SARS-CoV-2 S (Biotinylated, sf9, Avi-His)

The SARS-Cov-2 S glycoprotein is a SARS-Cov-2 S glycoprotein. The amino acid sequence 1261-1267a.a of the SARS-Cov-2 S glycoprotein is transmembrane. The SARS-Cov-2 S glycoprotein is a highly glycosylated trimer, each of which consists of 1260 amino acids (residues 14-1273), divided into four structural domains: the n-terminal domain (NTD), the c-terminal domain (CTD, also known as the receptor-binding domain, RBD), and two subdomains (SD1 and SD2) . SARS-CoV-2 S Protein (Biotinylated, sf9, Avi-His) is the recombinant Virus-derived SARS-CoV-2 S protein, expressed by Sf9 insect cells , with C-Avi, C-His labeled tag.

Product Specifications

Product Name Alternative

SARS-CoV-2 S Protein (Biotinylated, sf9, Avi-His), Virus, Sf9 insect cells

UNSPSC

12352202

Type

Recombinant Proteins

Assay Protocol

https://www.medchemexpress.com/cytokines/sars-cov-2-s-protein-biotinylated-sf9-avi-his.html

Molecular Formula

43740568 (Gene_ID) P0DTC2/YP_009724390.1 (V16-P1213) (Accession)

Molecular Weight

Approximately 136.20 kDa.

References & Citations

[1]Vettori M, et al. Effects of Different Types of Recombinant SARS-CoV-2 Spike Protein on Circulating Monocytes' Structure. Int J Mol Sci. 2023 May 27;24 (11) :9373.|[2]Lorenz P, et al. A linear B-cell epitope close to the furin cleavage site within the S1 domain of SARS-CoV-2 Spike protein discriminates the humoral immune response of nucleic acid- and protein-based vaccine cohorts. Front Immunol. 2023 May 5;14:1192395.|[3]Wang X, et al. Evaluating the effect of SARS-CoV-2 spike mutations with a linear doubly robust learner. Front Cell Infect Microbiol. 2023 Apr 19;13:1161445.|[4]Bestle D, et al. TMPRSS2 and furin are both essential for proteolytic activation of SARS-CoV-2 in human airway cells. Life Sci Alliance. 2020 Jul 23;3 (9) :e202000786.|[5]Duan L, et al. The SARS-CoV-2 Spike Glycoprotein Biosynthesis, Structure, Function, and Antigenicity: Implications for the Design of Spike-Based Vaccine Immunogens. Front Immunol. 2020 Oct 7;11:576622.