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smad3 antibody (Bio-Techne corporation)

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Bio-Techne corporation smad3 antibody
Smad3 Antibody, supplied by Bio-Techne corporation, used in various techniques. Bioz Stars score: 94/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/smad3 antibody/product/Bio-Techne corporation
Average 94 stars, based on 8 article reviews

smad3 antibody - by Bioz Stars, 2026-05

94/100 stars

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Pinitol enhanced the phosphorylation of Smad 3. The HDEs were irradiated with UVA (10 J/cm 2 ) and subsequently treated with pinitol for 24 h. The phosphorylation or total of each Smad isoform was detected with corresponding antibodies. The results show representative images of three independent experiments.

Journal: Biomolecules & Therapeutics

Article Title: The Anti-Diabetic Pinitol Improves Damaged Fibroblasts

doi: 10.4062/biomolther.2023.220

Figure Lengend Snippet: Pinitol enhanced the phosphorylation of Smad 3. The HDEs were irradiated with UVA (10 J/cm 2 ) and subsequently treated with pinitol for 24 h. The phosphorylation or total of each Smad isoform was detected with corresponding antibodies. The results show representative images of three independent experiments.

Article Snippet: The level of phospho- and total mitogen-activated protein kinases (MAPKs), c-Jun, and Smad3 were detected using a rabbit polyclonal anti-phospho-JNK antibody (Cell signaling technology, Danvers, MA, USA), rabbit polyclonal anti-JNK antibody (Cell signaling technology), rabbit polyclonal anti-phospho-ERK antibody (Cell signaling technology), rabbit polyclonal anti-ERK antibody (Cell signaling technology), rabbit polyclonal anti-phospho-p38 antibody (Cell signaling technology), rabbit polyclonal anti-p38 antibody (Cell signaling technology), rabbit polyclonal anti-phospho-c-Jun antibody (Cell signaling technology), rabbit polyclonal anti-c-Jun antibody (Cell signaling technology), rabbit monoclonal anti-phospho-Smad3 antibody (Cell signaling technology), and rabbit polyclonal anti-Smad3 antibody (Novus biological, Littleton, CO, USA).

Techniques: Phospho-proteomics, Irradiation

( A ) qPCR analyses reveal Tgfβ2 expression does not change in chick (blue circles; n=8) and quail (red squares; n=8) over time; however, in duck (yellow triangles; n=10), there is a decrease at HH37 and HH40; Tgfβ2 is higher in duck than chick or quail at HH31. ( B ) Acvrl1 does not change over time in chick; however, quail show an increase at HH37. There is a reduction in duck at HH40. Duck have higher Acvrl1 at HH34 compared to chick and quail. However, at HH37 and HH40, quail have more Acvrl1 compared to chick or duck. ( C ) Tgfβr2 does not change over time in chick or duck, but in quail, there is an induction at HH37. ( D ) Tgfβr3 does not change over time in chick, quail, or duck. ( E ) Smad3 in chick does not change until HH40 with a reduction. In quail and duck, Smad3 decreases at HH37 and continues to decrease for duck at HH40. Smad3 is higher in chick than quail at HH34 and is higher at HH37 compared to quail and duck. ( F ) Pai1 does not change over time in chick, but quail increase at HH37 and HH40, while duck decrease at the same time points. Duck Pai1 is higher at HH31 and HH34 compared to chick and quail, but at HH37 and HH40 quail it is significantly higher compared to chick and duck. ( G ) Mmp2 increases in chick and quail at HH37, whereas duck decrease at HH40. Chick have higher Mmp2 compared to duck at HH34 and HH37. Quail have higher Mmp2 compared to duck at HH37 and HH40. ( H ) Mmp9 increases in chick, quail, and duck at HH37. Quail have more Mmp9 compared to chick and duck at HH37 and HH40. p≤0.05 and * denotes significance from HH31 within each group, # denotes significance between quail and duck at same stage, † denotes significance between chick and quail, and ‡ denotes significance between chick and duck.

Journal: eLife

Article Title: Species-specific sensitivity to TGFβ signaling and changes to the Mmp13 promoter underlie avian jaw development and evolution

doi: 10.7554/eLife.66005

Figure Lengend Snippet: ( A ) qPCR analyses reveal Tgfβ2 expression does not change in chick (blue circles; n=8) and quail (red squares; n=8) over time; however, in duck (yellow triangles; n=10), there is a decrease at HH37 and HH40; Tgfβ2 is higher in duck than chick or quail at HH31. ( B ) Acvrl1 does not change over time in chick; however, quail show an increase at HH37. There is a reduction in duck at HH40. Duck have higher Acvrl1 at HH34 compared to chick and quail. However, at HH37 and HH40, quail have more Acvrl1 compared to chick or duck. ( C ) Tgfβr2 does not change over time in chick or duck, but in quail, there is an induction at HH37. ( D ) Tgfβr3 does not change over time in chick, quail, or duck. ( E ) Smad3 in chick does not change until HH40 with a reduction. In quail and duck, Smad3 decreases at HH37 and continues to decrease for duck at HH40. Smad3 is higher in chick than quail at HH34 and is higher at HH37 compared to quail and duck. ( F ) Pai1 does not change over time in chick, but quail increase at HH37 and HH40, while duck decrease at the same time points. Duck Pai1 is higher at HH31 and HH34 compared to chick and quail, but at HH37 and HH40 quail it is significantly higher compared to chick and duck. ( G ) Mmp2 increases in chick and quail at HH37, whereas duck decrease at HH40. Chick have higher Mmp2 compared to duck at HH34 and HH37. Quail have higher Mmp2 compared to duck at HH37 and HH40. ( H ) Mmp9 increases in chick, quail, and duck at HH37. Quail have more Mmp9 compared to chick and duck at HH37 and HH40. p≤0.05 and * denotes significance from HH31 within each group, # denotes significance between quail and duck at same stage, † denotes significance between chick and quail, and ‡ denotes significance between chick and duck.

Article Snippet: Membranes were probed with 1:1000 rabbit anti-human pSer423/pSer425 SMAD3 antibody (NBP1-77836, Novus Biologicals, Littleton, CO), 1:1000 rabbit anti-human SMAD3 antibody (NB100-56479, Novus Biologicals, Littleton, CO), 1 μg/ml rabbit anti-chick MMP13 custom-made primary antibody (GenScript, Piscataway, NJ; ), 1:1000 rabbit anti-human MMP2 antibody (NB200-193, Novus Biologicals, Littleton, CO), 1:4000 mouse anti-human β-actin antibody (NB600-501, Novus Biologicals, Littleton, CO), 1:15,000 goat anti-rabbit IRDye 800CW (925–32211, LI-COR, Lincoln, NE), and 1:15,000 donkey anti-mouse IRDye 680RD antibody ( ; 925–68072, LI-COR, Lincoln, NE).

Techniques: Expressing

Protein levels for ( A ) phosphorylated (p) SMAD3 (50 kDa) and ( B ) MMP13 (54 kDa) in chick (n=9), quail (n=12), and duck (n=12) jaws from stages HH31 to HH40 with β-Actin (42 kDa) as a loading control. Dashed lines represent images taken from two separate fluorescent channels on the same gel, 680RD for β-Actin, and 800CW for pSMAD3 or MMP13. Figure 2—figure supplement 2—source data 1. Western blot images for phosphorylated SMAD and β-Actin. Figure 2—figure supplement 2—source data 2. Western blot images for MMP13 and β-Actin.

Journal: eLife

Article Title: Species-specific sensitivity to TGFβ signaling and changes to the Mmp13 promoter underlie avian jaw development and evolution

doi: 10.7554/eLife.66005

Figure Lengend Snippet: Protein levels for ( A ) phosphorylated (p) SMAD3 (50 kDa) and ( B ) MMP13 (54 kDa) in chick (n=9), quail (n=12), and duck (n=12) jaws from stages HH31 to HH40 with β-Actin (42 kDa) as a loading control. Dashed lines represent images taken from two separate fluorescent channels on the same gel, 680RD for β-Actin, and 800CW for pSMAD3 or MMP13. Figure 2—figure supplement 2—source data 1. Western blot images for phosphorylated SMAD and β-Actin. Figure 2—figure supplement 2—source data 2. Western blot images for MMP13 and β-Actin.

Techniques: Control, Western Blot

( A ) pSMAD3 protein levels in cells treated for 2 hr with 5 ng/ml rTGFβ1 (dark gray) in chick (blue) and duck (yellow) cells show a significant induction in chick (n=8). ( B ) Chick and duck cells treated with rTGFβ1 for 1–24 hr. Chick Runx2 mRNA increases with rTGFβ1 treatment at 3 and 6 hr and at 24 hr, while duck Runx2 does not increase until 24 hr. In rTGFβ1 treated cells, duck have significantly lower Runx2 at every time point compared to chick (n=8). ( C ) Chick Mmp13 mRNA increases with rTGFβ1 treatment at 6 hr and at 24 hr, while duck Runx2 does not increase until 24 hr. In rTGFβ1 treated cells, duck have lower Mmp13 at every time point compared to chick (n=8). ( D ) MMP13 protein in cells treated for 24 hr with rTGFβ1 shows an induction in chick but no response in duck (n=8). ( E ) RUNX2 protein levels in chick cells treated for 24 hr with rTGFβ1 (dark gray), TGFβR1 inhibitor (medium gray), a combination of both rTGFβ1 and TGFβR1 inhibitor (black), SMAD3 inhibitor (white), and a combination of both rTGFβ1 and SMAD3 inhibitor (light gray). RUNX2 protein increases with rTGFβ1, but when rTGFβ1 is combined with either a TGFβr1 or a SMAD3 inhibitor, there is a significant decrease compared to rTGFβ1 alone (n=12). ( F ) MMP13 protein increases with rTGFβ1 treatment, but when rTGFβ1 is combined with either a TGFβR1 or a SMAD3 inhibitor, there is a significant decrease compared to rTGFβ1 alone (n=12). * denotes significance from control p≤0.05, ** denotes significance from control p≤0.01, *** denotes significance from control p≤0.001, # denotes significance from rTGFβ1, † denotes significance between chick and quail, and ‡ denotes significance between chick and duck.

Journal: eLife

Article Title: Species-specific sensitivity to TGFβ signaling and changes to the Mmp13 promoter underlie avian jaw development and evolution

doi: 10.7554/eLife.66005

Figure Lengend Snippet: ( A ) pSMAD3 protein levels in cells treated for 2 hr with 5 ng/ml rTGFβ1 (dark gray) in chick (blue) and duck (yellow) cells show a significant induction in chick (n=8). ( B ) Chick and duck cells treated with rTGFβ1 for 1–24 hr. Chick Runx2 mRNA increases with rTGFβ1 treatment at 3 and 6 hr and at 24 hr, while duck Runx2 does not increase until 24 hr. In rTGFβ1 treated cells, duck have significantly lower Runx2 at every time point compared to chick (n=8). ( C ) Chick Mmp13 mRNA increases with rTGFβ1 treatment at 6 hr and at 24 hr, while duck Runx2 does not increase until 24 hr. In rTGFβ1 treated cells, duck have lower Mmp13 at every time point compared to chick (n=8). ( D ) MMP13 protein in cells treated for 24 hr with rTGFβ1 shows an induction in chick but no response in duck (n=8). ( E ) RUNX2 protein levels in chick cells treated for 24 hr with rTGFβ1 (dark gray), TGFβR1 inhibitor (medium gray), a combination of both rTGFβ1 and TGFβR1 inhibitor (black), SMAD3 inhibitor (white), and a combination of both rTGFβ1 and SMAD3 inhibitor (light gray). RUNX2 protein increases with rTGFβ1, but when rTGFβ1 is combined with either a TGFβr1 or a SMAD3 inhibitor, there is a significant decrease compared to rTGFβ1 alone (n=12). ( F ) MMP13 protein increases with rTGFβ1 treatment, but when rTGFβ1 is combined with either a TGFβR1 or a SMAD3 inhibitor, there is a significant decrease compared to rTGFβ1 alone (n=12). * denotes significance from control p≤0.05, ** denotes significance from control p≤0.01, *** denotes significance from control p≤0.001, # denotes significance from rTGFβ1, † denotes significance between chick and quail, and ‡ denotes significance between chick and duck.

Techniques: Control

Protein levels for ( A ) phosphorylated (p) SMAD3 (50 kDa) and ( B ) MMP13 (54 kDa) in chick (DF-1) and duck (CCL-141) cells treated with 5 ng/ml rTGFβ1 for 2 hr. β-Actin (42 kDa) is used as a loading control (n=8). Figure 3—figure supplement 1—source data 1. Western blot images for pSMAD and β-Actin. Figure 3—figure supplement 1—source data 2. Western blot images for MMP13 and β-Actin.

Journal: eLife

Article Title: Species-specific sensitivity to TGFβ signaling and changes to the Mmp13 promoter underlie avian jaw development and evolution

doi: 10.7554/eLife.66005

Figure Lengend Snippet: Protein levels for ( A ) phosphorylated (p) SMAD3 (50 kDa) and ( B ) MMP13 (54 kDa) in chick (DF-1) and duck (CCL-141) cells treated with 5 ng/ml rTGFβ1 for 2 hr. β-Actin (42 kDa) is used as a loading control (n=8). Figure 3—figure supplement 1—source data 1. Western blot images for pSMAD and β-Actin. Figure 3—figure supplement 1—source data 2. Western blot images for MMP13 and β-Actin.

Techniques: Control, Western Blot

Protein levels for ( A ) RUNX2 (55 kDa) and ( B ) MMP13 (54 kDa) in chick cells treated for 24 hr with rTGFβ1, TGFβR1 inhibitor, a combination of both rTGFβ1 and TGFβR1 inhibitor, SMAD3 inhibitor, and a combination of both rTGFβ1 and SMAD3 inhibitor (n=8). β-Actin (42 kDa) is used as a loading control. Figure 3—figure supplement 3—source data 1. Western blot images for RUNX2 and β-Actin. Figure 3—figure supplement 3—source data 2. Western blot images for MMP13 and β-Actin.

Journal: eLife

Article Title: Species-specific sensitivity to TGFβ signaling and changes to the Mmp13 promoter underlie avian jaw development and evolution

doi: 10.7554/eLife.66005

Figure Lengend Snippet: Protein levels for ( A ) RUNX2 (55 kDa) and ( B ) MMP13 (54 kDa) in chick cells treated for 24 hr with rTGFβ1, TGFβR1 inhibitor, a combination of both rTGFβ1 and TGFβR1 inhibitor, SMAD3 inhibitor, and a combination of both rTGFβ1 and SMAD3 inhibitor (n=8). β-Actin (42 kDa) is used as a loading control. Figure 3—figure supplement 3—source data 1. Western blot images for RUNX2 and β-Actin. Figure 3—figure supplement 3—source data 2. Western blot images for MMP13 and β-Actin.

Techniques: Control, Western Blot

Quail lower jaws harvested at HH35 and placed in culture with control beads (left side) and treatment beads (right side) soaked in ( A ) TGFβR1 inhibitor (TGFβi, n=5), ( B ) SMAD3 inhibitor (SMAD3i, n=5), and ( C ) MMP13 inhibitor (MMP13i, n=5). The effects of inhibitor treatments can be seen on TRAP staining (red) after 5 days of culture (red dashed lines). Quantification of the % area of TRAP-positive staining for ( D ) TGFβR1 inhibitor (medium gray), ( E ) SMAD3 inhibitor (white), and ( F ) MMP13 inhibitor (dark gray) in comparison to the contralateral control side. ( G ) In ovo electroporations of the pPIDNB- Mmp13 OE construct were performed at HH8.5 and embryos were allowed to develop until HH35 when they were treated with a single dose of dox. Electroporation efficiency and extent of OE were evaluated during embryo collection at HH40 by detecting RFP (red). Microcomputed tomography (µCT) analysis of duck specimens electroporated with ( H ) empty vector or ( I ) Mmp13 OE construct. A 3D model was annotated with landmarks from which ( J ) lower jaw distances were calculated. Embryos overexpressing Mmp13 showed significantly shorter jaws compared to empty vector controls. * denotes significance from control within each group p≤0.05, ** denotes significance from control within each group p≤0.01, and *** denotes significance from control within each group p≤0.001. Figure 5—source data 1. Effects of TGFβR1, SMAD3, and MMP13 inhibition on TRAP staining in quail embryos. Figure 5—source data 2. Effects of MMP13 overexpression on jaw length in duck embryos as visualized by µCT.

Journal: eLife

Article Title: Species-specific sensitivity to TGFβ signaling and changes to the Mmp13 promoter underlie avian jaw development and evolution

doi: 10.7554/eLife.66005

Figure Lengend Snippet: Quail lower jaws harvested at HH35 and placed in culture with control beads (left side) and treatment beads (right side) soaked in ( A ) TGFβR1 inhibitor (TGFβi, n=5), ( B ) SMAD3 inhibitor (SMAD3i, n=5), and ( C ) MMP13 inhibitor (MMP13i, n=5). The effects of inhibitor treatments can be seen on TRAP staining (red) after 5 days of culture (red dashed lines). Quantification of the % area of TRAP-positive staining for ( D ) TGFβR1 inhibitor (medium gray), ( E ) SMAD3 inhibitor (white), and ( F ) MMP13 inhibitor (dark gray) in comparison to the contralateral control side. ( G ) In ovo electroporations of the pPIDNB- Mmp13 OE construct were performed at HH8.5 and embryos were allowed to develop until HH35 when they were treated with a single dose of dox. Electroporation efficiency and extent of OE were evaluated during embryo collection at HH40 by detecting RFP (red). Microcomputed tomography (µCT) analysis of duck specimens electroporated with ( H ) empty vector or ( I ) Mmp13 OE construct. A 3D model was annotated with landmarks from which ( J ) lower jaw distances were calculated. Embryos overexpressing Mmp13 showed significantly shorter jaws compared to empty vector controls. * denotes significance from control within each group p≤0.05, ** denotes significance from control within each group p≤0.01, and *** denotes significance from control within each group p≤0.001. Figure 5—source data 1. Effects of TGFβR1, SMAD3, and MMP13 inhibition on TRAP staining in quail embryos. Figure 5—source data 2. Effects of MMP13 overexpression on jaw length in duck embryos as visualized by µCT.

Techniques: Control, Staining, Comparison, In Ovo, Construct, Electroporation, Tomography, Plasmid Preparation, Inhibition, Over Expression

Graphical representation of the binding profiles of the position weight matrices taken from the JASPAR 2020 database for ( A ) RUNX2, ( B ) SMAD2/3 heterodimer, ( C ) SMAD3, and ( D ) SMAD4. The relative sizes of the letters indicate their frequency in the sequences, whereas the height of the letters shows the information content of the position.

Journal: eLife

Article Title: Species-specific sensitivity to TGFβ signaling and changes to the Mmp13 promoter underlie avian jaw development and evolution

doi: 10.7554/eLife.66005

Figure Lengend Snippet: Graphical representation of the binding profiles of the position weight matrices taken from the JASPAR 2020 database for ( A ) RUNX2, ( B ) SMAD2/3 heterodimer, ( C ) SMAD3, and ( D ) SMAD4. The relative sizes of the letters indicate their frequency in the sequences, whereas the height of the letters shows the information content of the position.

Techniques: Binding Assay

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