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. Author manuscript; available in PMC: 2020 Jul 1.
Published in final edited form as: Biochim Biophys Acta Biomembr. 2019 May 1;1861(7):1293–1301. doi: 10.1016/j.bbamem.2019.04.007

Fig. 5. Effect of Senp2 on hOAT3 expression.

Fig. 5.

(a). Cell surface expression of hOAT3. Top panel: hOAT3 together with control vector, Senp2 or the inactive mutant of Senp2 were cotransfected into COS-7 cells for 48h. Transfected cells were labeled with biotin. Biotinylated/cell surface proteins were separated with streptavidin beads, followed by immunoblotting (IB) with an anti-Myc antibody (epitope Myc was tagged to hOAT3 to facilitate the immunodetection). Bottom panel: The same blot as the top panel was re-probed with anti-E-cadherin antibody. E-cadherin is a cell membrane marker protein. (b). Densitometry plot of results from Fig. 5a, Top panel, as well as from other experiments. The values are mean ± SD. (n = 3). *P<0.05. NS: statistically not significant. (c). Total expression of hOAT3. hOAT3 together with control vector, Senp2 or the inactive mutant of Senp2 were co-transfected into COS-7 cells for 48h. Cells were lysed, followed by immunoblotting (IB) with an anti-Myc antibody. (d). Densitometry plot of results from Fig. 5c, top panel as well as from other experiments. The values are mean ± SD (n = 3). *P<0.05. NS: statistically not significant.