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. 2002 Sep;76(18):9556–9561. doi: 10.1128/JVI.76.18.9556-9561.2002

FIG. 2.

FIG. 2.

Detection of the phosphorylation status of three major components of MAPK families (ERK, JNK, and p38) in LMP2A-expressing cells. (A) Western blot analyses with phosphospecific ERK (p-ERK), JNK (p-JNK), and p38 (p-p38) antibodies were performed to detect the phosphorylation status of these MAPKs in stable LMP2A (2A) and vector control (V) clones. (B) Total amounts of ERK, JNK, and p38 were also detected. (C) Total proteins from transient transfectants (trans) or stable clones (stable) of LMP2A (2A) and vector control (V) were blotted on the membrane and reacted with anti-phosphorylated JNK (p-JNK) antibody and anti-phosphorylated ERK (p-ERK) antibody. The detection of tubulin served as an internal control of protein amounts. The numbers to the left of each panel represent molecular mass in kilodaltons.