Fig. 7

Sandwich ELISA displaying the binding curves of the different antibodies to different species of Aβ. a Schematic representation of sandwich Aβ ELISA setup where the antigens (cross-linked Aβ42 fractions) are captured by an antibody coated on the well surface. The capture antibody binds to the C-terminal end of the antigen. This is followed by the addition of the generated recombinant antibodies that detect the N-terminal part of the antigen. b, c To the large Aβ1-42 aggregates, corresponding to fractions 1 and 2, similar binding strengths were seen among all antibodies. d, e Hexa-RmAb158 displayed stronger binding than all the other antibodies to the medium-sized aggregates corresponding to fractions 3 and 4. f Hexa-RmAb158 displayed some binding to the low-sized aggregates corresponding to fraction 5. The antibody 82E1 has been reported to bind equally strong to both monomers and aggregates and was used as a control. Data are presented as mean ± SD, n = 2 for fractions 1 & 4, n = 4 for fractions 2, 3 & 5