Fig. 2

Comparison of scFvFc 2G8 purified from HR and N. benthamiana leaves. a SDS-PAGE of antibodies purified by protein A-based affinity chromatography from extracts of N. benthamiana and S. lycopersicum HR and agro-infiltrated N. benthamiana leaves. The purified antibodies (400 ng) were loaded on 10% SDS polyacrylamide gel under reducing (left part of the gel) and non-reducing conditions (right part of the gel) and stained with colloidal Coomassie blue. M: ColorBurst Electrophoresis Marker (M.W. 8000–220,000 Da)(Sigma-Aldrich). b Functional binding of scFvFc 2G8 recombinant antibodies purified from HR and N. benthamiana leaves to immobilized laminarin assessed by ELISA. Anti-human γ chain antibody conjugated to alkaline phosphatase was used as secondary reagent for assay development. Specific binding (O.D. 405 nm) is plotted as function of the scFvFc 2G8 concentration (ng/mL) after subtraction of negative controls absorbance. Values represent average ± standard deviation (n = 3)