Expression of Erk, Akt, Stat3, AMPKα and c-myc proteins by wildtype cells, negative controls and Kras clones in Panc-1, SUIT-2 and TB32047 cell lines. Here, the prefix “p” indicates the phosphorylated version of the protein. (A) Panc-1 2.1, 2.8 and 2.14 expressed slightly less Erk than the others. Clone 2.1 also produced less pErk. Akt expression in Panc-1 showed no difference between WT, NC and clones. pAkt was reduced in Panc-1 clones 2.8, 2.9 and 2.14. Stat3 was expressed by all Panc-1 clones, except 2.14. Panc-1 showed reduced pStat3 expression in clone 2.1, 2.8 and 2.14. Lower AMPKα expression could be observed in Panc-1 WT, NC and clone 2.1. The pAMPKα expression level was lower in clone 2.1 than the other samples. Panc-1 NC and 2.1 produced less c-myc compared to the others. (B) SUIT-2 clones expressed Erk similar to the wildtype cells. SUIT-2 clones 1.6 and 2.7 produced less pErk. Akt expression in SUIT-2 cells showed no difference in expression between WT, NC and clones. Only WT cells, NC and clone 2.8 expressed pAkt. Clone 1.10 produced decreased Stat3 levels. pStat3 was only produced by SUIT-2 WT, pX2 and clone 2.6. Lower AMPKα expression could be observed in clones 1.10 and 2.4 compared to the WT cells. Just SUIT-2 pX2 and clone 2.6 produced pAMPKα. SUIT-2 clones 1.6, 2.7 and 2.4 produced less c-myc compared to the others. (C) Erk expression in TB32047 clones was similar to the wildtype. pErk was only expressed by TB32047 NC. Akt, pAkt, Stat3, AMPKα and c-myc protein levels were similar throughout all TB32047 samples. pStat3 was only produced by TB32047 NC, clones 1.12 and 1.18. TB32047 clones 1.12, 1.14, 1.8 and 1.18 expressed higher pAMPKα than the remaining samples. β-Actin, GAPDH and Na,K-ATPase served as loading controls.