Recombinant Mouse Anti-Glycoprotein Antibody (523-11) (CAT#: PABX-163)

Figure 1 ELISA-binding profiles.

Mean values were determined from three independent experiments and are presented with SD values indicated by error bars.

Yang, F., Lin, S., Ye, F., Yang, J., Qi, J., Chen, Z., ... & Lu, G. (2020). Structural analysis of rabies virus glycoprotein reveals pH-dependent conformational changes and interactions with a neutralizing antibody. Cell host & microbe, 27(3), 441-453.

Figure 2 Blockage of the glycoprotein-mediated cell-cell fusion by 523-11.

Syncytia formed are marked with arrows. Scale bar: 200 μm.

Yang, F., Lin, S., Ye, F., Yang, J., Qi, J., Chen, Z., ... & Lu, G. (2020). Structural analysis of rabies virus glycoprotein reveals pH-dependent conformational changes and interactions with a neutralizing antibody. Cell host & microbe, 27(3), 441-453.

Figure 3 Inhibition of RABV infection by 523-11.

BHK-21 cells are left uninfected (Blank) or infected with the Flury strain of RABV in the absence (RABV) or presence of the indicated antibodies (RABV + Iso-control and RABV + 523-11) and stained with a FITC-labeled RABV N-protein antibody (green) and Evans blue (light red). Representative cell images are shown. Scale bar: 200 μm.

Yang, F., Lin, S., Ye, F., Yang, J., Qi, J., Chen, Z., ... & Lu, G. (2020). Structural analysis of rabies virus glycoprotein reveals pH-dependent conformational changes and interactions with a neutralizing antibody. Cell host & microbe, 27(3), 441-453.

Figure 4 A western blot assay characterizing the interactions of the indicated antibodies with denatured RABV-G-ΔFuLp.

Yang, F., Lin, S., Ye, F., Yang, J., Qi, J., Chen, Z., ... & Lu, G. (2020). Structural analysis of rabies virus glycoprotein reveals pH-dependent conformational changes and interactions with a neutralizing antibody. Cell host & microbe, 27(3), 441-453.

Figure 5 Characterization of the antigen/antibody interaction by surface plasmon resonance.

The binding profiles are shown. The marked χ2/RUmax value (< 10%) highlights the goodness of fit between the experimental data and the model algorithm. Characterization of the interaction at pH 8.0.

Yang, F., Lin, S., Ye, F., Yang, J., Qi, J., Chen, Z., ... & Lu, G. (2020). Structural analysis of rabies virus glycoprotein reveals pH-dependent conformational changes and interactions with a neutralizing antibody. Cell host & microbe, 27(3), 441-453.

Figure 6 Characterization of the antigen/antibody interaction by surface plasmon resonance.

The binding profiles are shown. The marked χ2/RUmax value (< 10%) highlights the goodness of fit between the experimental data and the model algorithm. Characterization of the interaction at pH 6.5.

Yang, F., Lin, S., Ye, F., Yang, J., Qi, J., Chen, Z., ... & Lu, G. (2020). Structural analysis of rabies virus glycoprotein reveals pH-dependent conformational changes and interactions with a neutralizing antibody. Cell host & microbe, 27(3), 441-453.