Tissue Expression and Actin Binding of a Novel N-Terminal Utrophin Isoform

Figure 4

Expression and purification of the recombinant utrophin (UT11 and UT12) and dystrophin (DYS12) fragments used for in vitro actin-binding studies. Fragments were expressed in E. coli by induction with isopropyl-β-D-1-thiogalactopyranoside (IPTG), subsequently purified by Ni-NTA (Ni-nitrilotriacetic acid) affinity chromatography, and finally checked on 10% SDS-PAGE. Protein staining with Coomassie brilliant blue R250 of bacterial expression (lanes 1) and purified fragments (lanes 2). The fragments were also immunostained with an anti-His-tag mAB.