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Cell Signaling Technology Inc phospho raf 1
Effects of <t>Raf-1</t> kinase inhibition on PE-induced MLC 20 ( a ) and MYPT1 ( b ) phosphorylation in rat VSMCs. Left and right panels show concentration- and time-dependent effects of PE, respectively. Cultured cells were pretreated with vehicle or GW5074 (10 μ M ) for 30 min before stimulated with 10 μ M PE. Treated cells were processed as described in Methods. The phosphorylation levels of MLC 20 or MYPT1 were determined by immunoblotting. Top panels show representative blots of phospho-MLC 20 or phospho-MYPT1 and β-actin, bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to control. Data represent means of 3–5 independent experiments. * p
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1) Product Images from "Raf-1 Kinase Regulates Smooth Muscle Contraction in the Rat Mesenteric Arteries"

Article Title: Raf-1 Kinase Regulates Smooth Muscle Contraction in the Rat Mesenteric Arteries

Journal: Journal of Vascular Research

doi: 10.1159/000277726

Effects of Raf-1 kinase inhibition on PE-induced MLC 20 ( a ) and MYPT1 ( b ) phosphorylation in rat VSMCs. Left and right panels show concentration- and time-dependent effects of PE, respectively. Cultured cells were pretreated with vehicle or GW5074 (10 μ M ) for 30 min before stimulated with 10 μ M PE. Treated cells were processed as described in Methods. The phosphorylation levels of MLC 20 or MYPT1 were determined by immunoblotting. Top panels show representative blots of phospho-MLC 20 or phospho-MYPT1 and β-actin, bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to control. Data represent means of 3–5 independent experiments. * p
Figure Legend Snippet: Effects of Raf-1 kinase inhibition on PE-induced MLC 20 ( a ) and MYPT1 ( b ) phosphorylation in rat VSMCs. Left and right panels show concentration- and time-dependent effects of PE, respectively. Cultured cells were pretreated with vehicle or GW5074 (10 μ M ) for 30 min before stimulated with 10 μ M PE. Treated cells were processed as described in Methods. The phosphorylation levels of MLC 20 or MYPT1 were determined by immunoblotting. Top panels show representative blots of phospho-MLC 20 or phospho-MYPT1 and β-actin, bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to control. Data represent means of 3–5 independent experiments. * p

Techniques Used: Inhibition, Concentration Assay, Cell Culture

Reversal of PE-induced contraction by Raf-1 kinase inhibitors in rat mesenteric arteries (semi-log plot). Submaximal PE contraction was elicited, increasing concentrations of Raf-1 kinase inhibitors, GW5074, L779450 and ZM33637, were added, and then the percentage of relaxation to PE contraction was measured. Data points represent mean ± SEM of measurements in 10–12 mesenteric arterial rings from 5–6 rats.
Figure Legend Snippet: Reversal of PE-induced contraction by Raf-1 kinase inhibitors in rat mesenteric arteries (semi-log plot). Submaximal PE contraction was elicited, increasing concentrations of Raf-1 kinase inhibitors, GW5074, L779450 and ZM33637, were added, and then the percentage of relaxation to PE contraction was measured. Data points represent mean ± SEM of measurements in 10–12 mesenteric arterial rings from 5–6 rats.

Techniques Used:

a Basal MAP in rats in the absence and presence of GW5074 (250 μg/kg). b Effect of Raf-1 kinase inhibition on PE-induced increase in mean arterial pressure in rats. Dose-response curve for PE evoked increase in blood pressure in the absence and presence of GW5074 (semi-log plot). Rats were pretreated with GW5074 (250 μg/kg; i.v.) or vehicle for 15 min and then increasing concentration of PE was infused (10–300 μg/kg/min). Each dose of PE was infused for a 3-min period and the MAP was determined as the mean value recorded within the last minute of infusion. Hypertensive responses were calculated as percent increase in MAP with respect to the baseline MAP. Values are expressed as mean ± SEM of 5–6 animals.
Figure Legend Snippet: a Basal MAP in rats in the absence and presence of GW5074 (250 μg/kg). b Effect of Raf-1 kinase inhibition on PE-induced increase in mean arterial pressure in rats. Dose-response curve for PE evoked increase in blood pressure in the absence and presence of GW5074 (semi-log plot). Rats were pretreated with GW5074 (250 μg/kg; i.v.) or vehicle for 15 min and then increasing concentration of PE was infused (10–300 μg/kg/min). Each dose of PE was infused for a 3-min period and the MAP was determined as the mean value recorded within the last minute of infusion. Hypertensive responses were calculated as percent increase in MAP with respect to the baseline MAP. Values are expressed as mean ± SEM of 5–6 animals.

Techniques Used: Inhibition, Concentration Assay

Dose and time course of PE-stimulated phosphorylation of Raf-1 ( a ), MEK ( b ) and ERK ( c ). Left and right panels show concentration- and time-dependent effects of PE, respectively. Cultured VSMCs were treated with varying concentration of PE for 5 min. For time course studies cells pretreated with GW5074 (10 μ M ) or vehicle for 30 min before stimulated with PE (10 μ M ) for indicated time periods. Treated cells were processed as described in Methods. The phosphorylation levels of Raf-1, MEK and ERK were determined by immunoblotting. Top panels show representative blots of respective phosphorylated proteins and β-actin; bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to control. Data represent mean of 4–5 independent experiments. * p
Figure Legend Snippet: Dose and time course of PE-stimulated phosphorylation of Raf-1 ( a ), MEK ( b ) and ERK ( c ). Left and right panels show concentration- and time-dependent effects of PE, respectively. Cultured VSMCs were treated with varying concentration of PE for 5 min. For time course studies cells pretreated with GW5074 (10 μ M ) or vehicle for 30 min before stimulated with PE (10 μ M ) for indicated time periods. Treated cells were processed as described in Methods. The phosphorylation levels of Raf-1, MEK and ERK were determined by immunoblotting. Top panels show representative blots of respective phosphorylated proteins and β-actin; bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to control. Data represent mean of 4–5 independent experiments. * p

Techniques Used: Concentration Assay, Cell Culture

Effects of Raf-1 kinase inhibition on PKC-induced Raf-1 ( a ), MLC 20 ( b ), MYPT1 ( c ), MEK ( d ) and ERK ( e ) phosphorylation in rat VSMCs. Cultured cells were pretreated with vehicle or GW5074 (10 μ M ) or U0126 (10 μ M ) or calphostin C (100 n M ) for 30 min before stimulated with 3 μ M PDBu for 15 min. Treated cells were processed as described in Methods. The phosphorylation levels of these proteins were determined by immunoblotting. Top panels show representative blots of the respective phospho-protein and β-actin, bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to untreated control. Data represent means of 3 independent experiments. * p
Figure Legend Snippet: Effects of Raf-1 kinase inhibition on PKC-induced Raf-1 ( a ), MLC 20 ( b ), MYPT1 ( c ), MEK ( d ) and ERK ( e ) phosphorylation in rat VSMCs. Cultured cells were pretreated with vehicle or GW5074 (10 μ M ) or U0126 (10 μ M ) or calphostin C (100 n M ) for 30 min before stimulated with 3 μ M PDBu for 15 min. Treated cells were processed as described in Methods. The phosphorylation levels of these proteins were determined by immunoblotting. Top panels show representative blots of the respective phospho-protein and β-actin, bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to untreated control. Data represent means of 3 independent experiments. * p

Techniques Used: Inhibition, Cell Culture

Effect of Raf-1 kinase inhibition on PE-induced increases in [Ca 2+ ] i . Fura-2-loaded cultured VSMCs were pretreated with vehicle ( a ) or GW5074 (10 μ M ) ( b ) for 30 min and then PE-induced increase in [Ca 2+ ] i was recorded in HBSS. c Effect of GW5074 when added at the plateau of PE-induced increase in [Ca 2+ ] i . d Average peak F340/380 values for PE in absence and presence of GW5074. Data are expressed as F340/380 ratio after background correction, and each point represents mean ± SE of 10–15 cells. Tracings are representatives and values are mean ± SE from 3 separate experiments.
Figure Legend Snippet: Effect of Raf-1 kinase inhibition on PE-induced increases in [Ca 2+ ] i . Fura-2-loaded cultured VSMCs were pretreated with vehicle ( a ) or GW5074 (10 μ M ) ( b ) for 30 min and then PE-induced increase in [Ca 2+ ] i was recorded in HBSS. c Effect of GW5074 when added at the plateau of PE-induced increase in [Ca 2+ ] i . d Average peak F340/380 values for PE in absence and presence of GW5074. Data are expressed as F340/380 ratio after background correction, and each point represents mean ± SE of 10–15 cells. Tracings are representatives and values are mean ± SE from 3 separate experiments.

Techniques Used: Inhibition, Cell Culture

2) Product Images from "Phosphodiesterase-8A binds to and regulates Raf-1 kinase"

Article Title: Phosphodiesterase-8A binds to and regulates Raf-1 kinase

Journal: Proceedings of the National Academy of Sciences of the United States of America

doi: 10.1073/pnas.1303004110

Manipulation of the PDE8–Raf-1 complex alters the strength of basal and EGF-stimulated phospho-ERK signals. ( A ) Treatment of HEK293 cells with the disruptor peptide (Dis) significantly down-regulated basal phospho-ERK Map kinase levels compared
Figure Legend Snippet: Manipulation of the PDE8–Raf-1 complex alters the strength of basal and EGF-stimulated phospho-ERK signals. ( A ) Treatment of HEK293 cells with the disruptor peptide (Dis) significantly down-regulated basal phospho-ERK Map kinase levels compared

Techniques Used:

Dissociation of the PDE8A–Raf-1 complex by site-directed mutagenesis and peptide disruption. ( A ) Mutation of PDE8A1 residues 460 E 461 Y to alanines attenuated the interaction between PDE8A and Raf-1 as measured by coimmunoprecipitation. ( B ) Quadruple
Figure Legend Snippet: Dissociation of the PDE8A–Raf-1 complex by site-directed mutagenesis and peptide disruption. ( A ) Mutation of PDE8A1 residues 460 E 461 Y to alanines attenuated the interaction between PDE8A and Raf-1 as measured by coimmunoprecipitation. ( B ) Quadruple

Techniques Used: Mutagenesis

Disruption of the PDE8–Raf-1 complex alters functional responses to EGF and stress signals. ( A ) The EGF-induced change of cell shape in HeLa cells measured by real-time impedance measurement is dose dependent. ( B ) The PDE8–Raf-1 disruptor
Figure Legend Snippet: Disruption of the PDE8–Raf-1 complex alters functional responses to EGF and stress signals. ( A ) The EGF-induced change of cell shape in HeLa cells measured by real-time impedance measurement is dose dependent. ( B ) The PDE8–Raf-1 disruptor

Techniques Used: Functional Assay

PDE8 activity regulates phosphorylation of Raf-1 at serine 259. ( A ) HEK293 cells were transfected with Flag-PDE8A1 (lanes 2, 4, and 5) or dominant-negative PDE8A1 (lanes 7 and 8) and/or were treated with dipyridamole (DiP, lanes 5 and 6) or forskolin
Figure Legend Snippet: PDE8 activity regulates phosphorylation of Raf-1 at serine 259. ( A ) HEK293 cells were transfected with Flag-PDE8A1 (lanes 2, 4, and 5) or dominant-negative PDE8A1 (lanes 7 and 8) and/or were treated with dipyridamole (DiP, lanes 5 and 6) or forskolin

Techniques Used: Activity Assay, Transfection, Dominant Negative Mutation

PDE8 and Raf-1 form a constitutively assembled complex. ( A ) Immunoprecipitations (IP) of Raf-1 or control IgG from HeLa cells were analyzed for associated PDE activity. Raf-1 Immunoprecipitations contained PDE activity that was inhibited by 100 µM
Figure Legend Snippet: PDE8 and Raf-1 form a constitutively assembled complex. ( A ) Immunoprecipitations (IP) of Raf-1 or control IgG from HeLa cells were analyzed for associated PDE activity. Raf-1 Immunoprecipitations contained PDE activity that was inhibited by 100 µM

Techniques Used: Activity Assay

Mapping of the Raf-1 binding site on PDE8A. ( A ) A peptide array of human PDE8A consisting of 25mer peptides overlapping by five amino acids that encompassed the entire PDE8A sequence was overlaid with either GST or GST–Raf-1. Positive interactions
Figure Legend Snippet: Mapping of the Raf-1 binding site on PDE8A. ( A ) A peptide array of human PDE8A consisting of 25mer peptides overlapping by five amino acids that encompassed the entire PDE8A sequence was overlaid with either GST or GST–Raf-1. Positive interactions

Techniques Used: Binding Assay, Peptide Microarray, Sequencing

PDE8A binds to Raf-1 with high affinity. ( A ). ( B ) GST–Raf-1 was coupled to a Biacore chip using
Figure Legend Snippet: PDE8A binds to Raf-1 with high affinity. ( A ). ( B ) GST–Raf-1 was coupled to a Biacore chip using

Techniques Used: Chromatin Immunoprecipitation

3) Product Images from "Striatal microRNA controls cocaine intake through CREB signaling"

Article Title: Striatal microRNA controls cocaine intake through CREB signaling

Journal: Nature

doi: 10.1038/nature09202

miR-212 amplifies CREB signaling through Raf-1 a , miR-212 activates Raf-1 signaling, reflected in increased levels of phosphorylated endogenous and exogenous (Raf-1-GFP) Raf-1 protein. b, Dominant-negative Raf-1 (DN-Raf-1) abolished the stimulatory effects of miR-212 on cAMP accumulation. c, DN-Raf-1abolished miR-212-induced increases in p-CREB. d, DN-Raf-1 also abolished miR-212-induced increases in TORC2. e, Enhancing Raf-1 signaling by pulsing cells with the Raf-1 inhibitor GW5074 potentiated cAMP accumulation. f, Potentiation of Raf-1 signaling increased p-CREB levels. g, Potentiation of Raf-1 signaling increased TORC2 levels. h, Knockdown of the Raf-1 repressor SPRED1, a target for miR-212, increased p-CREB levels. i, SPRED1 knockdown also increased TORC2 levels. Data are presented as mean ± SEM.
Figure Legend Snippet: miR-212 amplifies CREB signaling through Raf-1 a , miR-212 activates Raf-1 signaling, reflected in increased levels of phosphorylated endogenous and exogenous (Raf-1-GFP) Raf-1 protein. b, Dominant-negative Raf-1 (DN-Raf-1) abolished the stimulatory effects of miR-212 on cAMP accumulation. c, DN-Raf-1abolished miR-212-induced increases in p-CREB. d, DN-Raf-1 also abolished miR-212-induced increases in TORC2. e, Enhancing Raf-1 signaling by pulsing cells with the Raf-1 inhibitor GW5074 potentiated cAMP accumulation. f, Potentiation of Raf-1 signaling increased p-CREB levels. g, Potentiation of Raf-1 signaling increased TORC2 levels. h, Knockdown of the Raf-1 repressor SPRED1, a target for miR-212, increased p-CREB levels. i, SPRED1 knockdown also increased TORC2 levels. Data are presented as mean ± SEM.

Techniques Used: Dominant Negative Mutation

4) Product Images from "IL-6 Increases MMP-13 Expression and Motility in Human Chondrosarcoma Cells *"

Article Title: IL-6 Increases MMP-13 Expression and Motility in Human Chondrosarcoma Cells *

Journal: The Journal of Biological Chemistry

doi: 10.1074/jbc.M110.204081

Involvement of Ras and Raf-1 signaling pathways in response to IL-6 in chondrosarcoma cells. A , cells were pretreated with manumycin A (3 μ m ) and GW5074 (3 μ m ) for 30 min followed by stimulation with IL-6 for 24 h, and in vitro migration
Figure Legend Snippet: Involvement of Ras and Raf-1 signaling pathways in response to IL-6 in chondrosarcoma cells. A , cells were pretreated with manumycin A (3 μ m ) and GW5074 (3 μ m ) for 30 min followed by stimulation with IL-6 for 24 h, and in vitro migration

Techniques Used: In Vitro, Migration

5) Product Images from "Induction of differentiation of human leukemia cells by combinations of COX inhibitors and 1,25-dihydroxyvitamin D3 involves Raf1 but not Erk 1/2 signaling"

Article Title: Induction of differentiation of human leukemia cells by combinations of COX inhibitors and 1,25-dihydroxyvitamin D3 involves Raf1 but not Erk 1/2 signaling

Journal: Cell cycle (Georgetown, Tex.)

doi: 10.4161/cc.7.7.5620

Effects of si Raf-1 on ERK1/2 activation by COX inhibitor/1,25D treatments of U937 cells. (A) ASA +/- 1,25D reduces the levels of activated Raf-1 (P-Raf1) and p90RSK1 (P-RSK1), but increases the levels of P-ERK1/2, and to lesser extent of P-MEK1. The first lane shows cells not treated or transfected, lanes 2 and 3 cells transfected with scrambled (SC), non-specific, siRNA. (B) INDO +/- 1,25D exposure also increases P-ERK levels. For further details see Materials and Methods.
Figure Legend Snippet: Effects of si Raf-1 on ERK1/2 activation by COX inhibitor/1,25D treatments of U937 cells. (A) ASA +/- 1,25D reduces the levels of activated Raf-1 (P-Raf1) and p90RSK1 (P-RSK1), but increases the levels of P-ERK1/2, and to lesser extent of P-MEK1. The first lane shows cells not treated or transfected, lanes 2 and 3 cells transfected with scrambled (SC), non-specific, siRNA. (B) INDO +/- 1,25D exposure also increases P-ERK levels. For further details see Materials and Methods.

Techniques Used: Activation Assay, Transfection

6) Product Images from "A new bisphosphonate derivative, CP, induces gastric cancer cell apoptosis via activation of the ERK1/2 signaling pathway"

Article Title: A new bisphosphonate derivative, CP, induces gastric cancer cell apoptosis via activation of the ERK1/2 signaling pathway

Journal: Acta Pharmacologica Sinica

doi: 10.1038/aps.2013.103

CP stimulates MAP kinase activation. After treatment with 40 μmol/L of CP or vehicle (0.16% NaHCO 3 ), SGC-7901 cells were harvested at the indicated times. Protein expression of (A) ERK1/2 and phospho-ERK1/2, (B) p38 and JNK, and (C) MEK1/2 and Raf-1 was determined by Western blot analysis. β-Actin was used as a control to determine equal protein loading for each sample. The data are representative of three independent experiments.
Figure Legend Snippet: CP stimulates MAP kinase activation. After treatment with 40 μmol/L of CP or vehicle (0.16% NaHCO 3 ), SGC-7901 cells were harvested at the indicated times. Protein expression of (A) ERK1/2 and phospho-ERK1/2, (B) p38 and JNK, and (C) MEK1/2 and Raf-1 was determined by Western blot analysis. β-Actin was used as a control to determine equal protein loading for each sample. The data are representative of three independent experiments.

Techniques Used: Activation Assay, Expressing, Western Blot

7) Product Images from "A novel radioresistant mechanism of galectin-1 mediated by H-Ras-dependent pathways in cervical cancer cells"

Article Title: A novel radioresistant mechanism of galectin-1 mediated by H-Ras-dependent pathways in cervical cancer cells

Journal: Cell Death & Disease

doi: 10.1038/cddis.2011.120

Effects of galectin-1 on the Ras-transmitted downstream signals. Scrambled RNA or galectin-1 shRNA were transfected in HeLa cells. GFP or galectin-1 cDNA were transfected in C33A cells. The cells were irradiated with 6 Gy and harvested 5 or 10 min later. Expressions of activated H-Ras, p-Raf-1, and p-ERK using western blots in HeLa and C33A cells were compared with or without galectin-1 modulation
Figure Legend Snippet: Effects of galectin-1 on the Ras-transmitted downstream signals. Scrambled RNA or galectin-1 shRNA were transfected in HeLa cells. GFP or galectin-1 cDNA were transfected in C33A cells. The cells were irradiated with 6 Gy and harvested 5 or 10 min later. Expressions of activated H-Ras, p-Raf-1, and p-ERK using western blots in HeLa and C33A cells were compared with or without galectin-1 modulation

Techniques Used: shRNA, Transfection, Irradiation, Western Blot

A proposed model of cooperation between H-Ras and galectin-1 for radioresistance. Galectin-1 enhances activation (GTP form) of H-Ras following irradiation. Galectin-1 potentiates downstream signals of H-Ras, such as Raf-1 and ERK, that may mediate DNA damage repair 33 and radioresistance. 31 , 32 Galectin-1 may regulate p21 expression 36 through Raf-1. 34 Hence, Raf-1 may have a significant role in galectin-1-mediated radioresistance
Figure Legend Snippet: A proposed model of cooperation between H-Ras and galectin-1 for radioresistance. Galectin-1 enhances activation (GTP form) of H-Ras following irradiation. Galectin-1 potentiates downstream signals of H-Ras, such as Raf-1 and ERK, that may mediate DNA damage repair 33 and radioresistance. 31 , 32 Galectin-1 may regulate p21 expression 36 through Raf-1. 34 Hence, Raf-1 may have a significant role in galectin-1-mediated radioresistance

Techniques Used: Activation Assay, Irradiation, Expressing

Related Articles

Incubation:

Article Title: Raf-1 Kinase Regulates Smooth Muscle Contraction in the Rat Mesenteric Arteries
Article Snippet: .. Membranes were blocked in a PBS solution containing 5% dry milk for 2 h before an overnight incubation in a Tris-buffered saline solution containing 5% milk and probed with phospho-Raf-1 (1:1,000 dilution; Cell Signaling, Danvers, Mass., USA), phospho-MEK (1:2,000 dilution; Cell Signaling), phospho-ERK (1:1,000 dilution; Cell Signaling), phospho-MLC20 (1:4,000 dilution; Sigma), phospho-myosin phosphatase target, MYPT1Thr696 antibody (1:2,000; Upstate, Lake Placid, N.Y., USA). .. Membranes were washed using Tris-buffered saline containing 1% milk and then incubated with horseradish peroxidase-conjugated secondary antibody (dilution 1:2,000; Cell Signaling) for 1 h. Immunoreactive bands were visualized by enhanced chemiluminescence (Pierce Biotechnology, Rockford, Ill., USA).

other:

Article Title: Induction of differentiation of human leukemia cells by combinations of COX inhibitors and 1,25-dihydroxyvitamin D3 involves Raf1 but not Erk 1/2 signaling
Article Snippet: Phospho-Raf-1 (Ser 338), phospho-MEK1 (Ser217/221), Phospho-p44/42 MAPK (Thr202/Tyr204), and Phospho-p90RSK (Ser380) antibodies were purchased from Cell Signaling (Beverly, MA).

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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, 2020-07
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    Cell Signaling Technology Inc phospho raf 1
    Effects of <t>Raf-1</t> kinase inhibition on PE-induced MLC 20 ( a ) and MYPT1 ( b ) phosphorylation in rat VSMCs. Left and right panels show concentration- and time-dependent effects of PE, respectively. Cultured cells were pretreated with vehicle or GW5074 (10 μ M ) for 30 min before stimulated with 10 μ M PE. Treated cells were processed as described in Methods. The phosphorylation levels of MLC 20 or MYPT1 were determined by immunoblotting. Top panels show representative blots of phospho-MLC 20 or phospho-MYPT1 and β-actin, bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to control. Data represent means of 3–5 independent experiments. * p
    Phospho Raf 1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 88/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho raf 1/product/Cell Signaling Technology Inc
    Average 88 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    phospho raf 1 - by Bioz Stars, 2020-07
    88/100 stars
      Buy from Supplier

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    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

    Effects of Raf-1 kinase inhibition on PE-induced MLC 20 ( a ) and MYPT1 ( b ) phosphorylation in rat VSMCs. Left and right panels show concentration- and time-dependent effects of PE, respectively. Cultured cells were pretreated with vehicle or GW5074 (10 μ M ) for 30 min before stimulated with 10 μ M PE. Treated cells were processed as described in Methods. The phosphorylation levels of MLC 20 or MYPT1 were determined by immunoblotting. Top panels show representative blots of phospho-MLC 20 or phospho-MYPT1 and β-actin, bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to control. Data represent means of 3–5 independent experiments. * p

    Journal: Journal of Vascular Research

    Article Title: Raf-1 Kinase Regulates Smooth Muscle Contraction in the Rat Mesenteric Arteries

    doi: 10.1159/000277726

    Figure Lengend Snippet: Effects of Raf-1 kinase inhibition on PE-induced MLC 20 ( a ) and MYPT1 ( b ) phosphorylation in rat VSMCs. Left and right panels show concentration- and time-dependent effects of PE, respectively. Cultured cells were pretreated with vehicle or GW5074 (10 μ M ) for 30 min before stimulated with 10 μ M PE. Treated cells were processed as described in Methods. The phosphorylation levels of MLC 20 or MYPT1 were determined by immunoblotting. Top panels show representative blots of phospho-MLC 20 or phospho-MYPT1 and β-actin, bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to control. Data represent means of 3–5 independent experiments. * p

    Article Snippet: Membranes were blocked in a PBS solution containing 5% dry milk for 2 h before an overnight incubation in a Tris-buffered saline solution containing 5% milk and probed with phospho-Raf-1 (1:1,000 dilution; Cell Signaling, Danvers, Mass., USA), phospho-MEK (1:2,000 dilution; Cell Signaling), phospho-ERK (1:1,000 dilution; Cell Signaling), phospho-MLC20 (1:4,000 dilution; Sigma), phospho-myosin phosphatase target, MYPT1Thr696 antibody (1:2,000; Upstate, Lake Placid, N.Y., USA).

    Techniques: Inhibition, Concentration Assay, Cell Culture

    Reversal of PE-induced contraction by Raf-1 kinase inhibitors in rat mesenteric arteries (semi-log plot). Submaximal PE contraction was elicited, increasing concentrations of Raf-1 kinase inhibitors, GW5074, L779450 and ZM33637, were added, and then the percentage of relaxation to PE contraction was measured. Data points represent mean ± SEM of measurements in 10–12 mesenteric arterial rings from 5–6 rats.

    Journal: Journal of Vascular Research

    Article Title: Raf-1 Kinase Regulates Smooth Muscle Contraction in the Rat Mesenteric Arteries

    doi: 10.1159/000277726

    Figure Lengend Snippet: Reversal of PE-induced contraction by Raf-1 kinase inhibitors in rat mesenteric arteries (semi-log plot). Submaximal PE contraction was elicited, increasing concentrations of Raf-1 kinase inhibitors, GW5074, L779450 and ZM33637, were added, and then the percentage of relaxation to PE contraction was measured. Data points represent mean ± SEM of measurements in 10–12 mesenteric arterial rings from 5–6 rats.

    Article Snippet: Membranes were blocked in a PBS solution containing 5% dry milk for 2 h before an overnight incubation in a Tris-buffered saline solution containing 5% milk and probed with phospho-Raf-1 (1:1,000 dilution; Cell Signaling, Danvers, Mass., USA), phospho-MEK (1:2,000 dilution; Cell Signaling), phospho-ERK (1:1,000 dilution; Cell Signaling), phospho-MLC20 (1:4,000 dilution; Sigma), phospho-myosin phosphatase target, MYPT1Thr696 antibody (1:2,000; Upstate, Lake Placid, N.Y., USA).

    Techniques:

    a Basal MAP in rats in the absence and presence of GW5074 (250 μg/kg). b Effect of Raf-1 kinase inhibition on PE-induced increase in mean arterial pressure in rats. Dose-response curve for PE evoked increase in blood pressure in the absence and presence of GW5074 (semi-log plot). Rats were pretreated with GW5074 (250 μg/kg; i.v.) or vehicle for 15 min and then increasing concentration of PE was infused (10–300 μg/kg/min). Each dose of PE was infused for a 3-min period and the MAP was determined as the mean value recorded within the last minute of infusion. Hypertensive responses were calculated as percent increase in MAP with respect to the baseline MAP. Values are expressed as mean ± SEM of 5–6 animals.

    Journal: Journal of Vascular Research

    Article Title: Raf-1 Kinase Regulates Smooth Muscle Contraction in the Rat Mesenteric Arteries

    doi: 10.1159/000277726

    Figure Lengend Snippet: a Basal MAP in rats in the absence and presence of GW5074 (250 μg/kg). b Effect of Raf-1 kinase inhibition on PE-induced increase in mean arterial pressure in rats. Dose-response curve for PE evoked increase in blood pressure in the absence and presence of GW5074 (semi-log plot). Rats were pretreated with GW5074 (250 μg/kg; i.v.) or vehicle for 15 min and then increasing concentration of PE was infused (10–300 μg/kg/min). Each dose of PE was infused for a 3-min period and the MAP was determined as the mean value recorded within the last minute of infusion. Hypertensive responses were calculated as percent increase in MAP with respect to the baseline MAP. Values are expressed as mean ± SEM of 5–6 animals.

    Article Snippet: Membranes were blocked in a PBS solution containing 5% dry milk for 2 h before an overnight incubation in a Tris-buffered saline solution containing 5% milk and probed with phospho-Raf-1 (1:1,000 dilution; Cell Signaling, Danvers, Mass., USA), phospho-MEK (1:2,000 dilution; Cell Signaling), phospho-ERK (1:1,000 dilution; Cell Signaling), phospho-MLC20 (1:4,000 dilution; Sigma), phospho-myosin phosphatase target, MYPT1Thr696 antibody (1:2,000; Upstate, Lake Placid, N.Y., USA).

    Techniques: Inhibition, Concentration Assay

    Dose and time course of PE-stimulated phosphorylation of Raf-1 ( a ), MEK ( b ) and ERK ( c ). Left and right panels show concentration- and time-dependent effects of PE, respectively. Cultured VSMCs were treated with varying concentration of PE for 5 min. For time course studies cells pretreated with GW5074 (10 μ M ) or vehicle for 30 min before stimulated with PE (10 μ M ) for indicated time periods. Treated cells were processed as described in Methods. The phosphorylation levels of Raf-1, MEK and ERK were determined by immunoblotting. Top panels show representative blots of respective phosphorylated proteins and β-actin; bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to control. Data represent mean of 4–5 independent experiments. * p

    Journal: Journal of Vascular Research

    Article Title: Raf-1 Kinase Regulates Smooth Muscle Contraction in the Rat Mesenteric Arteries

    doi: 10.1159/000277726

    Figure Lengend Snippet: Dose and time course of PE-stimulated phosphorylation of Raf-1 ( a ), MEK ( b ) and ERK ( c ). Left and right panels show concentration- and time-dependent effects of PE, respectively. Cultured VSMCs were treated with varying concentration of PE for 5 min. For time course studies cells pretreated with GW5074 (10 μ M ) or vehicle for 30 min before stimulated with PE (10 μ M ) for indicated time periods. Treated cells were processed as described in Methods. The phosphorylation levels of Raf-1, MEK and ERK were determined by immunoblotting. Top panels show representative blots of respective phosphorylated proteins and β-actin; bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to control. Data represent mean of 4–5 independent experiments. * p

    Article Snippet: Membranes were blocked in a PBS solution containing 5% dry milk for 2 h before an overnight incubation in a Tris-buffered saline solution containing 5% milk and probed with phospho-Raf-1 (1:1,000 dilution; Cell Signaling, Danvers, Mass., USA), phospho-MEK (1:2,000 dilution; Cell Signaling), phospho-ERK (1:1,000 dilution; Cell Signaling), phospho-MLC20 (1:4,000 dilution; Sigma), phospho-myosin phosphatase target, MYPT1Thr696 antibody (1:2,000; Upstate, Lake Placid, N.Y., USA).

    Techniques: Concentration Assay, Cell Culture

    Effects of Raf-1 kinase inhibition on PKC-induced Raf-1 ( a ), MLC 20 ( b ), MYPT1 ( c ), MEK ( d ) and ERK ( e ) phosphorylation in rat VSMCs. Cultured cells were pretreated with vehicle or GW5074 (10 μ M ) or U0126 (10 μ M ) or calphostin C (100 n M ) for 30 min before stimulated with 3 μ M PDBu for 15 min. Treated cells were processed as described in Methods. The phosphorylation levels of these proteins were determined by immunoblotting. Top panels show representative blots of the respective phospho-protein and β-actin, bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to untreated control. Data represent means of 3 independent experiments. * p

    Journal: Journal of Vascular Research

    Article Title: Raf-1 Kinase Regulates Smooth Muscle Contraction in the Rat Mesenteric Arteries

    doi: 10.1159/000277726

    Figure Lengend Snippet: Effects of Raf-1 kinase inhibition on PKC-induced Raf-1 ( a ), MLC 20 ( b ), MYPT1 ( c ), MEK ( d ) and ERK ( e ) phosphorylation in rat VSMCs. Cultured cells were pretreated with vehicle or GW5074 (10 μ M ) or U0126 (10 μ M ) or calphostin C (100 n M ) for 30 min before stimulated with 3 μ M PDBu for 15 min. Treated cells were processed as described in Methods. The phosphorylation levels of these proteins were determined by immunoblotting. Top panels show representative blots of the respective phospho-protein and β-actin, bottom panels are the summary of densitometric results. Results were normalized against β-actin and expressed as folds change relative to untreated control. Data represent means of 3 independent experiments. * p

    Article Snippet: Membranes were blocked in a PBS solution containing 5% dry milk for 2 h before an overnight incubation in a Tris-buffered saline solution containing 5% milk and probed with phospho-Raf-1 (1:1,000 dilution; Cell Signaling, Danvers, Mass., USA), phospho-MEK (1:2,000 dilution; Cell Signaling), phospho-ERK (1:1,000 dilution; Cell Signaling), phospho-MLC20 (1:4,000 dilution; Sigma), phospho-myosin phosphatase target, MYPT1Thr696 antibody (1:2,000; Upstate, Lake Placid, N.Y., USA).

    Techniques: Inhibition, Cell Culture

    Effect of Raf-1 kinase inhibition on PE-induced increases in [Ca 2+ ] i . Fura-2-loaded cultured VSMCs were pretreated with vehicle ( a ) or GW5074 (10 μ M ) ( b ) for 30 min and then PE-induced increase in [Ca 2+ ] i was recorded in HBSS. c Effect of GW5074 when added at the plateau of PE-induced increase in [Ca 2+ ] i . d Average peak F340/380 values for PE in absence and presence of GW5074. Data are expressed as F340/380 ratio after background correction, and each point represents mean ± SE of 10–15 cells. Tracings are representatives and values are mean ± SE from 3 separate experiments.

    Journal: Journal of Vascular Research

    Article Title: Raf-1 Kinase Regulates Smooth Muscle Contraction in the Rat Mesenteric Arteries

    doi: 10.1159/000277726

    Figure Lengend Snippet: Effect of Raf-1 kinase inhibition on PE-induced increases in [Ca 2+ ] i . Fura-2-loaded cultured VSMCs were pretreated with vehicle ( a ) or GW5074 (10 μ M ) ( b ) for 30 min and then PE-induced increase in [Ca 2+ ] i was recorded in HBSS. c Effect of GW5074 when added at the plateau of PE-induced increase in [Ca 2+ ] i . d Average peak F340/380 values for PE in absence and presence of GW5074. Data are expressed as F340/380 ratio after background correction, and each point represents mean ± SE of 10–15 cells. Tracings are representatives and values are mean ± SE from 3 separate experiments.

    Article Snippet: Membranes were blocked in a PBS solution containing 5% dry milk for 2 h before an overnight incubation in a Tris-buffered saline solution containing 5% milk and probed with phospho-Raf-1 (1:1,000 dilution; Cell Signaling, Danvers, Mass., USA), phospho-MEK (1:2,000 dilution; Cell Signaling), phospho-ERK (1:1,000 dilution; Cell Signaling), phospho-MLC20 (1:4,000 dilution; Sigma), phospho-myosin phosphatase target, MYPT1Thr696 antibody (1:2,000; Upstate, Lake Placid, N.Y., USA).

    Techniques: Inhibition, Cell Culture

    DC Cytokine Inhibition by Salp15 Is Raf-1-Dependent (A) Salp15 induces phosphorylation of Raf-1. DCs were pretreated with medium or with blocking anti-DC-SIGN antibodies (AZN-D2) before addition of 25 μg/ml Salp15. Intracellular phosphorylation of Raf-1 was measured by flow cytometry using rabbit anti-phospho-c-Raf (Ser338) mAb and rabbit anti-c-Raf (Tyr341) pAb. (B) Raf-1 was specifically silenced by siRNA. DCs were transfected with 100 nM siRNA (Raf-1 or non-targeting siRNA as a control). Raf-1 and B-Raf mRNA was quantified by real-time PCR using gene-specific primers. Relative mRNA expression was corrected for GAPDH expression. (C) RNAi-mediated silencing of Raf-1 abrogates Salp15-mediated cytokine inhibition. siRNA-treated cells were stimulated for 6 h with LPS in the presence or absence of 25 μg/ml Salp15. Cytokine gene expression was measured by real time PCR and corrected for GAPDH expression. Relative mRNA expression of LPS-stimulated non-targeting siRNA-treated cells was set at 1. (D) Raf-1 inhibition by GW5704 abrogates Salp15-mediated cytokine inhibition. DCs were incubated with 1 μM GW5704, or DMSO as a negative control, for 2 h before stimulation with LPS for 6 h (mRNA) or 18 h (protein) in the presence or absence of 25 μg/ml Salp15. Cytokine gene expression was measured by real time PCR and corrected for GAPDH expression. Relative mRNA expression of LPS-stimulated cells was set at 1. For protein levels, LPS was set at 100%, which is representative of 133 ± 17 pg/ml IL-12p70; 9,188 ± 850 pg/ml TNF-α, and 1,563 ± 800 pg/ml IL-6. GW5704 alone did not induce cytokine production (unpublished data). (E) MEK1/2-inhibitor U0126 blocks Salp15-mediated cytokine inhibition. DCs were pre-incubated for 2 h with anacardic acid (AA), an inhibitor of the histone acetyltransferases p300 and CBP, U0126, an inhibitor of MEK1 and MEK2, or DMSO as a negative control. Cells were stimulated as described in (C) and cytokine gene expression was measured by real time PCR and corrected for GAPDH expression. Relative mRNA expression of LPS-stimulated cells was set at 1. (F and G) Salp15 does not induce phosphorylation of ERK. DCs were stimulated for 0 to 45 min with Salp15 (25 μg /ml), LPS, or PMA/Ionomycin as a positive control. Phosphorylation of ERK was determined by flow cytometry using a rabbit anti-phospho-p44/42 MAPK (Thr202/Tyr402) mAb. Bars represent the mean of at least three independent experiments ± SE. For (C) mRNA expression levels in non-target siRNA-treated DCs activated with LPS + Salp15 were compared to Raf-1 siRNA-treated DCs activated with LPS + Salp15. In (D) and (E) levels in DCs treated with LPS + Salp15 were compared to levels in DCs treated with LPS + Salp15 in the presence of the indicated inhibitor. A two-sided unpaired Student t -test was applied and a p -value

    Journal: PLoS Pathogens

    Article Title: Salp15 Binding to DC-SIGN Inhibits Cytokine Expression by Impairing both Nucleosome Remodeling and mRNA Stabilization

    doi: 10.1371/journal.ppat.0040031

    Figure Lengend Snippet: DC Cytokine Inhibition by Salp15 Is Raf-1-Dependent (A) Salp15 induces phosphorylation of Raf-1. DCs were pretreated with medium or with blocking anti-DC-SIGN antibodies (AZN-D2) before addition of 25 μg/ml Salp15. Intracellular phosphorylation of Raf-1 was measured by flow cytometry using rabbit anti-phospho-c-Raf (Ser338) mAb and rabbit anti-c-Raf (Tyr341) pAb. (B) Raf-1 was specifically silenced by siRNA. DCs were transfected with 100 nM siRNA (Raf-1 or non-targeting siRNA as a control). Raf-1 and B-Raf mRNA was quantified by real-time PCR using gene-specific primers. Relative mRNA expression was corrected for GAPDH expression. (C) RNAi-mediated silencing of Raf-1 abrogates Salp15-mediated cytokine inhibition. siRNA-treated cells were stimulated for 6 h with LPS in the presence or absence of 25 μg/ml Salp15. Cytokine gene expression was measured by real time PCR and corrected for GAPDH expression. Relative mRNA expression of LPS-stimulated non-targeting siRNA-treated cells was set at 1. (D) Raf-1 inhibition by GW5704 abrogates Salp15-mediated cytokine inhibition. DCs were incubated with 1 μM GW5704, or DMSO as a negative control, for 2 h before stimulation with LPS for 6 h (mRNA) or 18 h (protein) in the presence or absence of 25 μg/ml Salp15. Cytokine gene expression was measured by real time PCR and corrected for GAPDH expression. Relative mRNA expression of LPS-stimulated cells was set at 1. For protein levels, LPS was set at 100%, which is representative of 133 ± 17 pg/ml IL-12p70; 9,188 ± 850 pg/ml TNF-α, and 1,563 ± 800 pg/ml IL-6. GW5704 alone did not induce cytokine production (unpublished data). (E) MEK1/2-inhibitor U0126 blocks Salp15-mediated cytokine inhibition. DCs were pre-incubated for 2 h with anacardic acid (AA), an inhibitor of the histone acetyltransferases p300 and CBP, U0126, an inhibitor of MEK1 and MEK2, or DMSO as a negative control. Cells were stimulated as described in (C) and cytokine gene expression was measured by real time PCR and corrected for GAPDH expression. Relative mRNA expression of LPS-stimulated cells was set at 1. (F and G) Salp15 does not induce phosphorylation of ERK. DCs were stimulated for 0 to 45 min with Salp15 (25 μg /ml), LPS, or PMA/Ionomycin as a positive control. Phosphorylation of ERK was determined by flow cytometry using a rabbit anti-phospho-p44/42 MAPK (Thr202/Tyr402) mAb. Bars represent the mean of at least three independent experiments ± SE. For (C) mRNA expression levels in non-target siRNA-treated DCs activated with LPS + Salp15 were compared to Raf-1 siRNA-treated DCs activated with LPS + Salp15. In (D) and (E) levels in DCs treated with LPS + Salp15 were compared to levels in DCs treated with LPS + Salp15 in the presence of the indicated inhibitor. A two-sided unpaired Student t -test was applied and a p -value

    Article Snippet: Subsequently, cells were fixed in 3% para-formaldehyde for 10 min and permeabilized in 90% methanol at 4 °C for 10 (Raf-1) or 30 (ERK) min. To assess phosphorylation of Raf-1 we used a rabbit anti-phospho-c-Raf (Ser338) mAb (Cell Signaling) and a rabbit anti-c-Raf (pTyr340, Tyr341) pAb (Calbiochem) and to assess phosphorylation of ERK a rabbit-anti-phospho-p44/42 MAPK (Thr202/Tyr204) mAb (Cell Signaling).

    Techniques: Inhibition, Blocking Assay, Flow Cytometry, Cytometry, Transfection, Real-time Polymerase Chain Reaction, Expressing, Incubation, Negative Control, Positive Control

    B-Raf/Raf-1 heterodimerization in QTRRE cells

    Journal: Molecular carcinogenesis

    Article Title: Transcriptional and Post-translational Modifications of B-Raf in Quinol-Thioether Induced Tuberous Sclerosis Renal Cell Carcinoma

    doi: 10.1002/mc.22366

    Figure Lengend Snippet: B-Raf/Raf-1 heterodimerization in QTRRE cells

    Article Snippet: Phosphorylation of Raf-1 within its activation domain facilitates 14-3-3 binding and subsequent activation by B-Raf [ , ].

    Techniques: