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Cell Signaling Technology Inc phosphorylated raf 1 antibodies
Insulin activates <t>Raf-1</t> and ERK in transformed MIN6 cells. Panel A, ERK phosphorylation in MIN6 cells treated with low glucose (5 m m ) or high glucose (25 m m ) for 15 min with or without somatostatin (Soma, 1 μ m ; n = 3). Panel B, Insulin
Phosphorylated Raf 1 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Acute Insulin Signaling in Pancreatic Beta-Cells Is Mediated by Multiple Raf-1 Dependent Pathways"

Article Title: Acute Insulin Signaling in Pancreatic Beta-Cells Is Mediated by Multiple Raf-1 Dependent Pathways

Journal: Endocrinology

doi: 10.1210/en.2009-0678

Insulin activates Raf-1 and ERK in transformed MIN6 cells. Panel A, ERK phosphorylation in MIN6 cells treated with low glucose (5 m m ) or high glucose (25 m m ) for 15 min with or without somatostatin (Soma, 1 μ m ; n = 3). Panel B, Insulin
Figure Legend Snippet: Insulin activates Raf-1 and ERK in transformed MIN6 cells. Panel A, ERK phosphorylation in MIN6 cells treated with low glucose (5 m m ) or high glucose (25 m m ) for 15 min with or without somatostatin (Soma, 1 μ m ; n = 3). Panel B, Insulin

Techniques Used: Transformation Assay

Insulin promotes Raf-1 and ERK activation in mouse islets. A, Acute insulin signaling stimulation for 15 min in primary mouse islets with 0.2 and 200 n m insulin resulted in a loss of inhibitory phosphorylation of Raf-1 (pRaf-1) at serine 259. B, Mouse
Figure Legend Snippet: Insulin promotes Raf-1 and ERK activation in mouse islets. A, Acute insulin signaling stimulation for 15 min in primary mouse islets with 0.2 and 200 n m insulin resulted in a loss of inhibitory phosphorylation of Raf-1 (pRaf-1) at serine 259. B, Mouse

Techniques Used: Activation Assay

Insulin promotes Raf-1 translocation to the mitochondria. A, Insulin (0.2 n m ) promoted Raf-1 mitochondrial localization compared with serum free in mouse pancreatic β-cell (n = 3). Scale bars , 10 μm. B, A plot of Pearson correlation
Figure Legend Snippet: Insulin promotes Raf-1 translocation to the mitochondria. A, Insulin (0.2 n m ) promoted Raf-1 mitochondrial localization compared with serum free in mouse pancreatic β-cell (n = 3). Scale bars , 10 μm. B, A plot of Pearson correlation

Techniques Used: Translocation Assay

Endogenous Bcl-2 family members and Raf-1 form protein-protein interactions in pancreatic β-cell. A, Immunofluorescence imaging of endogenous Raf-1 and Bad in primary human and mouse β-cells. Pearson correlation r values between Raf-1
Figure Legend Snippet: Endogenous Bcl-2 family members and Raf-1 form protein-protein interactions in pancreatic β-cell. A, Immunofluorescence imaging of endogenous Raf-1 and Bad in primary human and mouse β-cells. Pearson correlation r values between Raf-1

Techniques Used: Immunofluorescence, Imaging

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    Cell Signaling Technology Inc phosphorylated raf 1 antibodies
    Insulin activates <t>Raf-1</t> and ERK in transformed MIN6 cells. Panel A, ERK phosphorylation in MIN6 cells treated with low glucose (5 m m ) or high glucose (25 m m ) for 15 min with or without somatostatin (Soma, 1 μ m ; n = 3). Panel B, Insulin
    Phosphorylated Raf 1 Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phosphorylated raf 1 antibodies/product/Cell Signaling Technology Inc
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    phosphorylated raf 1 antibodies - by Bioz Stars, 2020-11
    85/100 stars
      Buy from Supplier

    88
    Cell Signaling Technology Inc anti phospho raf 1
    Membrane fusion-associated activation of ERK in HepG2 cells. (A) Probing of fusion-associated MAPK pathways. After FV-, HCFV-, or HNFV-HepG2 cell fusion (dose dependent) under the indicated conditions, lysates were probed with anti-pERK, -pJNK, or -pp38 in Western blots, followed by stripping and reprobing with anti-ERK, -JNK, or -p38, respectively. The amount of lysate loaded is indicated. Relative fold activation (expressed as mean ± SD for three independent experiments) is represented graphically (densitometric analysis). (B) Kinetic profile of ERK activation during FV-HepG2 cell fusion upon incubation with 80 μg FV. (C) Assessment of functional activity of activated ERKs. The indicated lysates (from panel A) were assayed for MBP phosphorylation. Reaction mixtures were resolved by SDS-15% PAGE. The lower half of the gel was autoradiographed (middle panel) after CB staining (lower panel), and the upper half was incubated with anti-ERK to ensure equal loading (upper panel). The graph indicates fold activation (expressed as mean ± SD for three independent experiments) of MBP phosphorylation (lanes 3 to 10). MBP bands were excised and radioactivity was measured. (D) Detection of pERK, pJNK, and pp38 levels during FV-HepG2 cell fusion. Fused cells were fixed, stained for pERK (rows 1 and 2), pJNK (row 3), or pp38 (row 4) with FITC-labeled secondary antibody (green), and merged with RITC-L (red) delivered to the cytosol after FV fusion. Nuclei were stained with DAPI (blue). Bar, 15.59 μm. (E) <t>Raf-1</t> activation in cells after fusion with FV, HCFV, HNFV, or (H247A)HNFV was checked by anti-pRaf-1 Western analysis (upper panel), followed by stripping and reprobing with anti-cRaf (lower panel). (F) EMSA was performed with nuclear extracts to detect AP-1 activation. Lane 8 was loaded with a 50-fold molar excess of cold competitor during DNA-protein interaction.
    Anti Phospho Raf 1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 88/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti phospho raf 1/product/Cell Signaling Technology Inc
    Average 88 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti phospho raf 1 - by Bioz Stars, 2020-11
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    99
    Cell Signaling Technology Inc phospho c raf
    Western blot for <t>phospho-c-raf</t> in whole cell lysates. Dose-range study of 24-h G 56 G 80 G 81 -rhIGFBP-3 transfection (A) with corresponding densitometry normalized to “0” control (B). Time course (C) with corresponding densitometry normalized to “0” control (D) (** p
    Phospho C Raf, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho c raf/product/Cell Signaling Technology Inc
    Average 99 stars, based on 20 article reviews
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    phospho c raf - by Bioz Stars, 2020-11
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    Cell Signaling Technology Inc phospho erk1 2
    Ethionamide stimulated proliferation of MSCs via activating phosphatidylinositol 3-kinase (PI3K)/Akt and mitogen-activated protein kinase/extracellular signal-regulated protein kinase kinase <t>(MEK/ERK1/2)</t> signaling pathways. ( A ) MSCs were exposed to varying concentrations of ethionamide. The proliferation of MSCs was measured by BrdU ELISA after 72 h incubation. ( B ) The proliferation of MSCs was measured by BrdU ELISA after treatment with 10 μM and 100 μM of ethionamide for 24 h, 48 h, 72 h. ( C ) PI3K/Akt and ( D ) MEK/ERK1/2 signaling pathways were evaluated by Western blotting. The cells were treated with LY294002 (30 μM), the inhibitors of PI3K and PD98059 (50 μM), the inhibitors of MEK to suppress signaling pathways. β-actin was used as an internal control. ( E , F ) After the treatment of the cells with ethionamide and inhibitors, the proliferation of MSCs was measured by the BrdU ELISA. The results obtained from three independent experiments were expressed as a percent of untreated control ± SEM; * p
    Phospho Erk1 2, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 821 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Insulin activates Raf-1 and ERK in transformed MIN6 cells. Panel A, ERK phosphorylation in MIN6 cells treated with low glucose (5 m m ) or high glucose (25 m m ) for 15 min with or without somatostatin (Soma, 1 μ m ; n = 3). Panel B, Insulin

    Journal: Endocrinology

    Article Title: Acute Insulin Signaling in Pancreatic Beta-Cells Is Mediated by Multiple Raf-1 Dependent Pathways

    doi: 10.1210/en.2009-0678

    Figure Lengend Snippet: Insulin activates Raf-1 and ERK in transformed MIN6 cells. Panel A, ERK phosphorylation in MIN6 cells treated with low glucose (5 m m ) or high glucose (25 m m ) for 15 min with or without somatostatin (Soma, 1 μ m ; n = 3). Panel B, Insulin

    Article Snippet: Insulin receptor and phosphorylated Raf-1 antibodies were from Cell Signaling and phosphorylated insulin receptor, Raf-1, and insulin antibodies were from Stressgen (Ann Arbor, MI), BD Biosciences, and Linco Research (St. Charles, MO), respectively.

    Techniques: Transformation Assay

    Insulin promotes Raf-1 and ERK activation in mouse islets. A, Acute insulin signaling stimulation for 15 min in primary mouse islets with 0.2 and 200 n m insulin resulted in a loss of inhibitory phosphorylation of Raf-1 (pRaf-1) at serine 259. B, Mouse

    Journal: Endocrinology

    Article Title: Acute Insulin Signaling in Pancreatic Beta-Cells Is Mediated by Multiple Raf-1 Dependent Pathways

    doi: 10.1210/en.2009-0678

    Figure Lengend Snippet: Insulin promotes Raf-1 and ERK activation in mouse islets. A, Acute insulin signaling stimulation for 15 min in primary mouse islets with 0.2 and 200 n m insulin resulted in a loss of inhibitory phosphorylation of Raf-1 (pRaf-1) at serine 259. B, Mouse

    Article Snippet: Insulin receptor and phosphorylated Raf-1 antibodies were from Cell Signaling and phosphorylated insulin receptor, Raf-1, and insulin antibodies were from Stressgen (Ann Arbor, MI), BD Biosciences, and Linco Research (St. Charles, MO), respectively.

    Techniques: Activation Assay

    Insulin promotes Raf-1 translocation to the mitochondria. A, Insulin (0.2 n m ) promoted Raf-1 mitochondrial localization compared with serum free in mouse pancreatic β-cell (n = 3). Scale bars , 10 μm. B, A plot of Pearson correlation

    Journal: Endocrinology

    Article Title: Acute Insulin Signaling in Pancreatic Beta-Cells Is Mediated by Multiple Raf-1 Dependent Pathways

    doi: 10.1210/en.2009-0678

    Figure Lengend Snippet: Insulin promotes Raf-1 translocation to the mitochondria. A, Insulin (0.2 n m ) promoted Raf-1 mitochondrial localization compared with serum free in mouse pancreatic β-cell (n = 3). Scale bars , 10 μm. B, A plot of Pearson correlation

    Article Snippet: Insulin receptor and phosphorylated Raf-1 antibodies were from Cell Signaling and phosphorylated insulin receptor, Raf-1, and insulin antibodies were from Stressgen (Ann Arbor, MI), BD Biosciences, and Linco Research (St. Charles, MO), respectively.

    Techniques: Translocation Assay

    Endogenous Bcl-2 family members and Raf-1 form protein-protein interactions in pancreatic β-cell. A, Immunofluorescence imaging of endogenous Raf-1 and Bad in primary human and mouse β-cells. Pearson correlation r values between Raf-1

    Journal: Endocrinology

    Article Title: Acute Insulin Signaling in Pancreatic Beta-Cells Is Mediated by Multiple Raf-1 Dependent Pathways

    doi: 10.1210/en.2009-0678

    Figure Lengend Snippet: Endogenous Bcl-2 family members and Raf-1 form protein-protein interactions in pancreatic β-cell. A, Immunofluorescence imaging of endogenous Raf-1 and Bad in primary human and mouse β-cells. Pearson correlation r values between Raf-1

    Article Snippet: Insulin receptor and phosphorylated Raf-1 antibodies were from Cell Signaling and phosphorylated insulin receptor, Raf-1, and insulin antibodies were from Stressgen (Ann Arbor, MI), BD Biosciences, and Linco Research (St. Charles, MO), respectively.

    Techniques: Immunofluorescence, Imaging

    Membrane fusion-associated activation of ERK in HepG2 cells. (A) Probing of fusion-associated MAPK pathways. After FV-, HCFV-, or HNFV-HepG2 cell fusion (dose dependent) under the indicated conditions, lysates were probed with anti-pERK, -pJNK, or -pp38 in Western blots, followed by stripping and reprobing with anti-ERK, -JNK, or -p38, respectively. The amount of lysate loaded is indicated. Relative fold activation (expressed as mean ± SD for three independent experiments) is represented graphically (densitometric analysis). (B) Kinetic profile of ERK activation during FV-HepG2 cell fusion upon incubation with 80 μg FV. (C) Assessment of functional activity of activated ERKs. The indicated lysates (from panel A) were assayed for MBP phosphorylation. Reaction mixtures were resolved by SDS-15% PAGE. The lower half of the gel was autoradiographed (middle panel) after CB staining (lower panel), and the upper half was incubated with anti-ERK to ensure equal loading (upper panel). The graph indicates fold activation (expressed as mean ± SD for three independent experiments) of MBP phosphorylation (lanes 3 to 10). MBP bands were excised and radioactivity was measured. (D) Detection of pERK, pJNK, and pp38 levels during FV-HepG2 cell fusion. Fused cells were fixed, stained for pERK (rows 1 and 2), pJNK (row 3), or pp38 (row 4) with FITC-labeled secondary antibody (green), and merged with RITC-L (red) delivered to the cytosol after FV fusion. Nuclei were stained with DAPI (blue). Bar, 15.59 μm. (E) Raf-1 activation in cells after fusion with FV, HCFV, HNFV, or (H247A)HNFV was checked by anti-pRaf-1 Western analysis (upper panel), followed by stripping and reprobing with anti-cRaf (lower panel). (F) EMSA was performed with nuclear extracts to detect AP-1 activation. Lane 8 was loaded with a 50-fold molar excess of cold competitor during DNA-protein interaction.

    Journal: Journal of Virology

    Article Title: Reciprocal Regulation of AKT and MAP Kinase Dictates Virus-Host Cell Fusion ▿

    doi: 10.1128/JVI.01940-09

    Figure Lengend Snippet: Membrane fusion-associated activation of ERK in HepG2 cells. (A) Probing of fusion-associated MAPK pathways. After FV-, HCFV-, or HNFV-HepG2 cell fusion (dose dependent) under the indicated conditions, lysates were probed with anti-pERK, -pJNK, or -pp38 in Western blots, followed by stripping and reprobing with anti-ERK, -JNK, or -p38, respectively. The amount of lysate loaded is indicated. Relative fold activation (expressed as mean ± SD for three independent experiments) is represented graphically (densitometric analysis). (B) Kinetic profile of ERK activation during FV-HepG2 cell fusion upon incubation with 80 μg FV. (C) Assessment of functional activity of activated ERKs. The indicated lysates (from panel A) were assayed for MBP phosphorylation. Reaction mixtures were resolved by SDS-15% PAGE. The lower half of the gel was autoradiographed (middle panel) after CB staining (lower panel), and the upper half was incubated with anti-ERK to ensure equal loading (upper panel). The graph indicates fold activation (expressed as mean ± SD for three independent experiments) of MBP phosphorylation (lanes 3 to 10). MBP bands were excised and radioactivity was measured. (D) Detection of pERK, pJNK, and pp38 levels during FV-HepG2 cell fusion. Fused cells were fixed, stained for pERK (rows 1 and 2), pJNK (row 3), or pp38 (row 4) with FITC-labeled secondary antibody (green), and merged with RITC-L (red) delivered to the cytosol after FV fusion. Nuclei were stained with DAPI (blue). Bar, 15.59 μm. (E) Raf-1 activation in cells after fusion with FV, HCFV, HNFV, or (H247A)HNFV was checked by anti-pRaf-1 Western analysis (upper panel), followed by stripping and reprobing with anti-cRaf (lower panel). (F) EMSA was performed with nuclear extracts to detect AP-1 activation. Lane 8 was loaded with a 50-fold molar excess of cold competitor during DNA-protein interaction.

    Article Snippet: Phospho-p44/42 mitogen-activated protein kinase (MAPK) antibody (pERK1/2; 9106S), phospho-p38 antibody (9211S), phospho-ezrin(Thr567)/radixin(Thr564)/moesin(Thr558) antibody (3141), ezrin/radixin/moesin antibody (3142), anti-phospho-Raf-1 (9421), anti-c-Raf (9422), anti-phospho-PKA C (Thr197) (4781), and anti-PKA C-α (4782) were purchased from Cell Signaling Technology.

    Techniques: Activation Assay, Western Blot, Stripping Membranes, Incubation, Functional Assay, Activity Assay, Polyacrylamide Gel Electrophoresis, Staining, Radioactivity, Labeling

    Western blot for phospho-c-raf in whole cell lysates. Dose-range study of 24-h G 56 G 80 G 81 -rhIGFBP-3 transfection (A) with corresponding densitometry normalized to “0” control (B). Time course (C) with corresponding densitometry normalized to “0” control (D) (** p

    Journal: Growth hormone & IGF research : official journal of the Growth Hormone Research Society and the International IGF Research Society

    Article Title: Novel actions of IGFBP-3 on intracellular signaling pathways of insulin-secreting cells

    doi: 10.1016/j.ghir.2005.09.003

    Figure Lengend Snippet: Western blot for phospho-c-raf in whole cell lysates. Dose-range study of 24-h G 56 G 80 G 81 -rhIGFBP-3 transfection (A) with corresponding densitometry normalized to “0” control (B). Time course (C) with corresponding densitometry normalized to “0” control (D) (** p

    Article Snippet: Polyclonal antibodies to phospho-ERK, total ERK, phospho-MEK1/2, MEK1/2, phospho-c-raf, c-raf, phospho-p38, total p38, phospho-SAPK/JNK, and total SAPK/JNK were purchased from Cell Signaling Technology, Inc. (Beverly, MA, USA).

    Techniques: Western Blot, Transfection

    Ethionamide stimulated proliferation of MSCs via activating phosphatidylinositol 3-kinase (PI3K)/Akt and mitogen-activated protein kinase/extracellular signal-regulated protein kinase kinase (MEK/ERK1/2) signaling pathways. ( A ) MSCs were exposed to varying concentrations of ethionamide. The proliferation of MSCs was measured by BrdU ELISA after 72 h incubation. ( B ) The proliferation of MSCs was measured by BrdU ELISA after treatment with 10 μM and 100 μM of ethionamide for 24 h, 48 h, 72 h. ( C ) PI3K/Akt and ( D ) MEK/ERK1/2 signaling pathways were evaluated by Western blotting. The cells were treated with LY294002 (30 μM), the inhibitors of PI3K and PD98059 (50 μM), the inhibitors of MEK to suppress signaling pathways. β-actin was used as an internal control. ( E , F ) After the treatment of the cells with ethionamide and inhibitors, the proliferation of MSCs was measured by the BrdU ELISA. The results obtained from three independent experiments were expressed as a percent of untreated control ± SEM; * p

    Journal: International Journal of Molecular Sciences

    Article Title: Ethionamide Preconditioning Enhances the Proliferation and Migration of Human Wharton’s Jelly-Derived Mesenchymal Stem Cells

    doi: 10.3390/ijms21197013

    Figure Lengend Snippet: Ethionamide stimulated proliferation of MSCs via activating phosphatidylinositol 3-kinase (PI3K)/Akt and mitogen-activated protein kinase/extracellular signal-regulated protein kinase kinase (MEK/ERK1/2) signaling pathways. ( A ) MSCs were exposed to varying concentrations of ethionamide. The proliferation of MSCs was measured by BrdU ELISA after 72 h incubation. ( B ) The proliferation of MSCs was measured by BrdU ELISA after treatment with 10 μM and 100 μM of ethionamide for 24 h, 48 h, 72 h. ( C ) PI3K/Akt and ( D ) MEK/ERK1/2 signaling pathways were evaluated by Western blotting. The cells were treated with LY294002 (30 μM), the inhibitors of PI3K and PD98059 (50 μM), the inhibitors of MEK to suppress signaling pathways. β-actin was used as an internal control. ( E , F ) After the treatment of the cells with ethionamide and inhibitors, the proliferation of MSCs was measured by the BrdU ELISA. The results obtained from three independent experiments were expressed as a percent of untreated control ± SEM; * p

    Article Snippet: After treatment with blocking solution (5% skim milk, 10 mM Tris-HCl, pH 7.5, 150 mM NaCl and 0.4% Tween-20) for 1 h at room temperature, the membrane was incubated overnight with the appropriate antibodies [Phospho-Akt (1:1000), Total Akt (1:1000), Phospho-ERK1/2 (1:1000), Total ERK1/2 (1:1000), Phospho-STAT3 (1:1000), Total STAT3 (1:1000)] (Cell Signaling Technology) and β-actin (1:5000, Santacruz Biotechnology) at 4 °C, followed by horseradish peroxidase-conjugated secondary antibodies for 3 h at room temperature.

    Techniques: Enzyme-linked Immunosorbent Assay, Incubation, Western Blot