Provided is a monoclonal antibody A8 against human amyloid. The antibody can be used for diagnosing and treating Alzheimer's disease.
Figure 1 Immunoreactivity of anti-Aβ scFv expressed in baculovirus.
Dot blot analysis shows the immunoreactivity of scFvs; the following antibodies were used: (1) His-VL-(G₄S)₃-VH, (2) VL-(G₄S)₃-VH-His, (3) monoclonal antibody A8 as a positive control, and (4) PBS as a negative control.
Zhang, Y., Yang, H. Q., Fang, F., Song, L. L., Jiao, Y. Y., Wang, H., ... & Hung, T. (2015). Single chain variable fragment against Aβ expressed in baculovirus inhibits Abeta fibril elongation and promotes its disaggregation. Plos one, 10(4), e0124736.
Figure 2 Inhibition of Aβ aggregation via the addition of an anti-Aβ scFv to the assembly reaction.
TEM image of fibrils formed in the absence (a) or presence (b, c, d) of anti-Aβ scFvs (100 μM). (A) Aβ42 was incubated with (a) boric acid buffer control, (b) VL-(G₄S)₃-VH from E. coli, (c) His-VL-(G₄S)₃-VH, or (d) VL-(G₄S)₃-VH-His from baculovirus, for 96 h (scale bar = 100 nm).
Zhang, Y., Yang, H. Q., Fang, F., Song, L. L., Jiao, Y. Y., Wang, H., ... & Hung, T. (2015). Single chain variable fragment against Aβ expressed in baculovirus inhibits Abeta fibril elongation and promotes its disaggregation. Plos one, 10(4), e0124736.
Figure 3 The dose-dependent increase in the anti-Aβ scFv effect.
TEM images of Aβ fibrils formed in the absence (a) or presence (b, c, d) of scFv. The scFvs were used at different concentrations, and Aβ was incubated with equal (b), five-fold (c) or ten-fold (d) molar excesses of scFv in boric acid buffer for 48 h (scale bar = 100 nm);
Zhang, Y., Yang, H. Q., Fang, F., Song, L. L., Jiao, Y. Y., Wang, H., ... & Hung, T. (2015). Single chain variable fragment against Aβ expressed in baculovirus inhibits Abeta fibril elongation and promotes its disaggregation. Plos one, 10(4), e0124736.
Figure 4 Blocking the effects of anti-Aβ scFv on Aβ aggregation and disaggregation by Aβ1–11 peptides.
The anti-Aβ scFv [His-VL-(G4S)3-VH)] was incubated with Aβ1–11 and Aβ12–24 before being added to the Aβ aggregation and disaggregation reaction systems.
Zhang, Y., Yang, H. Q., Fang, F., Song, L. L., Jiao, Y. Y., Wang, H., ... & Hung, T. (2015). Single chain variable fragment against Aβ expressed in baculovirus inhibits Abeta fibril elongation and promotes its disaggregation. Plos one, 10(4), e0124736.
Figure 5 Disaggregation of mature Aβ fibrils (48 h incubation) by anti-Aβ scFv.
The histogram shows the corresponding lengths of the fibrils from each group mentioned in (A). **: p<0.01.
Zhang, Y., Yang, H. Q., Fang, F., Song, L. L., Jiao, Y. Y., Wang, H., ... & Hung, T. (2015). Single chain variable fragment against Aβ expressed in baculovirus inhibits Abeta fibril elongation and promotes its disaggregation. Plos one, 10(4), e0124736.
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• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production
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