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Protein (40 μg) from each sample was separated using a 10% polyacrylamide gel and transferred onto a nitrocellulose membrane.
To perform Western blot analysis for AREB6, ELF3, PAX8 and E2F5, 20 μg of protein from each sample was separated using 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
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Each sample was separated using a 4 h gradient from 2%to5050% Acetonitrile with 0.1% formic acid as a proton source.
Equal amounts of protein from each sample were separated using SDS/PAGE.
Equal amounts of protein from each sample were separated using SDS-PAGE (10% gel).
For western blot analysis, equal amounts of protein from each sample were separated using 10% SDS-PAGE.
The samples were separated using SDS-PAGE.
Samples were separated using the NuPAGE system (Invitrogen).
Fifty micrograms of total proteins from each sample were separated on SDS-PAGE using 4% stacking and 12% separating polyacrylamide gels.
Samples were boiled for 5 min and equal amounts of protein (as determined using bound Coumassie blue [below]) from each sample were separated by SDS-PAGE.
For rHBD1 identification and sequence verification, samples from selected FPLC fractions were separated using 12% SDS-PAGE gel.
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