SARS-CoV-2 (COVID-19) S protein, GFP/His-Tag, stabilized trimer
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SKU: P2020-030 trenzyme
Description
Recombinant Spike protein of SARS-CoV-2 (COVID-19) from Wuhan pneumonia virus as a stabilized trimer with deletion of the internal Furin-site, C-terminal Strep/His-Tag and GFP as fusion partner. 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) SARS-CoV-2 (COVID-19) S protein, GFP/His-Tag, stabilized trimer
- Catalog No.: P2020-030
- 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
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: Strep/His-Tag and GFP, C-terminal
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Sequence without tags (AA 16-1211):
MVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTN GTKRFDNPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQ FCNDPFLGVYYHKNNKSWMESEFRVYSSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVF KNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQTLLALHRSYLTPGDS SSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQ TSNFRVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASF STFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVI AWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPLQS YGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTE SNKKFLPFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNQVAVLYQD VNCTEVPVAIHADQLTPTWRVYSTGSNVFQTRAGCLIGAEHVNNSYECDIPIGAGICASY QTQTNSPGASVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTISVTTEILPVSMTKTSV
DCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKD
FGGFNFSQILPDPSKPSKRSFIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFN
GLTVLPPLLTDEMIAQYTSALLAGTITSGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVL
YENQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSNFGAISSV
LNDILSRLDPPEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQ
SKRVDFCGKGYHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFV
SNGTHWFVTQRNFYEPQIITTDNTFVSGNCDVVIGIVNNTVYDPLQPELDSFKEELDKYF
KNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIK
Product Information
- Expression Host: human, HEK293
- Formulation: PBS, pH 7,4
- Format: Liquid, stored and shipped at -80°C
- Purity: > 55% 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 confirmation (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. The protein contains furthermore GFP as fusion partner at the C-terminal end. Above all, the spike is a major immunogen and an interesting target for vaccine development as well as for serological assays.
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SDS-PAGE/Coll. Coomassie |
Histogram of marked lane in gel picture |
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Citations
The table below lists publications that mention this catalog protein. To sort the table, click on the first row.
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| Citation Date | Citation Title | Citation Authors | Citation Abstract | Citation DOI |
|---|---|---|---|---|
| 21 November 2022 | Increased circulating microparticles contribute to severe infection and adverse outcomes of COVID-19 in patients with diabetes | Haoyu Sun, Yong Du, Rinki Kumar, Nicholas Buchkovich, and Pingnian He | Patients with diabetes infected with COVID-19 have greater mortality than those without comorbidities, but the underlying mechanisms remain unknown. This study aims to identify the mechanistic interactions between diabetes and severe COVID-19. Microparticles (MPs), the cell membrane-derived vesicles released on cell activation, are largely increased in patients with ... read more | https://doi.org/10.1152/ajpheart.00409.2022 |
