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pegfr y1068  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc pegfr y1068
    A. U251 cells were treated by TMZ. Cells were harvested, fixed and stained by pTBK1 antibody coupled to fluorescent secondary antibody. pTBK1 specific fluorescence was detected by flow cytometry and expressed as a ratio to D0 fluorescence (*: p<0.05 vs D0). B. EGFR phosphorylation was measured by flow cytometry by the use of phospho-specific antibodies (pEGFR Y845 or pEGFR <t>Y1068)</t> on U251 or U251 Rho0 cells. Fluorescence was normalized to the fluorescence measured at D0 (*: p<0.05, **: p<0.01). C. EGFR Y845 as measured as in B. in the presence or absence of NAC 5mM (*: p<0.05, **: p<0.01). D. Phosphorylation of EGFR (Y845 and Y1068) and TBK1 was measured as in B in the presence or absence of PP1 (Src inhibitor). E. Src and TBK1 phosphorylation was measured as in B in U251 and U251 EGFR-cells treated by TMZ for the time indicated on the graph (*: p<0.05, **: p<0.01, ***: p<0.001). F. U251 and U251 EGFR-cells were treated by TMZ 50µM twice a week and cells were counted by flow cytometry at each time point. Cell number was normalized by the cell count at D0. G. The sensitivity of U251 cells to erlotinib was evaluated by MTT during TMZ treatment and the IC50 was calculated by AAT Bioquest “IC50 Calculator” tool ( https://www.aatbio.com/tools/ic50-calculator ).
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    Images

    1) Product Images from "EGFR/TBK1-dependent mitochondrial quality control contributes to acquired resistance to temozolomide"

    Article Title: EGFR/TBK1-dependent mitochondrial quality control contributes to acquired resistance to temozolomide

    Journal: bioRxiv

    doi: 10.64898/2025.12.19.695123

    A. U251 cells were treated by TMZ. Cells were harvested, fixed and stained by pTBK1 antibody coupled to fluorescent secondary antibody. pTBK1 specific fluorescence was detected by flow cytometry and expressed as a ratio to D0 fluorescence (*: p<0.05 vs D0). B. EGFR phosphorylation was measured by flow cytometry by the use of phospho-specific antibodies (pEGFR Y845 or pEGFR Y1068) on U251 or U251 Rho0 cells. Fluorescence was normalized to the fluorescence measured at D0 (*: p<0.05, **: p<0.01). C. EGFR Y845 as measured as in B. in the presence or absence of NAC 5mM (*: p<0.05, **: p<0.01). D. Phosphorylation of EGFR (Y845 and Y1068) and TBK1 was measured as in B in the presence or absence of PP1 (Src inhibitor). E. Src and TBK1 phosphorylation was measured as in B in U251 and U251 EGFR-cells treated by TMZ for the time indicated on the graph (*: p<0.05, **: p<0.01, ***: p<0.001). F. U251 and U251 EGFR-cells were treated by TMZ 50µM twice a week and cells were counted by flow cytometry at each time point. Cell number was normalized by the cell count at D0. G. The sensitivity of U251 cells to erlotinib was evaluated by MTT during TMZ treatment and the IC50 was calculated by AAT Bioquest “IC50 Calculator” tool ( https://www.aatbio.com/tools/ic50-calculator ).
    Figure Legend Snippet: A. U251 cells were treated by TMZ. Cells were harvested, fixed and stained by pTBK1 antibody coupled to fluorescent secondary antibody. pTBK1 specific fluorescence was detected by flow cytometry and expressed as a ratio to D0 fluorescence (*: p<0.05 vs D0). B. EGFR phosphorylation was measured by flow cytometry by the use of phospho-specific antibodies (pEGFR Y845 or pEGFR Y1068) on U251 or U251 Rho0 cells. Fluorescence was normalized to the fluorescence measured at D0 (*: p<0.05, **: p<0.01). C. EGFR Y845 as measured as in B. in the presence or absence of NAC 5mM (*: p<0.05, **: p<0.01). D. Phosphorylation of EGFR (Y845 and Y1068) and TBK1 was measured as in B in the presence or absence of PP1 (Src inhibitor). E. Src and TBK1 phosphorylation was measured as in B in U251 and U251 EGFR-cells treated by TMZ for the time indicated on the graph (*: p<0.05, **: p<0.01, ***: p<0.001). F. U251 and U251 EGFR-cells were treated by TMZ 50µM twice a week and cells were counted by flow cytometry at each time point. Cell number was normalized by the cell count at D0. G. The sensitivity of U251 cells to erlotinib was evaluated by MTT during TMZ treatment and the IC50 was calculated by AAT Bioquest “IC50 Calculator” tool ( https://www.aatbio.com/tools/ic50-calculator ).

    Techniques Used: Staining, Fluorescence, Flow Cytometry, Phospho-proteomics, Cell Counting

    Related Articles

    Bioprocessing:

    Article Title: Novel CDK12/13 Inhibitors AU-15506 and AU-16770 Are Potent Anti-Cancer Agents in EGFR Mutant Lung Adenocarcinoma with and without Osimertinib Resistance.
    Article Snippet: .. Polyclonal or monoclonal antibodies to pEGFR-Y1068 (#2234), AKT (#4691), ERK (#4370), AMPK-alpha (#5831), ATR (#13934), ATM (#2873), RAD51 (#8875), CHK1 (#2360), CHK2 (#6334), pAKT (#4370, #4370), pERK (#4370), pACC (#11818), and pS6 (#4858) were obtained from Cell Signaling Technology (Danvers, MA, USA). .. Polyclonal or monoclonal antibodies to CDK12 (ABE1861), RNA Pol II [630849], pSer 2 RNA Pol II (MABE953), and pSer 5 RNA Pol II (MABE954) were obtained from Millipore-Sigma.

    other:

    Article Title: EGFR/TBK1-dependent mitochondrial quality control contributes to acquired resistance to temozolomide
    Article Snippet: TOM20 #612278, BD (Le Pont de Claix, France); TFAM #8076, Cell Signaling Technology (Danvers, MA, USA); EGFR #4267, Cell Signaling Technology; pEGFR Y845 #6963, Cell Signaling Technology; pEGFR Y1068 #3777, Cell Signaling Technology; TBK1 #3504, Cell Signaling Technology; pTBK1 #5483, Cell Signaling Technology; pSrc #sc-81521, Santa Cruz Biotechnology (Dallas, TX, France); VDAC #ab14734 Abcam, (Cambridge, UK); IP3R #sc-28614, Santa Cruz Biotechnology; LC3 #83506, Cell Signaling Technology or #L7543, Sigma Aldrich.

    Membrane:

    Article Title: Loss of E-cadherin Induces IGF1R Activation and Reveals a Targetable Pathway in Invasive Lobular Breast Carcinoma
    Article Snippet: .. Membrane blocking was performed with Intercept PBS blocking buffer (LiCOr #927–40000) for one hour at room temperature and probed with primary antibodies overnight at 4 C: pIGF1R/IR (Cell Signaling Technology #3024; RRID: AB_331253), IGF1R (Cell Signaling Technology #3027; RRID: AB_2122378), pAkt S473 (Cell Signaling Technology #4060; RRID: AB_2315049), Akt (Cell Signaling Technology #9272; RRID: AB_329827), InsR (Cell Signaling Technology #3025; RRID: AB_2280448), E-cadherin (BD Biosciences #610182; RRID: AB_397581), b-catenin (BD Biosciences #610154; RRID:AB_397555), p120 catenin (BD Biosciences; #610134; RRID:AB_397537), pEGFR Y1068 (Cell Signaling Technology #2234; RRID:AB_331701), EGFR (Cell Signaling Technology #4267; RRID:AB_2246311),a-Biotin (Cell Signaling Technology #5597; RRID:AB_10828011), non-phospho b-catenin (Cell Signaling Technology #1980; RRID:AB_2650576), pFGFR4 Y642 (Signalway #11836), FGFR4 (Cell Signaling Technology #8562; RRID:AB_10891199), pFRS2 Y196 (Cell Signaling Technology #3864; RRID:AB_2106222), pSTAT3Y705 (Cell Signaling Technology #9131; RRID:AB_331586), and p-p44/42MAPK (Cell Signaling Technology #4377; RRID:AB_331775). .. This was followed by 1 hour room temperature incubation with secondary antibodies (1:10,000; antimouse 680LT: LiCor #925–68020; anti-rabbit 800CW: LiCor #925– 32211).

    Blocking Assay:

    Article Title: Loss of E-cadherin Induces IGF1R Activation and Reveals a Targetable Pathway in Invasive Lobular Breast Carcinoma
    Article Snippet: .. Membrane blocking was performed with Intercept PBS blocking buffer (LiCOr #927–40000) for one hour at room temperature and probed with primary antibodies overnight at 4 C: pIGF1R/IR (Cell Signaling Technology #3024; RRID: AB_331253), IGF1R (Cell Signaling Technology #3027; RRID: AB_2122378), pAkt S473 (Cell Signaling Technology #4060; RRID: AB_2315049), Akt (Cell Signaling Technology #9272; RRID: AB_329827), InsR (Cell Signaling Technology #3025; RRID: AB_2280448), E-cadherin (BD Biosciences #610182; RRID: AB_397581), b-catenin (BD Biosciences #610154; RRID:AB_397555), p120 catenin (BD Biosciences; #610134; RRID:AB_397537), pEGFR Y1068 (Cell Signaling Technology #2234; RRID:AB_331701), EGFR (Cell Signaling Technology #4267; RRID:AB_2246311),a-Biotin (Cell Signaling Technology #5597; RRID:AB_10828011), non-phospho b-catenin (Cell Signaling Technology #1980; RRID:AB_2650576), pFGFR4 Y642 (Signalway #11836), FGFR4 (Cell Signaling Technology #8562; RRID:AB_10891199), pFRS2 Y196 (Cell Signaling Technology #3864; RRID:AB_2106222), pSTAT3Y705 (Cell Signaling Technology #9131; RRID:AB_331586), and p-p44/42MAPK (Cell Signaling Technology #4377; RRID:AB_331775). .. This was followed by 1 hour room temperature incubation with secondary antibodies (1:10,000; antimouse 680LT: LiCor #925–68020; anti-rabbit 800CW: LiCor #925– 32211).

    Western Blot:

    Article Title: Complexity of progranulin mechanisms of action in mesothelioma
    Article Snippet: Cell lysates were prepared using RIPA buffer (Thermo Fisher Scientific) supplemented with halt protease and phosphatase inhibitors cocktail (Thermo Fisher Scientific). .. The following primary antibodies were used for immunoblot analysis: pEphA2 S897 (6347), EphA2 (6997), pAKT S473 (4060), pan-AKT (4691), pERK1/2 (4370), ERK1/2 (9102), pFAK Y397 (3285), FAK (8556), pEGFR Y1068 (3777), EGFR (4267), and EphA7 (64,801) from Cell Signaling Technology (Danvers, MA, USA), progranulin (P-9182-35B, US Biologicals, Salem, MA, USA), pEphA2 S901 (PA5-105,552, Thermo Scientific), and GAPDH (sc-365062) (Santa Cruz Biotechnology, Dallas, TX, USA). .. The following secondary antibodies were used: anti-rabbit HRP-linked (7074) (Cell Signaling Technology) and the antibodies from Santa Cruz Biotechnology mouse anti-rabbit IgG-HRP (sc-2357) and m-IgGk BP-HRP (sc-516102).



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    A. U251 cells were treated by TMZ. Cells were harvested, fixed and stained by pTBK1 antibody coupled to fluorescent secondary antibody. pTBK1 specific fluorescence was detected by flow cytometry and expressed as a ratio to D0 fluorescence (*: p<0.05 vs D0). B. EGFR phosphorylation was measured by flow cytometry by the use of phospho-specific antibodies (pEGFR Y845 or pEGFR <t>Y1068)</t> on U251 or U251 Rho0 cells. Fluorescence was normalized to the fluorescence measured at D0 (*: p<0.05, **: p<0.01). C. EGFR Y845 as measured as in B. in the presence or absence of NAC 5mM (*: p<0.05, **: p<0.01). D. Phosphorylation of EGFR (Y845 and Y1068) and TBK1 was measured as in B in the presence or absence of PP1 (Src inhibitor). E. Src and TBK1 phosphorylation was measured as in B in U251 and U251 EGFR-cells treated by TMZ for the time indicated on the graph (*: p<0.05, **: p<0.01, ***: p<0.001). F. U251 and U251 EGFR-cells were treated by TMZ 50µM twice a week and cells were counted by flow cytometry at each time point. Cell number was normalized by the cell count at D0. G. The sensitivity of U251 cells to erlotinib was evaluated by MTT during TMZ treatment and the IC50 was calculated by AAT Bioquest “IC50 Calculator” tool ( https://www.aatbio.com/tools/ic50-calculator ).
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    Cell Signaling Technology Inc anti-pegfr (y1068) 3777
    (A) Representative immunoblots of phosphorylated EGFR (pEGFR <t>Y1068</t> ), phosphorylated GAB1 (GAB1 Y627 ), phosphorylated ERK1/2 (pERK T202/Y204 ), and phosphorylated AKT (pAKT S473 ) following treatment with DMSO (solvent), erlotinib (EGFRi, 5 μM), 1938 (1 μM), or their combination (Combo) for 0.5 hour in 8988T-KO: KRAS WT cells. HSP90 is loading control. Bar graphs represent quantification (mean ± SD normalized to DMSO from n = 3 biological replicates). ns = non-significant, * p < 0.05, ** p < 0.01, *** p < 0.001, repeated measures ANOVA (rmANOVA) with Šidák’s post-hoc test. (B) Representative immunoblots of pERK1/2 and pAKT following treatment with DMSO (solvent), RMC-4550 (SHP2i, 2 μM), 1938 (1 μM), or their combination (Combo) for 0.5 hour in 8988T-KO: KRAS WT cells. Bar graphs represent quantification (mean ± SD normalized to DMSO from n = 3 biological replicates). ns = non-significant, * p < 0.05, ** p < 0.01, *** p < 0.001, repeated measures ANOVA (rmANOVA) with Šidák’s post-hoc test. (C) Representative immunoblots of pERK1/2 and pAKT following treatment with DMSO (solvent), BI-3406 (SOSi, 1 μM), 1938 (1 μM), or their combination (Combo) for 0.5 hour in 8988T-KO: KRAS WT cells. Bar graphs represent quantification (mean ± SD normalized to DMSO from n = 3 biological replicates). ns = non-significant, * p < 0.05, ** p < 0.01, *** p < 0.001, repeated measures ANOVA (rmANOVA) with Šidák’s post-hoc test. (D) Representative immunoblots of phosphorylated pERK1/2, pAKT, and phosphorylated FAK (pFAK Y397 ) following treatment with DMSO (solvent), defactinib (FAKi, 5 μM), 1938 (1 μM), or their combination (Combo) for 0.5 hour in 8988T-KO: KRAS WT cells. Bar graphs represent quantification (mean ± SD normalized to DMSO from n = 3 biological replicates). ns = non-significant, * p < 0.05, ** p < 0.01, repeated measures ANOVA (rmANOVA) with Šidák’s post-hoc test.
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    A. U251 cells were treated by TMZ. Cells were harvested, fixed and stained by pTBK1 antibody coupled to fluorescent secondary antibody. pTBK1 specific fluorescence was detected by flow cytometry and expressed as a ratio to D0 fluorescence (*: p<0.05 vs D0). B. EGFR phosphorylation was measured by flow cytometry by the use of phospho-specific antibodies (pEGFR Y845 or pEGFR Y1068) on U251 or U251 Rho0 cells. Fluorescence was normalized to the fluorescence measured at D0 (*: p<0.05, **: p<0.01). C. EGFR Y845 as measured as in B. in the presence or absence of NAC 5mM (*: p<0.05, **: p<0.01). D. Phosphorylation of EGFR (Y845 and Y1068) and TBK1 was measured as in B in the presence or absence of PP1 (Src inhibitor). E. Src and TBK1 phosphorylation was measured as in B in U251 and U251 EGFR-cells treated by TMZ for the time indicated on the graph (*: p<0.05, **: p<0.01, ***: p<0.001). F. U251 and U251 EGFR-cells were treated by TMZ 50µM twice a week and cells were counted by flow cytometry at each time point. Cell number was normalized by the cell count at D0. G. The sensitivity of U251 cells to erlotinib was evaluated by MTT during TMZ treatment and the IC50 was calculated by AAT Bioquest “IC50 Calculator” tool ( https://www.aatbio.com/tools/ic50-calculator ).

    Journal: bioRxiv

    Article Title: EGFR/TBK1-dependent mitochondrial quality control contributes to acquired resistance to temozolomide

    doi: 10.64898/2025.12.19.695123

    Figure Lengend Snippet: A. U251 cells were treated by TMZ. Cells were harvested, fixed and stained by pTBK1 antibody coupled to fluorescent secondary antibody. pTBK1 specific fluorescence was detected by flow cytometry and expressed as a ratio to D0 fluorescence (*: p<0.05 vs D0). B. EGFR phosphorylation was measured by flow cytometry by the use of phospho-specific antibodies (pEGFR Y845 or pEGFR Y1068) on U251 or U251 Rho0 cells. Fluorescence was normalized to the fluorescence measured at D0 (*: p<0.05, **: p<0.01). C. EGFR Y845 as measured as in B. in the presence or absence of NAC 5mM (*: p<0.05, **: p<0.01). D. Phosphorylation of EGFR (Y845 and Y1068) and TBK1 was measured as in B in the presence or absence of PP1 (Src inhibitor). E. Src and TBK1 phosphorylation was measured as in B in U251 and U251 EGFR-cells treated by TMZ for the time indicated on the graph (*: p<0.05, **: p<0.01, ***: p<0.001). F. U251 and U251 EGFR-cells were treated by TMZ 50µM twice a week and cells were counted by flow cytometry at each time point. Cell number was normalized by the cell count at D0. G. The sensitivity of U251 cells to erlotinib was evaluated by MTT during TMZ treatment and the IC50 was calculated by AAT Bioquest “IC50 Calculator” tool ( https://www.aatbio.com/tools/ic50-calculator ).

    Article Snippet: TOM20 #612278, BD (Le Pont de Claix, France); TFAM #8076, Cell Signaling Technology (Danvers, MA, USA); EGFR #4267, Cell Signaling Technology; pEGFR Y845 #6963, Cell Signaling Technology; pEGFR Y1068 #3777, Cell Signaling Technology; TBK1 #3504, Cell Signaling Technology; pTBK1 #5483, Cell Signaling Technology; pSrc #sc-81521, Santa Cruz Biotechnology (Dallas, TX, France); VDAC #ab14734 Abcam, (Cambridge, UK); IP3R #sc-28614, Santa Cruz Biotechnology; LC3 #83506, Cell Signaling Technology or #L7543, Sigma Aldrich.

    Techniques: Staining, Fluorescence, Flow Cytometry, Phospho-proteomics, Cell Counting

    (A) Representative immunoblots of phosphorylated EGFR (pEGFR Y1068 ), phosphorylated GAB1 (GAB1 Y627 ), phosphorylated ERK1/2 (pERK T202/Y204 ), and phosphorylated AKT (pAKT S473 ) following treatment with DMSO (solvent), erlotinib (EGFRi, 5 μM), 1938 (1 μM), or their combination (Combo) for 0.5 hour in 8988T-KO: KRAS WT cells. HSP90 is loading control. Bar graphs represent quantification (mean ± SD normalized to DMSO from n = 3 biological replicates). ns = non-significant, * p < 0.05, ** p < 0.01, *** p < 0.001, repeated measures ANOVA (rmANOVA) with Šidák’s post-hoc test. (B) Representative immunoblots of pERK1/2 and pAKT following treatment with DMSO (solvent), RMC-4550 (SHP2i, 2 μM), 1938 (1 μM), or their combination (Combo) for 0.5 hour in 8988T-KO: KRAS WT cells. Bar graphs represent quantification (mean ± SD normalized to DMSO from n = 3 biological replicates). ns = non-significant, * p < 0.05, ** p < 0.01, *** p < 0.001, repeated measures ANOVA (rmANOVA) with Šidák’s post-hoc test. (C) Representative immunoblots of pERK1/2 and pAKT following treatment with DMSO (solvent), BI-3406 (SOSi, 1 μM), 1938 (1 μM), or their combination (Combo) for 0.5 hour in 8988T-KO: KRAS WT cells. Bar graphs represent quantification (mean ± SD normalized to DMSO from n = 3 biological replicates). ns = non-significant, * p < 0.05, ** p < 0.01, *** p < 0.001, repeated measures ANOVA (rmANOVA) with Šidák’s post-hoc test. (D) Representative immunoblots of phosphorylated pERK1/2, pAKT, and phosphorylated FAK (pFAK Y397 ) following treatment with DMSO (solvent), defactinib (FAKi, 5 μM), 1938 (1 μM), or their combination (Combo) for 0.5 hour in 8988T-KO: KRAS WT cells. Bar graphs represent quantification (mean ± SD normalized to DMSO from n = 3 biological replicates). ns = non-significant, * p < 0.05, ** p < 0.01, repeated measures ANOVA (rmANOVA) with Šidák’s post-hoc test.

    Journal: bioRxiv

    Article Title: Phosphoinositide 3-kinase regulates wild-type RAS signaling to confer resistance to KRAS inhibition

    doi: 10.1101/2025.06.20.660715

    Figure Lengend Snippet: (A) Representative immunoblots of phosphorylated EGFR (pEGFR Y1068 ), phosphorylated GAB1 (GAB1 Y627 ), phosphorylated ERK1/2 (pERK T202/Y204 ), and phosphorylated AKT (pAKT S473 ) following treatment with DMSO (solvent), erlotinib (EGFRi, 5 μM), 1938 (1 μM), or their combination (Combo) for 0.5 hour in 8988T-KO: KRAS WT cells. HSP90 is loading control. Bar graphs represent quantification (mean ± SD normalized to DMSO from n = 3 biological replicates). ns = non-significant, * p < 0.05, ** p < 0.01, *** p < 0.001, repeated measures ANOVA (rmANOVA) with Šidák’s post-hoc test. (B) Representative immunoblots of pERK1/2 and pAKT following treatment with DMSO (solvent), RMC-4550 (SHP2i, 2 μM), 1938 (1 μM), or their combination (Combo) for 0.5 hour in 8988T-KO: KRAS WT cells. Bar graphs represent quantification (mean ± SD normalized to DMSO from n = 3 biological replicates). ns = non-significant, * p < 0.05, ** p < 0.01, *** p < 0.001, repeated measures ANOVA (rmANOVA) with Šidák’s post-hoc test. (C) Representative immunoblots of pERK1/2 and pAKT following treatment with DMSO (solvent), BI-3406 (SOSi, 1 μM), 1938 (1 μM), or their combination (Combo) for 0.5 hour in 8988T-KO: KRAS WT cells. Bar graphs represent quantification (mean ± SD normalized to DMSO from n = 3 biological replicates). ns = non-significant, * p < 0.05, ** p < 0.01, *** p < 0.001, repeated measures ANOVA (rmANOVA) with Šidák’s post-hoc test. (D) Representative immunoblots of phosphorylated pERK1/2, pAKT, and phosphorylated FAK (pFAK Y397 ) following treatment with DMSO (solvent), defactinib (FAKi, 5 μM), 1938 (1 μM), or their combination (Combo) for 0.5 hour in 8988T-KO: KRAS WT cells. Bar graphs represent quantification (mean ± SD normalized to DMSO from n = 3 biological replicates). ns = non-significant, * p < 0.05, ** p < 0.01, repeated measures ANOVA (rmANOVA) with Šidák’s post-hoc test.

    Article Snippet: The following antibodies were used for immunoblotting: rabbit anti-HSP90 (Cell Signaling Technologies (CST), 4877, 1:1000), rabbit anti-GAB1 (CST, 3232, 1:1000), rabbit anti-pGAB1(Y627) (CST, 3231, 1:1000), rabbit anti-EGFR (CST, 4267, 1:1000), rabbit anti-pEGFR (Y1068) (CST, 3777, 1:1000), rabbit anti-SHP2 (CST, 3397, 1:1000), rabbit anti-GRB2 (CST, 3972, 1:1000), rabbit anti-NF1 (CST, 14623, 1:1000), rabbit anti-RASA1 (Invitrogen MA4-001, 1:200), rabbit anti-RASAL1 (Abcam, ab168610, 1:1000), rabbit anti-GFP (CST, 2956, 1:1000), rabbit anti-pERK1/2(T202/Y204) (CST, 4370, 1:1000), mouse anti-ERK1/2 (CST, 9107, 1:1000), rabbit anti-pAKT(S473) (CST, 4060, 1:2000), mouse anti-AKT (CST, 2966, 1:2000), rabbit anti-BirA (Agrisera, AS20, 4440, 1:1000), rabbit anti-biotin (CST, 5597, 1:1000), mouse anti-KRAS (Sigma-Aldrich, 3B10-2F2, 1:1000), mouse anti-KRAS (Santa Cruz, sc-30, 1:1000).

    Techniques: Western Blot, Solvent, Control