Anti e cadherin and anti n cadherin

Western blot analysis was performed as described previously28 (link), using equal amounts (10 or 50 μg) of protein from each cell lysate. The following antibodies were used: anti-SerpinB2, anti-uPA, anti-LAMP1, anti-phosphorylated p38 (p-p38), anti-p38, anti-phosphorylated ERK (p-ERK), anti-ERK, anti-β-actin (Santa Cruz Biotechnology, Santa Cruz, CA, USA); anti-MMP-2 (Cell Signaling Technology, Danvers, MA, USA); and anti-E-cadherin and anti-N-cadherin (BD Biosciences, San Diego, CA, USA).

Total cell lysates were prepared in 2× sample loading buffer [250 mM Tris-HCl (pH 6.8), 10% glycerol, 4% sodium dodecyl sulfate (SDS), 2% β-mercaptoethanol, 0.006% bromophenol blue, 5 mM sodium orthovanadate, and 50 mM sodium fluoride; Bio-Rad, Hercules, CA, USA]. The protein concentrations of samples were quantified using the bicinchoninic acid (BCA) method [38 (link)] and a BCA Protein Assay Kit (Thermo Fisher Scientific, Waltham, MA, USA). Equal amounts of protein (5–20 μg) were separated by 6–13% SDS-polyacrylamide gel electrophoresis (PAGE) and transferred to polyvinylidene fluoride membranes (Millipore, Bedford, MA, USA). The membranes were blocked with 5% bovine serum albumin (Sigma-Aldrich) and then probed with anti-DOT1L, anti-H3K79me2, anti-β-Actin, anti-histone H3, anti-H3K4me2, anti-H3K9me2, anti-H3K27me2, anti-H3K36me2, and anti-Vimentin antibodies purchased from Cell Signaling Technology (Beverly, MA, USA) or with anti-E-cadherin and anti-N-cadherin antibodies purchased from BD Biosciences (San Jose, CA, USA). The blots were detected using a WEST-Queen detection system (iNtRON Biotechnology, Seongnam, Republic of Korea).