.
Characteristics: This protein carries a polyhistidine tag at the C-terminus, followed by an Avi tag (Avitag™). The protein has a calculated MW of 139.5 kDa. The protein migrates as 180-210 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Purity: 95%.
Buffer: PBS.
Storage Conditions: -20℃.
Shipping Conditions: RT
