NeuroMab™ Anti-TfR BBB Shuttle Antibody, Clone NR54P

Fig.1 depict FACS analysis of mouse hybridoma parental clone supernatants binding to human and cynomolgus TfR transiently expressed in 293 cells in the presence of 1 μM human holo-Tf.

The results shown are a titration of 5 concentrations.
1: monomer, free N-terminus, 4.2 mg/mL, never thawed;
2: monomer, His-tagged N-terminus, 4.8 mg/mL;
3: dimer, free N-terminus, 1.6 mg/mL.

Fig.2 depicts the binding of hu7A4.v15, hu15G11.v5 and hu7G7.v1 to huTfR in the presence of 6.3 μM holo-Tf.

Antibody binding to immobilized huTfR is shown in the presence (open symbols and dashed lines) or absence (filled symbols and solid lines) of 6.3 μM holo-Tf.

Fig.3 depict the results of the HFE-HuTfR binding and the HFE blocking assays.

The binding of antibody to increasing concentrations of huTfR captured via immobilized HFE. FIG. 6B shows the binding of huTfR to immobilized HFE in the presence of increasing concentrations of antibody.

Fig.4 depict the results of the HFE-HuTfR binding and the HFE blocking assays.

The binding of huTfR to immobilized HFE in the presence of increasing concentrations of antibody.

Fig.5 depict the results of experiments assessing the impact of effector function status on ADCC activity of anti-human TfR (“anti-hTFR”) antibodies in primary human bone marrow mononuclear cells or in a human erythroblast cell line.

The binding of huTfR to immobilized HFE in the presence of increasing concentrations of antibody.

Fig.6 depict the brain antibody concentrations of the experiments.

The figure shows individual anti-TfR1/BACE1, anti-TfR2/BACE1, anti-gD, and anti-BACE1 concentrations of antibody in various brain regions at 24 hours post-dose.

Fig.7 The pharmacodynamic results of the experiments in cynomolgus monkeys.

sAPPβ/sAPPα ratio over time.