Recombinant SARS-CoV-2 S-trimer (Y453F, D614G) (His Tag) | 763-PKSV030390
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Recombinant SARS-CoV-2 S-trimer (Y453F, D614G) (His Tag) | PKSV030390 | Elabscience.
Synonym: SARS-CoV-2 Spike; 2019-nCoV Spike glycoprotein; 2019-nCoV S glycoprotein; 2019-nCoV S-trimer Protein
Activity: Test in progress
Protein Construction: Recombinant 2019-nCoV S-trimer Protein (Y453F, D614G) is produced by our Mammalian and the target gene encoding Cys15-Gln1208 is expression system with a 6His tag at the C-terminus.
Fusion tag: C-6His
Expressed Host: Human Cells
Shipping Conditions: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs.Upon receipt, store it immediately at<-20°C.
Purity: Greater than 90% as determined by reducing SDS-PAGE and SEC-HPLC.
Endotoxin: Please contact us for more information.
Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
Mol Mass: 136.6kDa
AP Mol Mass: 170-220kDa
Formulation: Supplied as a 0.2 μm filtered solution of PBS, pH 7.4
Reconstitution: Not Applicable
Background: 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. It's been reported that 2019-nCoV 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.