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SDS–PAGE analysis of the purified rLC.

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posted on 27.09.2013, 01:54 by Paola Rognoni, Francesca Lavatelli, Simona Casarini, Giovanni Palladini, Laura Verga, Paolo Pedrazzoli, Giovanna Valentini, Giampaolo Merlini, Vittorio Perfetti

Coomassie Brilliant Blue staining (A) and western blotting (B) analysis of purified rLC compared to AL-2 Bence Jones protein (AL-2 BJ), purified from urine. Protein samples (5 µg loaded) were resolved on 12% SDS-PAGE run under non reducing and reducing conditions. Western blot analysis was performed using a rabbit anti-human λ LC antiserum as primary antibody (Dako Cytomation, Glostrup, Denmark), revealed by a goat anti-rabbit conjugated with horseradish peroxidase (Dako Cytomation), probed with diaminobenzidine (DAB) substrate. Molecular mass markers are shown in the left lane. The proteins presented the typical dimeric-monomeric species of free LC. Different degrees of protein denaturation are responsible of the minor differences in electrophoretic migration of monoclonal free LC (A), a common finding in SDS PAGE running under denaturing conditions of these proteins.

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