Fig. 1
Transduction of C2C12 myotubes with a HERG1A-encoded adenovirus results in elevated HERG1A protein. a Immunoblot of equal protein content (50 μg) from lysates of non-transduced cells reveals that native ERG1 protein is 40.7% (p < 0.01; n = 6; Student’s t test) more abundant in myotubes than in myoblasts. Coomassie stained membrane confirms that equal amounts of cell lysate protein were loaded into each lane. b Immunohistochemistry labeling ERG1 protein with Alexfluor 488 (green) secondary antibody confirms that native ERG1 protein is more abundant in myotubes than in myoblasts. Representative images of immune-stained cells: (1) myoblasts immunostained with ERG1 primary antibody; (2) myoblasts immunostained without ERG1 primary antibody as control; (3) myotubes immunostained with ERG1 primary antibody; (4) myotubes immunostained without ERG1 primary antibody as control. Scale bar = 50 μm. c Transduction of C2C12 myotubes with a HERG1A-encoded adenovirus results in synthesis of HERG1A protein as demonstrated by immunoblot (p < 0.05; n = 6; two-way ANOVA). Coomassie stained membrane (blue) reveals that equal amounts of cell lysate protein were loaded into each lane