Figure 4.
Figure 4. The disruptive mAbs target an overlapping epitope. (A) Alignment of the murine and human VE-cadherin amino acid sequence up to position 56. Differences in the amino acid sequence are underlined and in boldface. Shown are the murine amino acids sequences 15-20, 27-31, 36-38, 41-42, 45-51, and 54-56 that were substituted with corresponding human sequence to generate the human-murine VE-cadherin chimeras (shown in brackets). (B) Binding activity of BV13 and 10G4 on 293 cells transfected with the VE-cadherin chimeras, as compared to mock-transfected and mWT VE-cadherin, as measured by flow cytometry. Cells were stained with BV13 and 10G4 followed by goat anti–rat-PE secondary antibody to determine relative MFI by flow cytometry analysis (n = 3); error bars represent the standard deviation.

The disruptive mAbs target an overlapping epitope. (A) Alignment of the murine and human VE-cadherin amino acid sequence up to position 56. Differences in the amino acid sequence are underlined and in boldface. Shown are the murine amino acids sequences 15-20, 27-31, 36-38, 41-42, 45-51, and 54-56 that were substituted with corresponding human sequence to generate the human-murine VE-cadherin chimeras (shown in brackets). (B) Binding activity of BV13 and 10G4 on 293 cells transfected with the VE-cadherin chimeras, as compared to mock-transfected and mWT VE-cadherin, as measured by flow cytometry. Cells were stained with BV13 and 10G4 followed by goat anti–rat-PE secondary antibody to determine relative MFI by flow cytometry analysis (n = 3); error bars represent the standard deviation.

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