Deglycosylation and Western Blot analysis of secreted sFUT9. Protein from 30 μl of cell supernatant was incubated with PNGaseF, EndoH, or buffer alone (Ctl) and analyzed by Western Blot. As primary antibody, the C-17 anti-FUT9 polyclonal antibody at 1:500 dilution was used. Chemiluminescent detection was performed by the ECL Plus system
PNGaseF treatment yielded two bands that presented a shift to lower
molecular masses (Fig. 5 ).
EndoH had no effect on secreted sFUT9 (Fig. 5 ), indicating
that the three N- glycans of sFUT9 sensitive to PNGaseF
were of the paucimannosidic-type oligosaccharides with proximal
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