Fig. 2.
Fig. 2. (A) Expression of c-Myc in CTCL cell lines studied by Western blotting with a polyclonal c-Myc antiserum (Santa Cruz Biotechnology). C, positive control with a 65-kD recombinant c-Myc–Glutathione-S-transferase (GST) fusion protein (Santa Cruz Biotechnology). Lanes 1 to 3, nuclear extracts from HUT78 (lane 1), MyLa (lane 2), and SeAx (lane 3) cells. The expected position of the differently modified c-Myc proteins (approximately 60 to 65 kD) is indicated on the right by an asterisk. The different bands in the area may result from differently phosphorylated forms of c-Myc. (B) Expression of Max in CTCL cell lines tested by a polyclonal Max antibody (Santa Cruz Biotechnology). M, marker; lanes 1 to 3, nuclear extracts from HUT78 (lane 1), MyLa (lane 2), and SeAx (lane 3) cells. The positions of the two forms of the Max protein are indicated on the right.

(A) Expression of c-Myc in CTCL cell lines studied by Western blotting with a polyclonal c-Myc antiserum (Santa Cruz Biotechnology). C, positive control with a 65-kD recombinant c-Myc–Glutathione-S-transferase (GST) fusion protein (Santa Cruz Biotechnology). Lanes 1 to 3, nuclear extracts from HUT78 (lane 1), MyLa (lane 2), and SeAx (lane 3) cells. The expected position of the differently modified c-Myc proteins (approximately 60 to 65 kD) is indicated on the right by an asterisk. The different bands in the area may result from differently phosphorylated forms of c-Myc. (B) Expression of Max in CTCL cell lines tested by a polyclonal Max antibody (Santa Cruz Biotechnology). M, marker; lanes 1 to 3, nuclear extracts from HUT78 (lane 1), MyLa (lane 2), and SeAx (lane 3) cells. The positions of the two forms of the Max protein are indicated on the right.

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