The receptor binding domain (RBD) is located 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 RBD (insect cells) protein covers amino acids R319 to S591 of the spike protein and contains a His-tag and an AviTag™. Recombinant SARS-CoV-2 RBD

Data and images for Recombinant SARS-CoV-2 RBD (insect cells)

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Figure 1

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Bead-based immunoassay for detection of patient-derived SARS-CoV-2 antibodies
. Schematic overview illustrating how our biotinylated antigens can be applied to detect patient-derived SARS-CoV-2 antibodies

Figure 1

Bead-based immunoassay for detection of patient-derived SARS-CoV-2 antibodies
. Schematic overview illustrating how our biotinylated antigens can be applied to detect patient-derived SARS-CoV-2 antibodies

Figure 2

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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 2

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 3

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Results of the bead-based immunoassay using biotinylated Recombinant SARS-CoV-2 RBD (insect cells).
The amount of captured SARS-CoV-2 antibodies was quantified at different plasma dilutions. Results for plasma from a COVID-19
+
patient (circle) or a healthy donor (square) are shown.

Figure 3

Results of the bead-based immunoassay using biotinylated Recombinant SARS-CoV-2 RBD (insect cells).
The amount of captured SARS-CoV-2 antibodies was quantified at different plasma dilutions. Results for plasma from a COVID-19
+
patient (circle) or a healthy donor (square) are shown.

Figure 4

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Results of the cell-based binding assay using biotinylated Recombinant SARS-CoV-2 RBD (insect cells).
ACE2-expressing cells were incubated with different concentrations of biotinylated Recombinant SARS-CoV-2 RBD (HEK). ACE2-bound RBD was subsequently detected by fluorescent staining and the amount of positive cells is shown.

Figure 4

Results of the cell-based binding assay using biotinylated Recombinant SARS-CoV-2 RBD (insect cells).
ACE2-expressing cells were incubated with different concentrations of biotinylated Recombinant SARS-CoV-2 RBD (HEK). ACE2-bound RBD was subsequently detected by fluorescent staining and the amount of positive cells is shown.

Figure 5

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SDS-PAGE of biotinylated Recombinant SARS-CoV-2 RBD (insect cells)
under reduced (R) and non-reduced (NR)

Figure 5

SDS-PAGE of biotinylated Recombinant SARS-CoV-2 RBD (insect cells)
under reduced (R) and non-reduced (NR)

Figure 6

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Mass spectrometry analysis (ESI-MS) of Recombinant SARS-CoV-2 RBD (insect cells).
The non-biotinylated protein was analyzed and the peak corresponds to the deglycosylated molecular mass (34168 Da).

Figure 6

Mass spectrometry analysis (ESI-MS) of Recombinant SARS-CoV-2 RBD (insect cells).
The non-biotinylated protein was analyzed and the peak corresponds to the deglycosylated molecular mass (34168 Da).

Figure 7

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

Figure 7

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

Specifications for Recombinant SARS-CoV-2 RBD (insect cells)

Overview

The receptor binding domain (RBD) is located 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 RBD (insect cells) protein covers amino acids R319 to S591 of the spike protein and contains a His-tag and an AviTag™. Recombinant SARS-CoV-2 RBD (insect cells)-Biotin is specifically biotinylated at a single site, preserving full functionality of the RBD.

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