Figure 1. Distribution of kcnmb2 message and demonstration of β2 (KCNMB2) protein in specific tissues. (A) Quantitative RT-PCR was used to define relative (normalized to β-actin) kcnmb2 message abundance. Each estimate corresponds to mean and standard error for RNA preparations from three mice, each done in triplicate. (B) Total proteins were first immunoprecipitated with the Alomone anti-Sloβ2 Ab. Subsequently, aliquots of proteins obtained by IP were then treated with (+) or without (−) N-glycanase, separated by Western blot (WB), and visualized with NeuroMab anti-BKbeta2 N53/32 Ab. All tested tissues reveal β2 protein that is absent in the kcnmb2−/− mice. Note the apparent diversity of molecular size of glycosylated β2 protein among various tissues. Glycanase-free lanes were omitted for adrenal medulla because of the small size of original tissue samples. Molecular mass is indicated in kilodaltons.
Figure 1.

Distribution of kcnmb2 message and demonstration of β2 (KCNMB2) protein in specific tissues. (A) Quantitative RT-PCR was used to define relative (normalized to β-actin) kcnmb2 message abundance. Each estimate corresponds to mean and standard error for RNA preparations from three mice, each done in triplicate. (B) Total proteins were first immunoprecipitated with the Alomone anti-Sloβ2 Ab. Subsequently, aliquots of proteins obtained by IP were then treated with (+) or without (−) N-glycanase, separated by Western blot (WB), and visualized with NeuroMab anti-BKbeta2 N53/32 Ab. All tested tissues reveal β2 protein that is absent in the kcnmb2−/− mice. Note the apparent diversity of molecular size of glycosylated β2 protein among various tissues. Glycanase-free lanes were omitted for adrenal medulla because of the small size of original tissue samples. Molecular mass is indicated in kilodaltons.

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