rabbit monoclonal anti perk1 2 antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit monoclonal anti perk1 2 antibody
    Rabbit Monoclonal Anti Perk1 2 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    phospho p44 42 mapk perk1 2 thr202 tyr204 rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p44 42 mapk perk1 2 thr202 tyr204 rabbit mab
    Effect of liprin‐α1 knockdown to ERK phosphorylation and to oncogenic signaling. (A) Localization and expression of p‐ERK1/2 <t>(Thr202/Tyr204)</t> in MDA‐MB‐231 shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (B) Localization and expression of p‐ERK1/2 (Thr202/Tyr204) in UT‐SCC‐42A shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (C) Quantification of p‐ERK1/2 staining in A and B is shown in bar chart as a fold change (FC) between shScramble and shPPFIA1 cells and asterisk (*) means statistical significance ( P < 0.05). Student's two‐tailed t ‐test was used to calculate the statistical significance. Error bar indicates the standard deviation of the mean. A minimum of 70 individual cells were quantitated three times from two (shScramble) or three (shPPFIA1) different experiments for both of the cell lines and representative images are shown for MDA‐MB‐231 cell line in 2A and for UT‐SCC‐42A in 2B. (D) Western blot showing protein levels of liprin‐α1, p‐ERK1/2 (Thr202/Tyr204), ERK1/2, MEK1/2 and p‐MEK1/2 (Ser217/221) in a panel of studied shScramble and shPPFIA1 cells. GAPDH, α‐tubulin and vinculin were used as the loading controls. The intensity of p‐ERK1/2 bands was quantified for individual cell lines and the values are described under the blot. In addition, western blot for UT‐SCC‐42A and UT‐SCC‐42B was performed with two different constructs for p‐ERK (Fig. ). (E) Heatmap showing MAPK pathway activity score in MDA‐MB‐231 and UT‐SCC‐42A shScr and shPPFIA1 cells, and in UT‐SCC‐95 control and PPFIA1 overexpressing cells. For MDA‐MB‐231 and UT‐SCC‐42A cells, z ‐scores were computed from previously published RNAseq data . For UT‐SCC‐95 cell line, z ‐scores were computed from the RMA‐normalized expression values from microarrays . The EPHA4 gene had two probe sets mapping to the same gene, so the mean expression value was used as a basis for the z ‐score. Finally, the mean z ‐scores from different constructs were calculated. For MDA‐MB‐231 cell line, three replicates of shScr and shPPFIA1 cells were included into the analysis whereas for UT‐SCC‐42A cell line, three replicates from shScr cells and two replicates from shPPFIA1 cells were analyzed. For UT‐SCC‐95, one control and two overexpressing samples were included into the analysis. (F, G) Western blot analysis from MDA‐MB‐231 (F) and UT‐SCC‐42A (G) cells treated 48 h with trametinib. Protein levels of liprin‐α1, ERK1/2, p‐ERK1/2 (T202/Y204), p‐AKT (Ser473) and p‐rS6 (Ser235/236) proteins are shown for shScramble and shPPFIA1 cells. DMSO‐treated cells were used as a negative control for trametinib treatment, whereas α‐tubulin and vinculin served as loading controls. Figure shows quantification of p‐ERK1/2 immunoblot results calculated from four experiments for MDA‐MB‐231 and five experiments for UT‐SCC‐42A. Liprin‐α1, p‐AKT and p‐rS6 western blot experiments were performed twice for each cell line and each condition (Fig. ; Fig. ).
    Phospho P44 42 Mapk Perk1 2 Thr202 Tyr204 Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho p44 42 mapk perk1 2 thr202 tyr204 rabbit mab/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phospho p44 42 mapk perk1 2 thr202 tyr204 rabbit mab - by Bioz Stars, 2024-07
    86/100 stars

    Images

    1) Product Images from "Liprin‐α1 contributes to oncogenic MAPK signaling by counteracting ERK activity"

    Article Title: Liprin‐α1 contributes to oncogenic MAPK signaling by counteracting ERK activity

    Journal: Molecular Oncology

    doi: 10.1002/1878-0261.13593

    Effect of liprin‐α1 knockdown to ERK phosphorylation and to oncogenic signaling. (A) Localization and expression of p‐ERK1/2 (Thr202/Tyr204) in MDA‐MB‐231 shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (B) Localization and expression of p‐ERK1/2 (Thr202/Tyr204) in UT‐SCC‐42A shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (C) Quantification of p‐ERK1/2 staining in A and B is shown in bar chart as a fold change (FC) between shScramble and shPPFIA1 cells and asterisk (*) means statistical significance ( P < 0.05). Student's two‐tailed t ‐test was used to calculate the statistical significance. Error bar indicates the standard deviation of the mean. A minimum of 70 individual cells were quantitated three times from two (shScramble) or three (shPPFIA1) different experiments for both of the cell lines and representative images are shown for MDA‐MB‐231 cell line in 2A and for UT‐SCC‐42A in 2B. (D) Western blot showing protein levels of liprin‐α1, p‐ERK1/2 (Thr202/Tyr204), ERK1/2, MEK1/2 and p‐MEK1/2 (Ser217/221) in a panel of studied shScramble and shPPFIA1 cells. GAPDH, α‐tubulin and vinculin were used as the loading controls. The intensity of p‐ERK1/2 bands was quantified for individual cell lines and the values are described under the blot. In addition, western blot for UT‐SCC‐42A and UT‐SCC‐42B was performed with two different constructs for p‐ERK (Fig. ). (E) Heatmap showing MAPK pathway activity score in MDA‐MB‐231 and UT‐SCC‐42A shScr and shPPFIA1 cells, and in UT‐SCC‐95 control and PPFIA1 overexpressing cells. For MDA‐MB‐231 and UT‐SCC‐42A cells, z ‐scores were computed from previously published RNAseq data . For UT‐SCC‐95 cell line, z ‐scores were computed from the RMA‐normalized expression values from microarrays . The EPHA4 gene had two probe sets mapping to the same gene, so the mean expression value was used as a basis for the z ‐score. Finally, the mean z ‐scores from different constructs were calculated. For MDA‐MB‐231 cell line, three replicates of shScr and shPPFIA1 cells were included into the analysis whereas for UT‐SCC‐42A cell line, three replicates from shScr cells and two replicates from shPPFIA1 cells were analyzed. For UT‐SCC‐95, one control and two overexpressing samples were included into the analysis. (F, G) Western blot analysis from MDA‐MB‐231 (F) and UT‐SCC‐42A (G) cells treated 48 h with trametinib. Protein levels of liprin‐α1, ERK1/2, p‐ERK1/2 (T202/Y204), p‐AKT (Ser473) and p‐rS6 (Ser235/236) proteins are shown for shScramble and shPPFIA1 cells. DMSO‐treated cells were used as a negative control for trametinib treatment, whereas α‐tubulin and vinculin served as loading controls. Figure shows quantification of p‐ERK1/2 immunoblot results calculated from four experiments for MDA‐MB‐231 and five experiments for UT‐SCC‐42A. Liprin‐α1, p‐AKT and p‐rS6 western blot experiments were performed twice for each cell line and each condition (Fig. ; Fig. ).
    Figure Legend Snippet: Effect of liprin‐α1 knockdown to ERK phosphorylation and to oncogenic signaling. (A) Localization and expression of p‐ERK1/2 (Thr202/Tyr204) in MDA‐MB‐231 shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (B) Localization and expression of p‐ERK1/2 (Thr202/Tyr204) in UT‐SCC‐42A shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (C) Quantification of p‐ERK1/2 staining in A and B is shown in bar chart as a fold change (FC) between shScramble and shPPFIA1 cells and asterisk (*) means statistical significance ( P < 0.05). Student's two‐tailed t ‐test was used to calculate the statistical significance. Error bar indicates the standard deviation of the mean. A minimum of 70 individual cells were quantitated three times from two (shScramble) or three (shPPFIA1) different experiments for both of the cell lines and representative images are shown for MDA‐MB‐231 cell line in 2A and for UT‐SCC‐42A in 2B. (D) Western blot showing protein levels of liprin‐α1, p‐ERK1/2 (Thr202/Tyr204), ERK1/2, MEK1/2 and p‐MEK1/2 (Ser217/221) in a panel of studied shScramble and shPPFIA1 cells. GAPDH, α‐tubulin and vinculin were used as the loading controls. The intensity of p‐ERK1/2 bands was quantified for individual cell lines and the values are described under the blot. In addition, western blot for UT‐SCC‐42A and UT‐SCC‐42B was performed with two different constructs for p‐ERK (Fig. ). (E) Heatmap showing MAPK pathway activity score in MDA‐MB‐231 and UT‐SCC‐42A shScr and shPPFIA1 cells, and in UT‐SCC‐95 control and PPFIA1 overexpressing cells. For MDA‐MB‐231 and UT‐SCC‐42A cells, z ‐scores were computed from previously published RNAseq data . For UT‐SCC‐95 cell line, z ‐scores were computed from the RMA‐normalized expression values from microarrays . The EPHA4 gene had two probe sets mapping to the same gene, so the mean expression value was used as a basis for the z ‐score. Finally, the mean z ‐scores from different constructs were calculated. For MDA‐MB‐231 cell line, three replicates of shScr and shPPFIA1 cells were included into the analysis whereas for UT‐SCC‐42A cell line, three replicates from shScr cells and two replicates from shPPFIA1 cells were analyzed. For UT‐SCC‐95, one control and two overexpressing samples were included into the analysis. (F, G) Western blot analysis from MDA‐MB‐231 (F) and UT‐SCC‐42A (G) cells treated 48 h with trametinib. Protein levels of liprin‐α1, ERK1/2, p‐ERK1/2 (T202/Y204), p‐AKT (Ser473) and p‐rS6 (Ser235/236) proteins are shown for shScramble and shPPFIA1 cells. DMSO‐treated cells were used as a negative control for trametinib treatment, whereas α‐tubulin and vinculin served as loading controls. Figure shows quantification of p‐ERK1/2 immunoblot results calculated from four experiments for MDA‐MB‐231 and five experiments for UT‐SCC‐42A. Liprin‐α1, p‐AKT and p‐rS6 western blot experiments were performed twice for each cell line and each condition (Fig. ; Fig. ).

    Techniques Used: Expressing, Construct, Immunofluorescence, Microscopy, Staining, Two Tailed Test, Standard Deviation, Western Blot, Activity Assay, Negative Control

    anti perk1 2 t202 y204 rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti perk1 2 t202 y204 rabbit mab
    Anti Perk1 2 T202 Y204 Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    anti phospho mapk perk1 2 rabbit monoclonal antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho mapk perk1 2 rabbit monoclonal antibody
    Estradiol decreases phosphorylation of ERK1/2. Phosphorylated extracellular signal-regulated kinase 1/2 <t>(pERK1/2)</t> protein expression in brains from placebo- and E2-treated ovariectomized female rats subjected to tMCAO. ( A ) Representative Western blots and ( B ) relative abundance of pERK1 and ( C ) pERK2 in whole-cell lysates of non-ischemic (NI) and ischemic (I) hemispheres. Two-way ANOVA for pERK1: brain hemisphere (ischemic vs. non-ischemic, p < 0.001, F 1,30 = 18.1), treatment (E2 vs. placebo, p < 0.001, F 1,30 = 84.6), and interaction ( p < 0.001, F 1,30 = 15.5). Two-way ANOVA for pERK2: brain hemisphere (ischemic vs. non-ischemic, p < 0.05, F 1,30 = 4.7) and treatment (E2 vs. placebo, p < 0.001, F 1,30 = 28.1). Post hoc Sidak’s multiple comparisons tests: significantly different from non-ischemic placebo group (* p < 0.05, ** p < 0.01, and *** p < 0.001), or from ischemic placebo group ( ### p < 0.001). Data are mean ± SEM of individual data points (normalized to total ERK1/2). E2, 17β-estradiol. tMCAO, transient middle cerebral artery occlusion.
    Anti Phospho Mapk Perk1 2 Rabbit Monoclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho mapk perk1 2 rabbit monoclonal antibody/product/Cell Signaling Technology Inc
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    anti phospho mapk perk1 2 rabbit monoclonal antibody - by Bioz Stars, 2024-07
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    1) Product Images from "Cerebroprotective Effect of 17β-Estradiol Replacement Therapy in Ovariectomy-Induced Post-Menopausal Rats Subjected to Ischemic Stroke: Role of MAPK/ERK1/2 Pathway and PI3K-Independent Akt Activation"

    Article Title: Cerebroprotective Effect of 17β-Estradiol Replacement Therapy in Ovariectomy-Induced Post-Menopausal Rats Subjected to Ischemic Stroke: Role of MAPK/ERK1/2 Pathway and PI3K-Independent Akt Activation

    Journal: International Journal of Molecular Sciences

    doi: 10.3390/ijms241814303

    Estradiol decreases phosphorylation of ERK1/2. Phosphorylated extracellular signal-regulated kinase 1/2 (pERK1/2) protein expression in brains from placebo- and E2-treated ovariectomized female rats subjected to tMCAO. ( A ) Representative Western blots and ( B ) relative abundance of pERK1 and ( C ) pERK2 in whole-cell lysates of non-ischemic (NI) and ischemic (I) hemispheres. Two-way ANOVA for pERK1: brain hemisphere (ischemic vs. non-ischemic, p < 0.001, F 1,30 = 18.1), treatment (E2 vs. placebo, p < 0.001, F 1,30 = 84.6), and interaction ( p < 0.001, F 1,30 = 15.5). Two-way ANOVA for pERK2: brain hemisphere (ischemic vs. non-ischemic, p < 0.05, F 1,30 = 4.7) and treatment (E2 vs. placebo, p < 0.001, F 1,30 = 28.1). Post hoc Sidak’s multiple comparisons tests: significantly different from non-ischemic placebo group (* p < 0.05, ** p < 0.01, and *** p < 0.001), or from ischemic placebo group ( ### p < 0.001). Data are mean ± SEM of individual data points (normalized to total ERK1/2). E2, 17β-estradiol. tMCAO, transient middle cerebral artery occlusion.
    Figure Legend Snippet: Estradiol decreases phosphorylation of ERK1/2. Phosphorylated extracellular signal-regulated kinase 1/2 (pERK1/2) protein expression in brains from placebo- and E2-treated ovariectomized female rats subjected to tMCAO. ( A ) Representative Western blots and ( B ) relative abundance of pERK1 and ( C ) pERK2 in whole-cell lysates of non-ischemic (NI) and ischemic (I) hemispheres. Two-way ANOVA for pERK1: brain hemisphere (ischemic vs. non-ischemic, p < 0.001, F 1,30 = 18.1), treatment (E2 vs. placebo, p < 0.001, F 1,30 = 84.6), and interaction ( p < 0.001, F 1,30 = 15.5). Two-way ANOVA for pERK2: brain hemisphere (ischemic vs. non-ischemic, p < 0.05, F 1,30 = 4.7) and treatment (E2 vs. placebo, p < 0.001, F 1,30 = 28.1). Post hoc Sidak’s multiple comparisons tests: significantly different from non-ischemic placebo group (* p < 0.05, ** p < 0.01, and *** p < 0.001), or from ischemic placebo group ( ### p < 0.001). Data are mean ± SEM of individual data points (normalized to total ERK1/2). E2, 17β-estradiol. tMCAO, transient middle cerebral artery occlusion.

    Techniques Used: Expressing, Western Blot

    anti phospho mapk perk1 2 rabbit monoclonal antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho mapk perk1 2 rabbit monoclonal antibody
    Anti Phospho Mapk Perk1 2 Rabbit Monoclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    monoclonal rabbit anti perk1 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc monoclonal rabbit anti perk1 2
    Monoclonal Rabbit Anti Perk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit monoclonal anti perk1 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit monoclonal anti perk1 2
    Rabbit Monoclonal Anti Perk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit monoclonal anti perk1 2  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit monoclonal anti perk1 2
    Rabbit Monoclonal Anti Perk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    perk1 2 y202 y204 cst rabbit mab d13 14 4 e 4370 ab 2315112  (Novus Biologicals)


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    Novus Biologicals perk1 2 y202 y204 cst rabbit mab d13 14 4 e 4370 ab 2315112
    Perk1 2 Y202 Y204 Cst Rabbit Mab D13 14 4 E 4370 Ab 2315112, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    perk1 2 rabbit mab  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc perk1 2 rabbit mab
    Perk1 2 Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit monoclonal anti perk1 2 antibody
    Rabbit Monoclonal Anti Perk1 2 Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit monoclonal anti perk1 2 antibody/product/Cell Signaling Technology Inc
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    Cell Signaling Technology Inc phospho p44 42 mapk perk1 2 thr202 tyr204 rabbit mab
    Effect of liprin‐α1 knockdown to ERK phosphorylation and to oncogenic signaling. (A) Localization and expression of p‐ERK1/2 <t>(Thr202/Tyr204)</t> in MDA‐MB‐231 shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (B) Localization and expression of p‐ERK1/2 (Thr202/Tyr204) in UT‐SCC‐42A shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (C) Quantification of p‐ERK1/2 staining in A and B is shown in bar chart as a fold change (FC) between shScramble and shPPFIA1 cells and asterisk (*) means statistical significance ( P < 0.05). Student's two‐tailed t ‐test was used to calculate the statistical significance. Error bar indicates the standard deviation of the mean. A minimum of 70 individual cells were quantitated three times from two (shScramble) or three (shPPFIA1) different experiments for both of the cell lines and representative images are shown for MDA‐MB‐231 cell line in 2A and for UT‐SCC‐42A in 2B. (D) Western blot showing protein levels of liprin‐α1, p‐ERK1/2 (Thr202/Tyr204), ERK1/2, MEK1/2 and p‐MEK1/2 (Ser217/221) in a panel of studied shScramble and shPPFIA1 cells. GAPDH, α‐tubulin and vinculin were used as the loading controls. The intensity of p‐ERK1/2 bands was quantified for individual cell lines and the values are described under the blot. In addition, western blot for UT‐SCC‐42A and UT‐SCC‐42B was performed with two different constructs for p‐ERK (Fig. ). (E) Heatmap showing MAPK pathway activity score in MDA‐MB‐231 and UT‐SCC‐42A shScr and shPPFIA1 cells, and in UT‐SCC‐95 control and PPFIA1 overexpressing cells. For MDA‐MB‐231 and UT‐SCC‐42A cells, z ‐scores were computed from previously published RNAseq data . For UT‐SCC‐95 cell line, z ‐scores were computed from the RMA‐normalized expression values from microarrays . The EPHA4 gene had two probe sets mapping to the same gene, so the mean expression value was used as a basis for the z ‐score. Finally, the mean z ‐scores from different constructs were calculated. For MDA‐MB‐231 cell line, three replicates of shScr and shPPFIA1 cells were included into the analysis whereas for UT‐SCC‐42A cell line, three replicates from shScr cells and two replicates from shPPFIA1 cells were analyzed. For UT‐SCC‐95, one control and two overexpressing samples were included into the analysis. (F, G) Western blot analysis from MDA‐MB‐231 (F) and UT‐SCC‐42A (G) cells treated 48 h with trametinib. Protein levels of liprin‐α1, ERK1/2, p‐ERK1/2 (T202/Y204), p‐AKT (Ser473) and p‐rS6 (Ser235/236) proteins are shown for shScramble and shPPFIA1 cells. DMSO‐treated cells were used as a negative control for trametinib treatment, whereas α‐tubulin and vinculin served as loading controls. Figure shows quantification of p‐ERK1/2 immunoblot results calculated from four experiments for MDA‐MB‐231 and five experiments for UT‐SCC‐42A. Liprin‐α1, p‐AKT and p‐rS6 western blot experiments were performed twice for each cell line and each condition (Fig. ; Fig. ).
    Phospho P44 42 Mapk Perk1 2 Thr202 Tyr204 Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Effect of liprin‐α1 knockdown to ERK phosphorylation and to oncogenic signaling. (A) Localization and expression of p‐ERK1/2 <t>(Thr202/Tyr204)</t> in MDA‐MB‐231 shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (B) Localization and expression of p‐ERK1/2 (Thr202/Tyr204) in UT‐SCC‐42A shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (C) Quantification of p‐ERK1/2 staining in A and B is shown in bar chart as a fold change (FC) between shScramble and shPPFIA1 cells and asterisk (*) means statistical significance ( P < 0.05). Student's two‐tailed t ‐test was used to calculate the statistical significance. Error bar indicates the standard deviation of the mean. A minimum of 70 individual cells were quantitated three times from two (shScramble) or three (shPPFIA1) different experiments for both of the cell lines and representative images are shown for MDA‐MB‐231 cell line in 2A and for UT‐SCC‐42A in 2B. (D) Western blot showing protein levels of liprin‐α1, p‐ERK1/2 (Thr202/Tyr204), ERK1/2, MEK1/2 and p‐MEK1/2 (Ser217/221) in a panel of studied shScramble and shPPFIA1 cells. GAPDH, α‐tubulin and vinculin were used as the loading controls. The intensity of p‐ERK1/2 bands was quantified for individual cell lines and the values are described under the blot. In addition, western blot for UT‐SCC‐42A and UT‐SCC‐42B was performed with two different constructs for p‐ERK (Fig. ). (E) Heatmap showing MAPK pathway activity score in MDA‐MB‐231 and UT‐SCC‐42A shScr and shPPFIA1 cells, and in UT‐SCC‐95 control and PPFIA1 overexpressing cells. For MDA‐MB‐231 and UT‐SCC‐42A cells, z ‐scores were computed from previously published RNAseq data . For UT‐SCC‐95 cell line, z ‐scores were computed from the RMA‐normalized expression values from microarrays . The EPHA4 gene had two probe sets mapping to the same gene, so the mean expression value was used as a basis for the z ‐score. Finally, the mean z ‐scores from different constructs were calculated. For MDA‐MB‐231 cell line, three replicates of shScr and shPPFIA1 cells were included into the analysis whereas for UT‐SCC‐42A cell line, three replicates from shScr cells and two replicates from shPPFIA1 cells were analyzed. For UT‐SCC‐95, one control and two overexpressing samples were included into the analysis. (F, G) Western blot analysis from MDA‐MB‐231 (F) and UT‐SCC‐42A (G) cells treated 48 h with trametinib. Protein levels of liprin‐α1, ERK1/2, p‐ERK1/2 (T202/Y204), p‐AKT (Ser473) and p‐rS6 (Ser235/236) proteins are shown for shScramble and shPPFIA1 cells. DMSO‐treated cells were used as a negative control for trametinib treatment, whereas α‐tubulin and vinculin served as loading controls. Figure shows quantification of p‐ERK1/2 immunoblot results calculated from four experiments for MDA‐MB‐231 and five experiments for UT‐SCC‐42A. Liprin‐α1, p‐AKT and p‐rS6 western blot experiments were performed twice for each cell line and each condition (Fig. ; Fig. ).
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    Estradiol decreases phosphorylation of ERK1/2. Phosphorylated extracellular signal-regulated kinase 1/2 <t>(pERK1/2)</t> protein expression in brains from placebo- and E2-treated ovariectomized female rats subjected to tMCAO. ( A ) Representative Western blots and ( B ) relative abundance of pERK1 and ( C ) pERK2 in whole-cell lysates of non-ischemic (NI) and ischemic (I) hemispheres. Two-way ANOVA for pERK1: brain hemisphere (ischemic vs. non-ischemic, p < 0.001, F 1,30 = 18.1), treatment (E2 vs. placebo, p < 0.001, F 1,30 = 84.6), and interaction ( p < 0.001, F 1,30 = 15.5). Two-way ANOVA for pERK2: brain hemisphere (ischemic vs. non-ischemic, p < 0.05, F 1,30 = 4.7) and treatment (E2 vs. placebo, p < 0.001, F 1,30 = 28.1). Post hoc Sidak’s multiple comparisons tests: significantly different from non-ischemic placebo group (* p < 0.05, ** p < 0.01, and *** p < 0.001), or from ischemic placebo group ( ### p < 0.001). Data are mean ± SEM of individual data points (normalized to total ERK1/2). E2, 17β-estradiol. tMCAO, transient middle cerebral artery occlusion.
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    Image Search Results


    Effect of liprin‐α1 knockdown to ERK phosphorylation and to oncogenic signaling. (A) Localization and expression of p‐ERK1/2 (Thr202/Tyr204) in MDA‐MB‐231 shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (B) Localization and expression of p‐ERK1/2 (Thr202/Tyr204) in UT‐SCC‐42A shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (C) Quantification of p‐ERK1/2 staining in A and B is shown in bar chart as a fold change (FC) between shScramble and shPPFIA1 cells and asterisk (*) means statistical significance ( P < 0.05). Student's two‐tailed t ‐test was used to calculate the statistical significance. Error bar indicates the standard deviation of the mean. A minimum of 70 individual cells were quantitated three times from two (shScramble) or three (shPPFIA1) different experiments for both of the cell lines and representative images are shown for MDA‐MB‐231 cell line in 2A and for UT‐SCC‐42A in 2B. (D) Western blot showing protein levels of liprin‐α1, p‐ERK1/2 (Thr202/Tyr204), ERK1/2, MEK1/2 and p‐MEK1/2 (Ser217/221) in a panel of studied shScramble and shPPFIA1 cells. GAPDH, α‐tubulin and vinculin were used as the loading controls. The intensity of p‐ERK1/2 bands was quantified for individual cell lines and the values are described under the blot. In addition, western blot for UT‐SCC‐42A and UT‐SCC‐42B was performed with two different constructs for p‐ERK (Fig. ). (E) Heatmap showing MAPK pathway activity score in MDA‐MB‐231 and UT‐SCC‐42A shScr and shPPFIA1 cells, and in UT‐SCC‐95 control and PPFIA1 overexpressing cells. For MDA‐MB‐231 and UT‐SCC‐42A cells, z ‐scores were computed from previously published RNAseq data . For UT‐SCC‐95 cell line, z ‐scores were computed from the RMA‐normalized expression values from microarrays . The EPHA4 gene had two probe sets mapping to the same gene, so the mean expression value was used as a basis for the z ‐score. Finally, the mean z ‐scores from different constructs were calculated. For MDA‐MB‐231 cell line, three replicates of shScr and shPPFIA1 cells were included into the analysis whereas for UT‐SCC‐42A cell line, three replicates from shScr cells and two replicates from shPPFIA1 cells were analyzed. For UT‐SCC‐95, one control and two overexpressing samples were included into the analysis. (F, G) Western blot analysis from MDA‐MB‐231 (F) and UT‐SCC‐42A (G) cells treated 48 h with trametinib. Protein levels of liprin‐α1, ERK1/2, p‐ERK1/2 (T202/Y204), p‐AKT (Ser473) and p‐rS6 (Ser235/236) proteins are shown for shScramble and shPPFIA1 cells. DMSO‐treated cells were used as a negative control for trametinib treatment, whereas α‐tubulin and vinculin served as loading controls. Figure shows quantification of p‐ERK1/2 immunoblot results calculated from four experiments for MDA‐MB‐231 and five experiments for UT‐SCC‐42A. Liprin‐α1, p‐AKT and p‐rS6 western blot experiments were performed twice for each cell line and each condition (Fig. ; Fig. ).

    Journal: Molecular Oncology

    Article Title: Liprin‐α1 contributes to oncogenic MAPK signaling by counteracting ERK activity

    doi: 10.1002/1878-0261.13593

    Figure Lengend Snippet: Effect of liprin‐α1 knockdown to ERK phosphorylation and to oncogenic signaling. (A) Localization and expression of p‐ERK1/2 (Thr202/Tyr204) in MDA‐MB‐231 shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (B) Localization and expression of p‐ERK1/2 (Thr202/Tyr204) in UT‐SCC‐42A shScramble and shPPFIA1_1 (construct #69) cells as visualized by immunofluorescence microscopy. Scale bar is 10 μ m . (C) Quantification of p‐ERK1/2 staining in A and B is shown in bar chart as a fold change (FC) between shScramble and shPPFIA1 cells and asterisk (*) means statistical significance ( P < 0.05). Student's two‐tailed t ‐test was used to calculate the statistical significance. Error bar indicates the standard deviation of the mean. A minimum of 70 individual cells were quantitated three times from two (shScramble) or three (shPPFIA1) different experiments for both of the cell lines and representative images are shown for MDA‐MB‐231 cell line in 2A and for UT‐SCC‐42A in 2B. (D) Western blot showing protein levels of liprin‐α1, p‐ERK1/2 (Thr202/Tyr204), ERK1/2, MEK1/2 and p‐MEK1/2 (Ser217/221) in a panel of studied shScramble and shPPFIA1 cells. GAPDH, α‐tubulin and vinculin were used as the loading controls. The intensity of p‐ERK1/2 bands was quantified for individual cell lines and the values are described under the blot. In addition, western blot for UT‐SCC‐42A and UT‐SCC‐42B was performed with two different constructs for p‐ERK (Fig. ). (E) Heatmap showing MAPK pathway activity score in MDA‐MB‐231 and UT‐SCC‐42A shScr and shPPFIA1 cells, and in UT‐SCC‐95 control and PPFIA1 overexpressing cells. For MDA‐MB‐231 and UT‐SCC‐42A cells, z ‐scores were computed from previously published RNAseq data . For UT‐SCC‐95 cell line, z ‐scores were computed from the RMA‐normalized expression values from microarrays . The EPHA4 gene had two probe sets mapping to the same gene, so the mean expression value was used as a basis for the z ‐score. Finally, the mean z ‐scores from different constructs were calculated. For MDA‐MB‐231 cell line, three replicates of shScr and shPPFIA1 cells were included into the analysis whereas for UT‐SCC‐42A cell line, three replicates from shScr cells and two replicates from shPPFIA1 cells were analyzed. For UT‐SCC‐95, one control and two overexpressing samples were included into the analysis. (F, G) Western blot analysis from MDA‐MB‐231 (F) and UT‐SCC‐42A (G) cells treated 48 h with trametinib. Protein levels of liprin‐α1, ERK1/2, p‐ERK1/2 (T202/Y204), p‐AKT (Ser473) and p‐rS6 (Ser235/236) proteins are shown for shScramble and shPPFIA1 cells. DMSO‐treated cells were used as a negative control for trametinib treatment, whereas α‐tubulin and vinculin served as loading controls. Figure shows quantification of p‐ERK1/2 immunoblot results calculated from four experiments for MDA‐MB‐231 and five experiments for UT‐SCC‐42A. Liprin‐α1, p‐AKT and p‐rS6 western blot experiments were performed twice for each cell line and each condition (Fig. ; Fig. ).

    Article Snippet: Antibodies used were rabbit polyclonal liprin‐α1 (Proteintech, Manchester, UK), mouse monoclonal α‐tubulin (Sigma‐Aldrich, Saint Louis, MO, USA), p44/42 MAPK (ERK1/2) Antibody (#9102), phospho‐p44/42 MAPK (pERK1/2) (Thr202/Tyr204) rabbit mAb (#4377), rabbit monoclonal p‐AKT (Ser473) (#4060), p‐rS6 rabbit mAb (Ser 235/236) (#4858), p‐MEK1/2 (Ser217/221) (41G9) rabbit mAb (#9154), MEK1/2 (#8727) rabbit mAb (Cell Signaling, Danvers, MA, USA), mouse mAb RAF1 (E10, sc7267) (Santa Cruz, Dallas, TX, USA), rabbit mAb RAF1 (Abcam, Cambridge, UK), mouse monoclonal vinculin (Sigma‐Aldrich), and mouse monoclonal GAPDH (Europa Bioproducts, Wicken, UK).

    Techniques: Expressing, Construct, Immunofluorescence, Microscopy, Staining, Two Tailed Test, Standard Deviation, Western Blot, Activity Assay, Negative Control

    Estradiol decreases phosphorylation of ERK1/2. Phosphorylated extracellular signal-regulated kinase 1/2 (pERK1/2) protein expression in brains from placebo- and E2-treated ovariectomized female rats subjected to tMCAO. ( A ) Representative Western blots and ( B ) relative abundance of pERK1 and ( C ) pERK2 in whole-cell lysates of non-ischemic (NI) and ischemic (I) hemispheres. Two-way ANOVA for pERK1: brain hemisphere (ischemic vs. non-ischemic, p < 0.001, F 1,30 = 18.1), treatment (E2 vs. placebo, p < 0.001, F 1,30 = 84.6), and interaction ( p < 0.001, F 1,30 = 15.5). Two-way ANOVA for pERK2: brain hemisphere (ischemic vs. non-ischemic, p < 0.05, F 1,30 = 4.7) and treatment (E2 vs. placebo, p < 0.001, F 1,30 = 28.1). Post hoc Sidak’s multiple comparisons tests: significantly different from non-ischemic placebo group (* p < 0.05, ** p < 0.01, and *** p < 0.001), or from ischemic placebo group ( ### p < 0.001). Data are mean ± SEM of individual data points (normalized to total ERK1/2). E2, 17β-estradiol. tMCAO, transient middle cerebral artery occlusion.

    Journal: International Journal of Molecular Sciences

    Article Title: Cerebroprotective Effect of 17β-Estradiol Replacement Therapy in Ovariectomy-Induced Post-Menopausal Rats Subjected to Ischemic Stroke: Role of MAPK/ERK1/2 Pathway and PI3K-Independent Akt Activation

    doi: 10.3390/ijms241814303

    Figure Lengend Snippet: Estradiol decreases phosphorylation of ERK1/2. Phosphorylated extracellular signal-regulated kinase 1/2 (pERK1/2) protein expression in brains from placebo- and E2-treated ovariectomized female rats subjected to tMCAO. ( A ) Representative Western blots and ( B ) relative abundance of pERK1 and ( C ) pERK2 in whole-cell lysates of non-ischemic (NI) and ischemic (I) hemispheres. Two-way ANOVA for pERK1: brain hemisphere (ischemic vs. non-ischemic, p < 0.001, F 1,30 = 18.1), treatment (E2 vs. placebo, p < 0.001, F 1,30 = 84.6), and interaction ( p < 0.001, F 1,30 = 15.5). Two-way ANOVA for pERK2: brain hemisphere (ischemic vs. non-ischemic, p < 0.05, F 1,30 = 4.7) and treatment (E2 vs. placebo, p < 0.001, F 1,30 = 28.1). Post hoc Sidak’s multiple comparisons tests: significantly different from non-ischemic placebo group (* p < 0.05, ** p < 0.01, and *** p < 0.001), or from ischemic placebo group ( ### p < 0.001). Data are mean ± SEM of individual data points (normalized to total ERK1/2). E2, 17β-estradiol. tMCAO, transient middle cerebral artery occlusion.

    Article Snippet: Aliquots of protein (40 μg) were dissolved in NuPAGE LDS sample buffer (Invitrogen, Carlsbad, CA, USA) under reducing conditions, loaded on 4–12% Bis-Tris gels (Invitrogen), subjected to SDS-PAGE and electrotransferred to 0.2 μm nitrocellulose membranes for immunolabeling using the following primary antibodies: (1) anti-cleaved caspase-3 (Asp175), rabbit polyclonal antibody that detects endogenous levels of the large fragment (17/19 KDa) of activated caspase-3 (#9661;1:500; Cell Signaling Technology, Inc., Beverly, MA, USA); (2) anti-phospho MAPK (pERK1/2) rabbit monoclonal antibody, which recognizes ERK1 and ERK2 that are phosphorylated on both a Thr202 and a Tyr204 residue (D13.14.4E; #4370;1:2000; Cell Signaling Technology); (3) anti-MAPK1/2 (ERK1/2) rabbit polyclonal antibody (#06-182; 1:5000; Millipore, Temecula, CA, USA); (4) anti-phospho BAD (pBAD) rabbit monoclonal antibody, which detects endogenous levels of BAD only when phosphorylated at Ser136 (D25H8; #4366;1:500; Cell Signaling Technology); (5) anti-Bad rabbit polyclonal antibody (#9292; 1:500; Cell Signaling Technology); (6) anti-phospho Akt (pAkt) mouse monoclonal antibody, which recognizes Akt only when phosphorylated at Ser473 (193H12; #4058; 1:000; Cell Signaling Technology); (7) anti-Akt (Akt, pan) rabbit monoclonal antibody (C67E7; #4691; 1:1000, Cell Signaling Technology); (8) anti-CTMP, rabbit polyclonal antibody, which detects endogenous levels of total CTMP protein (#4612; 1:500; Cell Signaling Technology); and (9) anti-β-actin mouse monoclonal antibody (Clone AC-15, #A5441; 1:10000; Sigma, Saint Louis, MI, USA).

    Techniques: Expressing, Western Blot