Recombinant Mouse Anti-JEV E protein Antibody (E3.3) (CAT#: PABZ-153)

Figure 1 Western blot analysis of the recombinant JEV E-Trx fusion proteins from the transformed cell lysate.

The blot was probed with MAb E3.3 and was developed with an alkaline phosphatase-conjugated secondary antibody and NBT/BCIP substrates.

Lin, C. W., & Wu, S. C. (2003). A functional epitope determinant on domain III of the Japanese encephalitis virus envelope protein interacted with neutralizing-antibody combining sites. Journal of virology, 77(4), 2600-2606.

Figure 2 Relative immunoreactivities of the mutant domain III proteins to MAb E3.3 determined by ELISA.

The wild-type, alanine substitution mutants (A), Ser-331 mutants (B), and Asp-332 mutants (C) were captured onto 96-well plates with rabbit anti-Trx antibodies, followed by incubation with a serial dilution of MAb E3.3. Bound MAb E3.3 was detected by using goat anti-mouse IgG-horseradish peroxidase conjugate and ABTS/H₂O₂ substrates. OD (405 nm), optical density at 405 nm.

Lin, C. W., & Wu, S. C. (2003). A functional epitope determinant on domain III of the Japanese encephalitis virus envelope protein interacted with neutralizing-antibody combining sites. Journal of virology, 77(4), 2600-2606.

Figure 3 Relative affinities of mutant and wild-type domain III fusion proteins for MAb E3.3 determined by ELISA

Lin, C. W., & Wu, S. C. (2003). A functional epitope determinant on domain III of the Japanese encephalitis virus envelope protein interacted with neutralizing-antibody combining sites. Journal of virology, 77(4), 2600-2606.

Figure 4 JEV plaques recovered from inhibition of mAb E3.3-neutralization to JEV by the E6 phages (A), E14 phages (B) and E18 phages (C).

The mAb E3.3 was incubated with 100 pfu JEV and a desired number of indicated phages, then recovered JEV plaques were obtained from the plaque determination on monolayers of BHK-21 cells.

Wu, S. C., & Lin, C. W. (2001). Neutralizing peptide ligands selected from phage-displayed libraries mimic the conformational epitope on domain III of the Japanese encephalitis virus envelope protein. Virus Research, 76(1), 59-69.

Figure 5 Neutralization titration curves of mAb E3.3 concentration (ascitic fluid) in three Japanese encephalitis viruses: CH2195 (closed circles), Beijing-1 (open circles) and Nakayama-N1H (boxes).

Wu, S. C., Lian, W. C., Hsu, L. C., & Liau, M. Y. (1997). Japanese encephalitis virus antigenic variants with characteristic differences in neutralization resistance and mouse virulence. Virus research, 51(2), 173-181.