Dieses SARS-CoV-2 Spike S2 Protein ist gelabelt mit His tag.
Applikation
SDS-PAGE (SDS)
Verwendungszweck
SARS-CoV-2 (COVID-19) S2 protein, His Tag
Sequenz
AA 686-1213
Produktmerkmale
SARS-CoV-2 S2 protein, His Tag is expressed from human 293 cells (HEK293). It contains AA Ser 686 - Pro 1213 (Accession # QHD43416.1). Predicted N-terminus: Ser 686 This protein carries a polyhistidine tag at the C-terminus.
Optimal working dilution should be determined by the investigator.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Buffer
PBS, pH 7.4
Handhabung
Please avoid repeated freeze-thaw cycles.
Lagerung
4 °C,-20 °C,-80 °C
Informationen zur Lagerung
For long term storage, the product should be stored at lyophilized state at -20°C or lower. This product is stable after storage at: 4-8°C for 12 months in lyophilized state, -70°C for 3 years under sterile conditions after reconstitution.
Longworth, Dittmar: "An antigen microarray protocol for COVID-19 serological analysis." in: STAR protocols, Vol. 2, Issue 3, pp. 100815, (2021) (PubMed).
Tosif, Neeland, Sutton, Licciardi, Sarkar, Selva, Do, Donato, Quan Toh, Higgins, Van de Sandt, Lemke, Lee, Shoffner, Flanagan, Arnold, Mordant, Mulholland, Bines, Dohle, Pellicci, Curtis, McNab et al.: "Immune responses to SARS-CoV-2 in three children of parents with symptomatic COVID-19. ..." in: Nature communications, Vol. 11, Issue 1, pp. 5703, (2020) (PubMed).
E2 Protein, Surface Glycoprotein Protein, S Protein
Substanzklasse
Viral Protein
Hintergrund
It's been reported that SARS-CoV-2 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.