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. 2019 Jun 1;30(12):1425–1436. doi: 10.1091/mbc.E18-10-0687

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© 2019 Wiedmann et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.

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FIGURE 5: — N-glycosylation of hK_2P17.1 expressed in mammalian cells. (A) hK_2P17.1-WT channel subunits were heterologously expressed in HEK-293T cells in the presence or absence of the N-glycosylation inhibitor tunicamycin. Cell lysates were digested with PNGase F to remove N-linked sugar moieties as indicated. Immunoblots for glyceraldehyde-3-phosphate dehydrogenase (GAPDH) served as loading control. (B) WT hK_2P17.1 channel subunits and glutamine mutants were expressed in HEK-293T cells and treated as described in A. (C) Surface fractions of HEK-293T cells expressing indicated hK_2P17.1 variants were isolated by surface biotinylation followed by streptavidin precipitation. (D) Mean optical densities of the surface blots were normalized to the signal of WT hK_2P17.1. Data are provided as mean values ± SEM of three independent experiments.