Anti-Aβ1-42 Recombinant Antibody (3.4A10) (CAT#: TAB-0852CLV)

Figure 1 3.4A10 had higher affinity to Aβ₁₋₄₂ and did not bind native or denatured AβPP fragments.

400 ng of different Aβ fragments were immobilized onto the nitrocellulose membrane, 1 µg/ml 3.4A10 or 4G8 was used to detect the dots. 3.4A10 recognized Aβ₁₋₂₈, Aβ₁₋₄₀ and Aβ₁₋₄₂with an increasing signal density and did not bind Aβ₂₅₋₃₅ and Aβ₃₄₋₄₂.

Wang, J., Hara, H., Makifuchi, T., & Tabira, T. (2008). Development and characterization of a TAPIR-like mouse monoclonal antibody to amyloid-β. Journal of Alzheimer's disease, 14(2), 161-173.

Figure 2 3.4A10 inhibited Aβ₁₋₄₂ fibrillation and degraded pre-aggregated Aβ₁₋₄₂by thioflavin T-based fluorescence spectrophotometry

The freshly prepared 25 mM Aβ₁₋₄₂ in PBS was incubated with 2.5 mM 3.4A10 in a final volume of 25 µl at 37◦C for 1 week, and 1 ml of 5 mM thioflavin T was added to the system and fluorescence was measured at an excitation wavelength of 445 nm and an emission wavelength of 490 nm. The results showed that 3.4A10 decreased the fluorescence to 36.7% ± 0.67% of the control.

Wang, J., Hara, H., Makifuchi, T., & Tabira, T. (2008). Development and characterization of a TAPIR-like mouse monoclonal antibody to amyloid-β. Journal of Alzheimer's disease, 14(2), 161-173.

Figure 3 3.4A10 inhibited Aβ₁₋₄₂ fibrillation and degraded pre-aggregated Aβ₁₋₄₂by thioflavin T-based fluorescence spectrophotometry

For degradation assay, 3.4A10 was incubated with pre-aggregated Aβ₁₋₄₂ about 1:10 molar ratio at 37◦C for 2 days, and fluorescence spectrophotomtry assay showed that 3.4A10 reduced 490 nm emission value of pre-aggregated Aβ₁₋₄₂ by 22.3 ± 3.48% compared to the control.

Wang, J., Hara, H., Makifuchi, T., & Tabira, T. (2008). Development and characterization of a TAPIR-like mouse monoclonal antibody to amyloid-β. Journal of Alzheimer's disease, 14(2), 161-173.

Figure 4 3.4A10 recognized less plaque cores than 4G8.

Pairs of consecutive frozen sections of AD patient brain were stained with 1 µg/ml 3.4A10 or 4G8. 3.4A10 stained preferably the peripheral zone of senile plaques in the similar pattern with 4G8 and recognized less plaque cores compared with 4G8. The percentage of cored plaques was compared between 3.4A10 and 4G8 (7.5 ± 1.57% versus 14.93 ± 2.7%).

Wang, J., Hara, H., Makifuchi, T., & Tabira, T. (2008). Development and characterization of a TAPIR-like mouse monoclonal antibody to amyloid-β. Journal of Alzheimer's disease, 14(2), 161-173.

Figure 5 3.4A10 reduced the brain amyloid burden.

The percentage of the area occupied by Aβ deposits in the brain section.

Wang, J., Hara, H., Makifuchi, T., & Tabira, T. (2008). Development and characterization of a TAPIR-like mouse monoclonal antibody to amyloid-β. Journal of Alzheimer's disease, 14(2), 161-173.

Figure 6 Western blot results of Aβ oligomers in TBS fraction of the brain lysates.

Compared to the control, the 3.4A10 reduced the 12mer Aβ oligomer without obvious effects on other Aβ oligomer. The sAβPP and amyloid oligomers were detected by 6E10 and HRP conjugated goat anti-mouse IgG second antibody

Wang, J., Hara, H., Makifuchi, T., & Tabira, T. (2008). Development and characterization of a TAPIR-like mouse monoclonal antibody to amyloid-β. Journal of Alzheimer's disease, 14(2), 161-173.