Protein extraction and western blot. Control and treated muscle samples were homogenised in lysis buffer comprising 75 mmol/l Tris-HCl (pH 6.5) and 10% sodium dodecyl sulphate complemented with 5% 2-mercaptoethanol. Samples were heated at 100 °C for 3 minutes before centrifugation and removal of supernatant. Protein levels were measured by Bradford assay (Sigma) and quantified using BSA standards. Ten to fifteen micrograms of protein of untreated and treated mdx sample, and 50% and 10% of these concentrations of C57BL10 protein (positive control) were loaded onto 3-8% Tris-Acetate gels. Proteins were blotted onto polyvinylidene fluoride membrane and probed for dystrophin using DYS1 (Novocastra) and loading control, α-actinin (Sigma), antibodies. Primary antibody was detected by binding of horseradish peroxidase-conjugated anti-mouse immunoglobulin G with lumigen. Western blots were imaged (LiCOR Biosciences, Lincoln, NE) and analyzed using the Odyssey imaging system.