Front Cover: Specific glutamic acid residues in targeted proteins induce exaggerated retardations in Phos‐tag SDS‐PAGE migration

Electrophoresis 2017, 38, 1139–1146. DOI: 10.1002/elps.201600520 The front cover picture shows typical banding patterns of human histone proteins in phosphate‐affinity Phos‐tag SDS‐PAGE. Histone H2A shows extremely retarded migrations relative to the molecular weight in Phos‐tag SDS‐PAGE, despite being nonphosphorylated. In addition, Phos‐tag SDS‐PAGE permits us to detect a shift in the mobility of the phosphorylated form of histone H2A from that of the nonphosphorylated counterpart. We conclude that specific glutamic acid residues in the targeted protein induce exaggerated retardations in Phos‐tag SDS‐PAGE migration.