SARS-CoV-2 (COVID-19) S protein, His-Tag, stabilized trimer

€430.00 €480.00

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

SKU: P2020-025 trenzyme

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

Please contact us.

Description

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.

Overview

  • 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
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 and Strep-Tag, both C-terminal
  • Sequence without tags (AA 16-1211):
    MVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNG
    TKRFDNPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQF
    CNDPFLGVYYHKNNKSWMESEFRVYSSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFK
    NIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQTLLALHRSYLTPGDSS
    SGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQT
    SNFRVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFS
    TFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIA
    WNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPLQSY
    GFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTES
    NKKFLPFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQDV
    NCTEVPVAIHADQLTPTWRVYSTGSNVFQTRAGCLIGAEHVNNSYECDIPIGAGICASYQ
    TQTNSPGASVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTISVTTEILPVSMTKTSVD
    CTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDF
    GGFNFSQILPDPSKPSKRSFIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNG
    LTVLPPLLTDEMIAQYTSALLAGTITSGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLY
    ENQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVL
    NDILSRLDPPEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQS
    KRVDFCGKGYHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVS
    NGTHWFVTQRNFYEPQIITTDNTFVSGNCDVVIGIVNNTVYDPLQPELDSFKEELDKYFK
    NHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK

Product Information

  • 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

Background Information

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)

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.

SDS-PAGE/Coll. Coomassie

Histogram of marked lane in gel picture

SARS-CoV-2 (COVID-19) S protein, His-Tag, stabilized trimer SDS-PAGE
SARS-CoV-2 (COVID-19) S protein, His-Tag, stabilized trimer 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
3 October 2022 Lactoferrin Binding to SARS-CoV-2 Spike Glycoprotein Blocks Pseudoviral Entry and Relieves Iron Protein Dysregulation in Several In Vitro Models Antimo Cutone, Luigi Rosa, Maria Carmela Bonaccorsi di Patti, Federico Iacovelli, Maria Pia Conte, Giusi Ianiro, Alice Romeo, et al. SARS-CoV-2 causes COVID-19, a predominantly pulmonary disease characterized by a burst of pro-inflammatory cytokines and an increase in free iron. The viral glycoprotein Spike mediates fusion to the host cell membrane, but its role as a virulence factor is largely unknown. Recently, the antiviral activity of lactoferrin against SARS-CoV-2 was demonstrated in vitro and ... read more https://doi.org/10.3390/pharmaceutics14102111

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.