Fig. 1
R0-10C purified by mAb45.1-affinity chromatography. Purification and characterization of correctly folded monomeric R0.10C. a 2-site ELISA with the flow trough (FT) and immune purified antigen (500 ng/well) using mAb 85RF45.1, 85RF45.2b and 85RF45.3 as capture and anti-HIS-HRPO for detection. b Coomassie blue-stained 4–12 % Bis–Tris gel of R0.10C purification steps using 5 µg antigen/lane, c Western blot analysis using rat mAb 85RF45.1-HRP for detection. Lane 1, input antigen after Ni2++ column purification; Lane 2, Flow trough (FT: misfolded R0.10C) from the mAb Affinity column: lane 3, eluate (immune purified R0.10C (properly folded)) from the mAb affinity column; Lane 4, Markers, the sizes (kDa) of the molecular mass markers are indicated. d 2-site ELISA with the FT, mAb-Affinity eluted antigen (El) and mixed samples using mAb 85RF45.1 as capture and mAb 85RF45.2b-HRPO for detection. e correlation between EC50 titres and percentage of properly folded antigen (R = 0.9944: y = 4.59x + 0.505)