Figure 3.
Figure 3. Identification of the disruptive mAb-binding domain. (A) Diagram illustrates the hVE-cadherin1-31/mVE-cadherin32-739 (1-31 h/m), hVE-cadherin1-56/mVE-cadherin57-739 (1-56 h/m), and the mVE-cadherin1-56/hVE-cadherin57-737 (1-56 m/h) chimeric molecules tested. (B) Binding activity of BV13 and 10G4 on 293 cells transfected with the 1-31 h/m, 1-56 h/m, and 1-56 m/h chimeric VE-cadherin proteins, as compared to mock-transfected, and wild-type murine (mWT) and human wild-type (hWT) 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.

Identification of the disruptive mAb-binding domain. (A) Diagram illustrates the hVE-cadherin1-31/mVE-cadherin32-739 (1-31 h/m), hVE-cadherin1-56/mVE-cadherin57-739 (1-56 h/m), and the mVE-cadherin1-56/hVE-cadherin57-737 (1-56 m/h) chimeric molecules tested. (B) Binding activity of BV13 and 10G4 on 293 cells transfected with the 1-31 h/m, 1-56 h/m, and 1-56 m/h chimeric VE-cadherin proteins, as compared to mock-transfected, and wild-type murine (mWT) and human wild-type (hWT) 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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