Figure 6.
34-1-2S demonstrates increased complement activation compared with SF1.1.10 and AF6-88.5.5.3 that is Fc dependent and not significantly dependent on Fc glycosylation. Antibody- and C1q-binding ELISAs based on 34-1-2S and SF1.1.10 (full-length IgG, deglycosylated IgG, Fab fragments, and with a serum heat-inactivation control) binding to H-2Kd (A, left and right panel, respectively). Antibody- and C1q-binding ELISAs based on AF6-88.5.5.3 (full-length IgG and with serum heat-inactivation control) binding to H-2Kb (B, left and right panel, respectively). Statistical analysis for C1q binding is performed with two-way analysis of variance with a Tukey post hoc test (A) and an ordinary 2-way analysis of variance (B). A representative ELISA of n = 5 experiments is shown in each figure panel. ***P < .001, ****P < .0001.

34-1-2S demonstrates increased complement activation compared with SF1.1.10 and AF6-88.5.5.3 that is Fc dependent and not significantly dependent on Fc glycosylation. Antibody- and C1q-binding ELISAs based on 34-1-2S and SF1.1.10 (full-length IgG, deglycosylated IgG, Fab fragments, and with a serum heat-inactivation control) binding to H-2Kd (A, left and right panel, respectively). Antibody- and C1q-binding ELISAs based on AF6-88.5.5.3 (full-length IgG and with serum heat-inactivation control) binding to H-2Kb (B, left and right panel, respectively). Statistical analysis for C1q binding is performed with two-way analysis of variance with a Tukey post hoc test (A) and an ordinary 2-way analysis of variance (B). A representative ELISA of n = 5 experiments is shown in each figure panel. ***P < .001, ****P < .0001.

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