Recombinant Mouse Anti-HBeAg Antibody (e6) (CAT#: PABL-112)

Figure 1 Epitope mapping using surface plasmon resonance.

(A) Biacore sensograms indicating binding kinetics generated from immobilized Fab e13 (ligand) titrated with analyte mixtures containing a fixed amount of rHBeAg (1.5 µM) and a variable amount of Fab me6 (0 – 133 nM). (B) Immobilized Fab me6 (ligand) titrated with analyte mixtures containing either a fixed amount (0.4 µM) of rHBeAg and a variable amount of Fab e13, or a fixed amount (1.5 µM) rHBeAg and a variable amount of Fab me6. The steady-state maximum binding is plotted as a function of analyte Fab concentration (abscissa). For both panels A and B, the ordinate scales indicate SPR response in resonance units (RU).

Zhuang, X., Watts, N. R., Palmer, I. W., Kaufman, J. D., Dearborn, A. D., Trenbeath, J. L.,... & Wingfield, P. T. (2017). Chimeric Rabbit/Human Fab Antibodies Against the Hepatitis B e-antigen and Their Potential Applications in Assay, Characterization and Therapy. Journal of Biological Chemistry, jbc-M117.

Figure 2 Secondary antibody pairing.

A sandwich ELISA was used which incorporated Mab e6-coated plates for antigen capture, and Fabs e13, e21 or e38 for detection. Anti-human IgGHRP was used to generate the absorbance signal at 450 nm. The assay was performed over the range of 0 – 1 µg/ml rHBeAg. The experiment was performed three times, with similar results.

Zhuang, X., Watts, N. R., Palmer, I. W., Kaufman, J. D., Dearborn, A. D., Trenbeath, J. L.,... & Wingfield, P. T. (2017). Chimeric Rabbit/Human Fab Antibodies Against the Hepatitis B e-antigen and Their Potential Applications in Assay, Characterization and Therapy. Journal of Biological Chemistry, jbc-M117.