antiphospho p38 mapk p p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc antiphospho p38 mapk p p38
    Resolvin D1 inhibited the expression of RhoA/MAPK pathway after Ang II treatment in vivo / in vitro . (a and f) Protein expression of RhoA/MAPK signaling pathway in vivo / in vitro was tested by Western blotting. GAPDH was used as internal control and quantification of RhoA (b and g). T-ERK, T-JNK and <t>T-P38</t> were used as internal control and quantification of the P-ERK (c and h), P-JNK (d and i) and P-P38 (e and j) level in the indicated groups, respectively ( n = 4). Data are presented as the mean ± SD. ∗ P < 0.05 compared with the Vehicle/PBS group, # P < 0.05 compared with the Ang II group.
    Antiphospho P38 Mapk 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
    https://www.bioz.com/result/antiphospho p38 mapk p p38/product/Cell Signaling Technology Inc
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    1) Product Images from "Resolvin D1 attenuates Ang II-induced hypertension in mice by inhibiting the proliferation, migration and phenotypic transformation of vascular smooth muscle cells by blocking the RhoA/mitogen-activated protein kinase pathway"

    Article Title: Resolvin D1 attenuates Ang II-induced hypertension in mice by inhibiting the proliferation, migration and phenotypic transformation of vascular smooth muscle cells by blocking the RhoA/mitogen-activated protein kinase pathway

    Journal: Journal of Hypertension

    doi: 10.1097/HJH.0000000000003610

    Resolvin D1 inhibited the expression of RhoA/MAPK pathway after Ang II treatment in vivo / in vitro . (a and f) Protein expression of RhoA/MAPK signaling pathway in vivo / in vitro was tested by Western blotting. GAPDH was used as internal control and quantification of RhoA (b and g). T-ERK, T-JNK and T-P38 were used as internal control and quantification of the P-ERK (c and h), P-JNK (d and i) and P-P38 (e and j) level in the indicated groups, respectively ( n = 4). Data are presented as the mean ± SD. ∗ P < 0.05 compared with the Vehicle/PBS group, # P < 0.05 compared with the Ang II group.
    Figure Legend Snippet: Resolvin D1 inhibited the expression of RhoA/MAPK pathway after Ang II treatment in vivo / in vitro . (a and f) Protein expression of RhoA/MAPK signaling pathway in vivo / in vitro was tested by Western blotting. GAPDH was used as internal control and quantification of RhoA (b and g). T-ERK, T-JNK and T-P38 were used as internal control and quantification of the P-ERK (c and h), P-JNK (d and i) and P-P38 (e and j) level in the indicated groups, respectively ( n = 4). Data are presented as the mean ± SD. ∗ P < 0.05 compared with the Vehicle/PBS group, # P < 0.05 compared with the Ang II group.

    Techniques Used: Expressing, In Vivo, In Vitro, Western Blot

    U46619 reversed the inhibitory effect of resolvin D1 on the phenotypic transformation and the expression of RhoA/MAPK pathway in VSMCs after Ang II stimulation. (a) Protein expression of α-SMA, SM22α, OPN, PCNA and RhoA/MAPK signaling pathway in vitro was tested by Western blotting. GAPDH was used as internal control and quantification of the α-SMA (b), SM22α (c), OPN (d), PCNA (e), RhoA (f). T-ERK, T-JNK and T-P38 were used as internal control and quantification of the P-ERK (g), P-JNK (h) and P-P38 (i) level in the indicated groups respectively ( n = 4). Data are presented as the mean ± SD. ∗ P < 0.05 compared with the Ang II group, # P < 0.05 compared with the Ang II+RvD1 group.
    Figure Legend Snippet: U46619 reversed the inhibitory effect of resolvin D1 on the phenotypic transformation and the expression of RhoA/MAPK pathway in VSMCs after Ang II stimulation. (a) Protein expression of α-SMA, SM22α, OPN, PCNA and RhoA/MAPK signaling pathway in vitro was tested by Western blotting. GAPDH was used as internal control and quantification of the α-SMA (b), SM22α (c), OPN (d), PCNA (e), RhoA (f). T-ERK, T-JNK and T-P38 were used as internal control and quantification of the P-ERK (g), P-JNK (h) and P-P38 (i) level in the indicated groups respectively ( n = 4). Data are presented as the mean ± SD. ∗ P < 0.05 compared with the Ang II group, # P < 0.05 compared with the Ang II+RvD1 group.

    Techniques Used: Transformation Assay, Expressing, In Vitro, Western Blot

    p p38 mapk  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc p p38 mapk
    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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    p p38 mapk  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc p p38 mapk
    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
    https://www.bioz.com/result/p p38 mapk/product/Cell Signaling Technology Inc
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    p p38 mapk  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc p p38 mapk
    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
    https://www.bioz.com/result/p p38 mapk/product/Cell Signaling Technology Inc
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    p p38 mapk  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc p p38 mapk
    <t>p38-mediated</t> BMP signalling does not differ in fam20b −/− chondrocytes. (A-B′) Condensing ceratohyal mesenchyme of wild types (A,A′) and fam20b mutants (B,B′) did not show <t>p-p38</t> immunoreactivity at 48 hpf. (C-D′) p-p38 immunoreactivity appeared similar in ceratohyal chondrocytes of wild types (C,C′) and fam20b mutants (D,D′) at 72 hpf. (E) Quantitative image analyses ( n =6 for each group) revealed no significant differences in p-p38 levels of fam20b −/− chondrocytes. Scale bars: 50 μm. a.u., arbitrary units; wt, wild type.
    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
    https://www.bioz.com/result/p p38 mapk/product/Cell Signaling Technology Inc
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    Images

    1) Product Images from "Proteoglycan inhibition of canonical BMP-dependent cartilage maturation delays endochondral ossification"

    Article Title: Proteoglycan inhibition of canonical BMP-dependent cartilage maturation delays endochondral ossification

    Journal: Development (Cambridge, England)

    doi: 10.1242/dev.201716

    p38-mediated BMP signalling does not differ in fam20b −/− chondrocytes. (A-B′) Condensing ceratohyal mesenchyme of wild types (A,A′) and fam20b mutants (B,B′) did not show p-p38 immunoreactivity at 48 hpf. (C-D′) p-p38 immunoreactivity appeared similar in ceratohyal chondrocytes of wild types (C,C′) and fam20b mutants (D,D′) at 72 hpf. (E) Quantitative image analyses ( n =6 for each group) revealed no significant differences in p-p38 levels of fam20b −/− chondrocytes. Scale bars: 50 μm. a.u., arbitrary units; wt, wild type.
    Figure Legend Snippet: p38-mediated BMP signalling does not differ in fam20b −/− chondrocytes. (A-B′) Condensing ceratohyal mesenchyme of wild types (A,A′) and fam20b mutants (B,B′) did not show p-p38 immunoreactivity at 48 hpf. (C-D′) p-p38 immunoreactivity appeared similar in ceratohyal chondrocytes of wild types (C,C′) and fam20b mutants (D,D′) at 72 hpf. (E) Quantitative image analyses ( n =6 for each group) revealed no significant differences in p-p38 levels of fam20b −/− chondrocytes. Scale bars: 50 μm. a.u., arbitrary units; wt, wild type.

    Techniques Used:

    Inhibition of BMP signalling by DMH1 in wild types reduces cartilage maturation gene expression and perichondral bone formation. (A-D′) Immunostaining of wild-type chondrocytes at 72 hpf (i.e. after 24 h of treatment) demonstrated that DMH1 treatment reduced p-Smad1/5/9 (B,B′) and p-p38 (D,D′) immunoreactivity, compared with DMSO-treated control chondrocytes (A,A′,C,C′). (E) Quantitative image analyses ( n =3 for each group) revealed significant decreases in p-Smad1/5/9 and p-p38 levels in nuclei, as well as a significant decrease in p-Smad1/5/9 in non-nuclear regions, of DMH1-treated chondrocytes, compared with DMSO-treated control chondrocytes (* P <0.05, one-way ANOVA and paired Student's t -test). (F-I) Compared with DMSO-treated control chondrocytes (F,G), DMH1 treatment decreased expression of the chondrocyte maturation genes ihha and col10a1a at 4 dpf (i.e. after 2 days of treatment; H,I). These are representative images from at least 12 samples for each group (at least six samples each from two clutches). (J-K″) Compared with DMSO-treated controls (J-J″), DMH1 treatment appeared to decrease perichondral bone at 7 dpf (i.e. 3 days after treatment ended; K-K″). (L) Quantitation of 100 larvae (20 larvae each from five clutches) for each experimental group confirmed a significant decrease in perichondral bone in DMH-treated wild types (* P <0.05, one-way ANOVA and paired Student's t -test). Scale bars: 50 μm (A-D′,F-I); 200 μm (J,K). A, anterior; AB/AR, Alcian Blue/Alizarin Red; a.u., arbitrary units; Bsr, branchiostegal ray; Ch, ceratohyal cartilage; Chb, ceratohyal bone; Hm, hyomandibular bone; Hs, hyosymplectic cartilage; L, lateral; Op, opercle; wt, wild type.
    Figure Legend Snippet: Inhibition of BMP signalling by DMH1 in wild types reduces cartilage maturation gene expression and perichondral bone formation. (A-D′) Immunostaining of wild-type chondrocytes at 72 hpf (i.e. after 24 h of treatment) demonstrated that DMH1 treatment reduced p-Smad1/5/9 (B,B′) and p-p38 (D,D′) immunoreactivity, compared with DMSO-treated control chondrocytes (A,A′,C,C′). (E) Quantitative image analyses ( n =3 for each group) revealed significant decreases in p-Smad1/5/9 and p-p38 levels in nuclei, as well as a significant decrease in p-Smad1/5/9 in non-nuclear regions, of DMH1-treated chondrocytes, compared with DMSO-treated control chondrocytes (* P <0.05, one-way ANOVA and paired Student's t -test). (F-I) Compared with DMSO-treated control chondrocytes (F,G), DMH1 treatment decreased expression of the chondrocyte maturation genes ihha and col10a1a at 4 dpf (i.e. after 2 days of treatment; H,I). These are representative images from at least 12 samples for each group (at least six samples each from two clutches). (J-K″) Compared with DMSO-treated controls (J-J″), DMH1 treatment appeared to decrease perichondral bone at 7 dpf (i.e. 3 days after treatment ended; K-K″). (L) Quantitation of 100 larvae (20 larvae each from five clutches) for each experimental group confirmed a significant decrease in perichondral bone in DMH-treated wild types (* P <0.05, one-way ANOVA and paired Student's t -test). Scale bars: 50 μm (A-D′,F-I); 200 μm (J,K). A, anterior; AB/AR, Alcian Blue/Alizarin Red; a.u., arbitrary units; Bsr, branchiostegal ray; Ch, ceratohyal cartilage; Chb, ceratohyal bone; Hm, hyomandibular bone; Hs, hyosymplectic cartilage; L, lateral; Op, opercle; wt, wild type.

    Techniques Used: Inhibition, Expressing, Immunostaining, Quantitation Assay

    p38-mediated BMP signalling does not differ in chondrocytes of heat-shocked, dnBMPR zebrafish embryos. (A-D′) Condensing ceratohyal mesenchyme did not show much p-p38 immunoreactivity at 48 hpf in non-heat-shocked wild-type (A,A′) and dnBMPR (B,B′) embryos and heat-shocked wild-type (C,C′) and dnBMPR (D,D′) embryos (i.e. 24 h after 20-min heat shock). (E) Quantitative image analyses ( n =3 for each group) revealed no significant differences in p-p38 levels in condensing ceratohyal mesenchyme among experimental groups. One-way ANOVA and paired Student's t -test. (F-I′) Chondrocytes of heat-shocked dnBMPR zebrafish embryos (I,I′) showed similar levels of p-p38 immunoreactivity at 72 hpf (i.e. 48 h after heat shock) as control groups (F-H′). (J) Quantitative image analyses ( n =3 for each group) revealed no significant differences in p-p38 levels in chondrocytes of heat-shocked dnBMPR zebrafish, compared with each control group. One-way ANOVA and paired Student's t -test. Scale bars: 50 μm. a.u., arbitrary units; HS, heat-shocked; wt, wild type.
    Figure Legend Snippet: p38-mediated BMP signalling does not differ in chondrocytes of heat-shocked, dnBMPR zebrafish embryos. (A-D′) Condensing ceratohyal mesenchyme did not show much p-p38 immunoreactivity at 48 hpf in non-heat-shocked wild-type (A,A′) and dnBMPR (B,B′) embryos and heat-shocked wild-type (C,C′) and dnBMPR (D,D′) embryos (i.e. 24 h after 20-min heat shock). (E) Quantitative image analyses ( n =3 for each group) revealed no significant differences in p-p38 levels in condensing ceratohyal mesenchyme among experimental groups. One-way ANOVA and paired Student's t -test. (F-I′) Chondrocytes of heat-shocked dnBMPR zebrafish embryos (I,I′) showed similar levels of p-p38 immunoreactivity at 72 hpf (i.e. 48 h after heat shock) as control groups (F-H′). (J) Quantitative image analyses ( n =3 for each group) revealed no significant differences in p-p38 levels in chondrocytes of heat-shocked dnBMPR zebrafish, compared with each control group. One-way ANOVA and paired Student's t -test. Scale bars: 50 μm. a.u., arbitrary units; HS, heat-shocked; wt, wild type.

    Techniques Used:

    Inhibition of BMP signalling by DMH1 or by heat shocking dnBMPR zebrafish embryos rescues the increased BMP signalling in fam20b −/− chondrocytes. (A-D′) Compared with DMSO-treated (A,A′) or heat-shocked (C,C′) fam20b −/− chondrocytes, levels of p-Smad1/5/9 at 72 hpf appeared decreased in DMH1-treated fam20b −/− (i.e. after 24 h of treatment; B,B′) or heat-shocked dnBMPR ; fam20b −/− (i.e. 2 days after 20-min heat shock; D,D′) chondrocytes. (E) Quantitative image analyses ( n =3 for each group) revealed significant decreases in p-Smad1/5/9 levels in both nuclei and non-nuclear regions of DMH1-treated or heat-shocked fam20b −/− chondrocytes, compared with each control group (* P <0.05, one-way ANOVA and paired Student's t -test). (F-G′) Compared with DMSO-treated fam20b −/− chondrocytes (F,F′), levels of p-p38 at 72 hpf (i.e. after 24 h of treatment) appeared decreased in DMH1-treated fam20b −/− chondrocytes (G,G′). (H) Quantitative image analyses ( n =3 for each group) revealed significant decreases in p-p38 levels in nuclei of DMH1-treated fam20b −/− chondrocytes (* P <0.05, one-way ANOVA and paired Student's t -test). Scale bars: 50 μm. a.u., arbitrary units; HS, heat-shocked.
    Figure Legend Snippet: Inhibition of BMP signalling by DMH1 or by heat shocking dnBMPR zebrafish embryos rescues the increased BMP signalling in fam20b −/− chondrocytes. (A-D′) Compared with DMSO-treated (A,A′) or heat-shocked (C,C′) fam20b −/− chondrocytes, levels of p-Smad1/5/9 at 72 hpf appeared decreased in DMH1-treated fam20b −/− (i.e. after 24 h of treatment; B,B′) or heat-shocked dnBMPR ; fam20b −/− (i.e. 2 days after 20-min heat shock; D,D′) chondrocytes. (E) Quantitative image analyses ( n =3 for each group) revealed significant decreases in p-Smad1/5/9 levels in both nuclei and non-nuclear regions of DMH1-treated or heat-shocked fam20b −/− chondrocytes, compared with each control group (* P <0.05, one-way ANOVA and paired Student's t -test). (F-G′) Compared with DMSO-treated fam20b −/− chondrocytes (F,F′), levels of p-p38 at 72 hpf (i.e. after 24 h of treatment) appeared decreased in DMH1-treated fam20b −/− chondrocytes (G,G′). (H) Quantitative image analyses ( n =3 for each group) revealed significant decreases in p-p38 levels in nuclei of DMH1-treated fam20b −/− chondrocytes (* P <0.05, one-way ANOVA and paired Student's t -test). Scale bars: 50 μm. a.u., arbitrary units; HS, heat-shocked.

    Techniques Used: Inhibition

    phosphorylated p p38 mapk  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc phosphorylated p p38 mapk
    Phosphorylated 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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    p p38 mapk  (Cell Signaling Technology Inc)


    Bioz Manufacturer Symbol Cell Signaling Technology Inc manufactures this product  
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    Cell Signaling Technology Inc p p38 mapk
    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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    anti p p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti p p38 mapk
    Anti 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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    phosphorylated p p38 mapk  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc phosphorylated p p38 mapk
    Effects of OSM on the bFGF-induced <t>phosphorylation</t> <t>of</t> <t>p38</t> <t>MAPK,</t> SAPK/JNK and p44/p42 MAPK in MC3T3-E1 cells. The cultured cells were pretreated with 0, 30, 50 or 70 ng/ml OSM for 60 min, and then stimulated with 30 ng/ml bFGF or vehicle for (A) 10 or (B and C) 20 min. The cell extracts were then subjected to SDS-PAGE and western blot analysis with antibodies against <t>(A)</t> <t>p-p38</t> <t>MAPK,</t> <t>p38</t> <t>MAPK</t> and GAPDH; (B) p-SAPK/JNK, SAPK/JNK and GAPDH; or (C) p-p44/p42 MAPK, p44/p42 MAPK and GAPDH. The histograms show the semi-quantitative representations of the expression levels of (A) <t>p-p38</t> <t>MAPK</t> after normalization to p38 MAPK, (B) p-SAPK/JNK after normalization to SAPK/JNK, and (C) p-p44/p42 MAPK after normalization to p44/p42 MAPK obtained from densitometric analysis. The levels were expressed as the fold increase with respect to the basal levels presented in lane 1. Data are presented as the mean ± SEM of (A) quadruplicate determinations from four independent cell preparations or (B and C) triplicate determinations from three independent cell preparations. *P<0.05 vs. control; #P<0.05 vs. bFGF alone. bFGF, basic fibroblast growth factor; MAPK, mitogen-activated protein kinase; MW, molecular weight N.S., not significant; p-, phosphorylated; SAPK/JNK, stress-activated protein kinase/c-Jun N-terminal kinase.
    Phosphorylated 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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    Images

    1) Product Images from "Oncostatin M enhances osteoprotegerin synthesis but reduces macrophage colony‑stimulating factor synthesis in bFGF‑stimulated osteoblast‑like cells"

    Article Title: Oncostatin M enhances osteoprotegerin synthesis but reduces macrophage colony‑stimulating factor synthesis in bFGF‑stimulated osteoblast‑like cells

    Journal: Experimental and Therapeutic Medicine

    doi: 10.3892/etm.2023.12322

    Effects of OSM on the bFGF-induced phosphorylation of p38 MAPK, SAPK/JNK and p44/p42 MAPK in MC3T3-E1 cells. The cultured cells were pretreated with 0, 30, 50 or 70 ng/ml OSM for 60 min, and then stimulated with 30 ng/ml bFGF or vehicle for (A) 10 or (B and C) 20 min. The cell extracts were then subjected to SDS-PAGE and western blot analysis with antibodies against (A) p-p38 MAPK, p38 MAPK and GAPDH; (B) p-SAPK/JNK, SAPK/JNK and GAPDH; or (C) p-p44/p42 MAPK, p44/p42 MAPK and GAPDH. The histograms show the semi-quantitative representations of the expression levels of (A) p-p38 MAPK after normalization to p38 MAPK, (B) p-SAPK/JNK after normalization to SAPK/JNK, and (C) p-p44/p42 MAPK after normalization to p44/p42 MAPK obtained from densitometric analysis. The levels were expressed as the fold increase with respect to the basal levels presented in lane 1. Data are presented as the mean ± SEM of (A) quadruplicate determinations from four independent cell preparations or (B and C) triplicate determinations from three independent cell preparations. *P<0.05 vs. control; #P<0.05 vs. bFGF alone. bFGF, basic fibroblast growth factor; MAPK, mitogen-activated protein kinase; MW, molecular weight N.S., not significant; p-, phosphorylated; SAPK/JNK, stress-activated protein kinase/c-Jun N-terminal kinase.
    Figure Legend Snippet: Effects of OSM on the bFGF-induced phosphorylation of p38 MAPK, SAPK/JNK and p44/p42 MAPK in MC3T3-E1 cells. The cultured cells were pretreated with 0, 30, 50 or 70 ng/ml OSM for 60 min, and then stimulated with 30 ng/ml bFGF or vehicle for (A) 10 or (B and C) 20 min. The cell extracts were then subjected to SDS-PAGE and western blot analysis with antibodies against (A) p-p38 MAPK, p38 MAPK and GAPDH; (B) p-SAPK/JNK, SAPK/JNK and GAPDH; or (C) p-p44/p42 MAPK, p44/p42 MAPK and GAPDH. The histograms show the semi-quantitative representations of the expression levels of (A) p-p38 MAPK after normalization to p38 MAPK, (B) p-SAPK/JNK after normalization to SAPK/JNK, and (C) p-p44/p42 MAPK after normalization to p44/p42 MAPK obtained from densitometric analysis. The levels were expressed as the fold increase with respect to the basal levels presented in lane 1. Data are presented as the mean ± SEM of (A) quadruplicate determinations from four independent cell preparations or (B and C) triplicate determinations from three independent cell preparations. *P<0.05 vs. control; #P<0.05 vs. bFGF alone. bFGF, basic fibroblast growth factor; MAPK, mitogen-activated protein kinase; MW, molecular weight N.S., not significant; p-, phosphorylated; SAPK/JNK, stress-activated protein kinase/c-Jun N-terminal kinase.

    Techniques Used: Cell Culture, SDS Page, Western Blot, Expressing, Molecular Weight

    anti rabbit p p38 mapk p38  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc anti rabbit p p38 mapk p38
    PBM modulates the Smad3/Sox9 and <t>MAPK/Sox9</t> pathways in inflammation-induced astrocytes. (A, B) Representative western blots of proteins related to the Smad3/Sox9 pathway, Erk/Sox9 pathway, <t>P38/Sox9</t> pathway, and JNK/Sox9 pathway in astrocytes and quantification of the relative expression levels of p-Smad3, p-Erk, p-P38, p-JNK, Sox9, and versican. Data are shown as mean ± SD ( n = 3 for each group) and were analyzed by multiple repeated measures analysis of variance with least significance difference post hoc analysis. * P < 0.05, *** P < 0.001, **** P < 0.0001. Erk: Extracellular signal-regulated kinase; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; JNK: c-Jun N-terminal kinase.
    Anti Rabbit P P38 Mapk 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 "Photobiomodulation inhibits the expression of chondroitin sulfate proteoglycans after spinal cord injury via the Sox9 pathway"

    Article Title: Photobiomodulation inhibits the expression of chondroitin sulfate proteoglycans after spinal cord injury via the Sox9 pathway

    Journal: Neural Regeneration Research

    doi: 10.4103/1673-5374.374136

    PBM modulates the Smad3/Sox9 and MAPK/Sox9 pathways in inflammation-induced astrocytes. (A, B) Representative western blots of proteins related to the Smad3/Sox9 pathway, Erk/Sox9 pathway, P38/Sox9 pathway, and JNK/Sox9 pathway in astrocytes and quantification of the relative expression levels of p-Smad3, p-Erk, p-P38, p-JNK, Sox9, and versican. Data are shown as mean ± SD ( n = 3 for each group) and were analyzed by multiple repeated measures analysis of variance with least significance difference post hoc analysis. * P < 0.05, *** P < 0.001, **** P < 0.0001. Erk: Extracellular signal-regulated kinase; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; JNK: c-Jun N-terminal kinase.
    Figure Legend Snippet: PBM modulates the Smad3/Sox9 and MAPK/Sox9 pathways in inflammation-induced astrocytes. (A, B) Representative western blots of proteins related to the Smad3/Sox9 pathway, Erk/Sox9 pathway, P38/Sox9 pathway, and JNK/Sox9 pathway in astrocytes and quantification of the relative expression levels of p-Smad3, p-Erk, p-P38, p-JNK, Sox9, and versican. Data are shown as mean ± SD ( n = 3 for each group) and were analyzed by multiple repeated measures analysis of variance with least significance difference post hoc analysis. * P < 0.05, *** P < 0.001, **** P < 0.0001. Erk: Extracellular signal-regulated kinase; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; JNK: c-Jun N-terminal kinase.

    Techniques Used: Western Blot, Expressing

    The Smad3/Sox9 pathway and MAPK/Sox9 pathway are involved in photobiomodulation (PBM) modulation of versican expression in spinal cord injury (SCI) mice. (A–C) Representative western blots of proteins related to the Erk/Sox9 pathway (A), P38/Sox9 pathway (B), and Smad3/Sox9 pathway (C) at 7 dpi and quantification of the levels of p-Smad3, p-Erk, p-P38, Sox9, and versican ( n = 6 mice for each group). Data are shown as mean ± SD and were analyzed by one-way analysis of variance with least significance difference post hoc analysis. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. dpi: Day(s) post-injury; Erk: extracellular signal-regulated kinase; GAPDH: glyceraldehyde-3-phosphate dehydrogenase.
    Figure Legend Snippet: The Smad3/Sox9 pathway and MAPK/Sox9 pathway are involved in photobiomodulation (PBM) modulation of versican expression in spinal cord injury (SCI) mice. (A–C) Representative western blots of proteins related to the Erk/Sox9 pathway (A), P38/Sox9 pathway (B), and Smad3/Sox9 pathway (C) at 7 dpi and quantification of the levels of p-Smad3, p-Erk, p-P38, Sox9, and versican ( n = 6 mice for each group). Data are shown as mean ± SD and were analyzed by one-way analysis of variance with least significance difference post hoc analysis. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. dpi: Day(s) post-injury; Erk: extracellular signal-regulated kinase; GAPDH: glyceraldehyde-3-phosphate dehydrogenase.

    Techniques Used: Expressing, Western Blot

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    Resolvin D1 inhibited the expression of RhoA/MAPK pathway after Ang II treatment in vivo / in vitro . (a and f) Protein expression of RhoA/MAPK signaling pathway in vivo / in vitro was tested by Western blotting. GAPDH was used as internal control and quantification of RhoA (b and g). T-ERK, T-JNK and T-P38 were used as internal control and quantification of the P-ERK (c and h), P-JNK (d and i) and P-P38 (e and j) level in the indicated groups, respectively ( n = 4). Data are presented as the mean ± SD. ∗ P < 0.05 compared with the Vehicle/PBS group, # P < 0.05 compared with the Ang II group.

    Journal: Journal of Hypertension

    Article Title: Resolvin D1 attenuates Ang II-induced hypertension in mice by inhibiting the proliferation, migration and phenotypic transformation of vascular smooth muscle cells by blocking the RhoA/mitogen-activated protein kinase pathway

    doi: 10.1097/HJH.0000000000003610

    Figure Lengend Snippet: Resolvin D1 inhibited the expression of RhoA/MAPK pathway after Ang II treatment in vivo / in vitro . (a and f) Protein expression of RhoA/MAPK signaling pathway in vivo / in vitro was tested by Western blotting. GAPDH was used as internal control and quantification of RhoA (b and g). T-ERK, T-JNK and T-P38 were used as internal control and quantification of the P-ERK (c and h), P-JNK (d and i) and P-P38 (e and j) level in the indicated groups, respectively ( n = 4). Data are presented as the mean ± SD. ∗ P < 0.05 compared with the Vehicle/PBS group, # P < 0.05 compared with the Ang II group.

    Article Snippet: The membranes were blocked with 5% nonfat milk at room temperature for 1 h and incubated overnight at 4 °C on a shaker with the following primary antibodies: antiα-SMA (ab5694, Abcam), anti-SM22α (GB11366, Servicebio), anti-OPN (22952-1-AP, Proteintech), antiproliferating cell nuclear antigen (PCNA) (GTX100539, GeneTex, Irvine, California, USA), anti-RhoA (10749-1-AP, Proteintech), antiphospho-p44/42 MAPK (P-ERK1/2) (4370, Cell Signaling Technology, Danvers, Massachusetts, USA), antip44/42 MAPK (T-ERK1/2) (4695, Cell Signaling Technology), antiphospho-SAPK/JNK (P-JNK1/2) (4668, Cell Signaling Technology), anti-SAPK/JNK (T-JNK1/2) (9258, Cell Signaling Technology), antiphospho-p38 MAPK (P-P38) (4511, Cell Signaling Technology), antip38 MAPK (T-P38) (8690, Cell Signaling Technology), and antiglyceraldehyde-3-phosphate dehydrogenase (GAPDH) (AC027, Abclonal, Wuhan, China).

    Techniques: Expressing, In Vivo, In Vitro, Western Blot

    U46619 reversed the inhibitory effect of resolvin D1 on the phenotypic transformation and the expression of RhoA/MAPK pathway in VSMCs after Ang II stimulation. (a) Protein expression of α-SMA, SM22α, OPN, PCNA and RhoA/MAPK signaling pathway in vitro was tested by Western blotting. GAPDH was used as internal control and quantification of the α-SMA (b), SM22α (c), OPN (d), PCNA (e), RhoA (f). T-ERK, T-JNK and T-P38 were used as internal control and quantification of the P-ERK (g), P-JNK (h) and P-P38 (i) level in the indicated groups respectively ( n = 4). Data are presented as the mean ± SD. ∗ P < 0.05 compared with the Ang II group, # P < 0.05 compared with the Ang II+RvD1 group.

    Journal: Journal of Hypertension

    Article Title: Resolvin D1 attenuates Ang II-induced hypertension in mice by inhibiting the proliferation, migration and phenotypic transformation of vascular smooth muscle cells by blocking the RhoA/mitogen-activated protein kinase pathway

    doi: 10.1097/HJH.0000000000003610

    Figure Lengend Snippet: U46619 reversed the inhibitory effect of resolvin D1 on the phenotypic transformation and the expression of RhoA/MAPK pathway in VSMCs after Ang II stimulation. (a) Protein expression of α-SMA, SM22α, OPN, PCNA and RhoA/MAPK signaling pathway in vitro was tested by Western blotting. GAPDH was used as internal control and quantification of the α-SMA (b), SM22α (c), OPN (d), PCNA (e), RhoA (f). T-ERK, T-JNK and T-P38 were used as internal control and quantification of the P-ERK (g), P-JNK (h) and P-P38 (i) level in the indicated groups respectively ( n = 4). Data are presented as the mean ± SD. ∗ P < 0.05 compared with the Ang II group, # P < 0.05 compared with the Ang II+RvD1 group.

    Article Snippet: The membranes were blocked with 5% nonfat milk at room temperature for 1 h and incubated overnight at 4 °C on a shaker with the following primary antibodies: antiα-SMA (ab5694, Abcam), anti-SM22α (GB11366, Servicebio), anti-OPN (22952-1-AP, Proteintech), antiproliferating cell nuclear antigen (PCNA) (GTX100539, GeneTex, Irvine, California, USA), anti-RhoA (10749-1-AP, Proteintech), antiphospho-p44/42 MAPK (P-ERK1/2) (4370, Cell Signaling Technology, Danvers, Massachusetts, USA), antip44/42 MAPK (T-ERK1/2) (4695, Cell Signaling Technology), antiphospho-SAPK/JNK (P-JNK1/2) (4668, Cell Signaling Technology), anti-SAPK/JNK (T-JNK1/2) (9258, Cell Signaling Technology), antiphospho-p38 MAPK (P-P38) (4511, Cell Signaling Technology), antip38 MAPK (T-P38) (8690, Cell Signaling Technology), and antiglyceraldehyde-3-phosphate dehydrogenase (GAPDH) (AC027, Abclonal, Wuhan, China).

    Techniques: Transformation Assay, Expressing, In Vitro, Western Blot

    PBM modulates the Smad3/Sox9 and MAPK/Sox9 pathways in inflammation-induced astrocytes. (A, B) Representative western blots of proteins related to the Smad3/Sox9 pathway, Erk/Sox9 pathway, P38/Sox9 pathway, and JNK/Sox9 pathway in astrocytes and quantification of the relative expression levels of p-Smad3, p-Erk, p-P38, p-JNK, Sox9, and versican. Data are shown as mean ± SD ( n = 3 for each group) and were analyzed by multiple repeated measures analysis of variance with least significance difference post hoc analysis. * P < 0.05, *** P < 0.001, **** P < 0.0001. Erk: Extracellular signal-regulated kinase; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; JNK: c-Jun N-terminal kinase.

    Journal: Neural Regeneration Research

    Article Title: Photobiomodulation inhibits the expression of chondroitin sulfate proteoglycans after spinal cord injury via the Sox9 pathway

    doi: 10.4103/1673-5374.374136

    Figure Lengend Snippet: PBM modulates the Smad3/Sox9 and MAPK/Sox9 pathways in inflammation-induced astrocytes. (A, B) Representative western blots of proteins related to the Smad3/Sox9 pathway, Erk/Sox9 pathway, P38/Sox9 pathway, and JNK/Sox9 pathway in astrocytes and quantification of the relative expression levels of p-Smad3, p-Erk, p-P38, p-JNK, Sox9, and versican. Data are shown as mean ± SD ( n = 3 for each group) and were analyzed by multiple repeated measures analysis of variance with least significance difference post hoc analysis. * P < 0.05, *** P < 0.001, **** P < 0.0001. Erk: Extracellular signal-regulated kinase; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; JNK: c-Jun N-terminal kinase.

    Article Snippet: The membranes were soaked in 5% skimmed milk for 1 hour at room temperature and incubated overnight at 4°C with the following primary antibodies: anti-mouse glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (1:3000, Proteintech, Wuhan, Hubei, China, Cat# 60004-1-Ig, RRID: AB_2107436), anti-mouse chondroitin sulfate proteoglycans (CSPG) (1:1000, Sigma-Aldrich, St. Louis, MO, USA, Cat# C8035, RRID: AB_476879), anti-mouse versican (1:1000, Thermo Fisher Scientific, Cat# S351-23, RRID: AB_2735409), anti-rabbit Sox9 (1:1000, Abcam, Cambridge, UK, Cat# ab185966, RRID: AB_2728660), anti-rabbit p-P38 MAPK (P38) (1:1000, CST, Danvers, MA, USA, Cat# D3F9, RRID: AB_2139682), anti-rabbit P38 (1:1000, CST, Cat# D13E1, RRID: TSC_SD02390), anti-rabbit p-extracellular signal-regulated kinase 1/2 (Erk1/2) (1:1000, CST, Cat# D13.14.4E, RRID: AB_10694057), anti-rabbit Erk1/2 (1:1000, CST, Cat# 137F5, RRID: AB_10693607), anti-rabbit p-Smad3 (1:1000, CST, Cat# C25A9, RRID: AB_2193207), anti-rabbit Smad2/3 (1:1000, CST, Cat# D7G7, RRID: AB_10889933), anti-rabbit p-c-Jun N-terminal kinase (JNK) (1:1000, Proteintech, Cat# 80024-1-RR, RRID: AB_2882943), and anti-rabbit JNK (1:1000, Proteintech, Cat# 66210-1-Ig, RRID: AB_2881601).

    Techniques: Western Blot, Expressing

    The Smad3/Sox9 pathway and MAPK/Sox9 pathway are involved in photobiomodulation (PBM) modulation of versican expression in spinal cord injury (SCI) mice. (A–C) Representative western blots of proteins related to the Erk/Sox9 pathway (A), P38/Sox9 pathway (B), and Smad3/Sox9 pathway (C) at 7 dpi and quantification of the levels of p-Smad3, p-Erk, p-P38, Sox9, and versican ( n = 6 mice for each group). Data are shown as mean ± SD and were analyzed by one-way analysis of variance with least significance difference post hoc analysis. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. dpi: Day(s) post-injury; Erk: extracellular signal-regulated kinase; GAPDH: glyceraldehyde-3-phosphate dehydrogenase.

    Journal: Neural Regeneration Research

    Article Title: Photobiomodulation inhibits the expression of chondroitin sulfate proteoglycans after spinal cord injury via the Sox9 pathway

    doi: 10.4103/1673-5374.374136

    Figure Lengend Snippet: The Smad3/Sox9 pathway and MAPK/Sox9 pathway are involved in photobiomodulation (PBM) modulation of versican expression in spinal cord injury (SCI) mice. (A–C) Representative western blots of proteins related to the Erk/Sox9 pathway (A), P38/Sox9 pathway (B), and Smad3/Sox9 pathway (C) at 7 dpi and quantification of the levels of p-Smad3, p-Erk, p-P38, Sox9, and versican ( n = 6 mice for each group). Data are shown as mean ± SD and were analyzed by one-way analysis of variance with least significance difference post hoc analysis. * P < 0.05, ** P < 0.01, *** P < 0.001, **** P < 0.0001. dpi: Day(s) post-injury; Erk: extracellular signal-regulated kinase; GAPDH: glyceraldehyde-3-phosphate dehydrogenase.

    Article Snippet: The membranes were soaked in 5% skimmed milk for 1 hour at room temperature and incubated overnight at 4°C with the following primary antibodies: anti-mouse glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (1:3000, Proteintech, Wuhan, Hubei, China, Cat# 60004-1-Ig, RRID: AB_2107436), anti-mouse chondroitin sulfate proteoglycans (CSPG) (1:1000, Sigma-Aldrich, St. Louis, MO, USA, Cat# C8035, RRID: AB_476879), anti-mouse versican (1:1000, Thermo Fisher Scientific, Cat# S351-23, RRID: AB_2735409), anti-rabbit Sox9 (1:1000, Abcam, Cambridge, UK, Cat# ab185966, RRID: AB_2728660), anti-rabbit p-P38 MAPK (P38) (1:1000, CST, Danvers, MA, USA, Cat# D3F9, RRID: AB_2139682), anti-rabbit P38 (1:1000, CST, Cat# D13E1, RRID: TSC_SD02390), anti-rabbit p-extracellular signal-regulated kinase 1/2 (Erk1/2) (1:1000, CST, Cat# D13.14.4E, RRID: AB_10694057), anti-rabbit Erk1/2 (1:1000, CST, Cat# 137F5, RRID: AB_10693607), anti-rabbit p-Smad3 (1:1000, CST, Cat# C25A9, RRID: AB_2193207), anti-rabbit Smad2/3 (1:1000, CST, Cat# D7G7, RRID: AB_10889933), anti-rabbit p-c-Jun N-terminal kinase (JNK) (1:1000, Proteintech, Cat# 80024-1-RR, RRID: AB_2882943), and anti-rabbit JNK (1:1000, Proteintech, Cat# 66210-1-Ig, RRID: AB_2881601).

    Techniques: Expressing, Western Blot