SARS-CoV-2 (COVID-19) Spike S1 Protein (RBD, Mutant (Y453F))

Recombinant protein of the receptor binding domain (RBD), mutant (Y453F) of SARS-CoV-2 (COVID-2019) Spike S1 from Wuhan pneumonia virus with C-terminal His-Tag. Danish Mink mutation / Cluster 5 mutation (ΔFVI-spike).

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Overview

Product Name SARS-CoV-2 (COVID-19) Spike S1 Protein (RBD, Mutant (Y453F))
Catalog No. P2020-033
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; RBD (Y453F); Danish Mink mutation; Cluster 5 Mutation; ΔFVI‑spike

Sequence Information

Species SARS-CoV-2; Wuhan seafood market pneumonia virus
Tags His-tag, C-terminal
Sequence without tags (AA 319-541) RVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYA
DSFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLfRLFRKSNLKPFERDISTEIYQAG
STPCNGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNF

Product Information

Expression Host human, HEK293
Formulation PBS, pH 7,4
Format Liquid, stored and shipped at -80°C
Purity > 60% 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 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). Several mutants of the spike protein are known. One mutation first discovered in Denmark is the so-called “Cluster 5” also referred as ΔFVI-spike is related to four genetic changes. One mutation (Y453F) is located in a conservative region of the RBD directly involved in ACE2 binding and thereby could have implications for viral fitness, transmissibility, and antigenicity.

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Reinhold Horlacher, PhD

Reinhold Horlacher, PhD

Managing Director & CSO

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