Alternative names:
SARS-CoV-2 Beta variant

Data and images for Recombinant SARS-CoV-2 RBD B.1.351 (HEK)

Figures

Figure 1

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Cell-based RBD binding assay
. Schematic overview illustrating how our biotinylated RBD can be applied to analyze binding to ACE2-expressing cells.
Different protein concentrations were used, and ACE2-bound spike protein was subsequently detected by fluorescent staining with streptavidin-PE. Quantification of stained cells at different protein concentrations illustrates that Miltenyi Biotec's recombinant spike monomer is biologically functional and shows a titratable, high-affinity binding to cell surface ACE2.

Figure 1

Cell-based RBD binding assay
. Schematic overview illustrating how our biotinylated RBD can be applied to analyze binding to ACE2-expressing cells.
Different protein concentrations were used, and ACE2-bound spike protein was subsequently detected by fluorescent staining with streptavidin-PE. Quantification of stained cells at different protein concentrations illustrates that Miltenyi Biotec's recombinant spike monomer is biologically functional and shows a titratable, high-affinity binding to cell surface ACE2.

Figure 2

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Results of the cell-based binding assay using biotinylated Recombinant SARS-CoV-2 RBD B.1.351 (HEK).
ACE2-expressing cells (Vero E6 cells) were incubated with biotinylated recombinant SARS-CoV-2 RBD of the SARS-CoV-2 variant B.1.351, Beta (Recombinant SARS-CoV-2 RBD B.1.351 (HEK)).
Different protein concentrations were used, and ACE2-bound spike protein was subsequently detected by fluorescent staining with streptavidin-PE. Quantification of stained cells at different protein concentrations illustrates that Miltenyi Biotec's recombinant spike monomer is biologically functional and shows a titratable, high-affinity binding to cell surface ACE2.

Figure 2

Results of the cell-based binding assay using biotinylated Recombinant SARS-CoV-2 RBD B.1.351 (HEK).
ACE2-expressing cells (Vero E6 cells) were incubated with biotinylated recombinant SARS-CoV-2 RBD of the SARS-CoV-2 variant B.1.351, Beta (Recombinant SARS-CoV-2 RBD B.1.351 (HEK)).
Different protein concentrations were used, and ACE2-bound spike protein was subsequently detected by fluorescent staining with streptavidin-PE. Quantification of stained cells at different protein concentrations illustrates that Miltenyi Biotec's recombinant spike monomer is biologically functional and shows a titratable, high-affinity binding to cell surface ACE2.

Figure 3

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SDS-PAGE of biotinylated Recombinant SARS-CoV-2 RBD B.1.351 (HEK)
under reduced (R) and non-reduced (NR) conditions.

Figure 3

SDS-PAGE of biotinylated Recombinant SARS-CoV-2 RBD B.1.351 (HEK)
under reduced (R) and non-reduced (NR) conditions.

Figure 4

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Size-exclusion chromatography (SEC) Recombinant SARS-CoV-2 RBD B.1.351 (HEK).
The non-biotinylated protein was analyzed and the peak corresponds to the monomeric protein.

Figure 4

Size-exclusion chromatography (SEC) Recombinant SARS-CoV-2 RBD B.1.351 (HEK).
The non-biotinylated protein was analyzed and the peak corresponds to the monomeric protein.

Specifications for Recombinant SARS-CoV-2 RBD B.1.351 (HEK)

Overview

The receptor binding domain (RBD) locates C-terminally within the S1 subunits of the spike (S) protein. The S protein forms a homotrimeric structure on the surface of the SARS-CoV-2 virus and binds to the angiotensin-converting enzyme 2 (ACE2) receptor of target cells. Recent studies have shown that the predominant activated form displays one RBD rotated upwards into an ACE2-accessible state and it is known that binding of RBD to ACE2 is a major contributor for interaction of the S protein with its target receptor.
The SARS-CoV-2 mutant strain B.1.351, also known as 501Y.V2 or Beta variant, was first identified during the Covid-19 pandemic in the Eastern Cape province of South Africa in December 2020 and rapidly spread globally partly owing to the increased transmissibility compared to the wild-type. The B.1.351 lineage (Beta variant) differs from the wild-type sequence by 21 amino acid mutations of which three key amino acid substitutions K417N, E484K and N501Y occur in the RBD. The N501Y mutation also emerged independently in SARS-CoV-2 variants in the B.1.1.7 lineage (Alpha variant) and P.1 lineage (Gamma variant). The B.1.351 lineage (Beta variant) is reported to have a higher infectivity due to its increased affinity to the ACE2 receptor and shows reduced susceptibility to neutralising antibodies.
The SARS-CoV-2 RBD B.1.351 (HEK) protein covers amino acids R319 to S591 of the spike protein, contains the N501Y, K417N and E484K mutations, as well as a C-terminal His-tag and a N-terminal AviTag™. Recombinant SARS-CoV-2 RBD B.1.351 (HEK)-Biotin is specifically biotinylated at a single site, preserving full functionality of the RBD.

Alternative names

SARS-CoV-2 Beta variant

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