SARS-CoV-2 (COVID-19) Spike S1 Protein (RBD), GFP/His-Tag

€1,490.00 €1,990.00

Price excl. shipping costs excl. VAT. For more information, see our shipping policy

SKU: P2020-031 trenzyme

Need a quote for an individual request or for a bulk order?

Please contact us.

Description

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 + His-Tag.

Overview

  • 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
Cellebrity Kolben Cell Cartoon trenzyme

Customer Testimonial

“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

Sequence Information

  • Species: SARS-CoV-2; Wuhan seafood market pneumonia virus
  • Tags: His-Tag, N-terminal and GFP+His-Tag, C-terminal
  • Sequence without tags (AA 319-541):
    MRVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYA
    DSFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAG
    STPCNGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNF

Product Information

  • Expression Host: human, HEK293
  • Formulation: PBS, pH 7,4
  • Format: Liquid, stored and shipped at -80°C
  • Purity: > 85% as determined by SDS-PAGE

Background Information

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.


Time-dependent binding of wild-type spike RBD to the membrane of ACE2 overexpressing cells

Binding of wild-type spike RBD to the membrane of ACE2 overexpressing cells

time dependence of binding of 5 µg/ml wild-type spike RBD to the membrane of ACE2 overexpressing cells
30 minutes of labeling at different wild-type spike RBD concentrations

Time dependence of binding of 5 µg/ml wild-type spike RBD-GFP to the membrane of ACE2 overexpressing cells (data after 5, 10, 20 and 30 minutes of labeling are shown)
Data provided by Kovacs T., Nagy P., Panyi G. and Zakany F., Department of Biophysics and Cell Biology, University of Debrecen, Hungary

Data obtained after 30 minutes of labeling at different wild-type spike RBD-GFP concentrations (0.2, 1 and 5 µg/ml)

Data provided by Kovacs T., Nagy P., Panyi G. and Zakany F., Department of Biophysics and Cell Biology, University of Debrecen, Hungary

SDS-PAGE/Coll. Coomassie

Histogram of marked lane in gel picture

SARS-CoV-2 (COVID-19) Spike S1 Protein (RBD), GFP/His-Tag SDS-Page
SARS-CoV-2 (COVID-19) Spike S1 Protein (RBD), GFP/His-Tag Histogram

Citations

The table below lists publications that mention this catalog protein. To sort the table, click on the first row.
Have you cited this product in a publication? Let us know so we can reference it here.


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

Get in contact with us


By submitting this form, I consent to trenzyme GmbH receiving and processing my data in order to process my inquiry. My consent is voluntary and I may revoke this consent at any time without providing any reasons, e.g. by sending an email to privacy(at)trenzyme.com with effect for the future. Further notices on data processing can be found in our privacy policy.