sapk jnk antibody Cell Signaling Technology Inc Search Results


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  • 90
    Cell Signaling Technology Inc sapk jnk antibody
    NK-4 attenuated H 2 O 2 -induced <t>SAPK/JNK</t> phosphorylation in PC12 cells. PC12 cells were treated with 400 µM H 2 O 2 in the presence of the indicated concentrations of NK-4 for 2 hr. Whole cell lysates were analyzed by Western blotting using anti-phospho-SAPK/JNK antibody (upper panel), or anti-SAPK/JNK antibody (bottom panel). The graph shows the ratio of phosphorylated SAPK/JNK to total SAPK/JNK at each time point.
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    Cell Signaling Technology Inc stress activated protein kinase jnk
    Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. <t>ERK,</t> extracellular signal–regulated kinase; <t>JNK,</t> c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.
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    Cell Signaling Technology Inc anti sapk jnk1 2
    Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. <t>ERK,</t> extracellular signal–regulated kinase; <t>JNK,</t> c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.
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    Cell Signaling Technology Inc phosphorylated stress activated protein kinase
    Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. <t>ERK,</t> extracellular signal–regulated kinase; <t>JNK,</t> c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.
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    Cell Signaling Technology Inc stress activated protein kinase c jun n terminal kinase sapk jnk
    Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. <t>ERK,</t> extracellular signal–regulated kinase; <t>JNK,</t> c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.
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    Cell Signaling Technology Inc stress activated protein kinase
    Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. <t>ERK,</t> extracellular signal–regulated kinase; <t>JNK,</t> c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.
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    Cell Signaling Technology Inc phospho sapk jnk1 2
    Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. <t>ERK,</t> extracellular signal–regulated kinase; <t>JNK,</t> c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.
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    Cell Signaling Technology Inc mouse monoclonal mapk8 sapk jnk
    Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. <t>ERK,</t> extracellular signal–regulated kinase; <t>JNK,</t> c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.
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    Cell Signaling Technology Inc anti p jnk stress activated protein kinase sapk
    Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. <t>ERK,</t> extracellular signal–regulated kinase; <t>JNK,</t> c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.
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    Cell Signaling Technology Inc anti stress activated protein kinase
    Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. <t>ERK,</t> extracellular signal–regulated kinase; <t>JNK,</t> c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.
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    Cell Signaling Technology Inc anti total stress activated protein kinase c jun nh2 terminal kinase sapk jnk mapk antibody
    Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. <t>ERK,</t> extracellular signal–regulated kinase; <t>JNK,</t> c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.
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    Cell Signaling Technology Inc phospho jnk stress activated protein kinase thr183 tyr185
    Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. <t>ERK,</t> extracellular signal–regulated kinase; <t>JNK,</t> c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.
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    Cell Signaling Technology Inc rabbit polyclonal anti sapk jnk1 2 antibodies
    Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. <t>ERK,</t> extracellular signal–regulated kinase; <t>JNK,</t> c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.
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    Cell Signaling Technology Inc phospho jnk stress activated protein kinase
    ProNGF/p75 NTR signaling Top panel shows Western blot and densitometry measurements of dimeric forms of NGF (proNGF, 27kDA) in nasal (A) , bronchial (B) , and alveolar (C) epithelial cells exposed to 10 μg/ml of TiO 2 -NP for 24 hr. Middle panel (D) shows the interaction between proNGF and its p75 NTR receptor in bronchial epithelial cells exposed to TiO 2 -NP with the corresponding densitometry analysis. Lower panel (E) shows the Western blot analysis of downstream stress-associated protein kinase/Jun-amino-terminal kinase <t>(SAPK/JNK)</t> in bronchial epithelial cells. Blots were probed with phospho SAPK/JNK [Thr183/Tyr185] and re-probed with JNK antibody as an internal control. Densitometry data are expressed as percentage of non-exposed controls after normalizing with GAPDH for NGF or with total JNK for p-JNK in corresponding graphs. Data shown are the means ± SDs of 3 independent experiments. *p
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    Cell Signaling Technology Inc phospho sapk jnk antibody
    ProNGF/p75 NTR signaling Top panel shows Western blot and densitometry measurements of dimeric forms of NGF (proNGF, 27kDA) in nasal (A) , bronchial (B) , and alveolar (C) epithelial cells exposed to 10 μg/ml of TiO 2 -NP for 24 hr. Middle panel (D) shows the interaction between proNGF and its p75 NTR receptor in bronchial epithelial cells exposed to TiO 2 -NP with the corresponding densitometry analysis. Lower panel (E) shows the Western blot analysis of downstream stress-associated protein kinase/Jun-amino-terminal kinase <t>(SAPK/JNK)</t> in bronchial epithelial cells. Blots were probed with phospho SAPK/JNK [Thr183/Tyr185] and re-probed with JNK antibody as an internal control. Densitometry data are expressed as percentage of non-exposed controls after normalizing with GAPDH for NGF or with total JNK for p-JNK in corresponding graphs. Data shown are the means ± SDs of 3 independent experiments. *p
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    Cell Signaling Technology Inc primary antibodies against jnk stress activated protein kinase
    ProNGF/p75 NTR signaling Top panel shows Western blot and densitometry measurements of dimeric forms of NGF (proNGF, 27kDA) in nasal (A) , bronchial (B) , and alveolar (C) epithelial cells exposed to 10 μg/ml of TiO 2 -NP for 24 hr. Middle panel (D) shows the interaction between proNGF and its p75 NTR receptor in bronchial epithelial cells exposed to TiO 2 -NP with the corresponding densitometry analysis. Lower panel (E) shows the Western blot analysis of downstream stress-associated protein kinase/Jun-amino-terminal kinase <t>(SAPK/JNK)</t> in bronchial epithelial cells. Blots were probed with phospho SAPK/JNK [Thr183/Tyr185] and re-probed with JNK antibody as an internal control. Densitometry data are expressed as percentage of non-exposed controls after normalizing with GAPDH for NGF or with total JNK for p-JNK in corresponding graphs. Data shown are the means ± SDs of 3 independent experiments. *p
    Primary Antibodies Against Jnk Stress Activated Protein Kinase, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 84/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc rabbit sapk jnk1 2
    ProNGF/p75 NTR signaling Top panel shows Western blot and densitometry measurements of dimeric forms of NGF (proNGF, 27kDA) in nasal (A) , bronchial (B) , and alveolar (C) epithelial cells exposed to 10 μg/ml of TiO 2 -NP for 24 hr. Middle panel (D) shows the interaction between proNGF and its p75 NTR receptor in bronchial epithelial cells exposed to TiO 2 -NP with the corresponding densitometry analysis. Lower panel (E) shows the Western blot analysis of downstream stress-associated protein kinase/Jun-amino-terminal kinase <t>(SAPK/JNK)</t> in bronchial epithelial cells. Blots were probed with phospho SAPK/JNK [Thr183/Tyr185] and re-probed with JNK antibody as an internal control. Densitometry data are expressed as percentage of non-exposed controls after normalizing with GAPDH for NGF or with total JNK for p-JNK in corresponding graphs. Data shown are the means ± SDs of 3 independent experiments. *p
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    Cell Signaling Technology Inc jnk
    MLK4 cannot function as a MAP3K for ERK, <t>JNK</t> and <t>p38.</t> ( a ) 293T cells were transfected with an expressing vector of Flag-JNK1 with or without an expression vector of V5-MLK4β or HA-MKK7 for 24 h. The cell lysates were immunoblotted with antibodies as indicated. ( b ) 293T cells were transfected with an expressing vector of Flag-ERK2 with or without an expression vector of V5-MLK4β or HA-MEK1 for 24 h. The cell lysates were immunoblotted with antibodies as indicated. ( c ) 293T cells were transfected with an expressing vector of Flag-p38 with an expression vector of V5-MLK4β or its deletion mutants as indicated. V5-TAK1 was included as a positive control. The cell lysates were immunoblotted with antibodies as indicated. Data are representative of two independent experiments. ERK, extracellular signal-regulated kinase; IB, immunoblotting; IP, immunoprecipitation; JNK, c-Jun N-terminal kinase; MAP3K, mitogen-activated protein kinase kinase kinase; MLK, mixed-lineage kinase.
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    Cell Signaling Technology Inc phosphospecific sapk jnk
    MLK4 cannot function as a MAP3K for ERK, <t>JNK</t> and <t>p38.</t> ( a ) 293T cells were transfected with an expressing vector of Flag-JNK1 with or without an expression vector of V5-MLK4β or HA-MKK7 for 24 h. The cell lysates were immunoblotted with antibodies as indicated. ( b ) 293T cells were transfected with an expressing vector of Flag-ERK2 with or without an expression vector of V5-MLK4β or HA-MEK1 for 24 h. The cell lysates were immunoblotted with antibodies as indicated. ( c ) 293T cells were transfected with an expressing vector of Flag-p38 with an expression vector of V5-MLK4β or its deletion mutants as indicated. V5-TAK1 was included as a positive control. The cell lysates were immunoblotted with antibodies as indicated. Data are representative of two independent experiments. ERK, extracellular signal-regulated kinase; IB, immunoblotting; IP, immunoprecipitation; JNK, c-Jun N-terminal kinase; MAP3K, mitogen-activated protein kinase kinase kinase; MLK, mixed-lineage kinase.
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    Cell Signaling Technology Inc sapk jnk 56g8
    The MAPK signal transduction pathway is regulated by FUZHENGHUAYU Tablet. Protein levels of rat p44/42 MAP kinase (137F5), <t>SAPK/JNK</t> (56G8), p38 MAP kinase, phospho-p44/42 MAPK (Thr202/Tyr204), phospho-p38 MAPK (Thr180/Tyr182), and phospho-SAPK/JNK (Thr183/Tyr185) were detected by Western blot.
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    Cell Signaling Technology Inc anti phospho stress activated protein kinase c jun n terminal kinase sapk jnk
    The MAPK signal transduction pathway is regulated by FUZHENGHUAYU Tablet. Protein levels of rat p44/42 MAP kinase (137F5), <t>SAPK/JNK</t> (56G8), p38 MAP kinase, phospho-p44/42 MAPK (Thr202/Tyr204), phospho-p38 MAPK (Thr180/Tyr182), and phospho-SAPK/JNK (Thr183/Tyr185) were detected by Western blot.
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    Cell Signaling Technology Inc stress activated protein kinase jun amino terminal kinase
    Western blot assays of liver tissue (right anterior segment) exposed to ischemia-reperfusion injury for detection of activity levels of proapoptotic proteins JNK <t>(stress-activated</t> <t>protein</t> <t>kinase/Jun-amino-terminal</t> kinase), ERK (mitogen-activated protein kinase p44/42), caspase-3, and PARP (poly-ADP-ribose-polymerase). (a) Representative images of Western blots demonstrating the differences in enzyme activity levels for each experimental group. Inactive proteins are shown on top for ERK (total ERK, 42 + 44 kDa), PARP (uncleaved, 116 kDa), caspase-3 (loading control GAPDH, 37 kDa), and JNK (total JNK, 46 + 54 kDa). Activated protein forms are shown in the middle for ERK (phosphorylated ERK, 42 + 44 kDa), PARP (cleaved, 89 kDa), caspase-3 (cleaved, 20 kDa), and JNK (phosphorylated JNK, 46 + 54 kDa). Loading controls are shown below in each group for glyceraldehyde 3-phosphate dehydrogenase (GAPDH, 37 kDa). (b) Quantitative photometric analyses of Western blots prove the mostly significant downregulation of proapoptotic enzyme activity levels after Baicalein pretreatment. Activated enzyme ratio is calculated as a quotient of active/inactive protein form. Changes in protein level activation after sole vehicle administration (DMSO) could also be observed. Data are presented as the mean ± SEM. ∗ p
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    Cell Signaling Technology Inc p46 sapk jnk
    Obese larvae show activation of <t>JNK/SAPK</t> signaling and increased ROS production . (a) Western blot from lysates of FBs showing the level of phosphorylation of JNK/SAPN <t>p46</t> kinase, in P0206-Gal4 (control) and P0206-Gal4; UAS-Ni animals. Actin was used as control loading. (b) Confocal photographs (20x) of cells from FBs stained with DHE (red) for ROS and Hoechst (blue) for nuclei.
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    Cell Signaling Technology Inc rabbit anti stress activated protein kinase
    Obese larvae show activation of <t>JNK/SAPK</t> signaling and increased ROS production . (a) Western blot from lysates of FBs showing the level of phosphorylation of JNK/SAPN <t>p46</t> kinase, in P0206-Gal4 (control) and P0206-Gal4; UAS-Ni animals. Actin was used as control loading. (b) Confocal photographs (20x) of cells from FBs stained with DHE (red) for ROS and Hoechst (blue) for nuclei.
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    Cell Signaling Technology Inc sapk jnk sc 827 antibodies
    Obese larvae show activation of <t>JNK/SAPK</t> signaling and increased ROS production . (a) Western blot from lysates of FBs showing the level of phosphorylation of JNK/SAPN <t>p46</t> kinase, in P0206-Gal4 (control) and P0206-Gal4; UAS-Ni animals. Actin was used as control loading. (b) Confocal photographs (20x) of cells from FBs stained with DHE (red) for ROS and Hoechst (blue) for nuclei.
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    Cell Signaling Technology Inc stress activated protein kinase jun n terminal kinase
    Obese larvae show activation of <t>JNK/SAPK</t> signaling and increased ROS production . (a) Western blot from lysates of FBs showing the level of phosphorylation of JNK/SAPN <t>p46</t> kinase, in P0206-Gal4 (control) and P0206-Gal4; UAS-Ni animals. Actin was used as control loading. (b) Confocal photographs (20x) of cells from FBs stained with DHE (red) for ROS and Hoechst (blue) for nuclei.
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    Cell Signaling Technology Inc phosphoplus sapk jnk
    Time course of <t>SAPK/JNK</t> and p38 MAPK phosphorylation by desiccation After complete removal of medium, T-REx 293 cells in multiwell plates were dried at 98% RH at room temperature for the indicated times and lysed directly in multiwell plates. Similar phosphorylation was also obtained by desiccation at 37°C but not by temperature shift alone (in the medium, from 37°C to room temperature for 4 h).
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    Cell Signaling Technology Inc anti mouse stress activated protein kinase jnk
    Analysis of signaling pathways involved in rLsa21-mediated cytokine production in mouse macrophages. ( A ) RAW264.7 cells were pretreated for 30 min at 37 °C with anti-TLR2 (30 μg/ml), anti-TLR4 (30 μg/ml), or an isotype control Ab (30 μg/ml) before stimulation with rLsa21 (5 μg/ml) for 30 min. Levels of phosphorylated <t>p38,</t> <t>JNK,</t> and ERK1/2 induced by rLsa21 and degraded IκBα were analyzed by western blot using anti–phospho-p38 (p-p38), or anti–phospho-ERK1/2 (p-ERK1/2), anti–phospho-JNK (p-JNK) and anti-mouse IκBα as well as a specific control Ab for each of the unphosphorylated kinases. Data are representative of those obtained in three independent experiments. ( B ) TLR2 −/− , TLR4 −/− or TLR2 −/− /TLR4 −/− DKO macrophages cell lines were stimulated with rLsa21 (5 μg/ml) for 30 min. Levels of phosphorylated p38, JNK, and ERK1/2 induced by rLsa21 were analyzed by western blot as described in materials and methods. ( C ) RAW 264.7 cells were pretreated for 30 min with NF-kB inhibitor (SN50; 20 μM), JNK inhibitor (SP600125; 40 μM) or p38MAPK inhibitor (SB203580; 30 μM) and then stimulated with rLsa21 (2 μg/ml). After incubation, supernatants were harvested and levels of IL-6 and TNF-α were measured by ELISA. Data are representative of three different experiments. (*Indicates P
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    Cell Signaling Technology Inc phospho specific sapk jnk 4671 antibodies
    Analysis of signaling pathways involved in rLsa21-mediated cytokine production in mouse macrophages. ( A ) RAW264.7 cells were pretreated for 30 min at 37 °C with anti-TLR2 (30 μg/ml), anti-TLR4 (30 μg/ml), or an isotype control Ab (30 μg/ml) before stimulation with rLsa21 (5 μg/ml) for 30 min. Levels of phosphorylated <t>p38,</t> <t>JNK,</t> and ERK1/2 induced by rLsa21 and degraded IκBα were analyzed by western blot using anti–phospho-p38 (p-p38), or anti–phospho-ERK1/2 (p-ERK1/2), anti–phospho-JNK (p-JNK) and anti-mouse IκBα as well as a specific control Ab for each of the unphosphorylated kinases. Data are representative of those obtained in three independent experiments. ( B ) TLR2 −/− , TLR4 −/− or TLR2 −/− /TLR4 −/− DKO macrophages cell lines were stimulated with rLsa21 (5 μg/ml) for 30 min. Levels of phosphorylated p38, JNK, and ERK1/2 induced by rLsa21 were analyzed by western blot as described in materials and methods. ( C ) RAW 264.7 cells were pretreated for 30 min with NF-kB inhibitor (SN50; 20 μM), JNK inhibitor (SP600125; 40 μM) or p38MAPK inhibitor (SB203580; 30 μM) and then stimulated with rLsa21 (2 μg/ml). After incubation, supernatants were harvested and levels of IL-6 and TNF-α were measured by ELISA. Data are representative of three different experiments. (*Indicates P
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    Cell Signaling Technology Inc sapk jnk igg
    Ischemia/reperfusion-mediated activation of MAPKs in the lung. PKC β +/+ and PKC β –/– mice underwent the indicated period of left-lung I/R. Animals were sacrificed and protein extracts from the I/R and uninstrumented lung were prepared and subjected to SDS-PAGE (12%, 50 ∝g of protein/lane). Immunoblotting with phospho-p44/42 MAPK antibody or total p44/42 MAPK antibody ( B ), phospho-p38 MAPK antibody, or total p38 MAPK antibody ( I ), and <t>phospho-SAPK/JNK</t> antibody or total SAPK/JNK antibody ( J ) was performed. Data are shown as mean ± SEM of five experiments. Immunohistochemical analysis of phospho-p44/42 expression in murine lung from uninstrumented ( B ) or I/R ( C ) PKC β +/+ mice, and from uninstrumented ( D ) or I/R ( E ) PKC β –/– mice was performed. Scale bar: 50 ∝m. I/R lungs from PKC β +/+ mice were subjected to immunofluorescence microscopy and double stained with an anti–phospho-p44/42 antibody (red) ( F ) and an anti-macrophage antibody (F4/80, green) ( G ). The merging of F (pERK1/2) and G (F4/80) is shown in H . Arrows in F and arrowheads in G indicate dually stained cells Original magnification in F – H , ∞1,000. * P
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    Cell Signaling Technology Inc rabbit anti sapk jnk
    Effects of GSI treatment on MAPK, PI3K/AKT and NF-κB pathway activation in LPS/IC-activated macrophages. (A-B) IFNγ-primed BMMs were pre-treated with vehicle control DMSO or GSI (25 μM) for 30 min and activated by LPS/ICs for 5, 15, 30 and 60 min. Phospho-p38, p38 phospho-p44-42, p44-42, <t>phospho-SAPK/JNK,</t> SAPK/JNK, phospho-Akt, Akt and the loading control β-actin were detected by Western blotting. Representative data from 1 of 3 independent experiments are shown. (C) IFNγ-primed BMMs were activated by LPS/ICs for 4 hrs in the presence of vehicle control DMSO or GSI (25 μM). NF-κB p50 was detected by immunofluorescence staining. The arrows indicate cells with decreased or no p50 nuclear translocation (green). Representative data from 1 of 2 independent experiments are shown.
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    Image Search Results


    NK-4 attenuated H 2 O 2 -induced SAPK/JNK phosphorylation in PC12 cells. PC12 cells were treated with 400 µM H 2 O 2 in the presence of the indicated concentrations of NK-4 for 2 hr. Whole cell lysates were analyzed by Western blotting using anti-phospho-SAPK/JNK antibody (upper panel), or anti-SAPK/JNK antibody (bottom panel). The graph shows the ratio of phosphorylated SAPK/JNK to total SAPK/JNK at each time point.

    Journal: PLoS ONE

    Article Title: Neurotrophic Effects of a Cyanine Dye via the PI3K-Akt Pathway: Attenuation of Motor Discoordination and Neurodegeneration in an Ataxic Animal Model

    doi: 10.1371/journal.pone.0017137

    Figure Lengend Snippet: NK-4 attenuated H 2 O 2 -induced SAPK/JNK phosphorylation in PC12 cells. PC12 cells were treated with 400 µM H 2 O 2 in the presence of the indicated concentrations of NK-4 for 2 hr. Whole cell lysates were analyzed by Western blotting using anti-phospho-SAPK/JNK antibody (upper panel), or anti-SAPK/JNK antibody (bottom panel). The graph shows the ratio of phosphorylated SAPK/JNK to total SAPK/JNK at each time point.

    Article Snippet: Phospho-Akt (Ser 473) antibody, Phospho-SAPK/JNK (Thr183/Thr185) antibody, Akt antibody, and SAPK/JNK antibody were obtained from Cell Signaling Technology, Inc. (Beverly, MA), anti-calbindin D28K antibody was from Chemicon International, Inc. (Temecula, CA) and Alexa488 -conjugated anti-rabbit IgG antibody was from Molecular Probes (Eugene, OR).

    Techniques: Western Blot

    Effects of PBCA–thymulin on stress-related intracellular systems in cells from rEAE mice. Phosphorylation of SAPK/JNK ( A ) and p53 ( C ), and expression of Hsp72 ( B ) in splenic lymphocytes of treated and untreated mice throughout the course of disease. Animal groups: untreated mice (rEAE), rEAE mice treated with PBCA–thymulin (rEAE + PBCA–thymulin), and age-matched controls. Protein levels were measured in spleen lymphocytes. Equal amounts (10 μg) of protein were analysed at different times after immunisation (day 0) by Western blot analysis using corresponding antibodies. Histograms show the amount of protein (± SEM) relative to that of total SAPK/JNK, or p53, and internal GAPDH control (not shown), and are the results of protein blot densitometry measurements by QAPA software from three independent experiments. * Significantly different from the control group, p

    Journal: International Journal of Molecular Sciences

    Article Title: Protective Effect of PBCA Nanoparticles Loaded with Thymulin Against the Relapsing-Remitting Form of Experimental Autoimmune Encephalomyelitis in Mice

    doi: 10.3390/ijms20215374

    Figure Lengend Snippet: Effects of PBCA–thymulin on stress-related intracellular systems in cells from rEAE mice. Phosphorylation of SAPK/JNK ( A ) and p53 ( C ), and expression of Hsp72 ( B ) in splenic lymphocytes of treated and untreated mice throughout the course of disease. Animal groups: untreated mice (rEAE), rEAE mice treated with PBCA–thymulin (rEAE + PBCA–thymulin), and age-matched controls. Protein levels were measured in spleen lymphocytes. Equal amounts (10 μg) of protein were analysed at different times after immunisation (day 0) by Western blot analysis using corresponding antibodies. Histograms show the amount of protein (± SEM) relative to that of total SAPK/JNK, or p53, and internal GAPDH control (not shown), and are the results of protein blot densitometry measurements by QAPA software from three independent experiments. * Significantly different from the control group, p

    Article Snippet: After blocking, the membrane was exposed to an antibody against one of the following mouse proteins for 2 h: heat shock protein (Hsp)70 (rabbit anti-Hsp72 antibody, clone SPA-812, inducible form; Enzo, Lausen, Switzerland; diluted 1:1000), phospho-NF-κB (rabbit anti-phospho-NF-κB p65 (Ser276) antibody; Cell Signaling Technology, Leiden, The Netherlands; diluted 1:1000), phospho-NF-κB (rabbit anti-phospho-NF-κB p65 (Ser536) antibody; Cell Signaling Technology, USA; diluted 1:1000), NF-κB (rabbit anti-NF-κB p65 antibody; Cell Signaling Technology; diluted 1:1000), phospho-IKKα/β (rabbit anti-phospho-IKKα/β antibody (Ser176/180); Cell Signaling Technology; diluted 1:1000), IKKβ (rabbit anti-IKKβ antibody; Cell Signaling Technology; diluted 1:1000), phospho-SAPK/JNK (rabbit anti-phospho-SAPK/JNK (Thr183/Tyr185) antibody; Cell Signaling Technology; diluted 1:1000), SAPK/JNK (rabbit anti-SAPK/JNK antibody; Cell Signaling Technology; diluted 1:1000), phospho-p53 (rabbit anti-phospho-p53 (Ser46) antibody; Cell Signaling Technology; diluted 1:1000), p53 (rabbit anti-p53 (1C12) antibody; Cell Signaling Technology; diluted 1:1000), or caspase-3 (rabbit anti-caspase-3 (8G10) antibody; Cell Signaling Technology; diluted 1:1000).

    Techniques: Mouse Assay, Expressing, Western Blot, Software

    Effect of cilostazol on LPS-induced phosphorylation of ERK-1/2, SAPK/JNK and p38 MAP kinase in BV-2 microglia. BV-2 microglia were treated with vehicle or the indicated concentrations of cilostazol for 6 h before being incubated with LPS (1 µg·mL −1 ) for 30 min. Cell extracts were then prepared and subjected to Western blotting with antibodies specific for phosphorylated forms of ERK-1/2, SAPK/JNK and p38. The results presented are representative of three independent experiments. * P

    Journal: British Journal of Pharmacology

    Article Title: Cilostazol is anti-inflammatory in BV2 microglial cells by inactivating nuclear factor-kappaB and inhibiting mitogen-activated protein kinases

    doi: 10.1111/j.1476-5381.2009.00615.x

    Figure Lengend Snippet: Effect of cilostazol on LPS-induced phosphorylation of ERK-1/2, SAPK/JNK and p38 MAP kinase in BV-2 microglia. BV-2 microglia were treated with vehicle or the indicated concentrations of cilostazol for 6 h before being incubated with LPS (1 µg·mL −1 ) for 30 min. Cell extracts were then prepared and subjected to Western blotting with antibodies specific for phosphorylated forms of ERK-1/2, SAPK/JNK and p38. The results presented are representative of three independent experiments. * P

    Article Snippet: Specific antibodies against inducible NO synthase (iNOS), COX-2, p65 (1:1000 dilution; Santa Cruz Biotechnology, Santa Cruz, CA, USA), extracellular signal-regulated kinase (ERK), phosphorylated (p)-ERK 1/2, p38, p-p38, c-Jun N-terminal kinase (JNK)/stress-activated protein kinase (SAPK) and p-JNK/SAPK (1:1000; Cell Signaling Technology, Beverly, MA, USA) were diluted in 5% BSA-TBST.

    Techniques: Incubation, Western Blot

    Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. ERK, extracellular signal–regulated kinase; JNK, c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.

    Journal: American Journal of Respiratory Cell and Molecular Biology

    Article Title: IL-17A Mediates a Selective Gene Expression Profile in Asthmatic Human Airway Smooth Muscle Cells

    doi: 10.1165/rcmb.2012-0267OC

    Figure Lengend Snippet: Activation of the mitogen-activated protein kinase (MAPK) signal transduction pathway. Immortalized hTERT ASM cells from three independent individuals were stimulated with IL-17A or IL-1β (10 ng/ml) for up to 1 hour. ( A ) Profiling antibody array and validation by ( B ) Western blot was used to quantify MAPK kinases at 5, 15, 30, and 60 minutes after stimulation. ERK, extracellular signal–regulated kinase; JNK, c-Jun NH2-terminal kinase; MSK, mitogen and stress–activated protein kinase; RSK, ribosomal S6 kinase.

    Article Snippet: Anti-human phosphorylated and total protein antibodies against p38, ERK, stress-activated protein kinase/JNK, phospho-IκB kinaseα/β, IkBα, IkBβ, IkBε, p65, p50, and secondary horseradish peroxidase–conjugated antibodies were purchased from Cell Signaling (Danvers, MA).

    Techniques: Activation Assay, Transduction, Ab Array, Western Blot

    ProNGF/p75 NTR signaling Top panel shows Western blot and densitometry measurements of dimeric forms of NGF (proNGF, 27kDA) in nasal (A) , bronchial (B) , and alveolar (C) epithelial cells exposed to 10 μg/ml of TiO 2 -NP for 24 hr. Middle panel (D) shows the interaction between proNGF and its p75 NTR receptor in bronchial epithelial cells exposed to TiO 2 -NP with the corresponding densitometry analysis. Lower panel (E) shows the Western blot analysis of downstream stress-associated protein kinase/Jun-amino-terminal kinase (SAPK/JNK) in bronchial epithelial cells. Blots were probed with phospho SAPK/JNK [Thr183/Tyr185] and re-probed with JNK antibody as an internal control. Densitometry data are expressed as percentage of non-exposed controls after normalizing with GAPDH for NGF or with total JNK for p-JNK in corresponding graphs. Data shown are the means ± SDs of 3 independent experiments. *p

    Journal: Journal of toxicology and environmental health. Part A

    Article Title: Nanoparticles-Induced Apoptosis of Human Airway Epithelium is mediated by ProNGF/p75NTR Signaling

    doi: 10.1080/15287394.2016.1238329

    Figure Lengend Snippet: ProNGF/p75 NTR signaling Top panel shows Western blot and densitometry measurements of dimeric forms of NGF (proNGF, 27kDA) in nasal (A) , bronchial (B) , and alveolar (C) epithelial cells exposed to 10 μg/ml of TiO 2 -NP for 24 hr. Middle panel (D) shows the interaction between proNGF and its p75 NTR receptor in bronchial epithelial cells exposed to TiO 2 -NP with the corresponding densitometry analysis. Lower panel (E) shows the Western blot analysis of downstream stress-associated protein kinase/Jun-amino-terminal kinase (SAPK/JNK) in bronchial epithelial cells. Blots were probed with phospho SAPK/JNK [Thr183/Tyr185] and re-probed with JNK antibody as an internal control. Densitometry data are expressed as percentage of non-exposed controls after normalizing with GAPDH for NGF or with total JNK for p-JNK in corresponding graphs. Data shown are the means ± SDs of 3 independent experiments. *p

    Article Snippet: The following primary antibodies, secondary antibodies, and isotype controls were used for immunostaining: NGF, BDNF, p75NTR , GAPDH and JNK (Santa Cruz Biotechnology, Santa Cruz, CA); phospho-SAPK/JNK (Cell Signaling, Danvers, MA); pro-NGF (Millipore, Billerica, MA); TrkA and TrkB (R & D Systems, Minneapolis, MN); AlexaFluor 488-conjugated secondary antibodies (Invitrogen, Carlsbad, CA); and horseradish peroxidase (HRP)-conjugated secondary antibodies (Santa Cruz Biotechnology).

    Techniques: Western Blot

    MLK4 cannot function as a MAP3K for ERK, JNK and p38. ( a ) 293T cells were transfected with an expressing vector of Flag-JNK1 with or without an expression vector of V5-MLK4β or HA-MKK7 for 24 h. The cell lysates were immunoblotted with antibodies as indicated. ( b ) 293T cells were transfected with an expressing vector of Flag-ERK2 with or without an expression vector of V5-MLK4β or HA-MEK1 for 24 h. The cell lysates were immunoblotted with antibodies as indicated. ( c ) 293T cells were transfected with an expressing vector of Flag-p38 with an expression vector of V5-MLK4β or its deletion mutants as indicated. V5-TAK1 was included as a positive control. The cell lysates were immunoblotted with antibodies as indicated. Data are representative of two independent experiments. ERK, extracellular signal-regulated kinase; IB, immunoblotting; IP, immunoprecipitation; JNK, c-Jun N-terminal kinase; MAP3K, mitogen-activated protein kinase kinase kinase; MLK, mixed-lineage kinase.

    Journal: Cellular and Molecular Immunology

    Article Title: MLK4 has negative effect on TLR4 signaling

    doi: 10.1038/cmi.2011.15

    Figure Lengend Snippet: MLK4 cannot function as a MAP3K for ERK, JNK and p38. ( a ) 293T cells were transfected with an expressing vector of Flag-JNK1 with or without an expression vector of V5-MLK4β or HA-MKK7 for 24 h. The cell lysates were immunoblotted with antibodies as indicated. ( b ) 293T cells were transfected with an expressing vector of Flag-ERK2 with or without an expression vector of V5-MLK4β or HA-MEK1 for 24 h. The cell lysates were immunoblotted with antibodies as indicated. ( c ) 293T cells were transfected with an expressing vector of Flag-p38 with an expression vector of V5-MLK4β or its deletion mutants as indicated. V5-TAK1 was included as a positive control. The cell lysates were immunoblotted with antibodies as indicated. Data are representative of two independent experiments. ERK, extracellular signal-regulated kinase; IB, immunoblotting; IP, immunoprecipitation; JNK, c-Jun N-terminal kinase; MAP3K, mitogen-activated protein kinase kinase kinase; MLK, mixed-lineage kinase.

    Article Snippet: LPS were from Escherichia coli O111:B4 (List Biological Laboratories, Campbell, CA, USA), Anti-Flag (F3165; Sigma, St Louis, MO, USA), anti-Myc (A-14), anti-V5 (Invitrogen, San Diego, CA, USA) and anti-IkBa (C-21; Santa Cruz Biotechnology, Santa Cruz, CA, USA), and antibodies to phosphorylated p38 (9211), Jnk (9251) and Erk (9010; Cell Signaling, Beverly, MA, USA).

    Techniques: Transfection, Expressing, Plasmid Preparation, Positive Control, Immunoprecipitation

    The MAPK signal transduction pathway is regulated by FUZHENGHUAYU Tablet. Protein levels of rat p44/42 MAP kinase (137F5), SAPK/JNK (56G8), p38 MAP kinase, phospho-p44/42 MAPK (Thr202/Tyr204), phospho-p38 MAPK (Thr180/Tyr182), and phospho-SAPK/JNK (Thr183/Tyr185) were detected by Western blot.

    Journal: Evidence-based Complementary and Alternative Medicine : eCAM

    Article Title: MAPK Signal Transduction Pathway Regulation: A Novel Mechanism of Rat HSC-T6 Cell Apoptosis Induced by FUZHENGHUAYU Tablet

    doi: 10.1155/2013/368103

    Figure Lengend Snippet: The MAPK signal transduction pathway is regulated by FUZHENGHUAYU Tablet. Protein levels of rat p44/42 MAP kinase (137F5), SAPK/JNK (56G8), p38 MAP kinase, phospho-p44/42 MAPK (Thr202/Tyr204), phospho-p38 MAPK (Thr180/Tyr182), and phospho-SAPK/JNK (Thr183/Tyr185) were detected by Western blot.

    Article Snippet: After blocking in 5% nonfat milk, the membranes were probed with rabbit monoclonal antibodies against rat p44/42 MAP kinase (137F5) (CST), SAPK/JNK (56G8) (CST), p38 MAP kinase (CST), phospho-p44/42 MAPK (Thr202/Tyr204) (CST), phospho-p38 MAPK (Thr180/Tyr182) (CST), phospho-SAPK/JNK (Thr183/Tyr185) (CST), and mouse monoclonal antibody against rat β -actin (Santa Cruz) as primary antibodies at 1 : 1000 dilution.

    Techniques: Transduction, Western Blot

    Western blot assays of liver tissue (right anterior segment) exposed to ischemia-reperfusion injury for detection of activity levels of proapoptotic proteins JNK (stress-activated protein kinase/Jun-amino-terminal kinase), ERK (mitogen-activated protein kinase p44/42), caspase-3, and PARP (poly-ADP-ribose-polymerase). (a) Representative images of Western blots demonstrating the differences in enzyme activity levels for each experimental group. Inactive proteins are shown on top for ERK (total ERK, 42 + 44 kDa), PARP (uncleaved, 116 kDa), caspase-3 (loading control GAPDH, 37 kDa), and JNK (total JNK, 46 + 54 kDa). Activated protein forms are shown in the middle for ERK (phosphorylated ERK, 42 + 44 kDa), PARP (cleaved, 89 kDa), caspase-3 (cleaved, 20 kDa), and JNK (phosphorylated JNK, 46 + 54 kDa). Loading controls are shown below in each group for glyceraldehyde 3-phosphate dehydrogenase (GAPDH, 37 kDa). (b) Quantitative photometric analyses of Western blots prove the mostly significant downregulation of proapoptotic enzyme activity levels after Baicalein pretreatment. Activated enzyme ratio is calculated as a quotient of active/inactive protein form. Changes in protein level activation after sole vehicle administration (DMSO) could also be observed. Data are presented as the mean ± SEM. ∗ p

    Journal: Oxidative Medicine and Cellular Longevity

    Article Title: Modulation of Glutathione Hemostasis by Inhibition of 12/15-Lipoxygenase Prevents ROS-Mediated Cell Death after Hepatic Ischemia and Reperfusion

    doi: 10.1155/2017/8325754

    Figure Lengend Snippet: Western blot assays of liver tissue (right anterior segment) exposed to ischemia-reperfusion injury for detection of activity levels of proapoptotic proteins JNK (stress-activated protein kinase/Jun-amino-terminal kinase), ERK (mitogen-activated protein kinase p44/42), caspase-3, and PARP (poly-ADP-ribose-polymerase). (a) Representative images of Western blots demonstrating the differences in enzyme activity levels for each experimental group. Inactive proteins are shown on top for ERK (total ERK, 42 + 44 kDa), PARP (uncleaved, 116 kDa), caspase-3 (loading control GAPDH, 37 kDa), and JNK (total JNK, 46 + 54 kDa). Activated protein forms are shown in the middle for ERK (phosphorylated ERK, 42 + 44 kDa), PARP (cleaved, 89 kDa), caspase-3 (cleaved, 20 kDa), and JNK (phosphorylated JNK, 46 + 54 kDa). Loading controls are shown below in each group for glyceraldehyde 3-phosphate dehydrogenase (GAPDH, 37 kDa). (b) Quantitative photometric analyses of Western blots prove the mostly significant downregulation of proapoptotic enzyme activity levels after Baicalein pretreatment. Activated enzyme ratio is calculated as a quotient of active/inactive protein form. Changes in protein level activation after sole vehicle administration (DMSO) could also be observed. Data are presented as the mean ± SEM. ∗ p

    Article Snippet: SDS-gel electrophoresis and protein transfer onto nitrocellulose membranes and followed by overnight incubation with antibodies at 4°C were performed for activity detection of stress-activated protein kinase/Jun-amino-terminal kinase (SAPK/JNK, rabbit, 46/54 kDa, Cell Signaling Technology, USA), mitogen-activated protein kinase p44/42 (ERK1/2, rabbit, 42/44 kDa, Cell Signaling Technology, USA), caspase-3 (rabbit, 17/19/35 kDa, Cell Signaling Technology, USA), and poly-ADP-ribose-polymerase (PARP, rabbit, 89/116 kDa, Cell Signaling Technology, USA).

    Techniques: Western Blot, Activity Assay, Activation Assay

    Obese larvae show activation of JNK/SAPK signaling and increased ROS production . (a) Western blot from lysates of FBs showing the level of phosphorylation of JNK/SAPN p46 kinase, in P0206-Gal4 (control) and P0206-Gal4; UAS-Ni animals. Actin was used as control loading. (b) Confocal photographs (20x) of cells from FBs stained with DHE (red) for ROS and Hoechst (blue) for nuclei.

    Journal: BioMed Research International

    Article Title: Anthocyanins Function as Anti-Inflammatory Agents in a Drosophila Model for Adipose Tissue Macrophage Infiltration

    doi: 10.1155/2018/6413172

    Figure Lengend Snippet: Obese larvae show activation of JNK/SAPK signaling and increased ROS production . (a) Western blot from lysates of FBs showing the level of phosphorylation of JNK/SAPN p46 kinase, in P0206-Gal4 (control) and P0206-Gal4; UAS-Ni animals. Actin was used as control loading. (b) Confocal photographs (20x) of cells from FBs stained with DHE (red) for ROS and Hoechst (blue) for nuclei.

    Article Snippet: Membrane was incubated with primary antibody anti-phospho-p46 SAPK/JNK (Cell Signaling #9521) or antiactin (Hybridoma Bank) overnight at 4°C in blocking buffer and then washed in 0.1% Tween 20 with TRIS-buffered saline (TBST).

    Techniques: Activation Assay, Western Blot, Staining

    Anthocyanins-rich diet reduces the infiltration of hemocytes in the FBs and the phosphorylation of JNK/SAPK . (a) Scheme of the different diets NF (Normal Food) or enriched in FL (flavonoids) or ACN (anthocyanins). (b) % of hemocytes in the cells of the FBs from animals at the indicated genotypes and fed with the indicated diets at 5 or 12 days AEL. (c) Confocal images showing hemocytes expressing Hml-RFP (red) and nuclei stained with Hoechst (blue) from animals at 12 days AEL, upon feeding with NF, FL, or ACN enriched diets. (d) Western blot from lysates of FBs showing the level of phosphorylation of JNK/SAPK p46 kinase, in P0206-Gal4 (control) and P0206-Gal4 ; UAS-Ni animals fed in FL or ACN enriched diets. FBs were taken at 5 or 12 days AEL. Actin was used as control loading. (e) Model of JNK signaling and potential action of anthocianins. Error bars represent SEM (standard error of the mean) of three independent experiments. ∗ P

    Journal: BioMed Research International

    Article Title: Anthocyanins Function as Anti-Inflammatory Agents in a Drosophila Model for Adipose Tissue Macrophage Infiltration

    doi: 10.1155/2018/6413172

    Figure Lengend Snippet: Anthocyanins-rich diet reduces the infiltration of hemocytes in the FBs and the phosphorylation of JNK/SAPK . (a) Scheme of the different diets NF (Normal Food) or enriched in FL (flavonoids) or ACN (anthocyanins). (b) % of hemocytes in the cells of the FBs from animals at the indicated genotypes and fed with the indicated diets at 5 or 12 days AEL. (c) Confocal images showing hemocytes expressing Hml-RFP (red) and nuclei stained with Hoechst (blue) from animals at 12 days AEL, upon feeding with NF, FL, or ACN enriched diets. (d) Western blot from lysates of FBs showing the level of phosphorylation of JNK/SAPK p46 kinase, in P0206-Gal4 (control) and P0206-Gal4 ; UAS-Ni animals fed in FL or ACN enriched diets. FBs were taken at 5 or 12 days AEL. Actin was used as control loading. (e) Model of JNK signaling and potential action of anthocianins. Error bars represent SEM (standard error of the mean) of three independent experiments. ∗ P

    Article Snippet: Membrane was incubated with primary antibody anti-phospho-p46 SAPK/JNK (Cell Signaling #9521) or antiactin (Hybridoma Bank) overnight at 4°C in blocking buffer and then washed in 0.1% Tween 20 with TRIS-buffered saline (TBST).

    Techniques: Expressing, Staining, Western Blot

    Time course of SAPK/JNK and p38 MAPK phosphorylation by desiccation After complete removal of medium, T-REx 293 cells in multiwell plates were dried at 98% RH at room temperature for the indicated times and lysed directly in multiwell plates. Similar phosphorylation was also obtained by desiccation at 37°C but not by temperature shift alone (in the medium, from 37°C to room temperature for 4 h).

    Journal: The Journal of Physiology

    Article Title: Response of human cells to desiccation: comparison with hyperosmotic stress response

    doi: 10.1113/jphysiol.2004.065540

    Figure Lengend Snippet: Time course of SAPK/JNK and p38 MAPK phosphorylation by desiccation After complete removal of medium, T-REx 293 cells in multiwell plates were dried at 98% RH at room temperature for the indicated times and lysed directly in multiwell plates. Similar phosphorylation was also obtained by desiccation at 37°C but not by temperature shift alone (in the medium, from 37°C to room temperature for 4 h).

    Article Snippet: PhosphoPlus SAPK/JNK (Thr183 /Tyr185 ) antibody kit, containing both phospho- and non-phospho-SAPK/JNK antibodies, was purchased from Cell Signalling Technology Inc. (Beverly, MA, USA).

    Techniques:

    Analysis of signaling pathways involved in rLsa21-mediated cytokine production in mouse macrophages. ( A ) RAW264.7 cells were pretreated for 30 min at 37 °C with anti-TLR2 (30 μg/ml), anti-TLR4 (30 μg/ml), or an isotype control Ab (30 μg/ml) before stimulation with rLsa21 (5 μg/ml) for 30 min. Levels of phosphorylated p38, JNK, and ERK1/2 induced by rLsa21 and degraded IκBα were analyzed by western blot using anti–phospho-p38 (p-p38), or anti–phospho-ERK1/2 (p-ERK1/2), anti–phospho-JNK (p-JNK) and anti-mouse IκBα as well as a specific control Ab for each of the unphosphorylated kinases. Data are representative of those obtained in three independent experiments. ( B ) TLR2 −/− , TLR4 −/− or TLR2 −/− /TLR4 −/− DKO macrophages cell lines were stimulated with rLsa21 (5 μg/ml) for 30 min. Levels of phosphorylated p38, JNK, and ERK1/2 induced by rLsa21 were analyzed by western blot as described in materials and methods. ( C ) RAW 264.7 cells were pretreated for 30 min with NF-kB inhibitor (SN50; 20 μM), JNK inhibitor (SP600125; 40 μM) or p38MAPK inhibitor (SB203580; 30 μM) and then stimulated with rLsa21 (2 μg/ml). After incubation, supernatants were harvested and levels of IL-6 and TNF-α were measured by ELISA. Data are representative of three different experiments. (*Indicates P

    Journal: Scientific Reports

    Article Title: Leptospira surface adhesin (Lsa21) induces Toll like receptor 2 and 4 mediated inflammatory responses in macrophages

    doi: 10.1038/srep39530

    Figure Lengend Snippet: Analysis of signaling pathways involved in rLsa21-mediated cytokine production in mouse macrophages. ( A ) RAW264.7 cells were pretreated for 30 min at 37 °C with anti-TLR2 (30 μg/ml), anti-TLR4 (30 μg/ml), or an isotype control Ab (30 μg/ml) before stimulation with rLsa21 (5 μg/ml) for 30 min. Levels of phosphorylated p38, JNK, and ERK1/2 induced by rLsa21 and degraded IκBα were analyzed by western blot using anti–phospho-p38 (p-p38), or anti–phospho-ERK1/2 (p-ERK1/2), anti–phospho-JNK (p-JNK) and anti-mouse IκBα as well as a specific control Ab for each of the unphosphorylated kinases. Data are representative of those obtained in three independent experiments. ( B ) TLR2 −/− , TLR4 −/− or TLR2 −/− /TLR4 −/− DKO macrophages cell lines were stimulated with rLsa21 (5 μg/ml) for 30 min. Levels of phosphorylated p38, JNK, and ERK1/2 induced by rLsa21 were analyzed by western blot as described in materials and methods. ( C ) RAW 264.7 cells were pretreated for 30 min with NF-kB inhibitor (SN50; 20 μM), JNK inhibitor (SP600125; 40 μM) or p38MAPK inhibitor (SB203580; 30 μM) and then stimulated with rLsa21 (2 μg/ml). After incubation, supernatants were harvested and levels of IL-6 and TNF-α were measured by ELISA. Data are representative of three different experiments. (*Indicates P

    Article Snippet: After blocking with 5% nonfat milk in PBS (pH 7.4, 0.05% (v/v) Tween-20), the membranes were incubated overnight at 4 °C with primary Abs, including rabbit anti-mouse-p38, anti–mouse phospho-p38, anti-mouse-ERK2, anti–mouse phospho-ERK1/2, anti–mouse stress-activated protein kinase/JNK, anti–mouse phospho–stress-activated protein kinase/JNK, anti-mouse IκBα (Cell Signaling Technology, Beverly, MA), according to the manufacturer’s instructions.

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

    Ischemia/reperfusion-mediated activation of MAPKs in the lung. PKC β +/+ and PKC β –/– mice underwent the indicated period of left-lung I/R. Animals were sacrificed and protein extracts from the I/R and uninstrumented lung were prepared and subjected to SDS-PAGE (12%, 50 ∝g of protein/lane). Immunoblotting with phospho-p44/42 MAPK antibody or total p44/42 MAPK antibody ( B ), phospho-p38 MAPK antibody, or total p38 MAPK antibody ( I ), and phospho-SAPK/JNK antibody or total SAPK/JNK antibody ( J ) was performed. Data are shown as mean ± SEM of five experiments. Immunohistochemical analysis of phospho-p44/42 expression in murine lung from uninstrumented ( B ) or I/R ( C ) PKC β +/+ mice, and from uninstrumented ( D ) or I/R ( E ) PKC β –/– mice was performed. Scale bar: 50 ∝m. I/R lungs from PKC β +/+ mice were subjected to immunofluorescence microscopy and double stained with an anti–phospho-p44/42 antibody (red) ( F ) and an anti-macrophage antibody (F4/80, green) ( G ). The merging of F (pERK1/2) and G (F4/80) is shown in H . Arrows in F and arrowheads in G indicate dually stained cells Original magnification in F – H , ∞1,000. * P

    Journal: Journal of Clinical Investigation

    Article Title: PKC? regulates ischemia/reperfusion injury in the lung

    doi: 10.1172/JCI200419225

    Figure Lengend Snippet: Ischemia/reperfusion-mediated activation of MAPKs in the lung. PKC β +/+ and PKC β –/– mice underwent the indicated period of left-lung I/R. Animals were sacrificed and protein extracts from the I/R and uninstrumented lung were prepared and subjected to SDS-PAGE (12%, 50 ∝g of protein/lane). Immunoblotting with phospho-p44/42 MAPK antibody or total p44/42 MAPK antibody ( B ), phospho-p38 MAPK antibody, or total p38 MAPK antibody ( I ), and phospho-SAPK/JNK antibody or total SAPK/JNK antibody ( J ) was performed. Data are shown as mean ± SEM of five experiments. Immunohistochemical analysis of phospho-p44/42 expression in murine lung from uninstrumented ( B ) or I/R ( C ) PKC β +/+ mice, and from uninstrumented ( D ) or I/R ( E ) PKC β –/– mice was performed. Scale bar: 50 ∝m. I/R lungs from PKC β +/+ mice were subjected to immunofluorescence microscopy and double stained with an anti–phospho-p44/42 antibody (red) ( F ) and an anti-macrophage antibody (F4/80, green) ( G ). The merging of F (pERK1/2) and G (F4/80) is shown in H . Arrows in F and arrowheads in G indicate dually stained cells Original magnification in F – H , ∞1,000. * P

    Article Snippet: Sections were stained with the following primary antibodies: rabbit anti–Egr-1 IgG (8 ∝g/ml; Santa Cruz Biotechnology Inc.), rat F4/80 monoclonal antibody (10 ∝g/ml; PharMingen, San Diego, California, USA), rabbit anti–phospho- or total p44/42, p38, and SAPK/JNK IgG (1:10; Cell Signaling Technology Inc.) or nonimmune IgG, respectively.

    Techniques: Activation Assay, Mouse Assay, SDS Page, Immunohistochemistry, Expressing, Immunofluorescence, Microscopy, Staining

    Effects of GSI treatment on MAPK, PI3K/AKT and NF-κB pathway activation in LPS/IC-activated macrophages. (A-B) IFNγ-primed BMMs were pre-treated with vehicle control DMSO or GSI (25 μM) for 30 min and activated by LPS/ICs for 5, 15, 30 and 60 min. Phospho-p38, p38 phospho-p44-42, p44-42, phospho-SAPK/JNK, SAPK/JNK, phospho-Akt, Akt and the loading control β-actin were detected by Western blotting. Representative data from 1 of 3 independent experiments are shown. (C) IFNγ-primed BMMs were activated by LPS/ICs for 4 hrs in the presence of vehicle control DMSO or GSI (25 μM). NF-κB p50 was detected by immunofluorescence staining. The arrows indicate cells with decreased or no p50 nuclear translocation (green). Representative data from 1 of 2 independent experiments are shown.

    Journal: PLoS ONE

    Article Title: Notch signaling regulates the responses of lipopolysaccharide-stimulated macrophages in the presence of immune complexes

    doi: 10.1371/journal.pone.0198609

    Figure Lengend Snippet: Effects of GSI treatment on MAPK, PI3K/AKT and NF-κB pathway activation in LPS/IC-activated macrophages. (A-B) IFNγ-primed BMMs were pre-treated with vehicle control DMSO or GSI (25 μM) for 30 min and activated by LPS/ICs for 5, 15, 30 and 60 min. Phospho-p38, p38 phospho-p44-42, p44-42, phospho-SAPK/JNK, SAPK/JNK, phospho-Akt, Akt and the loading control β-actin were detected by Western blotting. Representative data from 1 of 3 independent experiments are shown. (C) IFNγ-primed BMMs were activated by LPS/ICs for 4 hrs in the presence of vehicle control DMSO or GSI (25 μM). NF-κB p50 was detected by immunofluorescence staining. The arrows indicate cells with decreased or no p50 nuclear translocation (green). Representative data from 1 of 2 independent experiments are shown.

    Article Snippet: The primary antibodies used in this study were as follows: rabbit anti-Notch1 (1:2000) (Santa Cruz Biotechnology, USA), rabbit anti-cleaved Notch1 (Val1744) (1:1000), rabbit anti-phospho-p38 (1:2000), rabbit anti p38 (1:2000), rabbit anti-phospho-p44-42 (1:4000), rabbit anti p44-42 (1:4000), rabbit anti-phospho-SAPK-JNK (1:2000), rabbit anti-SAPK-JNK (1:2000), rabbit anti-phospho-AKT (1:2000), rabbit anti-AKT (1:2000) and rabbit anti-RBPJSHU (1:1000) (all from Cell Signaling Technology, USA), mouse anti β-actin (1:1000) (Chemicon-Millipore, USA) and rabbit anti-GAPDH (1:4000) (Santa Cruz Biotechnology, USA).

    Techniques: Activation Assay, Western Blot, Immunofluorescence, Staining, Translocation Assay