Fig. 1: Discovery and characterization of anti-GGX mAbs.

a The chemical structure of GGM and K-ε-GG peptides highlights the high similarity between both peptides. b Schematic of the immunization and phage panning strategy used to discover the anti-GGX mAbs. Biotinylated (Bio-GGM) and BSA conjugated (BSA-GGM) were used for positive selections and a biotinylated K-ε-GG (red, Bio K-ε-GG) was used for negative selections. c ELISA characterization of the four anti-GGX mAbs and anti-K-ε-GG mAb confirms the GGM specificity of the antibodies. Binding to the GGM peptide is shown in blue, K-ε-GG peptide in red, and neutravidin in black. Results are representative of biological replicates (n = 3). Data are presented as mean ± SD. d ELISA characterization of anti-GGX mAbs against GGX peptides, in which X represents all twenty amino acids except for cysteine, shows degenerate recognition at the X position. The darker shading corresponds to the better binding. STV is the streptavidin control. Results are representative of biological replicates (n = 3). Data are presented as mean ± SD. Source data are provided as a Source Data file.