The effect of EGCG on protein expression in INA6 myeloma cells. Equal amounts of protein were fractionated on SDS-polyacrylamide gels and electroblotted onto nitrocellulose membranes. The membranes were sequentially treated with primary antibodies and HRP-conjugated secondary antibodies, and the proteins were detected using an enhanced chemiluminescence. The same blots were then stripped and incubated with a monoclonal antibody for α-tubulin. Signal intensity of each band was quantitated and the amount of each protein was normalized to that of α-tubulin. (A) Expression of DAPK2 and p18 proteins in INA6 cells, untreated or treated with 1 μM and 10 μM EGCG for 24 hours. (B) Bar graph shows relative expression of DAPK2 and p18 proteins, following normalization with corresponding α-tubulin levels. (C) Expression of p53 family of proteins (p53, p63, p73) in INA6 cells, untreated or treated with 10 μM EGCG for 24 hours. (D) Bar graph shows fold induction of p53 family members, following normalization with corresponding α-tubulin levels.