p p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38
    P P38, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38 mapk
    Activation of GCN2 by agents that invoke translation inhibition. ( A ) ZAK was deleted by genome editing and CRISPR and WT and ZAK KO cells, designated + and -, respectively, were cultured and ZAK and actin proteins were measured in the prepared lysates by immunoblot analyses with antibodies that specifically recognize each protein. Molecular weight (MW) markers are indicated in kDal. ( B ) WT HEK293T cells (+) and those deleted for ZAK (−) were treated with 1 μM anisomycin (ANS) for 1 h (+) or not treated (−), followed by immunoblot measurements of the phosphorylated and total <t>p38</t> proteins, along with ZAK. ( C ) WT (+, lanes 1–6) and ZAK (−, lanes 7–12) cells were treated with up to 200 nM ANS for 3 h. Levels of the indicated phosphorylated and total proteins were measured by immunoblot analyses. ANS treatment for lanes: 1 and 7 (0 nM, not treated -NT), 2 and 8 (5 nM), 3 and 9 (25 nM), 4 and 10 (50 nM), 5 and 11 (100 nM), and 6 and 12 (200 nM). ( D ) WT (+, lanes 1–5) and ZAK KO (−, lanes 6–10) HEK293T cells were treated with increasing amounts of HF for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). HF treatment for lanes: 1 and 6 (0 nM, not treated -NT), 2 and 7 (5 nM), 3 and 8 (25 nM), 4 and 9 (50 nM), and 5 and 10 (100 nM). Relative levels of P-GCN2 and P-eIF2α normalized for the respectively total protein (P-total) are shown in the bar graph (right panel). The P/total for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. ( E ) WT (+) and ZAK KO (−) HEK293T cells were treated with 25 nM HF, 4 mM histidinol (HIS), or 2 μM borrelidin (BOR) for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). Relative levels of P-GCN2 and P-eIF2α normalized for total levels of the corresponding proteins are shown in the bar graph (right panel). The P/total ratio for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. For panels D and E, statistical significance, denoted by *, was determined using a two-way analysis of variance (ANOVA); * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, **** P ≤ 0.0001. Error bars indicate mean with SD ( n = 3).
    P 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
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    1) Product Images from "Multiple mechanisms activate GCN2 eIF2 kinase in response to diverse stress conditions"

    Article Title: Multiple mechanisms activate GCN2 eIF2 kinase in response to diverse stress conditions

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkae006

    Activation of GCN2 by agents that invoke translation inhibition. ( A ) ZAK was deleted by genome editing and CRISPR and WT and ZAK KO cells, designated + and -, respectively, were cultured and ZAK and actin proteins were measured in the prepared lysates by immunoblot analyses with antibodies that specifically recognize each protein. Molecular weight (MW) markers are indicated in kDal. ( B ) WT HEK293T cells (+) and those deleted for ZAK (−) were treated with 1 μM anisomycin (ANS) for 1 h (+) or not treated (−), followed by immunoblot measurements of the phosphorylated and total p38 proteins, along with ZAK. ( C ) WT (+, lanes 1–6) and ZAK (−, lanes 7–12) cells were treated with up to 200 nM ANS for 3 h. Levels of the indicated phosphorylated and total proteins were measured by immunoblot analyses. ANS treatment for lanes: 1 and 7 (0 nM, not treated -NT), 2 and 8 (5 nM), 3 and 9 (25 nM), 4 and 10 (50 nM), 5 and 11 (100 nM), and 6 and 12 (200 nM). ( D ) WT (+, lanes 1–5) and ZAK KO (−, lanes 6–10) HEK293T cells were treated with increasing amounts of HF for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). HF treatment for lanes: 1 and 6 (0 nM, not treated -NT), 2 and 7 (5 nM), 3 and 8 (25 nM), 4 and 9 (50 nM), and 5 and 10 (100 nM). Relative levels of P-GCN2 and P-eIF2α normalized for the respectively total protein (P-total) are shown in the bar graph (right panel). The P/total for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. ( E ) WT (+) and ZAK KO (−) HEK293T cells were treated with 25 nM HF, 4 mM histidinol (HIS), or 2 μM borrelidin (BOR) for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). Relative levels of P-GCN2 and P-eIF2α normalized for total levels of the corresponding proteins are shown in the bar graph (right panel). The P/total ratio for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. For panels D and E, statistical significance, denoted by *, was determined using a two-way analysis of variance (ANOVA); * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, **** P ≤ 0.0001. Error bars indicate mean with SD ( n = 3).
    Figure Legend Snippet: Activation of GCN2 by agents that invoke translation inhibition. ( A ) ZAK was deleted by genome editing and CRISPR and WT and ZAK KO cells, designated + and -, respectively, were cultured and ZAK and actin proteins were measured in the prepared lysates by immunoblot analyses with antibodies that specifically recognize each protein. Molecular weight (MW) markers are indicated in kDal. ( B ) WT HEK293T cells (+) and those deleted for ZAK (−) were treated with 1 μM anisomycin (ANS) for 1 h (+) or not treated (−), followed by immunoblot measurements of the phosphorylated and total p38 proteins, along with ZAK. ( C ) WT (+, lanes 1–6) and ZAK (−, lanes 7–12) cells were treated with up to 200 nM ANS for 3 h. Levels of the indicated phosphorylated and total proteins were measured by immunoblot analyses. ANS treatment for lanes: 1 and 7 (0 nM, not treated -NT), 2 and 8 (5 nM), 3 and 9 (25 nM), 4 and 10 (50 nM), 5 and 11 (100 nM), and 6 and 12 (200 nM). ( D ) WT (+, lanes 1–5) and ZAK KO (−, lanes 6–10) HEK293T cells were treated with increasing amounts of HF for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). HF treatment for lanes: 1 and 6 (0 nM, not treated -NT), 2 and 7 (5 nM), 3 and 8 (25 nM), 4 and 9 (50 nM), and 5 and 10 (100 nM). Relative levels of P-GCN2 and P-eIF2α normalized for the respectively total protein (P-total) are shown in the bar graph (right panel). The P/total for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. ( E ) WT (+) and ZAK KO (−) HEK293T cells were treated with 25 nM HF, 4 mM histidinol (HIS), or 2 μM borrelidin (BOR) for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). Relative levels of P-GCN2 and P-eIF2α normalized for total levels of the corresponding proteins are shown in the bar graph (right panel). The P/total ratio for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. For panels D and E, statistical significance, denoted by *, was determined using a two-way analysis of variance (ANOVA); * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, **** P ≤ 0.0001. Error bars indicate mean with SD ( n = 3).

    Techniques Used: Activation Assay, Inhibition, CRISPR, Cell Culture, Western Blot, Molecular Weight

    phosphorylated p38 p p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphorylated p38 p p38
    Phosphorylated P38 P P38, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38
    PCSK9 regulates morphology, function of mitochondrial and VSMCs' apoptosis through activation of p38MAPK. (A) Volcano plot of differentially expressed genes between NC and sh‐PCSK9 HC‐VSMCs. (B) KEGG pathway analysis of enriched differentially expressed genes. (C) Heatmap of differentially expressed gene clustering. Red representing highly‐expressed genes and green representing lower expressed genes. (D) The effect of PCSK9 level on activation of <t>p38</t> was measured by western blot in HC‐VSMCs and HA‐VSMCs. (E) Morphological changes of mitochondria was compared by using Mitotracker (left panel) and quantitative analysis was performed (right panel) when activation of p38 was inhibited in Lenti‐PCSK9 HA‐VSMCs. (F, G) Detection and quantitative analysis of mitochondrial ROS (F) and mitochondrial membrane potential (G), when <t>phosphorylation</t> <t>of</t> <t>p38</t> was inhibited in Lenti‐PCSK9 HA‐VSMCs. (H) PI staining and quantitative analysis before and after inhibition of p38 in NC and Lenti‐PCSK9 HA‐VSMCs. Hoechst33342 (blue) labels nucleus and PI (red) labels apoptotic cells. AR, aspect ratio. Bar charts show the mean with SD. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001.
    P P38, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "PCSK9 increases vulnerability of carotid plaque by promoting mitochondrial dysfunction and apoptosis of vascular smooth muscle cells"

    Article Title: PCSK9 increases vulnerability of carotid plaque by promoting mitochondrial dysfunction and apoptosis of vascular smooth muscle cells

    Journal: CNS Neuroscience & Therapeutics

    doi: 10.1111/cns.14640

    PCSK9 regulates morphology, function of mitochondrial and VSMCs' apoptosis through activation of p38MAPK. (A) Volcano plot of differentially expressed genes between NC and sh‐PCSK9 HC‐VSMCs. (B) KEGG pathway analysis of enriched differentially expressed genes. (C) Heatmap of differentially expressed gene clustering. Red representing highly‐expressed genes and green representing lower expressed genes. (D) The effect of PCSK9 level on activation of p38 was measured by western blot in HC‐VSMCs and HA‐VSMCs. (E) Morphological changes of mitochondria was compared by using Mitotracker (left panel) and quantitative analysis was performed (right panel) when activation of p38 was inhibited in Lenti‐PCSK9 HA‐VSMCs. (F, G) Detection and quantitative analysis of mitochondrial ROS (F) and mitochondrial membrane potential (G), when phosphorylation of p38 was inhibited in Lenti‐PCSK9 HA‐VSMCs. (H) PI staining and quantitative analysis before and after inhibition of p38 in NC and Lenti‐PCSK9 HA‐VSMCs. Hoechst33342 (blue) labels nucleus and PI (red) labels apoptotic cells. AR, aspect ratio. Bar charts show the mean with SD. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001.
    Figure Legend Snippet: PCSK9 regulates morphology, function of mitochondrial and VSMCs' apoptosis through activation of p38MAPK. (A) Volcano plot of differentially expressed genes between NC and sh‐PCSK9 HC‐VSMCs. (B) KEGG pathway analysis of enriched differentially expressed genes. (C) Heatmap of differentially expressed gene clustering. Red representing highly‐expressed genes and green representing lower expressed genes. (D) The effect of PCSK9 level on activation of p38 was measured by western blot in HC‐VSMCs and HA‐VSMCs. (E) Morphological changes of mitochondria was compared by using Mitotracker (left panel) and quantitative analysis was performed (right panel) when activation of p38 was inhibited in Lenti‐PCSK9 HA‐VSMCs. (F, G) Detection and quantitative analysis of mitochondrial ROS (F) and mitochondrial membrane potential (G), when phosphorylation of p38 was inhibited in Lenti‐PCSK9 HA‐VSMCs. (H) PI staining and quantitative analysis before and after inhibition of p38 in NC and Lenti‐PCSK9 HA‐VSMCs. Hoechst33342 (blue) labels nucleus and PI (red) labels apoptotic cells. AR, aspect ratio. Bar charts show the mean with SD. * p < 0.05; ** p < 0.01; *** p < 0.001; **** p < 0.0001.

    Techniques Used: Activation Assay, Western Blot, Membrane, Staining, Inhibition

    Schematic diagram of PCSK9‐mediated mitochondrial dysfunction and apoptosis of VSMCs. In human VSMCs, elevated PCSK9 promotes DRP1 activation through enhancing phosphorylation of p38, which resulted to mitochondrial morphological shift toward fission state, followed by abnormal increase of ROS and leads to mitochondrial dysfunction. The irregular function of mitochondria increases apoptosis of VSMCs, which contributes to formation of vulnerable carotid atherosclerotic plaques. Therefore, the plaques tends to rupture and results to thrombotic events, finally leads to the incidence of ischemic stroke.
    Figure Legend Snippet: Schematic diagram of PCSK9‐mediated mitochondrial dysfunction and apoptosis of VSMCs. In human VSMCs, elevated PCSK9 promotes DRP1 activation through enhancing phosphorylation of p38, which resulted to mitochondrial morphological shift toward fission state, followed by abnormal increase of ROS and leads to mitochondrial dysfunction. The irregular function of mitochondria increases apoptosis of VSMCs, which contributes to formation of vulnerable carotid atherosclerotic plaques. Therefore, the plaques tends to rupture and results to thrombotic events, finally leads to the incidence of ischemic stroke.

    Techniques Used: Activation Assay

    p p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38
    A Immunofluorescence images of p65 nuclear translocation following RANKL stimulation without or with 80 μM Ppg treatment (scale = 100 μM). Cell nuclei were counterstained with DAPI. B NF-κB luciferase assay showing that Ppg inhibited NF-κB transcriptional activity dose-dependently ( n = 3 per group). C , F The expressions of NF-κB and MAPK proteins induced by RANKL in 0–60 mins were assessed by Western blot. D , E The ratios of p-P65/P65 and IκBα/β-actin ( n = 3). G – I The ratios of p-ERK/ERK, p-JNK/JNK, <t>p-P38/P38</t> ( n = 3). Bar graphs are shown as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001 compared with the control group (treated without Ppg).
    P P38, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Periplogenin attenuates LPS-mediated inflammatory osteolysis through the suppression of osteoclastogenesis via reducing the NF-κB and MAPK signaling pathways"

    Article Title: Periplogenin attenuates LPS-mediated inflammatory osteolysis through the suppression of osteoclastogenesis via reducing the NF-κB and MAPK signaling pathways

    Journal: Cell Death Discovery

    doi: 10.1038/s41420-024-01856-0

    A Immunofluorescence images of p65 nuclear translocation following RANKL stimulation without or with 80 μM Ppg treatment (scale = 100 μM). Cell nuclei were counterstained with DAPI. B NF-κB luciferase assay showing that Ppg inhibited NF-κB transcriptional activity dose-dependently ( n = 3 per group). C , F The expressions of NF-κB and MAPK proteins induced by RANKL in 0–60 mins were assessed by Western blot. D , E The ratios of p-P65/P65 and IκBα/β-actin ( n = 3). G – I The ratios of p-ERK/ERK, p-JNK/JNK, p-P38/P38 ( n = 3). Bar graphs are shown as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001 compared with the control group (treated without Ppg).
    Figure Legend Snippet: A Immunofluorescence images of p65 nuclear translocation following RANKL stimulation without or with 80 μM Ppg treatment (scale = 100 μM). Cell nuclei were counterstained with DAPI. B NF-κB luciferase assay showing that Ppg inhibited NF-κB transcriptional activity dose-dependently ( n = 3 per group). C , F The expressions of NF-κB and MAPK proteins induced by RANKL in 0–60 mins were assessed by Western blot. D , E The ratios of p-P65/P65 and IκBα/β-actin ( n = 3). G – I The ratios of p-ERK/ERK, p-JNK/JNK, p-P38/P38 ( n = 3). Bar graphs are shown as mean ± SD. * p < 0.05, ** p < 0.01, *** p < 0.001 compared with the control group (treated without Ppg).

    Techniques Used: Immunofluorescence, Translocation Assay, Luciferase, Activity Assay, Western Blot

    p p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38
    SOX9-mediated the phosphorylation of ERK1/2 but not <t>P38</t> and JNK. ( A ) Volcano plot showing the DEGs with the knockdown of SOX9 in OFs cultured from patients with TED by RNA sequencing ( n = 3). ( B ) Gene Ontology (GO) term enrichment analysis of DEGs. ( C ) Signaling pathways in Kyoto Encyclopedia of Genes and Genomes (KEGG) database enrichment analysis. ( D ) OFs cultured from TED patients were transfected with siRNA or lentivirus prior to stimulation with 10 ng/mL TGF-β1 for 1 hour ( n = 3). Protein levels of p-P38, P38, p-ERK1/2, ERK1/2, p-JNK, JNK, and GAPDH were determined by Western blot. ( E ) Quantification and statistical analysis of relative protein expression. ( F ) SOX9-overexpressing OFs were treated with 10 ng/mL TGF-β1 for 90 minutes with pretreatment with 20 µM U0126 or vehicle (0.1% DMSO) for 1 hour ( n = 3). The expression of ECM-related proteins (α-SMA and CTGF) was detected by western blot assays. ( G ) Quantification and statistical analysis of relative protein expression. * P < 0.05, ** P < 0.01, **** P < 0.0001.
    P P38, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "SOX9 Induces Orbital Fibroblast Activation in Thyroid Eye Disease Via MAPK/ERK1/2 Pathway"

    Article Title: SOX9 Induces Orbital Fibroblast Activation in Thyroid Eye Disease Via MAPK/ERK1/2 Pathway

    Journal: Investigative Ophthalmology & Visual Science

    doi: 10.1167/iovs.65.2.25

    SOX9-mediated the phosphorylation of ERK1/2 but not P38 and JNK. ( A ) Volcano plot showing the DEGs with the knockdown of SOX9 in OFs cultured from patients with TED by RNA sequencing ( n = 3). ( B ) Gene Ontology (GO) term enrichment analysis of DEGs. ( C ) Signaling pathways in Kyoto Encyclopedia of Genes and Genomes (KEGG) database enrichment analysis. ( D ) OFs cultured from TED patients were transfected with siRNA or lentivirus prior to stimulation with 10 ng/mL TGF-β1 for 1 hour ( n = 3). Protein levels of p-P38, P38, p-ERK1/2, ERK1/2, p-JNK, JNK, and GAPDH were determined by Western blot. ( E ) Quantification and statistical analysis of relative protein expression. ( F ) SOX9-overexpressing OFs were treated with 10 ng/mL TGF-β1 for 90 minutes with pretreatment with 20 µM U0126 or vehicle (0.1% DMSO) for 1 hour ( n = 3). The expression of ECM-related proteins (α-SMA and CTGF) was detected by western blot assays. ( G ) Quantification and statistical analysis of relative protein expression. * P < 0.05, ** P < 0.01, **** P < 0.0001.
    Figure Legend Snippet: SOX9-mediated the phosphorylation of ERK1/2 but not P38 and JNK. ( A ) Volcano plot showing the DEGs with the knockdown of SOX9 in OFs cultured from patients with TED by RNA sequencing ( n = 3). ( B ) Gene Ontology (GO) term enrichment analysis of DEGs. ( C ) Signaling pathways in Kyoto Encyclopedia of Genes and Genomes (KEGG) database enrichment analysis. ( D ) OFs cultured from TED patients were transfected with siRNA or lentivirus prior to stimulation with 10 ng/mL TGF-β1 for 1 hour ( n = 3). Protein levels of p-P38, P38, p-ERK1/2, ERK1/2, p-JNK, JNK, and GAPDH were determined by Western blot. ( E ) Quantification and statistical analysis of relative protein expression. ( F ) SOX9-overexpressing OFs were treated with 10 ng/mL TGF-β1 for 90 minutes with pretreatment with 20 µM U0126 or vehicle (0.1% DMSO) for 1 hour ( n = 3). The expression of ECM-related proteins (α-SMA and CTGF) was detected by western blot assays. ( G ) Quantification and statistical analysis of relative protein expression. * P < 0.05, ** P < 0.01, **** P < 0.0001.

    Techniques Used: Cell Culture, RNA Sequencing Assay, Transfection, Western Blot, Expressing

    p p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38
    P P38, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38
    Effects of PQ on the activation of mitogen-activated protein kinases (MAPKs). H4IIE cells were treated with PQ (0.5 mM) for 0.5–1.5 h, and the phosphorylation of JNK, ERK1/2, and <t>p38-MAPK</t> proteins was analyzed by western blotting. Representative images of at least three independent experiments are shown.
    P P38, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Roles of oxidative stress/JNK/ERK signals in paraquat-triggered hepatic apoptosis"

    Article Title: Roles of oxidative stress/JNK/ERK signals in paraquat-triggered hepatic apoptosis

    Journal: Current Research in Toxicology

    doi: 10.1016/j.crtox.2024.100155

    Effects of PQ on the activation of mitogen-activated protein kinases (MAPKs). H4IIE cells were treated with PQ (0.5 mM) for 0.5–1.5 h, and the phosphorylation of JNK, ERK1/2, and p38-MAPK proteins was analyzed by western blotting. Representative images of at least three independent experiments are shown.
    Figure Legend Snippet: Effects of PQ on the activation of mitogen-activated protein kinases (MAPKs). H4IIE cells were treated with PQ (0.5 mM) for 0.5–1.5 h, and the phosphorylation of JNK, ERK1/2, and p38-MAPK proteins was analyzed by western blotting. Representative images of at least three independent experiments are shown.

    Techniques Used: Activation Assay, Western Blot

    p p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38
    P P38, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    p p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc p p38
    P P38, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc p p38 mapk
    Activation of GCN2 by agents that invoke translation inhibition. ( A ) ZAK was deleted by genome editing and CRISPR and WT and ZAK KO cells, designated + and -, respectively, were cultured and ZAK and actin proteins were measured in the prepared lysates by immunoblot analyses with antibodies that specifically recognize each protein. Molecular weight (MW) markers are indicated in kDal. ( B ) WT HEK293T cells (+) and those deleted for ZAK (−) were treated with 1 μM anisomycin (ANS) for 1 h (+) or not treated (−), followed by immunoblot measurements of the phosphorylated and total <t>p38</t> proteins, along with ZAK. ( C ) WT (+, lanes 1–6) and ZAK (−, lanes 7–12) cells were treated with up to 200 nM ANS for 3 h. Levels of the indicated phosphorylated and total proteins were measured by immunoblot analyses. ANS treatment for lanes: 1 and 7 (0 nM, not treated -NT), 2 and 8 (5 nM), 3 and 9 (25 nM), 4 and 10 (50 nM), 5 and 11 (100 nM), and 6 and 12 (200 nM). ( D ) WT (+, lanes 1–5) and ZAK KO (−, lanes 6–10) HEK293T cells were treated with increasing amounts of HF for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). HF treatment for lanes: 1 and 6 (0 nM, not treated -NT), 2 and 7 (5 nM), 3 and 8 (25 nM), 4 and 9 (50 nM), and 5 and 10 (100 nM). Relative levels of P-GCN2 and P-eIF2α normalized for the respectively total protein (P-total) are shown in the bar graph (right panel). The P/total for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. ( E ) WT (+) and ZAK KO (−) HEK293T cells were treated with 25 nM HF, 4 mM histidinol (HIS), or 2 μM borrelidin (BOR) for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). Relative levels of P-GCN2 and P-eIF2α normalized for total levels of the corresponding proteins are shown in the bar graph (right panel). The P/total ratio for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. For panels D and E, statistical significance, denoted by *, was determined using a two-way analysis of variance (ANOVA); * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, **** P ≤ 0.0001. Error bars indicate mean with SD ( n = 3).
    P 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
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    Cell Signaling Technology Inc phosphorylated p38 p p38
    Activation of GCN2 by agents that invoke translation inhibition. ( A ) ZAK was deleted by genome editing and CRISPR and WT and ZAK KO cells, designated + and -, respectively, were cultured and ZAK and actin proteins were measured in the prepared lysates by immunoblot analyses with antibodies that specifically recognize each protein. Molecular weight (MW) markers are indicated in kDal. ( B ) WT HEK293T cells (+) and those deleted for ZAK (−) were treated with 1 μM anisomycin (ANS) for 1 h (+) or not treated (−), followed by immunoblot measurements of the phosphorylated and total <t>p38</t> proteins, along with ZAK. ( C ) WT (+, lanes 1–6) and ZAK (−, lanes 7–12) cells were treated with up to 200 nM ANS for 3 h. Levels of the indicated phosphorylated and total proteins were measured by immunoblot analyses. ANS treatment for lanes: 1 and 7 (0 nM, not treated -NT), 2 and 8 (5 nM), 3 and 9 (25 nM), 4 and 10 (50 nM), 5 and 11 (100 nM), and 6 and 12 (200 nM). ( D ) WT (+, lanes 1–5) and ZAK KO (−, lanes 6–10) HEK293T cells were treated with increasing amounts of HF for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). HF treatment for lanes: 1 and 6 (0 nM, not treated -NT), 2 and 7 (5 nM), 3 and 8 (25 nM), 4 and 9 (50 nM), and 5 and 10 (100 nM). Relative levels of P-GCN2 and P-eIF2α normalized for the respectively total protein (P-total) are shown in the bar graph (right panel). The P/total for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. ( E ) WT (+) and ZAK KO (−) HEK293T cells were treated with 25 nM HF, 4 mM histidinol (HIS), or 2 μM borrelidin (BOR) for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). Relative levels of P-GCN2 and P-eIF2α normalized for total levels of the corresponding proteins are shown in the bar graph (right panel). The P/total ratio for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. For panels D and E, statistical significance, denoted by *, was determined using a two-way analysis of variance (ANOVA); * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, **** P ≤ 0.0001. Error bars indicate mean with SD ( n = 3).
    Phosphorylated P38 P P38, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Activation of GCN2 by agents that invoke translation inhibition. ( A ) ZAK was deleted by genome editing and CRISPR and WT and ZAK KO cells, designated + and -, respectively, were cultured and ZAK and actin proteins were measured in the prepared lysates by immunoblot analyses with antibodies that specifically recognize each protein. Molecular weight (MW) markers are indicated in kDal. ( B ) WT HEK293T cells (+) and those deleted for ZAK (−) were treated with 1 μM anisomycin (ANS) for 1 h (+) or not treated (−), followed by immunoblot measurements of the phosphorylated and total p38 proteins, along with ZAK. ( C ) WT (+, lanes 1–6) and ZAK (−, lanes 7–12) cells were treated with up to 200 nM ANS for 3 h. Levels of the indicated phosphorylated and total proteins were measured by immunoblot analyses. ANS treatment for lanes: 1 and 7 (0 nM, not treated -NT), 2 and 8 (5 nM), 3 and 9 (25 nM), 4 and 10 (50 nM), 5 and 11 (100 nM), and 6 and 12 (200 nM). ( D ) WT (+, lanes 1–5) and ZAK KO (−, lanes 6–10) HEK293T cells were treated with increasing amounts of HF for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). HF treatment for lanes: 1 and 6 (0 nM, not treated -NT), 2 and 7 (5 nM), 3 and 8 (25 nM), 4 and 9 (50 nM), and 5 and 10 (100 nM). Relative levels of P-GCN2 and P-eIF2α normalized for the respectively total protein (P-total) are shown in the bar graph (right panel). The P/total for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. ( E ) WT (+) and ZAK KO (−) HEK293T cells were treated with 25 nM HF, 4 mM histidinol (HIS), or 2 μM borrelidin (BOR) for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). Relative levels of P-GCN2 and P-eIF2α normalized for total levels of the corresponding proteins are shown in the bar graph (right panel). The P/total ratio for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. For panels D and E, statistical significance, denoted by *, was determined using a two-way analysis of variance (ANOVA); * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, **** P ≤ 0.0001. Error bars indicate mean with SD ( n = 3).

    Journal: Nucleic Acids Research

    Article Title: Multiple mechanisms activate GCN2 eIF2 kinase in response to diverse stress conditions

    doi: 10.1093/nar/gkae006

    Figure Lengend Snippet: Activation of GCN2 by agents that invoke translation inhibition. ( A ) ZAK was deleted by genome editing and CRISPR and WT and ZAK KO cells, designated + and -, respectively, were cultured and ZAK and actin proteins were measured in the prepared lysates by immunoblot analyses with antibodies that specifically recognize each protein. Molecular weight (MW) markers are indicated in kDal. ( B ) WT HEK293T cells (+) and those deleted for ZAK (−) were treated with 1 μM anisomycin (ANS) for 1 h (+) or not treated (−), followed by immunoblot measurements of the phosphorylated and total p38 proteins, along with ZAK. ( C ) WT (+, lanes 1–6) and ZAK (−, lanes 7–12) cells were treated with up to 200 nM ANS for 3 h. Levels of the indicated phosphorylated and total proteins were measured by immunoblot analyses. ANS treatment for lanes: 1 and 7 (0 nM, not treated -NT), 2 and 8 (5 nM), 3 and 9 (25 nM), 4 and 10 (50 nM), 5 and 11 (100 nM), and 6 and 12 (200 nM). ( D ) WT (+, lanes 1–5) and ZAK KO (−, lanes 6–10) HEK293T cells were treated with increasing amounts of HF for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). HF treatment for lanes: 1 and 6 (0 nM, not treated -NT), 2 and 7 (5 nM), 3 and 8 (25 nM), 4 and 9 (50 nM), and 5 and 10 (100 nM). Relative levels of P-GCN2 and P-eIF2α normalized for the respectively total protein (P-total) are shown in the bar graph (right panel). The P/total for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. ( E ) WT (+) and ZAK KO (−) HEK293T cells were treated with 25 nM HF, 4 mM histidinol (HIS), or 2 μM borrelidin (BOR) for 3 h, followed by immunoblot measurements of the indicated phosphorylated and total proteins (left panel). Relative levels of P-GCN2 and P-eIF2α normalized for total levels of the corresponding proteins are shown in the bar graph (right panel). The P/total ratio for GCN2 and eIF2α proteins was normalized to the respective NT-WT group and presented as fold change. For panels D and E, statistical significance, denoted by *, was determined using a two-way analysis of variance (ANOVA); * P ≤ 0.05, ** P ≤ 0.01, *** P ≤ 0.001, **** P ≤ 0.0001. Error bars indicate mean with SD ( n = 3).

    Article Snippet: Target proteins and their primary antibodies with vendor information and experimental dilutions that were used in the immunoblot analyses include ZAK 1:1000 (Bethyl, #A301-993A), P-GCN2 (T899) 1:1000 (Abcam, #75836), total GCN2 1:1000 (Cell Signaling, #3302), P-eIF2α (S51) 1:1000 (Abcam, #32157), total eIF2α 1:1000 (Cell Signaling, #5342), P-p38 MAPK 1:2000 (Cell Signaling, #4511S), total p38 MAPK 1:2000 (Cell Signaling, #8690S), CReP 1:1000 (Proteintech, # 14634-1-AP), Actin 1:5000 (Sigma, #A5441).

    Techniques: Activation Assay, Inhibition, CRISPR, Cell Culture, Western Blot, Molecular Weight