SARS-CoV-2 (COVID-19) S protein, His-Tag, stabilized trimer
Price excl. shipping costs excl. VAT. For more information, see our shipping policy
SKU: P2020-025 trenzyme
Recombinant Spike protein of SARS-CoV-2 (COVID-19) from Wuhan pneumonia virus with C-terminal Strep- and His-Tag as a stabilized trimer and with deletion of the internal Furin-site. The S protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.
- Product Name: SARS-CoV-2 (COVID-19) S protein, His-Tag, stabilized trimer
- Catalog No.: P2020-025
- RefSeq Links: NC_045512.2; MN908947.3; YP_009724390.1; QHD43416.1; GeneID: 43740568; UniProt: P0DTC2
- Synonyms: SARS-CoV-2; coronavirus; SARS-CoV-2 spike protein; S glycoprotein; spike glycoprotein; 2019-nCoV; COVID-2019; COVID-19
“In our COVID-19 projects, we have had very good experience with the SARS-CoV-2 proteins produced by trenzyme: rapid and reliable production of the functional proteins from different cell lines continued to provide first-class support for our projects.”
Dr. Peter Rauch
CANDOR Bioscience GmbH, Wangen, Germany
- Species: SARS-CoV-2; Wuhan seafood market pneumonia virus
- Tags: His-Tag and Strep-Tag, both C-terminal
Sequence without tags (AA 16-1211):
- Expression Host: human, HEK293
- Formulation: PBS, 5% (w/v) Trehalose; pH 7,4
- Format: Liquid, stored and shipped at -80°C
- Purity: > 85% as determined by SDS-PAGE
The SARS-CoV-2 spike is presented as a trimeric structure on the surface of the virus. It consists of three identical transmembrane proteins, called spike proteins, each containing two subunits: the S1 and the S2 subunit. The S1 is necessary for the recognition of the receptor on the surface of a susceptible cell. In addition, the S2 subunit is responsible for the fusion of the virus with the cell membrane of the host cell. Upon binding of the host receptor hACE2, the distal S1 domain is cleaved. This reveals the fusion machinery of the S2 subunit, which mediates the entry into the cell. Moreover, the Spike protein is heavily glycosylated by N-linked glycans that are important for the proper folding of the protein and the recognition by neutralizing antibodies. The engineered recombinant Spike protein contains specific amino acid substitutions to stabilize the prefusion conformation (2P). Furthermore, the furin cleavage site at the boundary between the S1/S2 subunits was deleted and an artificial trimerization domain was added to the C-terminal end of the monomer. Above all, the spike is a major immunogen and an interesting target for vaccine development as well as for serological assays.
Size exclusion chromatography (SEC) of purified SARS-CoV-2 (COVID-19) S protein, His-Tag, stabilized trimer
Activity of SARS-CoV-2 S1(RBD) and SARS-CoV-2 S protein (His-Tag, trimer)
Activity of SARS-CoV-2 S1(RBD) and SARS-CoV-2 S protein (His-Tag, trimer) were compared using Sandwich-ELISA based on coating with hACE2 (Cat# P2020-016, trenzyme) and detection with CR3022 anti-spike antibody (Ab01680-23.0, Absolute Antibody Ltd). CR3022 was detected using goat-anti-rabbit-HRP. SARS-CoV-2 S protein (His-tag, trimer) amount was increased to compensate for its size.
Histogram of marked lane in gel picture