smad3 blocking peptide cell signaling Search Results


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Bioss rabbit smad3
Effects of vitamin D3 on transforming growth factor-β (TGF-β)/Smad signaling in lungs induced by ovalbumin (OVA) challenge. (A) Levels of TGF-β1 in bronchoalveolar lavage fluid (BALF), as determined by enzyme-linked immunosorbent assay. (B) Representative protein expression of TGF-β1 determined by western blotting. (C) Relative protein levels of TGF-β1 in lung tissues. (D) Representative protein expression of phosphorylated (p)-Smad2, Smad2, <t>p-Smad3</t> and Smad3 determined by western blotting. Relative protein levels of (E) p-Smad2 and (F) p-Smad3. Data are presented as the mean ± standard deviation of three repeat experiments, n=6. ** P<0.01 vs. the control group; ## P<0.01 vs. the OVA group.
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Cell Signaling Technology Inc anti p smad3 antibody
The <t>Smad3</t> activation analysis of HSC-T6 cells. Cells were incubated with 30 nM eTGFBR2 (A) or HSA-eTGFBR2 (B) for 0, 0.5, 1, 2 h, and then exposed to 0.4 nM TGF-β1 for 30 min. -: DMEM medium for negative control; +: 0.4 nM TGF-β1 for positive control.
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Cell Signaling Technology Inc smad3
The <t>Smad3</t> activation analysis of HSC-T6 cells. Cells were incubated with 30 nM eTGFBR2 (A) or HSA-eTGFBR2 (B) for 0, 0.5, 1, 2 h, and then exposed to 0.4 nM TGF-β1 for 30 min. -: DMEM medium for negative control; +: 0.4 nM TGF-β1 for positive control.
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Cell Signaling Technology Inc rabbit anti psmad2
The <t>Smad3</t> activation analysis of HSC-T6 cells. Cells were incubated with 30 nM eTGFBR2 (A) or HSA-eTGFBR2 (B) for 0, 0.5, 1, 2 h, and then exposed to 0.4 nM TGF-β1 for 30 min. -: DMEM medium for negative control; +: 0.4 nM TGF-β1 for positive control.
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Cell Signaling Technology Inc smad3 blocking peptide cell signaling #1933s
The <t>Smad3</t> activation analysis of HSC-T6 cells. Cells were incubated with 30 nM eTGFBR2 (A) or HSA-eTGFBR2 (B) for 0, 0.5, 1, 2 h, and then exposed to 0.4 nM TGF-β1 for 30 min. -: DMEM medium for negative control; +: 0.4 nM TGF-β1 for positive control.
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Cell Signaling Technology Inc bsa tbst
The <t>Smad3</t> activation analysis of HSC-T6 cells. Cells were incubated with 30 nM eTGFBR2 (A) or HSA-eTGFBR2 (B) for 0, 0.5, 1, 2 h, and then exposed to 0.4 nM TGF-β1 for 30 min. -: DMEM medium for negative control; +: 0.4 nM TGF-β1 for positive control.
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Proteintech anti smad3
The <t>Smad3</t> activation analysis of HSC-T6 cells. Cells were incubated with 30 nM eTGFBR2 (A) or HSA-eTGFBR2 (B) for 0, 0.5, 1, 2 h, and then exposed to 0.4 nM TGF-β1 for 30 min. -: DMEM medium for negative control; +: 0.4 nM TGF-β1 for positive control.
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Rockland Immunochemicals rabbit anti p smad3
The <t>Smad3</t> activation analysis of HSC-T6 cells. Cells were incubated with 30 nM eTGFBR2 (A) or HSA-eTGFBR2 (B) for 0, 0.5, 1, 2 h, and then exposed to 0.4 nM TGF-β1 for 30 min. -: DMEM medium for negative control; +: 0.4 nM TGF-β1 for positive control.
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Cell Signaling Technology Inc anti smad3 antibody
The <t>Smad3</t> activation analysis of HSC-T6 cells. Cells were incubated with 30 nM eTGFBR2 (A) or HSA-eTGFBR2 (B) for 0, 0.5, 1, 2 h, and then exposed to 0.4 nM TGF-β1 for 30 min. -: DMEM medium for negative control; +: 0.4 nM TGF-β1 for positive control.
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Cell Signaling Technology Inc phospho smad2 3
The <t>Smad3</t> activation analysis of HSC-T6 cells. Cells were incubated with 30 nM eTGFBR2 (A) or HSA-eTGFBR2 (B) for 0, 0.5, 1, 2 h, and then exposed to 0.4 nM TGF-β1 for 30 min. -: DMEM medium for negative control; +: 0.4 nM TGF-β1 for positive control.
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Cell Signaling Technology Inc phospho smad2
The <t>Smad3</t> activation analysis of HSC-T6 cells. Cells were incubated with 30 nM eTGFBR2 (A) or HSA-eTGFBR2 (B) for 0, 0.5, 1, 2 h, and then exposed to 0.4 nM TGF-β1 for 30 min. -: DMEM medium for negative control; +: 0.4 nM TGF-β1 for positive control.
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Cell Signaling Technology Inc antibodies against human smad3
The <t>Smad3</t> activation analysis of HSC-T6 cells. Cells were incubated with 30 nM eTGFBR2 (A) or HSA-eTGFBR2 (B) for 0, 0.5, 1, 2 h, and then exposed to 0.4 nM TGF-β1 for 30 min. -: DMEM medium for negative control; +: 0.4 nM TGF-β1 for positive control.
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Image Search Results


Effects of vitamin D3 on transforming growth factor-β (TGF-β)/Smad signaling in lungs induced by ovalbumin (OVA) challenge. (A) Levels of TGF-β1 in bronchoalveolar lavage fluid (BALF), as determined by enzyme-linked immunosorbent assay. (B) Representative protein expression of TGF-β1 determined by western blotting. (C) Relative protein levels of TGF-β1 in lung tissues. (D) Representative protein expression of phosphorylated (p)-Smad2, Smad2, p-Smad3 and Smad3 determined by western blotting. Relative protein levels of (E) p-Smad2 and (F) p-Smad3. Data are presented as the mean ± standard deviation of three repeat experiments, n=6. ** P<0.01 vs. the control group; ## P<0.01 vs. the OVA group.

Journal: Molecular Medicine Reports

Article Title: The protective role of vitamin D3 in a murine model of asthma via the suppression of TGF-β/Smad signaling and activation of the Nrf2/HO-1 pathway

doi: 10.3892/mmr.2016.5563

Figure Lengend Snippet: Effects of vitamin D3 on transforming growth factor-β (TGF-β)/Smad signaling in lungs induced by ovalbumin (OVA) challenge. (A) Levels of TGF-β1 in bronchoalveolar lavage fluid (BALF), as determined by enzyme-linked immunosorbent assay. (B) Representative protein expression of TGF-β1 determined by western blotting. (C) Relative protein levels of TGF-β1 in lung tissues. (D) Representative protein expression of phosphorylated (p)-Smad2, Smad2, p-Smad3 and Smad3 determined by western blotting. Relative protein levels of (E) p-Smad2 and (F) p-Smad3. Data are presented as the mean ± standard deviation of three repeat experiments, n=6. ** P<0.01 vs. the control group; ## P<0.01 vs. the OVA group.

Article Snippet: After blocking with 5% fat-free milk, the membranes were immunoblotted with primary antibodies as follows: Mouse α-SMA (1:400), rabbit HO-1 (1:200; Santa Cruz Biotechnology, Inc.; cat. no. sc-10789), mouse Nrf2 (1:400), rabbit TGF-β1 (1:200; Santa Cruz Biotechnology, Inc.; cat. no. sc-146), rabbit Smad2 (1:500, BIOSS, Beijing, China; cat. no. bs-0718R), rabbit phosphorylated (p)-Smad2 (1:500; BIOSS; cat. no. bs-5618R), rabbit Smad3 (1:500; BIOSS; cat. no. bs-3484R), rabbit p-Smad3 (1:500; BIOSS; cat. no. bs-5459R), mouse β-actin (1:1,000; Santa Cruz Biotechnology, Inc.; cat. no. sc-47778) and rabbit histone H3 (1:1,000; BIOSS; cat. no. bs-17422R) at 4°C overnight.

Techniques: Enzyme-linked Immunosorbent Assay, Expressing, Western Blot, Standard Deviation

The Smad3 activation analysis of HSC-T6 cells. Cells were incubated with 30 nM eTGFBR2 (A) or HSA-eTGFBR2 (B) for 0, 0.5, 1, 2 h, and then exposed to 0.4 nM TGF-β1 for 30 min. -: DMEM medium for negative control; +: 0.4 nM TGF-β1 for positive control.

Journal: Bioengineered

Article Title: Binding and biologic characterization of recombinant human serum albumin-eTGFBR2 fusion protein expressed in CHO cells

doi: 10.1080/21655979.2017.1292186

Figure Lengend Snippet: The Smad3 activation analysis of HSC-T6 cells. Cells were incubated with 30 nM eTGFBR2 (A) or HSA-eTGFBR2 (B) for 0, 0.5, 1, 2 h, and then exposed to 0.4 nM TGF-β1 for 30 min. -: DMEM medium for negative control; +: 0.4 nM TGF-β1 for positive control.

Article Snippet: After blocking with 5% non-fat milk, the membranes were incubated with anti-p-Smad3 antibody or anti-Smad3 antibody (Cell Signaling technology) for 4 h at room temperature.

Techniques: Activation Assay, Incubation, Negative Control, Positive Control