Fig. 3
From: Cav3.2 calcium channel interactions with the epithelial sodium channel ENaC
β-ENaC N-terminus lysines contribute to Cav3.2interactions. (a) Cav3.2 immunoprecipitates from tsA201 cells transfected with either wild type (WT) β-ENaC or mutant (Mut) β-ENaC (K4R/ K5R/ K9R/ K16R/ K23R) subunits were probed for β-ENaC, n = 5–6. Membranes were stripped and probed for Cav3.2 by Western blot. Actin loading controls are shown, n = 5–6. (b) Quantification analysis of β-ENaC bound to Cav3.2 immunoprecipitates