MOESM1 of Enhanced production of a single domain antibody with an engineered stabilizing extra disulfide bond

Additional file 1: Figure S1. Isoelectric focusing gel of sdAb. Measurement of isoelectric point using isoelectric focusing gel electrophoresis. Each well was loaded 10 µg of sample, except 4 µg of lane 5 sample was loaded. Lanes 1 and 10 represent the Serva pI marker (pH 3-10 from Life technologies Inc). Lane 2: Ac+neg: lane 3: AC+neg2; lane 4: AC+; lane 5: A3+; lane 6: A3+neg; lane 7: G2+; Lane 8: G2+neg; Lane 9: G2+neg2

MOESM4 of Enhanced production of a single domain antibody with an engineered stabilizing extra disulfide bond

Additional file 4: Figure S4. Molecular weight and purity assessment of sdAb. Figure S4. Assessment of purity for purified single domain antibodies on gel electrophoresis. The virtual gel was obtained from Experion Pro260 chip (Bio-Rad laboratories). Approximately 200 µg/mL for each protein sample was used. The peak density of purified single domain antibodies as indicated by the blue arrow is >95 %. The rest of the bands represent high and low markers and internal systematic bands as indicated by the magenta arrows and described as such in the manufacturer’s protocol (Bio-Rad). Sample order is as follows, Lane L: Molecular marker Ladder. L1: ACneg; L2: AC+neg; L3: AC+neg2; L4: AC+;L5: A3+; L6: A3+neg; L7: G2+; L8: G2+neg; L9: G2+neg2; L10: G2

MOESM3 of Enhanced production of a single domain antibody with an engineered stabilizing extra disulfide bond

Additional file 3: Figure S3. Sequence alignment of sdAb AC and variants. Sequence alignment of the SEB binding sdAb AC, AC+, AC+neg and AC+neg2 using MultAlin [29]. The initial two amino acids (MA) and the amino acids added due to the restriction sites and the His-tag are not show above (AAALEHHHHHH)