Figure 1
Ab338 binding to Aβ depends on a mid-domain region in Aβ and amino acid 34. (A) Average affinity of the ab338 antibody to immobilized KLH-Cys-Aβ21–34 peptide as measured by optic density (OD) absorbance with points presented as mean ± standard error of the mean (SEM; n = 3). The data are presented as an adapted sigmoid curve and the dotted line indicates the equillibrum dissociation constant, KD. (B) Indirect ELISA displaying binding of ab338 to various immobilized Aβ-peptides, some of which harbor a N-terminal cystein (C-Aβ-peptides). Binding are presented relative to Aβ21–34 as mean ± SEM after vehicle coat background subtraction. Data are from two independent experiments (n = 6 in two experiments, total n = 12). (C) Competitive ELISA with various Aβ-peptides competing in solution for binding to ab338 binding with the KLH-Cys-Aβ21–34 plate coat presented with the sigmoid adapted curves (n ≥ 6, from ≥ 2 independent experiments). (D) Half inhibitory concentration (IC50) of various Aβ-peptides competing for ab338 binding with coat in competitive ELISA.
