anti phospho p38 p p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho p38 p p38
    The mechanism how interleukin‐38 suppresses macrophage activation. (a) Representative western blot analysis of <t>p‐p38,</t> p38, p‐JNK, and JNK in the aortic wall on day 14. (b) Bar graphs showing the relative densitometry of p‐p38 ( n = 6, p = 0.0280 [ t test], p = 0.0411 [Mann–Whitney U test]) and p‐JNK ( n = 6, p = 0.6893 [ t test], p = 0.6991 [Mann–Whitney U test]). (c) Representative western blot analysis of p‐p38, p38, p‐JNK, and JNK in macrophages after TNF‐α stimulation with or without IL‐38. (d) Bar graphs showing the relative densitometry of p‐p38 ( n = 6, p < 0.0001 [ANOVA], p < 0.0001 [post hoc, Control vs. TNF‐α], p = 0.0234 [post hoc, Control vs. TNF‐α + IL‐38], p = 0.0125 [post hoc, TNF‐α vs. TNF‐α + IL‐38]) and p‐JNK ( n = 6, p = 0.0283 [ANOVA], p = 0.0264 [post hoc, Control vs. TNF‐α]). (e) Representative western blot analysis of iNOS, MMP‐9, MMP‐2, and GAPDH in macrophages after TNF‐α stimulation with or without IL‐38 in the presence of SB203580. (f) Bar graphs showing the relative densitometry of iNOS ( n = 3, p = 0.2000 [Mann–Whitney U test]), MMP‐9 ( n = 3, p = 0.7000 [Mann–Whitney U test]), and MMP‐2 ( n = 3, p = 0.7000 [Mann–Whitney U test]). (g) Representative photomicrographs of the aortic wall on day 14 in the presence of SB203580, stained with EVG (upper row) or anti‐CD68 antibody (lower row). (h) Bar graph showing the number of CD68 + cells in the aortic wall on day 14 in the presence of SB203580 ( n = 5–6, p = 0.6623 [Mann–Whitney U test]). (i) Bar graphs showing the aorta diameter ( n = 5–6, p = 0.2468 [Mann–Whitney U test]), AAA incidence ( n = 5–6, p = 0.2506 [χ 2 test]), adventitia ( n = 5–6, p > 0.9999 [Mann–Whitney U test]), intramedia ( n = 5–6, p = 0.1710 [Mann–Whitney U test]), and elastin degradation score ( n = 5–6, p = 0.4917 [ t test], p = 0.6753 [Mann–Whitney U test]) on day 14 in the presence of SB203580.
    Anti Phospho 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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    1) Product Images from "Interleukin‐38 suppresses abdominal aortic aneurysm formation in mice by regulating macrophages in an IL1RL2 ‐p38 pathway‐dependent manner"

    Article Title: Interleukin‐38 suppresses abdominal aortic aneurysm formation in mice by regulating macrophages in an IL1RL2 ‐p38 pathway‐dependent manner

    Journal: Physiological Reports

    doi: 10.14814/phy2.15581

    The mechanism how interleukin‐38 suppresses macrophage activation. (a) Representative western blot analysis of p‐p38, p38, p‐JNK, and JNK in the aortic wall on day 14. (b) Bar graphs showing the relative densitometry of p‐p38 ( n = 6, p = 0.0280 [ t test], p = 0.0411 [Mann–Whitney U test]) and p‐JNK ( n = 6, p = 0.6893 [ t test], p = 0.6991 [Mann–Whitney U test]). (c) Representative western blot analysis of p‐p38, p38, p‐JNK, and JNK in macrophages after TNF‐α stimulation with or without IL‐38. (d) Bar graphs showing the relative densitometry of p‐p38 ( n = 6, p < 0.0001 [ANOVA], p < 0.0001 [post hoc, Control vs. TNF‐α], p = 0.0234 [post hoc, Control vs. TNF‐α + IL‐38], p = 0.0125 [post hoc, TNF‐α vs. TNF‐α + IL‐38]) and p‐JNK ( n = 6, p = 0.0283 [ANOVA], p = 0.0264 [post hoc, Control vs. TNF‐α]). (e) Representative western blot analysis of iNOS, MMP‐9, MMP‐2, and GAPDH in macrophages after TNF‐α stimulation with or without IL‐38 in the presence of SB203580. (f) Bar graphs showing the relative densitometry of iNOS ( n = 3, p = 0.2000 [Mann–Whitney U test]), MMP‐9 ( n = 3, p = 0.7000 [Mann–Whitney U test]), and MMP‐2 ( n = 3, p = 0.7000 [Mann–Whitney U test]). (g) Representative photomicrographs of the aortic wall on day 14 in the presence of SB203580, stained with EVG (upper row) or anti‐CD68 antibody (lower row). (h) Bar graph showing the number of CD68 + cells in the aortic wall on day 14 in the presence of SB203580 ( n = 5–6, p = 0.6623 [Mann–Whitney U test]). (i) Bar graphs showing the aorta diameter ( n = 5–6, p = 0.2468 [Mann–Whitney U test]), AAA incidence ( n = 5–6, p = 0.2506 [χ 2 test]), adventitia ( n = 5–6, p > 0.9999 [Mann–Whitney U test]), intramedia ( n = 5–6, p = 0.1710 [Mann–Whitney U test]), and elastin degradation score ( n = 5–6, p = 0.4917 [ t test], p = 0.6753 [Mann–Whitney U test]) on day 14 in the presence of SB203580.
    Figure Legend Snippet: The mechanism how interleukin‐38 suppresses macrophage activation. (a) Representative western blot analysis of p‐p38, p38, p‐JNK, and JNK in the aortic wall on day 14. (b) Bar graphs showing the relative densitometry of p‐p38 ( n = 6, p = 0.0280 [ t test], p = 0.0411 [Mann–Whitney U test]) and p‐JNK ( n = 6, p = 0.6893 [ t test], p = 0.6991 [Mann–Whitney U test]). (c) Representative western blot analysis of p‐p38, p38, p‐JNK, and JNK in macrophages after TNF‐α stimulation with or without IL‐38. (d) Bar graphs showing the relative densitometry of p‐p38 ( n = 6, p < 0.0001 [ANOVA], p < 0.0001 [post hoc, Control vs. TNF‐α], p = 0.0234 [post hoc, Control vs. TNF‐α + IL‐38], p = 0.0125 [post hoc, TNF‐α vs. TNF‐α + IL‐38]) and p‐JNK ( n = 6, p = 0.0283 [ANOVA], p = 0.0264 [post hoc, Control vs. TNF‐α]). (e) Representative western blot analysis of iNOS, MMP‐9, MMP‐2, and GAPDH in macrophages after TNF‐α stimulation with or without IL‐38 in the presence of SB203580. (f) Bar graphs showing the relative densitometry of iNOS ( n = 3, p = 0.2000 [Mann–Whitney U test]), MMP‐9 ( n = 3, p = 0.7000 [Mann–Whitney U test]), and MMP‐2 ( n = 3, p = 0.7000 [Mann–Whitney U test]). (g) Representative photomicrographs of the aortic wall on day 14 in the presence of SB203580, stained with EVG (upper row) or anti‐CD68 antibody (lower row). (h) Bar graph showing the number of CD68 + cells in the aortic wall on day 14 in the presence of SB203580 ( n = 5–6, p = 0.6623 [Mann–Whitney U test]). (i) Bar graphs showing the aorta diameter ( n = 5–6, p = 0.2468 [Mann–Whitney U test]), AAA incidence ( n = 5–6, p = 0.2506 [χ 2 test]), adventitia ( n = 5–6, p > 0.9999 [Mann–Whitney U test]), intramedia ( n = 5–6, p = 0.1710 [Mann–Whitney U test]), and elastin degradation score ( n = 5–6, p = 0.4917 [ t test], p = 0.6753 [Mann–Whitney U test]) on day 14 in the presence of SB203580.

    Techniques Used: Activation Assay, Western Blot, MANN-WHITNEY, Staining

    anti phospho p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho p38 mapk
    (A) Protein expression of different human PKC isoforms in the membrane and cytosol fractions of different HEK293 transfected cell lines (with or without treatment of ANGII). GC-A and NaK-ATPase serve as quality control for the separation of membrane and cytosol fractions. GAPDH serves as loading control. (B) Protein expression of phosphorylated PKC substrates, phosphorylated <t>p38</t> <t>MAPK,</t> and <t>p38</t> <t>MAPK</t> in HEK293/GC-A + /AT 1 + cells treated with different PKC modulators. GAPDH serves as loading control. PMA, phorbol 12-myristate 13-acetate. (C) In vitro cGMP generation in HEK293/GC-A + /AT 1 + in response to ANP (10 −8 M) with or without ANGII (10 −8 M) and valsartan (1 μM) or Go6983 (5 μM). Values of cGMP were normalized to vehicle group (blue) under ANP treatment. * indicates P <0.05, one-way ANOVA with Dunnett multiple comparisons test. (D) Hypothetical mechanism underlying the crosstalk between ANGII and GC-A derived from our in vitro studies.
    Anti Phospho 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 "EVIDENCE FOR ANGIOTENSIN II AS A NATURALLY EXISTING SUPPRESSOR FOR THE NATRIURETIC PEPTIDE SYSTEM"

    Article Title: EVIDENCE FOR ANGIOTENSIN II AS A NATURALLY EXISTING SUPPRESSOR FOR THE NATRIURETIC PEPTIDE SYSTEM

    Journal: bioRxiv

    doi: 10.1101/2023.01.26.525806

    (A) Protein expression of different human PKC isoforms in the membrane and cytosol fractions of different HEK293 transfected cell lines (with or without treatment of ANGII). GC-A and NaK-ATPase serve as quality control for the separation of membrane and cytosol fractions. GAPDH serves as loading control. (B) Protein expression of phosphorylated PKC substrates, phosphorylated p38 MAPK, and p38 MAPK in HEK293/GC-A + /AT 1 + cells treated with different PKC modulators. GAPDH serves as loading control. PMA, phorbol 12-myristate 13-acetate. (C) In vitro cGMP generation in HEK293/GC-A + /AT 1 + in response to ANP (10 −8 M) with or without ANGII (10 −8 M) and valsartan (1 μM) or Go6983 (5 μM). Values of cGMP were normalized to vehicle group (blue) under ANP treatment. * indicates P <0.05, one-way ANOVA with Dunnett multiple comparisons test. (D) Hypothetical mechanism underlying the crosstalk between ANGII and GC-A derived from our in vitro studies.
    Figure Legend Snippet: (A) Protein expression of different human PKC isoforms in the membrane and cytosol fractions of different HEK293 transfected cell lines (with or without treatment of ANGII). GC-A and NaK-ATPase serve as quality control for the separation of membrane and cytosol fractions. GAPDH serves as loading control. (B) Protein expression of phosphorylated PKC substrates, phosphorylated p38 MAPK, and p38 MAPK in HEK293/GC-A + /AT 1 + cells treated with different PKC modulators. GAPDH serves as loading control. PMA, phorbol 12-myristate 13-acetate. (C) In vitro cGMP generation in HEK293/GC-A + /AT 1 + in response to ANP (10 −8 M) with or without ANGII (10 −8 M) and valsartan (1 μM) or Go6983 (5 μM). Values of cGMP were normalized to vehicle group (blue) under ANP treatment. * indicates P <0.05, one-way ANOVA with Dunnett multiple comparisons test. (D) Hypothetical mechanism underlying the crosstalk between ANGII and GC-A derived from our in vitro studies.

    Techniques Used: Expressing, Transfection, In Vitro, Derivative Assay

    phospho p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38
    Details of the antibodies used in this study.
    Phospho 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 "Clonorchis sinensis aggravates biliary fibrosis through promoting IL-6 production via toll-like receptor 2-mediated AKT and p38 signal pathways"

    Article Title: Clonorchis sinensis aggravates biliary fibrosis through promoting IL-6 production via toll-like receptor 2-mediated AKT and p38 signal pathways

    Journal: PLOS Neglected Tropical Diseases

    doi: 10.1371/journal.pntd.0011062

    Details of the antibodies used in this study.
    Figure Legend Snippet: Details of the antibodies used in this study.

    Techniques Used:

    (A, B) The phosphorylation of AKT, p65, ERK and p38 in liver were analyzed by Western blot. (C, D) 3 × 10 5 WT and TLR2 -/- mouse BECs were cultivated with C . sinensis ESPs (50 μg/mL) for 120 min, the cells were lysed in cells lysates and the phosphorylation of AKT, p65, ERK and p38 were analyzed by Western blot. (E) The production levels of IL-6 in the supernatant of BECs pretreated with or without AKT inhibitor, p38 inhibitor and ERK inhibitor for 1 h, then co-cultured with ESPs for 18 h were measured by ELISA.
    Figure Legend Snippet: (A, B) The phosphorylation of AKT, p65, ERK and p38 in liver were analyzed by Western blot. (C, D) 3 × 10 5 WT and TLR2 -/- mouse BECs were cultivated with C . sinensis ESPs (50 μg/mL) for 120 min, the cells were lysed in cells lysates and the phosphorylation of AKT, p65, ERK and p38 were analyzed by Western blot. (E) The production levels of IL-6 in the supernatant of BECs pretreated with or without AKT inhibitor, p38 inhibitor and ERK inhibitor for 1 h, then co-cultured with ESPs for 18 h were measured by ELISA.

    Techniques Used: Western Blot, Cell Culture, Enzyme-linked Immunosorbent Assay

    C . sinensis triggered AKT and p38 signal pathways dependent on TLR2 of BECs to promote the production of IL-6, which subsequently activated TGF-β1-Smad2/Smad3 pathways, myofibroblasts and up-regulated the expression of ECMs, finally resulting in biliary fibrosis in mice. In the figure, ‘ ↑ ’indicates positive regulation.
    Figure Legend Snippet: C . sinensis triggered AKT and p38 signal pathways dependent on TLR2 of BECs to promote the production of IL-6, which subsequently activated TGF-β1-Smad2/Smad3 pathways, myofibroblasts and up-regulated the expression of ECMs, finally resulting in biliary fibrosis in mice. In the figure, ‘ ↑ ’indicates positive regulation.

    Techniques Used: Expressing

    phospho p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38
    Phospho 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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    rabbit anti phospho p38 antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc rabbit anti phospho p38 antibody
    Rabbit Anti Phospho P38 Antibody, 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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    phospho p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38 mapk
    Phospho 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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    anti phospho p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti phospho p38
    Anti Phospho 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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    phospho p38 thr180 tyr182 antibody  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38 thr180 tyr182 antibody
    Phospho P38 Thr180 Tyr182 Antibody, 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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    phospho p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38
    Luteolin combined with asiatic acid induced apoptosis through inhibition of PI3K/AKT and regulation of MAPKs pathways in cervical cancer cells. Western blotting was used to detect PIK3CA, p-AKT, AKT, p-70S6K, 70S6K, <t>p-p38,</t> p38, p-ERK1/2, ERK1/2, p-JNK1/2 and JNK1/2 levels in CaSki ( A ) and HeLa ( B ) cells treated with Lut (50 μM) or AsA (50 μM) alone or in combination for 24 h. GAPDH served as the loading control. Quantitative results are shown in the lower plot. Values represent mean ± SD from three replicates. *, † and δ p ˂ 0.05 compared with CON, L50- or A50-treated group. CON, 0.1% DMSO; L50, 50 μM luteolin; A50, 50 μM asiatic acid; Comb., 50 μM luteolin + 50 μM asiatic acid.
    Phospho 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 "Synergistic Combination of Luteolin and Asiatic Acid on Cervical Cancer In Vitro and In Vivo"

    Article Title: Synergistic Combination of Luteolin and Asiatic Acid on Cervical Cancer In Vitro and In Vivo

    Journal: Cancers

    doi: 10.3390/cancers15020548

    Luteolin combined with asiatic acid induced apoptosis through inhibition of PI3K/AKT and regulation of MAPKs pathways in cervical cancer cells. Western blotting was used to detect PIK3CA, p-AKT, AKT, p-70S6K, 70S6K, p-p38, p38, p-ERK1/2, ERK1/2, p-JNK1/2 and JNK1/2 levels in CaSki ( A ) and HeLa ( B ) cells treated with Lut (50 μM) or AsA (50 μM) alone or in combination for 24 h. GAPDH served as the loading control. Quantitative results are shown in the lower plot. Values represent mean ± SD from three replicates. *, † and δ p ˂ 0.05 compared with CON, L50- or A50-treated group. CON, 0.1% DMSO; L50, 50 μM luteolin; A50, 50 μM asiatic acid; Comb., 50 μM luteolin + 50 μM asiatic acid.
    Figure Legend Snippet: Luteolin combined with asiatic acid induced apoptosis through inhibition of PI3K/AKT and regulation of MAPKs pathways in cervical cancer cells. Western blotting was used to detect PIK3CA, p-AKT, AKT, p-70S6K, 70S6K, p-p38, p38, p-ERK1/2, ERK1/2, p-JNK1/2 and JNK1/2 levels in CaSki ( A ) and HeLa ( B ) cells treated with Lut (50 μM) or AsA (50 μM) alone or in combination for 24 h. GAPDH served as the loading control. Quantitative results are shown in the lower plot. Values represent mean ± SD from three replicates. *, † and δ p ˂ 0.05 compared with CON, L50- or A50-treated group. CON, 0.1% DMSO; L50, 50 μM luteolin; A50, 50 μM asiatic acid; Comb., 50 μM luteolin + 50 μM asiatic acid.

    Techniques Used: Inhibition, Western Blot

    z-VAD-fmk altered apoptosis-related protein expressions. CaSki and HeLa cells were pretreated with z-VAD-fmk (2.5 μM) for 2 h and then treated with or without Lut (50 μM) and AsA (50 μM) for 24 h. CaSki ( A ) and HeLa ( B ) cell viabilities were examined using a CCK-8 assay. The expressions of PARP-1, Bcl-2, caspase-3, p-p38 and p38 were detected through western blotting. GAPDH served as the loading control. Quantitative results are shown in the lower plot. Values represent mean ± SD from three replicates. * and † p ˂ 0.05 compared with CON or AsA + Lut-treated group. CON, 0.1% DMSO; Comb., 50 μM luteolin + 50 μM asiatic acid; Comb. + z-VAD, 50 μM luteolin + 50 μM asiatic acid + 2.5 μM z-VAD-fmk.
    Figure Legend Snippet: z-VAD-fmk altered apoptosis-related protein expressions. CaSki and HeLa cells were pretreated with z-VAD-fmk (2.5 μM) for 2 h and then treated with or without Lut (50 μM) and AsA (50 μM) for 24 h. CaSki ( A ) and HeLa ( B ) cell viabilities were examined using a CCK-8 assay. The expressions of PARP-1, Bcl-2, caspase-3, p-p38 and p38 were detected through western blotting. GAPDH served as the loading control. Quantitative results are shown in the lower plot. Values represent mean ± SD from three replicates. * and † p ˂ 0.05 compared with CON or AsA + Lut-treated group. CON, 0.1% DMSO; Comb., 50 μM luteolin + 50 μM asiatic acid; Comb. + z-VAD, 50 μM luteolin + 50 μM asiatic acid + 2.5 μM z-VAD-fmk.

    Techniques Used: CCK-8 Assay, Western Blot

    Schematic diagram of luteolin combined with asiatic acid’s anticancer molecular mechanism in cervical cancer. Lut combined with AsA mainly modulates FAK signaling (integrin β1, paxillin and FAK) and PI3K/AKT signaling (PI3K, AKT and p70S6K) and causes JNK/p38 downregulation and ERK upregulation, inactivating or activating various signaling targets, such as Bcl2, Bax, mitROS, caspase-3 and RARP1; this leads to the induction of caspase-mediated intrinsic apoptosis, sub-G1 phase arrest and inhibition of cancer cell migration, which increase the anticancer effect on cervical cancer.
    Figure Legend Snippet: Schematic diagram of luteolin combined with asiatic acid’s anticancer molecular mechanism in cervical cancer. Lut combined with AsA mainly modulates FAK signaling (integrin β1, paxillin and FAK) and PI3K/AKT signaling (PI3K, AKT and p70S6K) and causes JNK/p38 downregulation and ERK upregulation, inactivating or activating various signaling targets, such as Bcl2, Bax, mitROS, caspase-3 and RARP1; this leads to the induction of caspase-mediated intrinsic apoptosis, sub-G1 phase arrest and inhibition of cancer cell migration, which increase the anticancer effect on cervical cancer.

    Techniques Used: Inhibition, Migration

    phospho p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phospho p38
    Phospho 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 anti phospho p38 p p38
    The mechanism how interleukin‐38 suppresses macrophage activation. (a) Representative western blot analysis of <t>p‐p38,</t> p38, p‐JNK, and JNK in the aortic wall on day 14. (b) Bar graphs showing the relative densitometry of p‐p38 ( n = 6, p = 0.0280 [ t test], p = 0.0411 [Mann–Whitney U test]) and p‐JNK ( n = 6, p = 0.6893 [ t test], p = 0.6991 [Mann–Whitney U test]). (c) Representative western blot analysis of p‐p38, p38, p‐JNK, and JNK in macrophages after TNF‐α stimulation with or without IL‐38. (d) Bar graphs showing the relative densitometry of p‐p38 ( n = 6, p < 0.0001 [ANOVA], p < 0.0001 [post hoc, Control vs. TNF‐α], p = 0.0234 [post hoc, Control vs. TNF‐α + IL‐38], p = 0.0125 [post hoc, TNF‐α vs. TNF‐α + IL‐38]) and p‐JNK ( n = 6, p = 0.0283 [ANOVA], p = 0.0264 [post hoc, Control vs. TNF‐α]). (e) Representative western blot analysis of iNOS, MMP‐9, MMP‐2, and GAPDH in macrophages after TNF‐α stimulation with or without IL‐38 in the presence of SB203580. (f) Bar graphs showing the relative densitometry of iNOS ( n = 3, p = 0.2000 [Mann–Whitney U test]), MMP‐9 ( n = 3, p = 0.7000 [Mann–Whitney U test]), and MMP‐2 ( n = 3, p = 0.7000 [Mann–Whitney U test]). (g) Representative photomicrographs of the aortic wall on day 14 in the presence of SB203580, stained with EVG (upper row) or anti‐CD68 antibody (lower row). (h) Bar graph showing the number of CD68 + cells in the aortic wall on day 14 in the presence of SB203580 ( n = 5–6, p = 0.6623 [Mann–Whitney U test]). (i) Bar graphs showing the aorta diameter ( n = 5–6, p = 0.2468 [Mann–Whitney U test]), AAA incidence ( n = 5–6, p = 0.2506 [χ 2 test]), adventitia ( n = 5–6, p > 0.9999 [Mann–Whitney U test]), intramedia ( n = 5–6, p = 0.1710 [Mann–Whitney U test]), and elastin degradation score ( n = 5–6, p = 0.4917 [ t test], p = 0.6753 [Mann–Whitney U test]) on day 14 in the presence of SB203580.
    Anti Phospho 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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    (A) Protein expression of different human PKC isoforms in the membrane and cytosol fractions of different HEK293 transfected cell lines (with or without treatment of ANGII). GC-A and NaK-ATPase serve as quality control for the separation of membrane and cytosol fractions. GAPDH serves as loading control. (B) Protein expression of phosphorylated PKC substrates, phosphorylated <t>p38</t> <t>MAPK,</t> and <t>p38</t> <t>MAPK</t> in HEK293/GC-A + /AT 1 + cells treated with different PKC modulators. GAPDH serves as loading control. PMA, phorbol 12-myristate 13-acetate. (C) In vitro cGMP generation in HEK293/GC-A + /AT 1 + in response to ANP (10 −8 M) with or without ANGII (10 −8 M) and valsartan (1 μM) or Go6983 (5 μM). Values of cGMP were normalized to vehicle group (blue) under ANP treatment. * indicates P <0.05, one-way ANOVA with Dunnett multiple comparisons test. (D) Hypothetical mechanism underlying the crosstalk between ANGII and GC-A derived from our in vitro studies.
    Anti Phospho 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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    Details of the antibodies used in this study.
    Phospho 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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    Details of the antibodies used in this study.
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    Details of the antibodies used in this study.
    Phospho 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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    Details of the antibodies used in this study.
    Anti Phospho 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


    The mechanism how interleukin‐38 suppresses macrophage activation. (a) Representative western blot analysis of p‐p38, p38, p‐JNK, and JNK in the aortic wall on day 14. (b) Bar graphs showing the relative densitometry of p‐p38 ( n = 6, p = 0.0280 [ t test], p = 0.0411 [Mann–Whitney U test]) and p‐JNK ( n = 6, p = 0.6893 [ t test], p = 0.6991 [Mann–Whitney U test]). (c) Representative western blot analysis of p‐p38, p38, p‐JNK, and JNK in macrophages after TNF‐α stimulation with or without IL‐38. (d) Bar graphs showing the relative densitometry of p‐p38 ( n = 6, p < 0.0001 [ANOVA], p < 0.0001 [post hoc, Control vs. TNF‐α], p = 0.0234 [post hoc, Control vs. TNF‐α + IL‐38], p = 0.0125 [post hoc, TNF‐α vs. TNF‐α + IL‐38]) and p‐JNK ( n = 6, p = 0.0283 [ANOVA], p = 0.0264 [post hoc, Control vs. TNF‐α]). (e) Representative western blot analysis of iNOS, MMP‐9, MMP‐2, and GAPDH in macrophages after TNF‐α stimulation with or without IL‐38 in the presence of SB203580. (f) Bar graphs showing the relative densitometry of iNOS ( n = 3, p = 0.2000 [Mann–Whitney U test]), MMP‐9 ( n = 3, p = 0.7000 [Mann–Whitney U test]), and MMP‐2 ( n = 3, p = 0.7000 [Mann–Whitney U test]). (g) Representative photomicrographs of the aortic wall on day 14 in the presence of SB203580, stained with EVG (upper row) or anti‐CD68 antibody (lower row). (h) Bar graph showing the number of CD68 + cells in the aortic wall on day 14 in the presence of SB203580 ( n = 5–6, p = 0.6623 [Mann–Whitney U test]). (i) Bar graphs showing the aorta diameter ( n = 5–6, p = 0.2468 [Mann–Whitney U test]), AAA incidence ( n = 5–6, p = 0.2506 [χ 2 test]), adventitia ( n = 5–6, p > 0.9999 [Mann–Whitney U test]), intramedia ( n = 5–6, p = 0.1710 [Mann–Whitney U test]), and elastin degradation score ( n = 5–6, p = 0.4917 [ t test], p = 0.6753 [Mann–Whitney U test]) on day 14 in the presence of SB203580.

    Journal: Physiological Reports

    Article Title: Interleukin‐38 suppresses abdominal aortic aneurysm formation in mice by regulating macrophages in an IL1RL2 ‐p38 pathway‐dependent manner

    doi: 10.14814/phy2.15581

    Figure Lengend Snippet: The mechanism how interleukin‐38 suppresses macrophage activation. (a) Representative western blot analysis of p‐p38, p38, p‐JNK, and JNK in the aortic wall on day 14. (b) Bar graphs showing the relative densitometry of p‐p38 ( n = 6, p = 0.0280 [ t test], p = 0.0411 [Mann–Whitney U test]) and p‐JNK ( n = 6, p = 0.6893 [ t test], p = 0.6991 [Mann–Whitney U test]). (c) Representative western blot analysis of p‐p38, p38, p‐JNK, and JNK in macrophages after TNF‐α stimulation with or without IL‐38. (d) Bar graphs showing the relative densitometry of p‐p38 ( n = 6, p < 0.0001 [ANOVA], p < 0.0001 [post hoc, Control vs. TNF‐α], p = 0.0234 [post hoc, Control vs. TNF‐α + IL‐38], p = 0.0125 [post hoc, TNF‐α vs. TNF‐α + IL‐38]) and p‐JNK ( n = 6, p = 0.0283 [ANOVA], p = 0.0264 [post hoc, Control vs. TNF‐α]). (e) Representative western blot analysis of iNOS, MMP‐9, MMP‐2, and GAPDH in macrophages after TNF‐α stimulation with or without IL‐38 in the presence of SB203580. (f) Bar graphs showing the relative densitometry of iNOS ( n = 3, p = 0.2000 [Mann–Whitney U test]), MMP‐9 ( n = 3, p = 0.7000 [Mann–Whitney U test]), and MMP‐2 ( n = 3, p = 0.7000 [Mann–Whitney U test]). (g) Representative photomicrographs of the aortic wall on day 14 in the presence of SB203580, stained with EVG (upper row) or anti‐CD68 antibody (lower row). (h) Bar graph showing the number of CD68 + cells in the aortic wall on day 14 in the presence of SB203580 ( n = 5–6, p = 0.6623 [Mann–Whitney U test]). (i) Bar graphs showing the aorta diameter ( n = 5–6, p = 0.2468 [Mann–Whitney U test]), AAA incidence ( n = 5–6, p = 0.2506 [χ 2 test]), adventitia ( n = 5–6, p > 0.9999 [Mann–Whitney U test]), intramedia ( n = 5–6, p = 0.1710 [Mann–Whitney U test]), and elastin degradation score ( n = 5–6, p = 0.4917 [ t test], p = 0.6753 [Mann–Whitney U test]) on day 14 in the presence of SB203580.

    Article Snippet: Primary antibodies included anti‐TNF‐α (rabbit monoclonal, dilution 1:400, #11948; Cell Signaling Technology), anti‐iNOS (rabbit monoclonal, dilution 1:400, #13120; Cell Signaling Technology), anti‐ MMP‐9 (rabbit polyclonal, dilution 1:1000, #ab38898; abcam), anti‐ MMP‐2 (rabbit polyclonal, dilution 1:1000, #ab97779; abcam), anti‐IL1RL2 (rabbit polyclonal, dilution 1:1000, # PA5‐38013; Invitrogen), anti‐p38 (rabbit polyclonal, dilution 1:5000, #9212; Cell signaling technology), anti‐phospho‐p38 (p‐p38) (rabbit polyclonal, dilution 1:1000, #9211; Cell signaling technology), anti‐JNK (rabbit polyclonal, dilution 1:5000, #9252; Cell signaling technology) and anti‐phospho‐JNK (p‐JNK) (rabbit polyclonal, dilution 1:1000, #9251; Cell signaling technology).

    Techniques: Activation Assay, Western Blot, MANN-WHITNEY, Staining

    (A) Protein expression of different human PKC isoforms in the membrane and cytosol fractions of different HEK293 transfected cell lines (with or without treatment of ANGII). GC-A and NaK-ATPase serve as quality control for the separation of membrane and cytosol fractions. GAPDH serves as loading control. (B) Protein expression of phosphorylated PKC substrates, phosphorylated p38 MAPK, and p38 MAPK in HEK293/GC-A + /AT 1 + cells treated with different PKC modulators. GAPDH serves as loading control. PMA, phorbol 12-myristate 13-acetate. (C) In vitro cGMP generation in HEK293/GC-A + /AT 1 + in response to ANP (10 −8 M) with or without ANGII (10 −8 M) and valsartan (1 μM) or Go6983 (5 μM). Values of cGMP were normalized to vehicle group (blue) under ANP treatment. * indicates P <0.05, one-way ANOVA with Dunnett multiple comparisons test. (D) Hypothetical mechanism underlying the crosstalk between ANGII and GC-A derived from our in vitro studies.

    Journal: bioRxiv

    Article Title: EVIDENCE FOR ANGIOTENSIN II AS A NATURALLY EXISTING SUPPRESSOR FOR THE NATRIURETIC PEPTIDE SYSTEM

    doi: 10.1101/2023.01.26.525806

    Figure Lengend Snippet: (A) Protein expression of different human PKC isoforms in the membrane and cytosol fractions of different HEK293 transfected cell lines (with or without treatment of ANGII). GC-A and NaK-ATPase serve as quality control for the separation of membrane and cytosol fractions. GAPDH serves as loading control. (B) Protein expression of phosphorylated PKC substrates, phosphorylated p38 MAPK, and p38 MAPK in HEK293/GC-A + /AT 1 + cells treated with different PKC modulators. GAPDH serves as loading control. PMA, phorbol 12-myristate 13-acetate. (C) In vitro cGMP generation in HEK293/GC-A + /AT 1 + in response to ANP (10 −8 M) with or without ANGII (10 −8 M) and valsartan (1 μM) or Go6983 (5 μM). Values of cGMP were normalized to vehicle group (blue) under ANP treatment. * indicates P <0.05, one-way ANOVA with Dunnett multiple comparisons test. (D) Hypothetical mechanism underlying the crosstalk between ANGII and GC-A derived from our in vitro studies.

    Article Snippet: The following primary antibodies were used: anti-GCA (catalog#MAB48601, R&D System, Minneapolis, MN) at 1:1000 dilution, anti-GCB (catalog#55113-1-AP, Proteintech, Rosemont, IL) at 1:200 dilution, anti-GFP (catalog#TA150041, OriGene, Rockville, MD) at 1:1000 dilution, anti-PKCα (catalog#2056, Cell Signaling Technology, Danvers, MA) at 1:500 dilution, anti-PKCε (catalog#2683, Cell Signaling Technology, Danvers, MA) at 1:1000 dilution, anti-Phspho-(Ser) PKC Substrate (catalog#2261, Cell Signaling Technology, Danvers, MA) at 1:1000 dilution, anti-NaK-ATPase (catalog#EP1845Y, abcam, Waltham, MA) at 1:2000 dilution, anti-p38 MAPK (catalog#8690, Cell Signaling Technology, Danvers, MA) at 1:1000 dilution, anti-Phospho-p38 MAPK (catalog#4511, Cell Signaling Technology, Danvers, MA) at 1:1000 dilution, and anti-GAPDH (catalog#2118, Cell Signaling Technology, Danvers, MA) at 1:5000 dilution.

    Techniques: Expressing, Transfection, In Vitro, Derivative Assay

    Details of the antibodies used in this study.

    Journal: PLOS Neglected Tropical Diseases

    Article Title: Clonorchis sinensis aggravates biliary fibrosis through promoting IL-6 production via toll-like receptor 2-mediated AKT and p38 signal pathways

    doi: 10.1371/journal.pntd.0011062

    Figure Lengend Snippet: Details of the antibodies used in this study.

    Article Snippet: Phospho-p38 , Rabbit monoclonal , Rabbit IgG , 1:1000 , Cell Signaling Technology.

    Techniques:

    (A, B) The phosphorylation of AKT, p65, ERK and p38 in liver were analyzed by Western blot. (C, D) 3 × 10 5 WT and TLR2 -/- mouse BECs were cultivated with C . sinensis ESPs (50 μg/mL) for 120 min, the cells were lysed in cells lysates and the phosphorylation of AKT, p65, ERK and p38 were analyzed by Western blot. (E) The production levels of IL-6 in the supernatant of BECs pretreated with or without AKT inhibitor, p38 inhibitor and ERK inhibitor for 1 h, then co-cultured with ESPs for 18 h were measured by ELISA.

    Journal: PLOS Neglected Tropical Diseases

    Article Title: Clonorchis sinensis aggravates biliary fibrosis through promoting IL-6 production via toll-like receptor 2-mediated AKT and p38 signal pathways

    doi: 10.1371/journal.pntd.0011062

    Figure Lengend Snippet: (A, B) The phosphorylation of AKT, p65, ERK and p38 in liver were analyzed by Western blot. (C, D) 3 × 10 5 WT and TLR2 -/- mouse BECs were cultivated with C . sinensis ESPs (50 μg/mL) for 120 min, the cells were lysed in cells lysates and the phosphorylation of AKT, p65, ERK and p38 were analyzed by Western blot. (E) The production levels of IL-6 in the supernatant of BECs pretreated with or without AKT inhibitor, p38 inhibitor and ERK inhibitor for 1 h, then co-cultured with ESPs for 18 h were measured by ELISA.

    Article Snippet: Phospho-p38 , Rabbit monoclonal , Rabbit IgG , 1:1000 , Cell Signaling Technology.

    Techniques: Western Blot, Cell Culture, Enzyme-linked Immunosorbent Assay

    C . sinensis triggered AKT and p38 signal pathways dependent on TLR2 of BECs to promote the production of IL-6, which subsequently activated TGF-β1-Smad2/Smad3 pathways, myofibroblasts and up-regulated the expression of ECMs, finally resulting in biliary fibrosis in mice. In the figure, ‘ ↑ ’indicates positive regulation.

    Journal: PLOS Neglected Tropical Diseases

    Article Title: Clonorchis sinensis aggravates biliary fibrosis through promoting IL-6 production via toll-like receptor 2-mediated AKT and p38 signal pathways

    doi: 10.1371/journal.pntd.0011062

    Figure Lengend Snippet: C . sinensis triggered AKT and p38 signal pathways dependent on TLR2 of BECs to promote the production of IL-6, which subsequently activated TGF-β1-Smad2/Smad3 pathways, myofibroblasts and up-regulated the expression of ECMs, finally resulting in biliary fibrosis in mice. In the figure, ‘ ↑ ’indicates positive regulation.

    Article Snippet: Phospho-p38 , Rabbit monoclonal , Rabbit IgG , 1:1000 , Cell Signaling Technology.

    Techniques: Expressing