MOESM4 of Enhanced production of a single domain antibody with an engineered stabilizing extra disulfide bond
Jinny Liu
Ellen Goldman
Dan Zabetakis
Scott Walper
Kendrick Turner
Lisa Shriver-Lake
George Anderson
10.6084/m9.figshare.c.3607484_D3.v1
https://springernature.figshare.com/articles/journal_contribution/MOESM4_of_Enhanced_production_of_a_single_domain_antibody_with_an_engineered_stabilizing_extra_disulfide_bond/4351988
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.
2015-10-09 05:00:00
Camelid
Single domain antibody
Disulfide bond
Thermal stability
Protein production