Recombinant protein of the receptor binding domain (RBD) of SARS-CoV-2 (COVID-2019) Spike S1 from Wuhan pneumonia virus with N-terminal His-Tag and C-terminal GFP.
- Product Name: SARS-CoV-2 (COVID-19) Spike S1 Protein (RBD), GFP/His-Tag
- Catalog No.: P2020-031
- 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 RBD; SARS-CoV-2 spike protein; 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, N-terminal and GFP, C-terminal
Sequence without tags (AA 319-541):
- Expression Host: human, HEK293
- Formulation: PBS, pH 7,4
- Format: Liquid, stored and shipped at -80°C
- Purity: > 85% as determined by SDS-PAGE
The spike (S) glycoprotein of coronaviruses is essential for binding of the virus to the host cell at the beginning of the infection process. The severe acute respiratory syndrome-coronavirus (SARS-CoV) spike (S) glycoprotein is responsible for membrane fusion and is therefore required for virus entry and cell fusion. The target protein is also a major immunogen and a possible target for entry inhibitors.
The SARS-CoV-2 spike (S) protein is a large type I transmembrane protein composed of two subunits, S1 and S2. The S1 subunit contains a receptor-binding domain (RBD) responsible for binding to the host cell receptor angiotensin-converting enzyme 2 (ACE2). The S2 subunit mediates fusion between the viral and host cell membranes. The S1 RBD protein plays key parts in the induction of neutralizing-antibody and T-cell responses, as well as protective immunity.
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|Citation Date||Citation Title||Citation Authors||Citation Abstract||Citation DOI|
|5 May 2023||Omicron infection-associated T- and B-cell immunity in antigen-naive and triple-COVID-19-vaccinated individuals||Joana Barros-Martins, Swantje I. Hammerschmidt, Gema Morillas Ramos, Anne Cossmann, Laura Hetzel, Ivan Odak, et al.||Since early 2022, various Omicron variants have dominated the SARS-CoV-2 pandemic in most countries. All Omicron variants are B-cell immune escape variants, and antibodies induced by first-generation COVID-19 vaccines or by infection with earlier SARS-CoV-2 variants largely fail to protect individuals from Omicron infection. In the present study, we investigated the effect of Omicron infections in triple-vaccinated and in antigen-naive individuals. We show that Omicron breakthrough infections occurring... read more||https://doi.org/10.3389/fimmu.2023.1166589|
|27 February 2023||Veklury® (remdesivir) formulations inhibit initial membrane-coupled events of SARS-CoV-2 infection due to their sulfobutylether-β-cyclodextrin content||Tamas Kovacs, Kitti Kurtan, Zoltan Varga, Peter Nagy, Gyorgy Panyi, Florina Zakany||Despite its contradictory clinical performance, remdesivir (Veklury®) has a pivotal role in COVID-19 therapy. Possible contributions of the vehicle, sulfobutylether-β-cyclodextrin (SBECD) to Veklury® effects have been overlooked. The powder and ... read more||https://doi.org/10.1111/bph.16063|
|27 October 2021||SARS-CoV-2 S1 Protein Induces Endolysosome Dysfunction and Neuritic Dystrophy||Gaurav Datta, Nicole M. Miller, Peter W. Halcrow, Nabab Khan, Timothy Colwell, Jonathan D. Geiger, Xuesong Chen||SARS-CoV-2 is the viral cause of the COVID-19 pandemic. Increasingly, significant neurological disorders have been associated with COVID-19. However, the pathogenesis of these neurological disorders remains unclear especially because only low or undetectable levels of SARS-CoV-2 have been reported in human brain specimens. Because SARS-CoV-2 S1 protein can... read more||https://doi.org/10.3389/fncel.2021.777738|