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    Name:
    Phospho p38 MAPK Thr180 Tyr182 Blocking Peptide
    Description:
    This peptide is used to specifically block Phospho p38 MAPK Thr180 Tyr182 12F8 Rabbit mAb 4631 reactivity
    Catalog Number:
    1170
    Price:
    None
    Category:
    Experimental Controls
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    Structured Review

    Cell Signaling Technology Inc p38 mapk
    <t>p38</t> <t>MAPK</t> induced an autophagy-dependent pathway in ASA-regulated CF proliferation. (A) CFs exposed to hypoxia were treated with doses of ASA at 0.5, 2.5, and 5 mmol/L for 12 h, and then the changes of phosphorylated p38, ERK, JNK were detected by Western blot. (B) Cardiac fibroblasts were pre-treated with the p38 inhibitor SB203580 (10 μmol/L) for 1 h and were then treated with 2.5 mmol/L ASA for 12 h. Western blot results showed the changes of LC3-II, phosphorylated Akt and cleaved PARP 1. Mean±SEM. n =3, ** P
    This peptide is used to specifically block Phospho p38 MAPK Thr180 Tyr182 12F8 Rabbit mAb 4631 reactivity
    https://www.bioz.com/result/p38 mapk/product/Cell Signaling Technology Inc
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    p38 mapk - by Bioz Stars, 2021-03
    99/100 stars

    Images

    1) Product Images from "Aspirin alleviates cardiac fibrosis in mice by inhibiting autophagy"

    Article Title: Aspirin alleviates cardiac fibrosis in mice by inhibiting autophagy

    Journal: Acta Pharmacologica Sinica

    doi: 10.1038/aps.2016.143

    p38 MAPK induced an autophagy-dependent pathway in ASA-regulated CF proliferation. (A) CFs exposed to hypoxia were treated with doses of ASA at 0.5, 2.5, and 5 mmol/L for 12 h, and then the changes of phosphorylated p38, ERK, JNK were detected by Western blot. (B) Cardiac fibroblasts were pre-treated with the p38 inhibitor SB203580 (10 μmol/L) for 1 h and were then treated with 2.5 mmol/L ASA for 12 h. Western blot results showed the changes of LC3-II, phosphorylated Akt and cleaved PARP 1. Mean±SEM. n =3, ** P
    Figure Legend Snippet: p38 MAPK induced an autophagy-dependent pathway in ASA-regulated CF proliferation. (A) CFs exposed to hypoxia were treated with doses of ASA at 0.5, 2.5, and 5 mmol/L for 12 h, and then the changes of phosphorylated p38, ERK, JNK were detected by Western blot. (B) Cardiac fibroblasts were pre-treated with the p38 inhibitor SB203580 (10 μmol/L) for 1 h and were then treated with 2.5 mmol/L ASA for 12 h. Western blot results showed the changes of LC3-II, phosphorylated Akt and cleaved PARP 1. Mean±SEM. n =3, ** P

    Techniques Used: Western Blot

    2) Product Images from "Reactive microglia drive tau pathology and contribute to the spreading of pathological tau in the brain"

    Article Title: Reactive microglia drive tau pathology and contribute to the spreading of pathological tau in the brain

    Journal: Brain

    doi: 10.1093/brain/awv081

    CX3CR1 deficiency accelerates tau hyperphosphorylation and p38 MAPK activation in hTau mice at early stages of development. ( A ) Western blot analysis of hippocampal lysates shows elevated tau phosphorylation on AT8, AT180 and PHF-1 sites and activation of p38 MAPK (pT180/pY182) in hTau Cx3cr1 −/− mice at 2 months of age. No significant alterations in total tau (Tau5 antibody) or total (t) p38 MAPK levels. GAPDH was the loading control. Lysates from tau knockout mice were included in the Mapt −/− lane and show no expression of tau. ( B–E ) Quantification of western blots for AT8, AT180, PHF-1 and phospho (p)-p38 MAPK reveal a statistically significant [ n = 5 per group for 2, 12 and 24-month-old groups; n = 6 for 6-month-old group; mean ± SEM integrated density value ratio for respective epitopes (* P
    Figure Legend Snippet: CX3CR1 deficiency accelerates tau hyperphosphorylation and p38 MAPK activation in hTau mice at early stages of development. ( A ) Western blot analysis of hippocampal lysates shows elevated tau phosphorylation on AT8, AT180 and PHF-1 sites and activation of p38 MAPK (pT180/pY182) in hTau Cx3cr1 −/− mice at 2 months of age. No significant alterations in total tau (Tau5 antibody) or total (t) p38 MAPK levels. GAPDH was the loading control. Lysates from tau knockout mice were included in the Mapt −/− lane and show no expression of tau. ( B–E ) Quantification of western blots for AT8, AT180, PHF-1 and phospho (p)-p38 MAPK reveal a statistically significant [ n = 5 per group for 2, 12 and 24-month-old groups; n = 6 for 6-month-old group; mean ± SEM integrated density value ratio for respective epitopes (* P

    Techniques Used: Activation Assay, Mouse Assay, Western Blot, Knock-Out, Expressing

    Inclusion of IL-1Ra in the microglial inoculum reduces overall reactivity for phosphorylated p38 MAPK within the recipient mouse brain. ( A , B and E ) Immunostained brain sections displaying overall reduced phosphorylated (p)-p38 MAPK (pT180/pY182) immunoreactivity around the needle track when the IL-1Ra was included with microglia from 6-month-old hTau Cx3cr1 −/− donor mice ( B ) compared to those receiving hTau Cx3cr1 −/− donor microglia alone ( A ). Scale bar = 30 µm. Quantification of percentage p-p38 MAPK immunoreactive area revealed a statistically significant (* P
    Figure Legend Snippet: Inclusion of IL-1Ra in the microglial inoculum reduces overall reactivity for phosphorylated p38 MAPK within the recipient mouse brain. ( A , B and E ) Immunostained brain sections displaying overall reduced phosphorylated (p)-p38 MAPK (pT180/pY182) immunoreactivity around the needle track when the IL-1Ra was included with microglia from 6-month-old hTau Cx3cr1 −/− donor mice ( B ) compared to those receiving hTau Cx3cr1 −/− donor microglia alone ( A ). Scale bar = 30 µm. Quantification of percentage p-p38 MAPK immunoreactive area revealed a statistically significant (* P

    Techniques Used: Mouse Assay

    Related Articles

    Binding Assay:

    Article Title: Treatment with TO901317, a synthetic liver X receptor agonist, reduces brain damage and attenuates neuroinflammation in experimental intracerebral hemorrhage
    Article Snippet: .. Equal amounts of protein (35 to 50 μg protein in 20 μL for tissue samples and 20 μg protein in 20 μL for cell lysates) were separated by sodium dodecyl sulfate-polyacrylamide gels, transferred to Immobilon-P membranes (Millipore), blocked using 5 % milk in PBS containing 0.1 % Tween-20, and probed overnight at 4 °C with primary antibodies including mouse anti-LXR-α (1:1000; Abcam), rabbit anti-LXR-β (1:1000; Santa Cruz), mouse anti-ATP binding cassette transporter-1 (ABCA-1; 1:1000; Abcam), mouse anti-iNOS (1:200; Sigma), rabbit anti-COX-2 (1:1000; Cayman), rabbit anti-NF-κB p65 (1:1000; Santa Cruz), rabbit phospho-p38 (1:1000; Cell Signaling, Danvers, MA, USA), rabbit total p38 (1:2000; Cell Signaling), rabbit phospho-Jun amino-terminal kinases (JNK; Thr183/Tyr185, 1:1000; Cell Signaling), rabbit total JNK (1:2000; Cell Signaling), rabbit phospho-extracellular signal-regulated kinases p44/42 (Erk p44/42; Thr202/Tyr204, 1:1000; Cell Signaling), and rabbit total Erk (1:2000; Cell Signaling). .. The membranes were then incubated with horseradish peroxidase-linked anti-rabbit or anti-mouse secondary antibodies (Santa Cruz Biotechnology; 1:1000) for 1 h at 4 °C.

    Article Title: Nitroxides Mitigate Neutrophil-Mediated Damage to the Myocardium after Experimental Myocardial Infarction in Rats
    Article Snippet: PVDF membranes were imaged on the Bio-Rad ChemiDoc imaging system. .. Non-specific binding was minimised by incubating the membranes with 5% (w /v ) BSA in Tris Buffered Saline with Tween-20 (TBST) [composition: 25 mM Tris base, 140 mM sodium chloride (NaCl), 4 mM potassium chloride (KCl), 0.1% Tween 20 in 1 L of MilliQ water] blocking solution on a rocker at 22 °C for 4 h. p-p38 was detected by incubation of the membrane with 1:1000 (v /v ) MAPK phospho-p38 (p-p38; Cell Signalling technology) primary antibody in 1% (w /v ) BSA in TBST. .. Excess primary antibody was washed, and binding antibody was labelled through incubation with 1:10,000 peroxidase labelled anti-rabbit IgG secondary antibody in 1% w/v BSA in TBST with rocking (22 °C; 1 h).

    Fluorescence In Situ Hybridization:

    Article Title: PGC-1α and exercise intensity dependent adaptations in mouse skeletal muscle
    Article Snippet: Phosphorylation levels and protein content were measured by SDS-PAGE and western blotting using self-casted gels. .. PVDF membranes were blocked in 3% fish gel, and protein and phosphorylation sites were measured using primary antibodies against AMPK Thr172 (#2535S, Cell Signaling), AMPKα2 protein (#G3013, Santa Cruz Biotechnology), p38 Thr180/Tyr182 (#4511, Cell Signaling), p38 protein (#9212, Cell Signaling), CREBSer133 (#9191, Cell Signaling), CAMKII (#3361, Cell Signalling), LC3A/B (#4108, Cell Signaling), p62 (#5114, Cell Signaling), ULKSer317 (#12753, Cell Signaling), ULKSer757 (#6888, Cell Signaling), ULK1 (#8054, Cell Signaling) and beta-actin (#4967, Cell Signaling). ..

    Expressing:

    Article Title: 4-1BB Signaling Promotes Alveolar Macrophages-Mediated Pro-Fibrotic Responses and Crystalline Silica-Induced Pulmonary Fibrosis in Mice
    Article Snippet: Western Blot AnalysisWestern blotting was performed essentially as previously described ( ). .. The expression of CD137 (1:500, rat, Abcam, Cambridge, UK), ASK1 (1:2,000, rabbit, Abcam), phospho-ASK1 [1:500, rabbit, Cell Signaling Technology (CST), Danvers, MA, USA], p38 (1:1,000, rabbit, CST), phospho-p38 (1:1,000, rabbit, CST), JNK (1:1,000, rabbit, CST), phospho-JNK (1:1,000, rabbit, CST), IκBα (1:1,000, rabbit, CST), phospho-IκBα (1:1,000, rabbit, CST), MMP9 (1:1,000, rabbit, Abcam), MMP12 (1:2,000, rabbit, Abcam), and β-actin (1:1,000, rabbit, CST) in MH-S cells or lung tissues was measured by western blot. .. Protein expression was normalized to β-actin.

    Western Blot:

    Article Title: 4-1BB Signaling Promotes Alveolar Macrophages-Mediated Pro-Fibrotic Responses and Crystalline Silica-Induced Pulmonary Fibrosis in Mice
    Article Snippet: Western Blot AnalysisWestern blotting was performed essentially as previously described ( ). .. The expression of CD137 (1:500, rat, Abcam, Cambridge, UK), ASK1 (1:2,000, rabbit, Abcam), phospho-ASK1 [1:500, rabbit, Cell Signaling Technology (CST), Danvers, MA, USA], p38 (1:1,000, rabbit, CST), phospho-p38 (1:1,000, rabbit, CST), JNK (1:1,000, rabbit, CST), phospho-JNK (1:1,000, rabbit, CST), IκBα (1:1,000, rabbit, CST), phospho-IκBα (1:1,000, rabbit, CST), MMP9 (1:1,000, rabbit, Abcam), MMP12 (1:2,000, rabbit, Abcam), and β-actin (1:1,000, rabbit, CST) in MH-S cells or lung tissues was measured by western blot. .. Protein expression was normalized to β-actin.

    Article Title: Active components from Radix Scrophulariae inhibits the ventricular remodeling induced by hypertension in rats
    Article Snippet: Western blotting Western blots were measured as previously described (Huang and Chen ). .. Briefly, active and total form of ERK1/2, JNK and p38 MAPK accumulation were detected by Western blot analysis with using the following antigenes: phospho-P44/42MAPK (ERK 1/2) Thr202 –Tyr204 (1:2000), phospho-SAPK/JNK Thr183 –Tyr185 (1:1000), phospho-p38 MAPK (Thr180 –Tyr182 ) (1:1000) (Cell Signaling Technology, Beverly, MA, USA), anti-GAPDH (Abmart, Shanghai, China), and a goat anti-rabbit horseradish peroxidase-conjugated secondary antibody (1:5000 dilution, Santa Cruz). ..

    Blocking Assay:

    Article Title: Nitroxides Mitigate Neutrophil-Mediated Damage to the Myocardium after Experimental Myocardial Infarction in Rats
    Article Snippet: PVDF membranes were imaged on the Bio-Rad ChemiDoc imaging system. .. Non-specific binding was minimised by incubating the membranes with 5% (w /v ) BSA in Tris Buffered Saline with Tween-20 (TBST) [composition: 25 mM Tris base, 140 mM sodium chloride (NaCl), 4 mM potassium chloride (KCl), 0.1% Tween 20 in 1 L of MilliQ water] blocking solution on a rocker at 22 °C for 4 h. p-p38 was detected by incubation of the membrane with 1:1000 (v /v ) MAPK phospho-p38 (p-p38; Cell Signalling technology) primary antibody in 1% (w /v ) BSA in TBST. .. Excess primary antibody was washed, and binding antibody was labelled through incubation with 1:10,000 peroxidase labelled anti-rabbit IgG secondary antibody in 1% w/v BSA in TBST with rocking (22 °C; 1 h).

    Incubation:

    Article Title: Nitroxides Mitigate Neutrophil-Mediated Damage to the Myocardium after Experimental Myocardial Infarction in Rats
    Article Snippet: PVDF membranes were imaged on the Bio-Rad ChemiDoc imaging system. .. Non-specific binding was minimised by incubating the membranes with 5% (w /v ) BSA in Tris Buffered Saline with Tween-20 (TBST) [composition: 25 mM Tris base, 140 mM sodium chloride (NaCl), 4 mM potassium chloride (KCl), 0.1% Tween 20 in 1 L of MilliQ water] blocking solution on a rocker at 22 °C for 4 h. p-p38 was detected by incubation of the membrane with 1:1000 (v /v ) MAPK phospho-p38 (p-p38; Cell Signalling technology) primary antibody in 1% (w /v ) BSA in TBST. .. Excess primary antibody was washed, and binding antibody was labelled through incubation with 1:10,000 peroxidase labelled anti-rabbit IgG secondary antibody in 1% w/v BSA in TBST with rocking (22 °C; 1 h).

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  • 99
    Cell Signaling Technology Inc phospho p38 mapk
    The increase in riok-1 is skn-1 -dependent in Caenorhabditis elegans with Aeromonas dhakensis infection. (A) Single knockdown of skn-1 or simultaneous knockdown of skn-1 and riok-1 resulted in a decrease in the life span in C. elegans with A. dhakensis infection. (B) riok-1 expression in riok-1 transcriptional reporter worms with RNAi control vector L4440. (C) riok-1 expression in riok-1 transcriptional reporter worms with RNAi knockdown of skn-1 . (D) riok-1 expression in riok-1 transcriptional reporter worms with A. dhakensis AAK1 infection. (E) riok-1 expression in riok-1 transcriptional reporter worms with RNAi knockdown of skn-1 and A. dhakensis AAK1 infection. (F) A summary of the florescence quantification of (B–E) . (G) The expression level of riok-1 as determined using quantitative real time-PCR (qRT-PCR) in the <t>p38</t> gain-of-function-mutant worms nsy-1(ums8 ) with and without A. dhakensis AAK1 infection was similar to those in wild-type N2 worms with A. dhakensis AAK1 infection. (H) The expression levels of riok-1 as determined using qRT-PCR in the p38 <t>MAPK/</t> pmk-1 -mutant worms pmk-1(km25) with A. dhakensis AAK1 infection were lower than in wild-type N2 worms with A. dhakensis AAK1 infection. The scale bars in (B–E) are all 100 µm. *** P
    Phospho P38 Mapk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phospho p38 mapk/product/Cell Signaling Technology Inc
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    86
    Cell Signaling Technology Inc rabbit polyclonal p38 mapk
    PAR1 and PAR2 signaling involves <t>MAPK</t> and PI3K signaling pathways in the induction of innate immune responses . Protease-activated receptors are G-protein-coupled receptors. Once activated, they signal via ERK1/2 and <t>p38</t> MAPK to induce innate immune responses. This action is limited by activation of PI3K-Akt signaling pathway. This inhibitory effect is predominantly via blocking of p38 activation.
    Rabbit Polyclonal P38 Mapk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit polyclonal p38 mapk/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    rabbit polyclonal p38 mapk - by Bioz Stars, 2021-03
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    86
    Cell Signaling Technology Inc rabbit anti p38 mapk
    Interleukin (IL)-1β triggers the phosphorylation of the mitogen-activated protein kinases (MAPKs) Jun kinase (JNK) and <t>p38</t> in hippocampal cultured neurons. Rat hippocampal neurons at 7 days in vitro (DIV), were exposed to various concentrations of IL-1β (1 to 100 ng/ml, prepared in Krebs buffer; pH 7.4) for different times (5, 10, 15, 20, 25, 30, 60 and 180 minutes), after which cells were either lysed on ice in radio-immunoprecipitation assay (RIPA) buffer for ( A–D ) western blotting analysis or fixed for ( E–F ) immunocytochemical analysis of the pattern of activation (phosphorylation) of the various MAPKs. ( A ) IL-1β (10 ng/ml) activated JNK in a time-dependent manner, reaching significance at 10 to 15 minutes of incubation with IL-1β. ( B ) Activation of JNK increased in line with increasing concentrations of IL-1β. ( C ) After 15 minutes of exposure to 100 ng/ml IL-1β, p38 <t>MAPK</t> was also activated. ( D ) However, under similar experimental conditions, IL-1β failed to significantly affect the amount of phosphorylated p42 ERK. In each panel, the bar graphs display the mean ± SEM of four to eight cultures, and the blots below illustrate a representative experiment. Membranes were first used to detect the phosphorylated MAPK, and then reprobed for the total amount of MAPK. MAPK activation was calculated as a ratio between the phosphorylated and total immunoreactivities, expressed as a percentage of the control values (that is, in the absence of IL-1β). The values are mean ± SEM of four to eight experiments, * P
    Rabbit Anti P38 Mapk, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/rabbit anti p38 mapk/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
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    Cell Signaling Technology Inc mapk proteins
    Effect of balanophonin on <t>MAPK</t> expression in LPS-activated BV-2 cells. (A) Effect of balanophonin on the production of pERK1/2. (B) Effect of balanophonin on the production of pJNK. (C) Effect of balanophonin on the production of <t>p-p38.</t> (D) Effect of balanophonin and SP600125 on the Phosphorylation of JNK. α-Tubulin was used as a loading control. Each value is presented as mean ± SD of at least three independent experiments. * p
    Mapk Proteins, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/mapk proteins/product/Cell Signaling Technology Inc
    Average 86 stars, based on 1 article reviews
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    Image Search Results


    The increase in riok-1 is skn-1 -dependent in Caenorhabditis elegans with Aeromonas dhakensis infection. (A) Single knockdown of skn-1 or simultaneous knockdown of skn-1 and riok-1 resulted in a decrease in the life span in C. elegans with A. dhakensis infection. (B) riok-1 expression in riok-1 transcriptional reporter worms with RNAi control vector L4440. (C) riok-1 expression in riok-1 transcriptional reporter worms with RNAi knockdown of skn-1 . (D) riok-1 expression in riok-1 transcriptional reporter worms with A. dhakensis AAK1 infection. (E) riok-1 expression in riok-1 transcriptional reporter worms with RNAi knockdown of skn-1 and A. dhakensis AAK1 infection. (F) A summary of the florescence quantification of (B–E) . (G) The expression level of riok-1 as determined using quantitative real time-PCR (qRT-PCR) in the p38 gain-of-function-mutant worms nsy-1(ums8 ) with and without A. dhakensis AAK1 infection was similar to those in wild-type N2 worms with A. dhakensis AAK1 infection. (H) The expression levels of riok-1 as determined using qRT-PCR in the p38 MAPK/ pmk-1 -mutant worms pmk-1(km25) with A. dhakensis AAK1 infection were lower than in wild-type N2 worms with A. dhakensis AAK1 infection. The scale bars in (B–E) are all 100 µm. *** P

    Journal: Frontiers in Immunology

    Article Title: RIOK-1 Is a Suppressor of the p38 MAPK Innate Immune Pathway in Caenorhabditis elegans

    doi: 10.3389/fimmu.2018.00774

    Figure Lengend Snippet: The increase in riok-1 is skn-1 -dependent in Caenorhabditis elegans with Aeromonas dhakensis infection. (A) Single knockdown of skn-1 or simultaneous knockdown of skn-1 and riok-1 resulted in a decrease in the life span in C. elegans with A. dhakensis infection. (B) riok-1 expression in riok-1 transcriptional reporter worms with RNAi control vector L4440. (C) riok-1 expression in riok-1 transcriptional reporter worms with RNAi knockdown of skn-1 . (D) riok-1 expression in riok-1 transcriptional reporter worms with A. dhakensis AAK1 infection. (E) riok-1 expression in riok-1 transcriptional reporter worms with RNAi knockdown of skn-1 and A. dhakensis AAK1 infection. (F) A summary of the florescence quantification of (B–E) . (G) The expression level of riok-1 as determined using quantitative real time-PCR (qRT-PCR) in the p38 gain-of-function-mutant worms nsy-1(ums8 ) with and without A. dhakensis AAK1 infection was similar to those in wild-type N2 worms with A. dhakensis AAK1 infection. (H) The expression levels of riok-1 as determined using qRT-PCR in the p38 MAPK/ pmk-1 -mutant worms pmk-1(km25) with A. dhakensis AAK1 infection were lower than in wild-type N2 worms with A. dhakensis AAK1 infection. The scale bars in (B–E) are all 100 µm. *** P

    Article Snippet: Monoclonal antibody to phospho-p38 MAPK (Cell Signaling Technology) and monoclonal antibody to tubulin (Sigma-Aldrich) were used for detection.

    Techniques: Infection, Expressing, Plasmid Preparation, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, Mutagenesis

    Model of a p38 MAPK, SKN-1, and RIOK-1 feedback loop upon infection in Caenorhabditis elegans . Pathogens activate the p38 MAPK pathway and increase the expression of riok-1 through the transcription of skn-1 . RIOK-1 has an important role in a feedback loop that regulates the expression of the p38 MAPK pathway in order to maintain immune homeostasis.

    Journal: Frontiers in Immunology

    Article Title: RIOK-1 Is a Suppressor of the p38 MAPK Innate Immune Pathway in Caenorhabditis elegans

    doi: 10.3389/fimmu.2018.00774

    Figure Lengend Snippet: Model of a p38 MAPK, SKN-1, and RIOK-1 feedback loop upon infection in Caenorhabditis elegans . Pathogens activate the p38 MAPK pathway and increase the expression of riok-1 through the transcription of skn-1 . RIOK-1 has an important role in a feedback loop that regulates the expression of the p38 MAPK pathway in order to maintain immune homeostasis.

    Article Snippet: Monoclonal antibody to phospho-p38 MAPK (Cell Signaling Technology) and monoclonal antibody to tubulin (Sigma-Aldrich) were used for detection.

    Techniques: Infection, Expressing

    riok-1 negatively regulates the p38 MAPK pathway. (A) Life spans of wild-type N2 and riok- 1( gk1101 ) worm knockdown with pmk-1 RNAi were both shortened. (B) MAPK ( pmk-1 ) mutants, (C) MAPKK ( sek-1 ) mutants, and (D) MAPKKK ( nsy-1 ) gain-of-function mutants with riok-1 knockdown using RNAi showed similar life spans when compared with those without RNAi knockdown under A. dhakensis infection. (E) A. dhakensis infection and RNAi-mediated riok-1 knockdown induced p38 phosphorylation as shown in a Western blot analysis. (F–J) Increasing expression of p38 MAPK downstream genes C29F3.7 (F) , C32H11.12 (G) , F08G5.6 (H) , K08D8.5 (I) , and T24B8.5 (J) as determined using qRT-PCR in worms with riok-1 knockdown mediated by RNAi under A. dhakensis infection. For the unprocessed data of western blot analysis in (E) , please see the Figure S6 in Supplementary Material. *** P

    Journal: Frontiers in Immunology

    Article Title: RIOK-1 Is a Suppressor of the p38 MAPK Innate Immune Pathway in Caenorhabditis elegans

    doi: 10.3389/fimmu.2018.00774

    Figure Lengend Snippet: riok-1 negatively regulates the p38 MAPK pathway. (A) Life spans of wild-type N2 and riok- 1( gk1101 ) worm knockdown with pmk-1 RNAi were both shortened. (B) MAPK ( pmk-1 ) mutants, (C) MAPKK ( sek-1 ) mutants, and (D) MAPKKK ( nsy-1 ) gain-of-function mutants with riok-1 knockdown using RNAi showed similar life spans when compared with those without RNAi knockdown under A. dhakensis infection. (E) A. dhakensis infection and RNAi-mediated riok-1 knockdown induced p38 phosphorylation as shown in a Western blot analysis. (F–J) Increasing expression of p38 MAPK downstream genes C29F3.7 (F) , C32H11.12 (G) , F08G5.6 (H) , K08D8.5 (I) , and T24B8.5 (J) as determined using qRT-PCR in worms with riok-1 knockdown mediated by RNAi under A. dhakensis infection. For the unprocessed data of western blot analysis in (E) , please see the Figure S6 in Supplementary Material. *** P

    Article Snippet: Monoclonal antibody to phospho-p38 MAPK (Cell Signaling Technology) and monoclonal antibody to tubulin (Sigma-Aldrich) were used for detection.

    Techniques: Infection, Western Blot, Expressing, Quantitative RT-PCR

    PAR1 and PAR2 signaling involves MAPK and PI3K signaling pathways in the induction of innate immune responses . Protease-activated receptors are G-protein-coupled receptors. Once activated, they signal via ERK1/2 and p38 MAPK to induce innate immune responses. This action is limited by activation of PI3K-Akt signaling pathway. This inhibitory effect is predominantly via blocking of p38 activation.

    Journal: BMC Immunology

    Article Title: PAR1- and PAR2-induced innate immune markers are negatively regulated by PI3K/Akt signaling pathway in oral keratinocytes

    doi: 10.1186/1471-2172-11-53

    Figure Lengend Snippet: PAR1 and PAR2 signaling involves MAPK and PI3K signaling pathways in the induction of innate immune responses . Protease-activated receptors are G-protein-coupled receptors. Once activated, they signal via ERK1/2 and p38 MAPK to induce innate immune responses. This action is limited by activation of PI3K-Akt signaling pathway. This inhibitory effect is predominantly via blocking of p38 activation.

    Article Snippet: Rabbit polyclonal p38 MAPK (9212) and Akt (9272), and monoclonal phospho-p38 MAPK (Thr180/Tyr182; D3F9), phospho-Akt (Thr308; 244F9), p44/p42 MAPK (ERK1/2; 137F5), and phospho-p44/p42 MAPK (Thr202/Tyr204;D13.14.4E, XP™) antibodies were obtained from Cell Signaling Technology, Inc. (Danvers, MA).

    Techniques: Activation Assay, Blocking Assay

    Interleukin (IL)-1β triggers the phosphorylation of the mitogen-activated protein kinases (MAPKs) Jun kinase (JNK) and p38 in hippocampal cultured neurons. Rat hippocampal neurons at 7 days in vitro (DIV), were exposed to various concentrations of IL-1β (1 to 100 ng/ml, prepared in Krebs buffer; pH 7.4) for different times (5, 10, 15, 20, 25, 30, 60 and 180 minutes), after which cells were either lysed on ice in radio-immunoprecipitation assay (RIPA) buffer for ( A–D ) western blotting analysis or fixed for ( E–F ) immunocytochemical analysis of the pattern of activation (phosphorylation) of the various MAPKs. ( A ) IL-1β (10 ng/ml) activated JNK in a time-dependent manner, reaching significance at 10 to 15 minutes of incubation with IL-1β. ( B ) Activation of JNK increased in line with increasing concentrations of IL-1β. ( C ) After 15 minutes of exposure to 100 ng/ml IL-1β, p38 MAPK was also activated. ( D ) However, under similar experimental conditions, IL-1β failed to significantly affect the amount of phosphorylated p42 ERK. In each panel, the bar graphs display the mean ± SEM of four to eight cultures, and the blots below illustrate a representative experiment. Membranes were first used to detect the phosphorylated MAPK, and then reprobed for the total amount of MAPK. MAPK activation was calculated as a ratio between the phosphorylated and total immunoreactivities, expressed as a percentage of the control values (that is, in the absence of IL-1β). The values are mean ± SEM of four to eight experiments, * P

    Journal: Journal of Neuroinflammation

    Article Title: Blockade of adenosine A2A receptors prevents interleukin-1?-induced exacerbation of neuronal toxicity through a p38 mitogen-activated protein kinase pathway

    doi: 10.1186/1742-2094-9-204

    Figure Lengend Snippet: Interleukin (IL)-1β triggers the phosphorylation of the mitogen-activated protein kinases (MAPKs) Jun kinase (JNK) and p38 in hippocampal cultured neurons. Rat hippocampal neurons at 7 days in vitro (DIV), were exposed to various concentrations of IL-1β (1 to 100 ng/ml, prepared in Krebs buffer; pH 7.4) for different times (5, 10, 15, 20, 25, 30, 60 and 180 minutes), after which cells were either lysed on ice in radio-immunoprecipitation assay (RIPA) buffer for ( A–D ) western blotting analysis or fixed for ( E–F ) immunocytochemical analysis of the pattern of activation (phosphorylation) of the various MAPKs. ( A ) IL-1β (10 ng/ml) activated JNK in a time-dependent manner, reaching significance at 10 to 15 minutes of incubation with IL-1β. ( B ) Activation of JNK increased in line with increasing concentrations of IL-1β. ( C ) After 15 minutes of exposure to 100 ng/ml IL-1β, p38 MAPK was also activated. ( D ) However, under similar experimental conditions, IL-1β failed to significantly affect the amount of phosphorylated p42 ERK. In each panel, the bar graphs display the mean ± SEM of four to eight cultures, and the blots below illustrate a representative experiment. Membranes were first used to detect the phosphorylated MAPK, and then reprobed for the total amount of MAPK. MAPK activation was calculated as a ratio between the phosphorylated and total immunoreactivities, expressed as a percentage of the control values (that is, in the absence of IL-1β). The values are mean ± SEM of four to eight experiments, * P

    Article Snippet: The following primary antibodies were used: mouse anti-phospho-p38 MAPK, rabbit anti-p38 MAPK, mouse anti-phospho-stress-activated protein kinase (SAPK)/JNK, rabbit anti-SAPK/JNK, mouse anti-phospho-p44/p42 MAPK, extracellular signal-regulated kinase (ERK)1/2 and rabbit anti-p44/p42 MAPK (all at 1:1000 all from Cell Signaling Technology, Beverly, MA, USA), rabbit anti-IL-1β receptor 1 (1:200; Santa Cruz Biotechnology, Santa Cruz, CA, USA), mouse monoclonal anti-SNAP25 (1:5000), mouse anti-PSD95 (1:20,000) and mouse anti-synaptophysin (1:20,000) (all from Sigma-Aldrich, St Louis, MO, USA).

    Techniques: Cell Culture, In Vitro, Radio Immunoprecipitation, Western Blot, Activation Assay, Incubation

    Blockade of adenosine A 2A receptors prevents the interleukin (IL)-1β-induced activation of the mitogen-activated protein kinases (MAPKs) Jun kinase (JNK) and p38 in hippocampal cultured neurons. Rat hippocampal neuronal cultures at 7 days in vitro (DIV) were exposed to 100 ng/ml IL-1β for 15 minutes in the absence or presence of 50 nmol/l SCH58261, an antagonist of adenosine A 2A receptors, which was added 20 minutes before addition of IL-1β. Cells were then lysed on ice in a minimum volume of radio-immunoprecipitation assay (RIPA) buffer for western blotting analysis to quantify the immunoreactivity of the activated (phosphorylated) form of ( A ) p38 (p-p38) and ( B ) JNK (p-JNK). In both panels, the bar graphs display the mean ± SEM of five to six experiments, and the blots below illustrate a representative experiment showing that SCH58261 prevented the IL-1β-induced phosphorylation of ( A ) p38 and ( B ) JNK, without having any effect itself on either of these. In each experiment, membranes were first used to detect each phosphorylated MAPK and then reprobed for the total amount of MAPK, so that the activation of each MAPK was calculated as a ratio between the phosphorylated and total immunoreactivities, which were expressed as a percentage of control (CTR) values (that is , in the absence of any added drug). * P

    Journal: Journal of Neuroinflammation

    Article Title: Blockade of adenosine A2A receptors prevents interleukin-1?-induced exacerbation of neuronal toxicity through a p38 mitogen-activated protein kinase pathway

    doi: 10.1186/1742-2094-9-204

    Figure Lengend Snippet: Blockade of adenosine A 2A receptors prevents the interleukin (IL)-1β-induced activation of the mitogen-activated protein kinases (MAPKs) Jun kinase (JNK) and p38 in hippocampal cultured neurons. Rat hippocampal neuronal cultures at 7 days in vitro (DIV) were exposed to 100 ng/ml IL-1β for 15 minutes in the absence or presence of 50 nmol/l SCH58261, an antagonist of adenosine A 2A receptors, which was added 20 minutes before addition of IL-1β. Cells were then lysed on ice in a minimum volume of radio-immunoprecipitation assay (RIPA) buffer for western blotting analysis to quantify the immunoreactivity of the activated (phosphorylated) form of ( A ) p38 (p-p38) and ( B ) JNK (p-JNK). In both panels, the bar graphs display the mean ± SEM of five to six experiments, and the blots below illustrate a representative experiment showing that SCH58261 prevented the IL-1β-induced phosphorylation of ( A ) p38 and ( B ) JNK, without having any effect itself on either of these. In each experiment, membranes were first used to detect each phosphorylated MAPK and then reprobed for the total amount of MAPK, so that the activation of each MAPK was calculated as a ratio between the phosphorylated and total immunoreactivities, which were expressed as a percentage of control (CTR) values (that is , in the absence of any added drug). * P

    Article Snippet: The following primary antibodies were used: mouse anti-phospho-p38 MAPK, rabbit anti-p38 MAPK, mouse anti-phospho-stress-activated protein kinase (SAPK)/JNK, rabbit anti-SAPK/JNK, mouse anti-phospho-p44/p42 MAPK, extracellular signal-regulated kinase (ERK)1/2 and rabbit anti-p44/p42 MAPK (all at 1:1000 all from Cell Signaling Technology, Beverly, MA, USA), rabbit anti-IL-1β receptor 1 (1:200; Santa Cruz Biotechnology, Santa Cruz, CA, USA), mouse monoclonal anti-SNAP25 (1:5000), mouse anti-PSD95 (1:20,000) and mouse anti-synaptophysin (1:20,000) (all from Sigma-Aldrich, St Louis, MO, USA).

    Techniques: Activation Assay, Cell Culture, In Vitro, Radio Immunoprecipitation, Western Blot

    Interleukin (IL)-1β type I receptor mediates the IL-1β-induced phosphorylation of the mitogen-activated protein kinases (MAPKs) Jun kinase (JNK) and p38 in hippocampal cultured neurons . Rat hippocampal neuronal cultures at 7 days in vitro (DIV) were exposed to 100 ng/ml IL-1β for 15 minutes in the absence or in the presence of the antagonist of the IL-1β type I receptor, IL-1Ra (5 μg/ml), added 30 minutes before addition of IL-1β. Cells were then lysed on ice in a minimum volume of radio-immunoprecipitation assay (RIPA) buffer for western blotting analysis to quantify the immunoreactivity of the activated (phosphorylated) form of ( A ) p38 (p-p38) and ( B ) JNK (p-JNK). In both panels, the bar graphs display the mean ± SEM of three to four experiments, and the blots below illustrate a representative experiment showing that IL-1Ra ( A ) prevented the IL-1β-induced phosphorylation of p38 and ( B ) attenuated the phosphorylation of JNK. In each experiment, membranes were first used to detect each phosphorylated MAPK, and then reprobed for the total amount of MAPK, so that the activation of each MAPK was calculated as a ratio between the phosphorylated and total immunoreactivities, which were expressed as a percentage of control (CTR) values (that is, in the absence of any added drug). * P

    Journal: Journal of Neuroinflammation

    Article Title: Blockade of adenosine A2A receptors prevents interleukin-1?-induced exacerbation of neuronal toxicity through a p38 mitogen-activated protein kinase pathway

    doi: 10.1186/1742-2094-9-204

    Figure Lengend Snippet: Interleukin (IL)-1β type I receptor mediates the IL-1β-induced phosphorylation of the mitogen-activated protein kinases (MAPKs) Jun kinase (JNK) and p38 in hippocampal cultured neurons . Rat hippocampal neuronal cultures at 7 days in vitro (DIV) were exposed to 100 ng/ml IL-1β for 15 minutes in the absence or in the presence of the antagonist of the IL-1β type I receptor, IL-1Ra (5 μg/ml), added 30 minutes before addition of IL-1β. Cells were then lysed on ice in a minimum volume of radio-immunoprecipitation assay (RIPA) buffer for western blotting analysis to quantify the immunoreactivity of the activated (phosphorylated) form of ( A ) p38 (p-p38) and ( B ) JNK (p-JNK). In both panels, the bar graphs display the mean ± SEM of three to four experiments, and the blots below illustrate a representative experiment showing that IL-1Ra ( A ) prevented the IL-1β-induced phosphorylation of p38 and ( B ) attenuated the phosphorylation of JNK. In each experiment, membranes were first used to detect each phosphorylated MAPK, and then reprobed for the total amount of MAPK, so that the activation of each MAPK was calculated as a ratio between the phosphorylated and total immunoreactivities, which were expressed as a percentage of control (CTR) values (that is, in the absence of any added drug). * P

    Article Snippet: The following primary antibodies were used: mouse anti-phospho-p38 MAPK, rabbit anti-p38 MAPK, mouse anti-phospho-stress-activated protein kinase (SAPK)/JNK, rabbit anti-SAPK/JNK, mouse anti-phospho-p44/p42 MAPK, extracellular signal-regulated kinase (ERK)1/2 and rabbit anti-p44/p42 MAPK (all at 1:1000 all from Cell Signaling Technology, Beverly, MA, USA), rabbit anti-IL-1β receptor 1 (1:200; Santa Cruz Biotechnology, Santa Cruz, CA, USA), mouse monoclonal anti-SNAP25 (1:5000), mouse anti-PSD95 (1:20,000) and mouse anti-synaptophysin (1:20,000) (all from Sigma-Aldrich, St Louis, MO, USA).

    Techniques: Cell Culture, In Vitro, Radio Immunoprecipitation, Western Blot, Activation Assay

    Effect of balanophonin on MAPK expression in LPS-activated BV-2 cells. (A) Effect of balanophonin on the production of pERK1/2. (B) Effect of balanophonin on the production of pJNK. (C) Effect of balanophonin on the production of p-p38. (D) Effect of balanophonin and SP600125 on the Phosphorylation of JNK. α-Tubulin was used as a loading control. Each value is presented as mean ± SD of at least three independent experiments. * p

    Journal: Biomolecules & Therapeutics

    Article Title: A New Neolignan Derivative, Balanophonin Isolated from Firmiana simplex Delays the Progress of Neuronal Cell Death by Inhibiting Microglial Activation

    doi: 10.4062/biomolther.2016.224

    Figure Lengend Snippet: Effect of balanophonin on MAPK expression in LPS-activated BV-2 cells. (A) Effect of balanophonin on the production of pERK1/2. (B) Effect of balanophonin on the production of pJNK. (C) Effect of balanophonin on the production of p-p38. (D) Effect of balanophonin and SP600125 on the Phosphorylation of JNK. α-Tubulin was used as a loading control. Each value is presented as mean ± SD of at least three independent experiments. * p

    Article Snippet: MAPK proteins (p-38, p-p38, ERK, p-ERK, JNK, p-JNK), iNOS and cleaved caspase-3 (c-caspase-3) were purchased from Cell Signaling (Beverly, MA, USA).

    Techniques: Expressing