goat anti sin3a Search Results


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The <t>Sin3A</t> co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect <t>Sin3A.</t> <t>β-actin</t> was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.
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The <t>Sin3A</t> co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect <t>Sin3A.</t> <t>β-actin</t> was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.
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The <t>Sin3A</t> co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect <t>Sin3A.</t> <t>β-actin</t> was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.
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The <t>Sin3A</t> co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect <t>Sin3A.</t> <t>β-actin</t> was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.
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The <t>Sin3A</t> co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect <t>Sin3A.</t> <t>β-actin</t> was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.
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The <t>Sin3A</t> co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect <t>Sin3A.</t> <t>β-actin</t> was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.
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The <t>Sin3A</t> co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect <t>Sin3A.</t> <t>β-actin</t> was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.
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The <t>Sin3A</t> co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect <t>Sin3A.</t> <t>β-actin</t> was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.
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The <t>Sin3A</t> co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect <t>Sin3A.</t> <t>β-actin</t> was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.
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The <t>Sin3A</t> co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect <t>Sin3A.</t> <t>β-actin</t> was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.
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The <t>Sin3A</t> co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect <t>Sin3A.</t> <t>β-actin</t> was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.
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The Sin3A co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect Sin3A. β-actin was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.

Journal: International Journal of Biological Sciences

Article Title: ELK3 Suppresses Angiogenesis by Inhibiting the Transcriptional Activity of ETS-1 on MT1-MMP

doi: 10.7150/ijbs.8095

Figure Lengend Snippet: The Sin3A co-repressor regulates ELK3 transcription in HUVECs. (A) The MT1-MMP promoter activity in several cell lines: 293 (human embryonic kidney cells), L-132 (human embryonic pulmonary epithelial cells) and HUVECs (human umbilical vein endothelial cells). The 1.5 kb MT1-MMP promoter was co-transfected with an empty vector (pcDNA3.1), ETS-1 or ELK3 cDNA. After 24 h, the luciferase activity was measured. (B) The protein expression levels of Sin3A in 293 cells, L-132 cells and HUVECs. The proteins were isolated from the 3 cell lines and separated by SDS-PAGE to detect Sin3A. β-actin was used as an internal control. The density of bands was measured by GelQuant.ELK3 software (lower table) (C) Confirmation of Sin3A protein expression in HUVECs following ELK3 overexpression by Western blotting. The ELK3 expression plasmid was transfected into the HUVECs. ELK3 overexpression was confirmed by Western blotting. Sin3A protein expression decreased in response to ELK3 overexpression in HUVECs. The intensity of bands was accessed by GelQuant.ELK3 software (lower table) (D) Sin3A overexpression in HUVECs almost completely abolished ELK3 expression. The intensity of bands was evaluated by GelQuant.ELK3 software (lower table). *p < 0.01 in comparison between ETS-1 and ELK3 transfected cells.

Article Snippet: Next, the membrane was incubated with monoclonal anti-Sin3A (Santa Cruz Biotechnology, sc-994) (1:1000 dilution), anti-ELK3 (Santa Cruz Biotechnology, sc-17860) (1:1000 dilution) or anti-β-actin antibody (1:3000 dilution) overnight at 4°C, then incubated with anti-rabbit IgG antibody (1:2000 dilution, secondary antibody against anti-Sin3A) or anti-goat IgG antibody (1:2000 dilution, secondary antibody against anti-ELK3 and anti-β-actin) for 1 h at room temperature.

Techniques: Activity Assay, Transfection, Plasmid Preparation, Luciferase, Expressing, Isolation, SDS Page, Software, Over Expression, Western Blot