glyceraldehyde 3 phosphate dehydrogenase gapdh Cell Signaling Technology Inc Search Results


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  • 99
    Cell Signaling Technology Inc glyceraldehyde 3 phosphate dehydrogenase gapdh
    Effect of transforming growth factor β (TGFβ 2 ) on SK-1, phospho-Smad2, connective tissue growth factor (CTGF), and fibronectin expression in HK2 cells. ( A ) HK2 cells were taken unstimulated (−) or stimulated with 5 ng/mL of TGFβ 2 for the indicated time periods up to 24 h. Thereafter, cell lysates were prepared and equal amounts of proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), transferred to a nitrocellulose membrane and subjected to Western blotting using antibodies against SK-1 (1:2000 dilution), glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> (1:2000), phospho-Smad2 (1:1000), CTGF (1:500), and fibronectin (1:500). To detect secreted CTGF, equal volumes of supernatants of stimulated cells were taken for protein precipitation by trichloroacetic acid (TCA) and were then analysed the same way as described for lysates using the CTGF antibody. Band intensities were evaluated by a LICOR R imaging system. Data in ( B – F ) show the evaluated respective bands. Results are expressed as fold increase and are means ± S.D. ( n = 3); * p
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1947 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc glyceraldehyde 3 phosphate dehydrogenase gapdh 1 1000
    Effect of transforming growth factor β (TGFβ 2 ) on SK-1, phospho-Smad2, connective tissue growth factor (CTGF), and fibronectin expression in HK2 cells. ( A ) HK2 cells were taken unstimulated (−) or stimulated with 5 ng/mL of TGFβ 2 for the indicated time periods up to 24 h. Thereafter, cell lysates were prepared and equal amounts of proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), transferred to a nitrocellulose membrane and subjected to Western blotting using antibodies against SK-1 (1:2000 dilution), glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> (1:2000), phospho-Smad2 (1:1000), CTGF (1:500), and fibronectin (1:500). To detect secreted CTGF, equal volumes of supernatants of stimulated cells were taken for protein precipitation by trichloroacetic acid (TCA) and were then analysed the same way as described for lysates using the CTGF antibody. Band intensities were evaluated by a LICOR R imaging system. Data in ( B – F ) show the evaluated respective bands. Results are expressed as fold increase and are means ± S.D. ( n = 3); * p
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    Cell Signaling Technology Inc total glyceraldehyde 3 phosphate dehydrogenase gapdh protein
    Effect of transforming growth factor β (TGFβ 2 ) on SK-1, phospho-Smad2, connective tissue growth factor (CTGF), and fibronectin expression in HK2 cells. ( A ) HK2 cells were taken unstimulated (−) or stimulated with 5 ng/mL of TGFβ 2 for the indicated time periods up to 24 h. Thereafter, cell lysates were prepared and equal amounts of proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), transferred to a nitrocellulose membrane and subjected to Western blotting using antibodies against SK-1 (1:2000 dilution), glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> (1:2000), phospho-Smad2 (1:1000), CTGF (1:500), and fibronectin (1:500). To detect secreted CTGF, equal volumes of supernatants of stimulated cells were taken for protein precipitation by trichloroacetic acid (TCA) and were then analysed the same way as described for lysates using the CTGF antibody. Band intensities were evaluated by a LICOR R imaging system. Data in ( B – F ) show the evaluated respective bands. Results are expressed as fold increase and are means ± S.D. ( n = 3); * p
    Total Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh Protein, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 78/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc human glyceraldehyde 3 phosphate dehydrogenase gapdh
    Evaluation of the protein synthesis of myofibroblast phenotype markers and extracellular matrix macromolecules in cultured human systemic sclerosis (SSc) skin fibroblasts. Western blotting and related densitometric analysis of the protein synthesis of α-smooth muscle actin (α-SMA), S100A4, type I collagen (COL-1) and fibronectin (FN) in cultured human SSc skin fibroblasts maintained in normal growth medium (untreated), treated with selexipag at the concentration of 30 μM, 3 μM, and 0.3 μM, and treated with ACT-333679 at the concentration of 10 μM, 1 μM, and 0.1 μM, for 48 h. For each experimental condition, the value of the synthesis of α-SMA, S100A4, COL-1, and FN was normalized to that of the corresponding glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH).</t> The resulting value with each treatment was compared to that of the untreated cells (taken as a unit value), in order to obtain the level of protein synthesis. A molecular weight (MW) lane was also included. The final results represent the mean ± standard deviation (SD) of the values obtained from six independent experiments on cultured human SSc skin fibroblasts: * p
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    Cell Signaling Technology Inc glyceraldehyde 3 phosphate dehydrogenase gapdh hrp
    Evaluation of the protein synthesis of myofibroblast phenotype markers and extracellular matrix macromolecules in cultured human systemic sclerosis (SSc) skin fibroblasts. Western blotting and related densitometric analysis of the protein synthesis of α-smooth muscle actin (α-SMA), S100A4, type I collagen (COL-1) and fibronectin (FN) in cultured human SSc skin fibroblasts maintained in normal growth medium (untreated), treated with selexipag at the concentration of 30 μM, 3 μM, and 0.3 μM, and treated with ACT-333679 at the concentration of 10 μM, 1 μM, and 0.1 μM, for 48 h. For each experimental condition, the value of the synthesis of α-SMA, S100A4, COL-1, and FN was normalized to that of the corresponding glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH).</t> The resulting value with each treatment was compared to that of the untreated cells (taken as a unit value), in order to obtain the level of protein synthesis. A molecular weight (MW) lane was also included. The final results represent the mean ± standard deviation (SD) of the values obtained from six independent experiments on cultured human SSc skin fibroblasts: * p
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    Cell Signaling Technology Inc glyceraldehyde 3 phosphate dehydrogenase
    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
    Antihuman Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh Antibodies, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 79/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Cell Signaling Technology Inc glyceraldehyde 3 phosphate dehydrogenase gapdh primary antibody
    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    Cell Signaling Technology Inc glyceraldehyde 3 phosphate dehydrogenase gapdh monoclonal antibody
    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh Monoclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 79/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    Cell Signaling Technology Inc reference protein glyceraldehyde 3 phosphate dehydrogenase
    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    Cell Signaling Technology Inc glyceraldehyde 3 phosphate dehydrogenase gapdh 1 2500
    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    Cell Signaling Technology Inc rabbit monoclonal antibody against glyceraldehyde 3 phosphate dehydrogenase gapdh
    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    Cell Signaling Technology Inc mouse anti glyceraldehyde 3 phosphate dehydrogenase gapdh igg
    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
    Hrp Conjugated Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 80/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    Cell Signaling Technology Inc rabbit monoclonal anti human glyceraldehyde 3 phosphate dehydrogenase gapdh
    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 
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    Cell Signaling Technology Inc hrp conjugated antibodies against glyceraldehyde 3 phosphate dehydrogenase gapdh hrp
    Increasing GLUT1 expression increases trans-plasma membrane electron transport (tPMET). ( a ) Western blot analysis confirms effective lipofectamine transfection. Glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> was utilized as the loading control. N = 3 ( b ) Western blot quantification demonstrates that the transfected samples have a ~30% increase in GLUT1 expression. N = 3/group, * p
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    TGF-β1 promotes phosphorylation of Smad2 linker region in human VSMCs. VSMCs were stimulated for 0.5, 1 and 2 h with TGF-β1 (2 ng/ml), harvested and total protein was extracted. Proteins were resolved by 10% SDS-PAGE and then transferred to PVDF membrane. Membranes were incubated with anti-phospho-Smad2 (Ser245/250/255) (1:1000) and then followed by incubation with peroxidase labeled anti-rabbit <t>IgG</t> (1:10000) and ECL detection. <t>Anti-GAPDH</t> was used as loading control. Normalized data in each case are shown as mean ± SEM from three independent experiments and statistical significance was determined by One-way ANOVA followed by least significant difference post-hoc analysis. * p
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    TGF-β1 promotes phosphorylation of Smad2 linker region in human VSMCs. VSMCs were stimulated for 0.5, 1 and 2 h with TGF-β1 (2 ng/ml), harvested and total protein was extracted. Proteins were resolved by 10% SDS-PAGE and then transferred to PVDF membrane. Membranes were incubated with anti-phospho-Smad2 (Ser245/250/255) (1:1000) and then followed by incubation with peroxidase labeled anti-rabbit <t>IgG</t> (1:10000) and ECL detection. <t>Anti-GAPDH</t> was used as loading control. Normalized data in each case are shown as mean ± SEM from three independent experiments and statistical significance was determined by One-way ANOVA followed by least significant difference post-hoc analysis. * p
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    TGF-β1 promotes phosphorylation of Smad2 linker region in human VSMCs. VSMCs were stimulated for 0.5, 1 and 2 h with TGF-β1 (2 ng/ml), harvested and total protein was extracted. Proteins were resolved by 10% SDS-PAGE and then transferred to PVDF membrane. Membranes were incubated with anti-phospho-Smad2 (Ser245/250/255) (1:1000) and then followed by incubation with peroxidase labeled anti-rabbit <t>IgG</t> (1:10000) and ECL detection. <t>Anti-GAPDH</t> was used as loading control. Normalized data in each case are shown as mean ± SEM from three independent experiments and statistical significance was determined by One-way ANOVA followed by least significant difference post-hoc analysis. * p
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    TGF-β1 promotes phosphorylation of Smad2 linker region in human VSMCs. VSMCs were stimulated for 0.5, 1 and 2 h with TGF-β1 (2 ng/ml), harvested and total protein was extracted. Proteins were resolved by 10% SDS-PAGE and then transferred to PVDF membrane. Membranes were incubated with anti-phospho-Smad2 (Ser245/250/255) (1:1000) and then followed by incubation with peroxidase labeled anti-rabbit <t>IgG</t> (1:10000) and ECL detection. <t>Anti-GAPDH</t> was used as loading control. Normalized data in each case are shown as mean ± SEM from three independent experiments and statistical significance was determined by One-way ANOVA followed by least significant difference post-hoc analysis. * p
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    Image Search Results


    Effect of transforming growth factor β (TGFβ 2 ) on SK-1, phospho-Smad2, connective tissue growth factor (CTGF), and fibronectin expression in HK2 cells. ( A ) HK2 cells were taken unstimulated (−) or stimulated with 5 ng/mL of TGFβ 2 for the indicated time periods up to 24 h. Thereafter, cell lysates were prepared and equal amounts of proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), transferred to a nitrocellulose membrane and subjected to Western blotting using antibodies against SK-1 (1:2000 dilution), glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (1:2000), phospho-Smad2 (1:1000), CTGF (1:500), and fibronectin (1:500). To detect secreted CTGF, equal volumes of supernatants of stimulated cells were taken for protein precipitation by trichloroacetic acid (TCA) and were then analysed the same way as described for lysates using the CTGF antibody. Band intensities were evaluated by a LICOR R imaging system. Data in ( B – F ) show the evaluated respective bands. Results are expressed as fold increase and are means ± S.D. ( n = 3); * p

    Journal: International Journal of Molecular Sciences

    Article Title: Downregulation of the S1P Transporter Spinster Homology Protein 2 (Spns2) Exerts an Anti-Fibrotic and Anti-Inflammatory Effect in Human Renal Proximal Tubular Epithelial Cells

    doi: 10.3390/ijms19051498

    Figure Lengend Snippet: Effect of transforming growth factor β (TGFβ 2 ) on SK-1, phospho-Smad2, connective tissue growth factor (CTGF), and fibronectin expression in HK2 cells. ( A ) HK2 cells were taken unstimulated (−) or stimulated with 5 ng/mL of TGFβ 2 for the indicated time periods up to 24 h. Thereafter, cell lysates were prepared and equal amounts of proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), transferred to a nitrocellulose membrane and subjected to Western blotting using antibodies against SK-1 (1:2000 dilution), glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (1:2000), phospho-Smad2 (1:1000), CTGF (1:500), and fibronectin (1:500). To detect secreted CTGF, equal volumes of supernatants of stimulated cells were taken for protein precipitation by trichloroacetic acid (TCA) and were then analysed the same way as described for lysates using the CTGF antibody. Band intensities were evaluated by a LICOR R imaging system. Data in ( B – F ) show the evaluated respective bands. Results are expressed as fold increase and are means ± S.D. ( n = 3); * p

    Article Snippet: S1P and all C17-sphingolipid standards were from Avanti Polar Lipids Inc. (Alabaster, AL, USA); caged-S1P was from Enzo Life Sciences Inc. (Farmingdale, NY, USA); human TGF-β2 , TNFα, and IL-1β were from Peprotech (London, UK); BAF312 was from Selleck Chemicals Inc. (Houston, TX, USA); CYM5442, CYM5520, CYM5541, puromycin, the lentiviral particles of human Spns2 and SK-1 shRNA constructs (MISSION® shRNA), diamidine-phenylindole (DAPI), and the antibodies against α-tubulin and Spns2 (SAB2104271) were from Sigma Aldrich Chemikalien, (Buchs, Switzerland); antibodies against phospho-ERK1/2, phospho-Smad2, and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) were from Cell Signaling Technology (Danvers, MA, USA); antibodies against CTGF (L-20) and fibronectin (EP5) were from Santa Cruz (Heidelberg, Germany); the AQP1 antibody ( (B)) was from Abcam plc (Cambridge, UK); the human SK-1 antibody was generated and characterized, as previously described [ , ].

    Techniques: Expressing, Polyacrylamide Gel Electrophoresis, SDS Page, Western Blot, Imaging

    Expression of peroxisome proliferator-activated receptor-gamma coactivator-1 β (PGC-1β) is over-expressed in rheumatoid arthritis (RA)-fibrolast-like synoviocytes (FLS). (A) Immunofluorescence staining of PGC-1β in primary cultures of FLS from osteoarthritis (OA) and RA patients. (a, DAPI (blue); b, PGC-1β (green); c, neutral light; d, merged a, b with c. a, b, c: original magnification × 400). (B) Left panel: PGC-1β mRNA expression in FLS from RA (n = 8) compared with that from OA (n =6) evaluated by qPCR. Right panel: PGC-1β protein level in FLS from RA patients (n = 8) and OA controls (n = 6) was detected by western blot. The intensity for each band was densitometrically quantified and normalized against the intensity of glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The data are represented by mean ± SD. * P

    Journal: Arthritis Research & Therapy

    Article Title: Down-regulating peroxisome proliferator-activated receptor-gamma coactivator-1beta alleviates the proinflammatory effect of rheumatoid arthritis fibroblast-like synoviocytes through inhibiting extracellular signal-regulated kinase, p38 and nuclear factor-kappaB activation

    doi: 10.1186/s13075-014-0472-6

    Figure Lengend Snippet: Expression of peroxisome proliferator-activated receptor-gamma coactivator-1 β (PGC-1β) is over-expressed in rheumatoid arthritis (RA)-fibrolast-like synoviocytes (FLS). (A) Immunofluorescence staining of PGC-1β in primary cultures of FLS from osteoarthritis (OA) and RA patients. (a, DAPI (blue); b, PGC-1β (green); c, neutral light; d, merged a, b with c. a, b, c: original magnification × 400). (B) Left panel: PGC-1β mRNA expression in FLS from RA (n = 8) compared with that from OA (n =6) evaluated by qPCR. Right panel: PGC-1β protein level in FLS from RA patients (n = 8) and OA controls (n = 6) was detected by western blot. The intensity for each band was densitometrically quantified and normalized against the intensity of glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The data are represented by mean ± SD. * P

    Article Snippet: Western blot analysis Protein lysates from cells were subjected to SDS-PAGE and target proteins were detected with primary antibodies recognizing p-p38, p38, P-extracellular signal-regulated kinase (P-ERK), ERK, p-JNK, JNK, p-NF-κB p65 (Ser536), NF-κβ p65 and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (CST, Danvers, Massachusetts, USA), PGC-1β and RANKL (Epitomics, San Francisco, USA), MMP-3 and MMP-13 (Abcam, Cambridge, USA) respectively.

    Techniques: Expressing, Pyrolysis Gas Chromatography, Immunofluorescence, Staining, Real-time Polymerase Chain Reaction, Western Blot

    Anesthesia with 2.5% sevoflurane for 2 hours in pregnant mice on the 15th day of gestation induced caspase-3 activation in the cochlear tissues of fetal mice. Notes: Representative Western blot images of caspase-3 and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in fetal tissue samples from the sevoflurane and control groups ( A ). Semiquantification of the Western blot showed that compared with the control conditions, sevoflurane anesthesia was associated with greater quantities of caspase-3 in fetal mice cochlear tissues ( B ). Expression of Bcl-2 in fetal cochlear tissues was higher in the sevoflurane group ( C and D ). *** P

    Journal: Drug Design, Development and Therapy

    Article Title: Sevoflurane anesthesia during pregnancy in mice induces hearing impairment in the offspring

    doi: 10.2147/DDDT.S156040

    Figure Lengend Snippet: Anesthesia with 2.5% sevoflurane for 2 hours in pregnant mice on the 15th day of gestation induced caspase-3 activation in the cochlear tissues of fetal mice. Notes: Representative Western blot images of caspase-3 and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in fetal tissue samples from the sevoflurane and control groups ( A ). Semiquantification of the Western blot showed that compared with the control conditions, sevoflurane anesthesia was associated with greater quantities of caspase-3 in fetal mice cochlear tissues ( B ). Expression of Bcl-2 in fetal cochlear tissues was higher in the sevoflurane group ( C and D ). *** P

    Article Snippet: Caspase-3 antibody (1:1,000, CY3457; Abways Technology, Beijing, People’s Republic of China), Bcl-2 (1:1,000, ab32124; Abcam, Cambridge, MA, USA), COX-2 (1:1,000, ab15191; Abcam), iNOS (1:1,000, ab15323; Abcam), glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibody (1:1,000, rabbit polyclonal; Cell Signaling Technology, Beverly, MA, USA), and β-actin (1:1,000, ab8226; Abcam) were the primary antibodies.

    Techniques: Mouse Assay, Activation Assay, Western Blot, Expressing

    Enrichment of HA-KCNQ3/KCNQ2 channels and CD4-Q2C at the axonal surface. Schematic drawings (not to scale) of a human KCNQ2 subunit (accession #Y15065), including the subunit interaction domain (Sid, amino acids 580–623) [52] , [53] , and CaM-binding domain (amino acids 323–579) [22] , [23] . (B) Immunoblot analysis of CaM in cultured rat hippocampal neurons at 5–9 days in vitro (DIV). Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) served as a loading control. (C) Schematic drawings (not to scale) of a human CD4 protein, and CD4 fused to KCNQ2 C-terminal tail (CD4-Q2C, [18] ). (D) Surface immunostaining of hippocampal neurons (DIV 7) transfected with KCNQ2 and KCNQ3 containing an extracellular hemagglutinin (HA) epitope (HA-KCNQ3). Neuronal soma and dendrites were visualized by immunostaining for MAP2. Surface HA-KCNQ3/KCNQ2 channels are enriched on a MAP2-negative neurite that originates directly from the soma. (E) Pseudo-color image of the inset in Fig. 1D displays differences in the surface HA intensity. Surface HA-KCNQ3/KCNQ2 channels are enriched at the initial segment of an axon. (F) Surface immunostaining of hippocampal neurons (DIV 8) transfected with CD4, or CD4-Q2C. (G) Pseudo-color images of the insets in Fig. 1F display differences in the surface CD4 intensity. Fusion of KCNQ2 C-terminal tail enriches CD4 at the axonal surface. Camera lucida drawings of the neuronal images (D, F) show the soma and dendrites (gray) and an axon (black). Arrows mark the main axon. Scale bars are 20 µm.

    Journal: PLoS ONE

    Article Title: Polarized Axonal Surface Expression of Neuronal KCNQ Potassium Channels Is Regulated by Calmodulin Interaction with KCNQ2 Subunit

    doi: 10.1371/journal.pone.0103655

    Figure Lengend Snippet: Enrichment of HA-KCNQ3/KCNQ2 channels and CD4-Q2C at the axonal surface. Schematic drawings (not to scale) of a human KCNQ2 subunit (accession #Y15065), including the subunit interaction domain (Sid, amino acids 580–623) [52] , [53] , and CaM-binding domain (amino acids 323–579) [22] , [23] . (B) Immunoblot analysis of CaM in cultured rat hippocampal neurons at 5–9 days in vitro (DIV). Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) served as a loading control. (C) Schematic drawings (not to scale) of a human CD4 protein, and CD4 fused to KCNQ2 C-terminal tail (CD4-Q2C, [18] ). (D) Surface immunostaining of hippocampal neurons (DIV 7) transfected with KCNQ2 and KCNQ3 containing an extracellular hemagglutinin (HA) epitope (HA-KCNQ3). Neuronal soma and dendrites were visualized by immunostaining for MAP2. Surface HA-KCNQ3/KCNQ2 channels are enriched on a MAP2-negative neurite that originates directly from the soma. (E) Pseudo-color image of the inset in Fig. 1D displays differences in the surface HA intensity. Surface HA-KCNQ3/KCNQ2 channels are enriched at the initial segment of an axon. (F) Surface immunostaining of hippocampal neurons (DIV 8) transfected with CD4, or CD4-Q2C. (G) Pseudo-color images of the insets in Fig. 1F display differences in the surface CD4 intensity. Fusion of KCNQ2 C-terminal tail enriches CD4 at the axonal surface. Camera lucida drawings of the neuronal images (D, F) show the soma and dendrites (gray) and an axon (black). Arrows mark the main axon. Scale bars are 20 µm.

    Article Snippet: Reagents used in immunoprecipitation and western blotting include human embryonic kidney (HEK) 293T cell lines (ATCC, CRL-11268) and antibodies including anti-CD4 (Santa Cruz Biotech, sc-13573), anti-HA (Covance, MMS-101P, Cell Signaling, 3724), anti-KCNQ2 (Alamone, APC-050; Neuromab, N26A/23), anti-CaM (Novus Biologicals, NB110-55649; Santa Cruz, SC137079; Cell Signaling, 4830), anti-HA, anti-β-actin, and anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibodies (Cell Signaling, 3724, 4967, and 2118).

    Techniques: Chick Chorioallantoic Membrane Assay, Binding Assay, Cell Culture, In Vitro, Immunostaining, Transfection

    Differences in the expression levels of vinculin and integrin-linked kinase-1 (ILK-1) between the MCF-7 and MCR-7/ADR cells. (A) Representative western blotting images of vinculin and ILK-1 proteins. (B) Quantitative evaluation of vinculin and ILK-1 expression levels in the MCF-7/ADR cells normalized to those in the MCF-7 cells. GAPDH, glyceraldehyde 3-phosphate dehydrogenase. * P

    Journal: Journal of Cancer Prevention

    Article Title: Mechanical Alteration Associated With Chemotherapeutic Resistance of Breast Cancer Cells

    doi: 10.15430/JCP.2018.23.2.87

    Figure Lengend Snippet: Differences in the expression levels of vinculin and integrin-linked kinase-1 (ILK-1) between the MCF-7 and MCR-7/ADR cells. (A) Representative western blotting images of vinculin and ILK-1 proteins. (B) Quantitative evaluation of vinculin and ILK-1 expression levels in the MCF-7/ADR cells normalized to those in the MCF-7 cells. GAPDH, glyceraldehyde 3-phosphate dehydrogenase. * P

    Article Snippet: The blots were detected with anti-glyceraldehyde 3-phosphate dehydrogenase (anti-GAPDH), anti-vinculin, and anti-ILK-1 primary antibodies bought from Cell Signaling Technology (Danvers, MA, USA) or Abcam (Cambridge, UK).

    Techniques: Expressing, Western Blot

    Blue honeysuckle extract (BHE) improved hepatic antioxidant capacity. (A) The level of thiobarbituric acid reactive substances (TBARS) in liver. (B) The representative blots of nuclear factor (erythroid-derived 2)-like 2 (Nrf2), heme oxygenase-1 (HO-1), and manganese-dependent superoxide dismutase (MnSOD) protein in liver by Western blotting. The induction folds of the proteins were calculated as the intensity of the treatment relative to that of control normalized to glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by densitometry. Data represent means ± SD of 4 mice, and the blots are representatives of 4 samples. Bars with different letters differ significantly ( P

    Journal: Animal Nutrition

    Article Title: Inhibitory effect of blue honeysuckle extract on high-fat-diet-induced fatty liver in mice

    doi: 10.1016/j.aninu.2018.06.001

    Figure Lengend Snippet: Blue honeysuckle extract (BHE) improved hepatic antioxidant capacity. (A) The level of thiobarbituric acid reactive substances (TBARS) in liver. (B) The representative blots of nuclear factor (erythroid-derived 2)-like 2 (Nrf2), heme oxygenase-1 (HO-1), and manganese-dependent superoxide dismutase (MnSOD) protein in liver by Western blotting. The induction folds of the proteins were calculated as the intensity of the treatment relative to that of control normalized to glyceraldehyde-3-phosphate dehydrogenase (GAPDH) by densitometry. Data represent means ± SD of 4 mice, and the blots are representatives of 4 samples. Bars with different letters differ significantly ( P

    Article Snippet: Antibodies against glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and corresponding secondary antibodies were purchased from Cell Signaling Technology (Beverly, MA, USA).

    Techniques: Derivative Assay, Western Blot, Mouse Assay

    Immunoblotting for 1α-hydroxylase, 24-hydroxylase, NPT-2a, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (a). Densitometric quantification of the corresponding bands was performed using an image analyzer, 1α-hydroxylase (b) 24-hydroxylase (c), and NPT-2a (d). Data are presented after normalization to GAPDH expression and are depicted as the percentage change from the respective controls (Sham+NP). Data are shown as mean ± s.e. ( n = 4 each). *P

    Journal: PLoS ONE

    Article Title: Intravenous Phosphate Loading Increases Fibroblast Growth Factor 23 in Uremic Rats

    doi: 10.1371/journal.pone.0091096

    Figure Lengend Snippet: Immunoblotting for 1α-hydroxylase, 24-hydroxylase, NPT-2a, and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (a). Densitometric quantification of the corresponding bands was performed using an image analyzer, 1α-hydroxylase (b) 24-hydroxylase (c), and NPT-2a (d). Data are presented after normalization to GAPDH expression and are depicted as the percentage change from the respective controls (Sham+NP). Data are shown as mean ± s.e. ( n = 4 each). *P

    Article Snippet: The source and concentration of each antibody were as follows: rabbit anti-1α-hydroxylase (Santa Cruz Biotechnology; 1∶200), rabbit anti-24-hydroxylase, goat anti-NPT2a (Santa Cruz Biotechnology; 1∶100), and rabbit anti- glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (Cell Signaling Technology; 1∶500).

    Techniques: Expressing

    Effect of administration of alirocumab (monoclonal antibody to PCSK9) or control antibody (10 mg/kg) on LDLR and CD81 levels in hyperlipidemic Pcsk9 hum/hum Ldlr +/- mice. Shown are mean ± SE serum LDL-C levels (A) and Western blot analysis of CD81 and LDLR levels in liver extracts using GAPDH as loading control (B). Western blot in B was quantified using Image J. The intensities of CD81 and LDLR bands were adjusted to respective loading control for each lane and presented as a fold change from control antibody treated group. Means ± SE are shown. Serum and livers were collected on Day 4 after antibody administration. In panel B, the three columns represent three livers collected for each of the two treatments. Ab, antibody; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; LDL-C, low-density lipoprotein cholesterol; LDLR, low-density lipoprotein receptor; mAb, monoclonal Ab.

    Journal: PLoS ONE

    Article Title: Alirocumab, a Therapeutic Human Antibody to PCSK9, Does Not Affect CD81 Levels or Hepatitis C Virus Entry and Replication into Hepatocytes

    doi: 10.1371/journal.pone.0154498

    Figure Lengend Snippet: Effect of administration of alirocumab (monoclonal antibody to PCSK9) or control antibody (10 mg/kg) on LDLR and CD81 levels in hyperlipidemic Pcsk9 hum/hum Ldlr +/- mice. Shown are mean ± SE serum LDL-C levels (A) and Western blot analysis of CD81 and LDLR levels in liver extracts using GAPDH as loading control (B). Western blot in B was quantified using Image J. The intensities of CD81 and LDLR bands were adjusted to respective loading control for each lane and presented as a fold change from control antibody treated group. Means ± SE are shown. Serum and livers were collected on Day 4 after antibody administration. In panel B, the three columns represent three livers collected for each of the two treatments. Ab, antibody; GAPDH, glyceraldehyde 3-phosphate dehydrogenase; LDL-C, low-density lipoprotein cholesterol; LDLR, low-density lipoprotein receptor; mAb, monoclonal Ab.

    Article Snippet: Anti-mouse CD81 antibody (EAT-2, sc-18877, monoclonal Armenian hamster; Santa Cruz Biotechnology Inc., Dallas, TX, USA), anti-human CD81 antibody (sc-9158, polyclonal rabbit; Santa Cruz Biotechnology Inc.), anti-mouse LDLR antibody (AF2255, polyclonal goat; R & D Systems, NE Minneapolis, MN, USA), anti-human LDLR antibody (AF2148, polyclonal goat; R & D Systems), anti-human transferrin receptor (TfR) antibody (loading controls) that cross reacts with mouse TfR (AF2474, polyclonal goat; R & D Systems), anti-human glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (loading control) that cross reacts with mouse (2118S, monoclonal rabbit; Cell Signaling Technology, Danvers, MA, USA), and anti-mouse actin (loading control) that cross reacts with human (ab3280, monoclonal mouse; Abcam, Cambridge, MA, USA) were used in Western blot analyses.

    Techniques: Mouse Assay, Western Blot

    Immunoblot analysis of the mammalian target of rapamycin (mTOR) protein content ( A ) and phosphorylation ( B ) at Ser 2448 in control and overloaded soleus muscles of lean Zucker (LZ) and obese Zucker (OZ) rats. Data are expressed as integrated optical density (IOD) × band area and expressed in arbitrary units relative to the amount of glyceraldehyde-3-phosphate dehydrogenase (GAPDH); n = 6. †Significantly different from contralateral control muscle, P

    Journal: American Journal of Physiology - Regulatory, Integrative and Comparative Physiology

    Article Title: Impaired overload-induced hypertrophy is associated with diminished mTOR signaling in insulin-resistant skeletal muscle of the obese Zucker rat

    doi: 10.1152/ajpregu.00229.2010

    Figure Lengend Snippet: Immunoblot analysis of the mammalian target of rapamycin (mTOR) protein content ( A ) and phosphorylation ( B ) at Ser 2448 in control and overloaded soleus muscles of lean Zucker (LZ) and obese Zucker (OZ) rats. Data are expressed as integrated optical density (IOD) × band area and expressed in arbitrary units relative to the amount of glyceraldehyde-3-phosphate dehydrogenase (GAPDH); n = 6. †Significantly different from contralateral control muscle, P

    Article Snippet: For immunodetection, membranes were blocked for 1 h at room temperature in blocking buffer [5% nonfat dry milk in 20 mM Tris-base, 150 mM NaCl, and 0.05% Tween 20 (TBS-T), pH 7.6], serially washed in TBS-T at room temperature, and then probed with antibodies for the detection of Akt (no. 9272), phospho-Akt (Ser473 ) (no. 9271), phospho-Akt (Thr308 ) (no. 9275), mTOR (no. 2972), phospho-mTOR (Ser2448 ) (no. 2971), p70S6k (no. 9202), phospho-p70S6k (Thr389 ) (no. 9205), phospho-p70S6k (Thr421 /Ser424 ) (no. 9204), rpS6 (no. 2217), phospho-rpS6 (Ser235/ 236 ) (no. 4858), 4E-BP1 (no. 9452), phospho 4E-BP1 (Thr37/46 ) (no. 9459), eEF2 (no. 2332), phospho-eEF2 (Thr56 ) (no. 2331), Raptor (no. 2280), Tuberin/TSC2 (no. 3612), phospho-Tuberin/TSC2 (Thr1462 ) (no. 3617), PTEN (no. 9552), phospho-PTEN (Ser380 /Thr382/383 ) (no. 9552), PI 3-kinase (no. 4257), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (no. 2118) (from Cell Signaling Technology, Beverly, MA), and myogenin (M-225) (sc-576) and myo-D (C-20) (sc-304) (from Santa Cruz Biotechnology, Santa Cruz, CA).

    Techniques:

    Effect of cannabidiol (CBD) on transepithelial electrical resistance (TEER) and barrier integrity of Clostridium difficile toxin A (TcdA)-exposed Caco-2 cells. (a) 24 h Time course TEER changes following treatment ( n = 4); (b) immunofluorescent staining showing the effects of TcdA on zonula occludens-1 (ZO-1) and occludin co-expression at 24 h. Nuclei were stained by DAPI (scalebar = 25 µm); (c) immunoreactive bands corresponding to ZO-1 and occludin expression at 24 h following the TcdA challenge; (d) relative densitometric analysis of immunoreactive bands (arbitrary units normalised against the expression of the housekeeping glyceraldehyde-3-phosphate dehydrogenase (GAPDH) protein; n = 5). Results are expressed as mean ± standard error of the mean (SEM) of experiments performed in triplicate. *** p

    Journal: United European Gastroenterology Journal

    Article Title: Cannabidiol restores intestinal barrier dysfunction and inhibits the apoptotic process induced by Clostridium difficile toxin A in Caco-2 cells

    doi: 10.1177/2050640617698622

    Figure Lengend Snippet: Effect of cannabidiol (CBD) on transepithelial electrical resistance (TEER) and barrier integrity of Clostridium difficile toxin A (TcdA)-exposed Caco-2 cells. (a) 24 h Time course TEER changes following treatment ( n = 4); (b) immunofluorescent staining showing the effects of TcdA on zonula occludens-1 (ZO-1) and occludin co-expression at 24 h. Nuclei were stained by DAPI (scalebar = 25 µm); (c) immunoreactive bands corresponding to ZO-1 and occludin expression at 24 h following the TcdA challenge; (d) relative densitometric analysis of immunoreactive bands (arbitrary units normalised against the expression of the housekeeping glyceraldehyde-3-phosphate dehydrogenase (GAPDH) protein; n = 5). Results are expressed as mean ± standard error of the mean (SEM) of experiments performed in triplicate. *** p

    Article Snippet: The antibodies rabbit anti-zonula occludens-1 (ZO-1), rabbit anti-occludin, rabbit anti-bax and rabbit anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibodies were procured from Cell Signalling Technology (Danvers, Massachusetts, USA).

    Techniques: Staining, Expressing

    Effect of cannabidiol (CBD) on Clostridium difficile toxin A (TcdA)-induced cells toxicity and apoptosis. (a) 3-[4,5-Dimethylthiazol-2-yl]-2,5 diphenyltetrazolium bromide (MTT) cell viability absorbance at 24 h ( n = 5); (b) immunoreactive bands corresponding to RhoA GTP and Bax expression at 24 h following the TcdA challenge; (c) relative densitometric analysis of immunoreactive bands (arbitrary units normalised against the expression of the housekeeping glyceraldehyde-3-phosphate dehydrogenase (GAPDH) protein; n = 5). Results are expressed as mean ± standard error of the mean (SEM) of experiments performed in triplicate. *** p

    Journal: United European Gastroenterology Journal

    Article Title: Cannabidiol restores intestinal barrier dysfunction and inhibits the apoptotic process induced by Clostridium difficile toxin A in Caco-2 cells

    doi: 10.1177/2050640617698622

    Figure Lengend Snippet: Effect of cannabidiol (CBD) on Clostridium difficile toxin A (TcdA)-induced cells toxicity and apoptosis. (a) 3-[4,5-Dimethylthiazol-2-yl]-2,5 diphenyltetrazolium bromide (MTT) cell viability absorbance at 24 h ( n = 5); (b) immunoreactive bands corresponding to RhoA GTP and Bax expression at 24 h following the TcdA challenge; (c) relative densitometric analysis of immunoreactive bands (arbitrary units normalised against the expression of the housekeeping glyceraldehyde-3-phosphate dehydrogenase (GAPDH) protein; n = 5). Results are expressed as mean ± standard error of the mean (SEM) of experiments performed in triplicate. *** p

    Article Snippet: The antibodies rabbit anti-zonula occludens-1 (ZO-1), rabbit anti-occludin, rabbit anti-bax and rabbit anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibodies were procured from Cell Signalling Technology (Danvers, Massachusetts, USA).

    Techniques: MTT Assay, Expressing

    Proliferative ability and proliferating cell nuclear antigen (PCNA) expression of cultured palpebral and fornical conjunctival epithelial cells (PFCECs), bulbar conjunctival epithelial cells (BCECs), and lacrimal duct epithelial cells (LDECs) (a) Proliferative ability of epithelial cells after cultured in vitro for 24, 48, and 72 h, respectively. Results, expressed as ratios of BCECs, are given in terms of the mean±standard deviation (SD) ( n =6 for three individual cultures). (b) Western blotting analysis of PCNA contents in epithelial cells after cultured in vitro for 72 h. Increased expression levels of PCNA, normalized with glyceraldehyde-3-phosphate dehydrogenase (GAPDH), were observed in the PFCECs and LDECs, respectively. Results of protein relative ratio are presented as mean±SD ( n =3 for three individual experiments). The significance of differences ( * P

    Journal: Journal of Zhejiang University. Science. B

    Article Title: Potential candidate cells for constructing tissue-engineered lacrimal duct epithelium: a histological and cytological study in rabbits *

    doi: 10.1631/jzus.B1500113

    Figure Lengend Snippet: Proliferative ability and proliferating cell nuclear antigen (PCNA) expression of cultured palpebral and fornical conjunctival epithelial cells (PFCECs), bulbar conjunctival epithelial cells (BCECs), and lacrimal duct epithelial cells (LDECs) (a) Proliferative ability of epithelial cells after cultured in vitro for 24, 48, and 72 h, respectively. Results, expressed as ratios of BCECs, are given in terms of the mean±standard deviation (SD) ( n =6 for three individual cultures). (b) Western blotting analysis of PCNA contents in epithelial cells after cultured in vitro for 72 h. Increased expression levels of PCNA, normalized with glyceraldehyde-3-phosphate dehydrogenase (GAPDH), were observed in the PFCECs and LDECs, respectively. Results of protein relative ratio are presented as mean±SD ( n =3 for three individual experiments). The significance of differences ( * P

    Article Snippet: The transferred polyvinylidene difluoride (PVDF) membranes were incubated with rabbit anti-PCNA antibody (1:2000, v/v) and rabbit anti-glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody (1:2000, v/v; CST).

    Techniques: Expressing, Cell Culture, In Vitro, Standard Deviation, Western Blot

    (A) Immunoblotting for aquaporin 1 (AQP1) and caveolin 1 (CAV1) in the rat urinary bladder. The anti-AQP1 antibody recognizes the 27-29 kDa bands that correspond to glycosylated AQP1. The anti-CAV1 antibody recognizes a 22 kDa band. The anti-GAPDH antibody recognizes a 42 kDa band. The expression of the AQP1 and CAV1 proteins was significantly increased in the bladder outlet obstruction (BOO) group. (B) The lower panel denotes the means±standard deviation of 10 experiments for each condition, as determined by densitometry relative to GAPDH. Con, control; GAPDH, glyceraldehyde 3-phosphate dehydrogenase. * P

    Journal: International Neurourology Journal

    Article Title: Overexpression of Aquaporin-1 and Caveolin-1 in the Rat Urinary Bladder Urothelium Following Bladder Outlet Obstruction

    doi: 10.5213/inj.2013.17.4.174

    Figure Lengend Snippet: (A) Immunoblotting for aquaporin 1 (AQP1) and caveolin 1 (CAV1) in the rat urinary bladder. The anti-AQP1 antibody recognizes the 27-29 kDa bands that correspond to glycosylated AQP1. The anti-CAV1 antibody recognizes a 22 kDa band. The anti-GAPDH antibody recognizes a 42 kDa band. The expression of the AQP1 and CAV1 proteins was significantly increased in the bladder outlet obstruction (BOO) group. (B) The lower panel denotes the means±standard deviation of 10 experiments for each condition, as determined by densitometry relative to GAPDH. Con, control; GAPDH, glyceraldehyde 3-phosphate dehydrogenase. * P

    Article Snippet: Monoclonal mouse antibodies against AQP1 (1:2,000; Chemicon, Temecula, CA, USA) and CAV1 (1:2,000; Chemicon), and a polyclonal rabbit antibody against glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (1:4,000; Cell Signaling Technology, Danvers, MA, USA) were used.

    Techniques: Expressing, Standard Deviation

    Mitochondrial respiratory defect in Drp1-KO heart. (A) Histochemical staining for mitochondrial cytochrome c oxidase (COX) activity and succinate dehydrogenase (SDH) activity in heart samples from P7 mice. (B) ImageJ analysis was used to define the threshold and to measure the COX activity-positive area. Control, n = 6; MS-Drp1-KO, n = 6. (C) ADP-driven oxygen consumption by the isolated P7 mouse heart mitochondrial fraction. TMPD, N , N , N ′, N ′-tetramethyl- p -phenylenediamine. Control, n = 5; MS-Drp1-KO, n = 7. (D) mtDNA content quantified by qPCR, shown as the relative ratio of mtDNA to nDNA. Dashed horizontal bars are presented as means. (E) Immunoblot analysis of several respiratory subunits in heart samples from P5 and P7 mice. (F) Protein levels of respiratory chain subunits were quantified by ImageQuant TL. Four independent experiments with two littermate control and MS-Drp1-KO mouse hearts were performed. (G) RT-PCR analysis of the heart to determine mRNAs encoded by mtDNA and the nuclear genome. NTC, no-template negative control. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was used to standardize reaction conditions and cDNA expression levels. Data are presented as the means ± standard deviations for all graphs. *, P

    Journal: Molecular and Cellular Biology

    Article Title: Dynamics of Mitochondrial DNA Nucleoids Regulated by Mitochondrial Fission Is Essential for Maintenance of Homogeneously Active Mitochondria during Neonatal Heart Development

    doi: 10.1128/MCB.01054-14

    Figure Lengend Snippet: Mitochondrial respiratory defect in Drp1-KO heart. (A) Histochemical staining for mitochondrial cytochrome c oxidase (COX) activity and succinate dehydrogenase (SDH) activity in heart samples from P7 mice. (B) ImageJ analysis was used to define the threshold and to measure the COX activity-positive area. Control, n = 6; MS-Drp1-KO, n = 6. (C) ADP-driven oxygen consumption by the isolated P7 mouse heart mitochondrial fraction. TMPD, N , N , N ′, N ′-tetramethyl- p -phenylenediamine. Control, n = 5; MS-Drp1-KO, n = 7. (D) mtDNA content quantified by qPCR, shown as the relative ratio of mtDNA to nDNA. Dashed horizontal bars are presented as means. (E) Immunoblot analysis of several respiratory subunits in heart samples from P5 and P7 mice. (F) Protein levels of respiratory chain subunits were quantified by ImageQuant TL. Four independent experiments with two littermate control and MS-Drp1-KO mouse hearts were performed. (G) RT-PCR analysis of the heart to determine mRNAs encoded by mtDNA and the nuclear genome. NTC, no-template negative control. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was used to standardize reaction conditions and cDNA expression levels. Data are presented as the means ± standard deviations for all graphs. *, P

    Article Snippet: The following commercial antibodies were used in the present study: mouse monoclonal anti-Drp1 (8/DLP1; BD Transduction), anti-cytochrome c (6H2.B4; BD Transduction), anti-OPA1 (18/OPA1; BD Transduction), anti-β-actin (AC74; Sigma-Aldrich), anti-α-actinin (EA-53; Sigma-Aldrich), anti-LC3B (L7543; Sigma-Aldrich), anti-Parkin (P6248; Sigma-Aldrich), anti-DNA (AC-3010; Progen), anti-COX1 (1D6E1A8; Abcam), MitoProfile Total Oxphos Rodent WB antibody cocktail (ab110413; Abcam), anti-Mfn1 (3C/9; Abnova), anti-HSP60 (SPA-807; Stressgen), rabbit monoclonal anti-glyceraldehyde-3-phosphate dehydrogenase (anti-GAPDH) (14C10; Cell Signaling), rabbit polyclonal anti-Tom20 (SC-11415; Santa Cruz Biotechnology), anti-Ki-67 (ab15580; Abcam), anti-cleaved caspase-3 (9661; Cell Signaling), anti-Fis1 (ALX-210-907; Alexis); anti-Mff (17090-1-AP; Proteintech), and goat polyclonal anti-LaminB (SC-6216; Santa Cruz Biotechnology).

    Techniques: Staining, Activity Assay, Mouse Assay, Mass Spectrometry, Isolation, Real-time Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction, Negative Control, Expressing

    Evaluation of the protein synthesis of myofibroblast phenotype markers and extracellular matrix macromolecules in cultured human systemic sclerosis (SSc) skin fibroblasts. Western blotting and related densitometric analysis of the protein synthesis of α-smooth muscle actin (α-SMA), S100A4, type I collagen (COL-1) and fibronectin (FN) in cultured human SSc skin fibroblasts maintained in normal growth medium (untreated), treated with selexipag at the concentration of 30 μM, 3 μM, and 0.3 μM, and treated with ACT-333679 at the concentration of 10 μM, 1 μM, and 0.1 μM, for 48 h. For each experimental condition, the value of the synthesis of α-SMA, S100A4, COL-1, and FN was normalized to that of the corresponding glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The resulting value with each treatment was compared to that of the untreated cells (taken as a unit value), in order to obtain the level of protein synthesis. A molecular weight (MW) lane was also included. The final results represent the mean ± standard deviation (SD) of the values obtained from six independent experiments on cultured human SSc skin fibroblasts: * p

    Journal: Arthritis Research & Therapy

    Article Title: Effects of selexipag and its active metabolite in contrasting the profibrotic myofibroblast activity in cultured scleroderma skin fibroblasts

    doi: 10.1186/s13075-018-1577-0

    Figure Lengend Snippet: Evaluation of the protein synthesis of myofibroblast phenotype markers and extracellular matrix macromolecules in cultured human systemic sclerosis (SSc) skin fibroblasts. Western blotting and related densitometric analysis of the protein synthesis of α-smooth muscle actin (α-SMA), S100A4, type I collagen (COL-1) and fibronectin (FN) in cultured human SSc skin fibroblasts maintained in normal growth medium (untreated), treated with selexipag at the concentration of 30 μM, 3 μM, and 0.3 μM, and treated with ACT-333679 at the concentration of 10 μM, 1 μM, and 0.1 μM, for 48 h. For each experimental condition, the value of the synthesis of α-SMA, S100A4, COL-1, and FN was normalized to that of the corresponding glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The resulting value with each treatment was compared to that of the untreated cells (taken as a unit value), in order to obtain the level of protein synthesis. A molecular weight (MW) lane was also included. The final results represent the mean ± standard deviation (SD) of the values obtained from six independent experiments on cultured human SSc skin fibroblasts: * p

    Article Snippet: The membranes were subsequently incubated with secondary antibodies (dilution 1:2000; Cell Signaling) and also incubated with primary HRP-conjugated antibody to human glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (dilution 1:5000; Cell Signaling) to confirm similar loading of protein samples into the gels and the efficiency in the electrophoretic transfer.

    Techniques: Cell Culture, Western Blot, Concentration Assay, Activated Clotting Time Assay, Molecular Weight, Standard Deviation

    Evaluation of the extracellular signal-regulated kinases 1 and 2 (Erk1/2) and protein kinase B (Akt) activation in cultured human systemic sclerosis (SSc) skin fibroblasts. a Western blotting and related densitometric analysis of phospho-Erk1/2 (p-Erk1/2), Erk1/2, phospho-Akt (p-Akt) and Akt in cultured human SSc skin fibroblasts maintained in normal growth medium (untreated) or treated with ACT-333679 at the concentration of 10 μM, 1 μM, and 0.1 μM for 48 h. The expression of phosphorylated proteins (p-Erk1/2 and p-Akt) was first normalized to that of the naïve proteins (Erk1/2 and Akt) and then normalized to that of the related expression of glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The resulting value of each treatment was compared to that of the untreated cells (taken as the unit value): * p

    Journal: Arthritis Research & Therapy

    Article Title: Effects of selexipag and its active metabolite in contrasting the profibrotic myofibroblast activity in cultured scleroderma skin fibroblasts

    doi: 10.1186/s13075-018-1577-0

    Figure Lengend Snippet: Evaluation of the extracellular signal-regulated kinases 1 and 2 (Erk1/2) and protein kinase B (Akt) activation in cultured human systemic sclerosis (SSc) skin fibroblasts. a Western blotting and related densitometric analysis of phospho-Erk1/2 (p-Erk1/2), Erk1/2, phospho-Akt (p-Akt) and Akt in cultured human SSc skin fibroblasts maintained in normal growth medium (untreated) or treated with ACT-333679 at the concentration of 10 μM, 1 μM, and 0.1 μM for 48 h. The expression of phosphorylated proteins (p-Erk1/2 and p-Akt) was first normalized to that of the naïve proteins (Erk1/2 and Akt) and then normalized to that of the related expression of glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The resulting value of each treatment was compared to that of the untreated cells (taken as the unit value): * p

    Article Snippet: The membranes were subsequently incubated with secondary antibodies (dilution 1:2000; Cell Signaling) and also incubated with primary HRP-conjugated antibody to human glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (dilution 1:5000; Cell Signaling) to confirm similar loading of protein samples into the gels and the efficiency in the electrophoretic transfer.

    Techniques: Activation Assay, Cell Culture, Western Blot, Activated Clotting Time Assay, Concentration Assay, Expressing

    The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 

    Journal: Scientific Reports

    Article Title: A peptide vaccine targeting angiotensin II attenuates the cardiac dysfunction induced by myocardial infarction

    doi: 10.1038/srep43920

    Figure Lengend Snippet: The potency of the antibody produced by the Ang II vaccine on post-MI remodeling-associated responses in cardiac fibroblasts. ( a ) The protocol to evaluate the potency of immunized serum addition on Ang II signaling. ( b ) Representative Western blots of NADPH oxidase 4 (NOX4), phospho-c-Jun, phospho-nuclear factor-κB p65 subunit (NF-κB p65), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in neonatal rat cardiac fibroblasts. The relative protein expression of ( c ) NOX4, n = 4 each; ( d ) phospho-c-Jun, n-4 each; and ( e ) phospho-NF-κB p65, n = 5-6 each. *p 

    Article Snippet: The membranes were incubated overnight at 4 °C with any of the following primary antibodies: glyceraldehyde 3-phosphate dehydrogenase (1:5000, GAPDH, Cell Signaling Technology, Danvers, MA, USA), phospho-NF-κB p65 (1:1000, Cell Signaling Technology), phospho-c-Jun (1:1000, Cell Signaling Technology), NADPH oxidase 4 (1:2000, Abcam, Cambridge,UK), angiotensin II (1:1000, monoclonal antibody, Novus, Littleton, CO, USA), and immunized serum derived from Ang II vaccine-injected rats (the Sham + Ang II vaccine group on day 28) (1:1000).

    Techniques: Produced, Western Blot, Expressing

    Effect of BDB on the NF-κB p65 phosphorylation in mice hearts of MI. (A) The protein level of phosphorylated NF-κB p65 in sham or infarcted hearts was analyzed by western blotting. (B) Quantification of phosphorylated NF-κB p65. Data are expressed as mean±SEM (n=4). BDB = 3-Bromo-4,5-dihydroxybenzaldehyde; GAPDH = glyceraldehyde 3-phosphate dehydrogenase; MI = myocardial infarction; NF = nuclear factor. * The p

    Journal: Korean Circulation Journal

    Article Title: Treatment with 3-Bromo-4,5-Dihydroxybenzaldehyde Improves Cardiac Function by Inhibiting Macrophage Infiltration in Mice

    doi: 10.4070/kcj.2017.0373

    Figure Lengend Snippet: Effect of BDB on the NF-κB p65 phosphorylation in mice hearts of MI. (A) The protein level of phosphorylated NF-κB p65 in sham or infarcted hearts was analyzed by western blotting. (B) Quantification of phosphorylated NF-κB p65. Data are expressed as mean±SEM (n=4). BDB = 3-Bromo-4,5-dihydroxybenzaldehyde; GAPDH = glyceraldehyde 3-phosphate dehydrogenase; MI = myocardial infarction; NF = nuclear factor. * The p

    Article Snippet: The membranes were incubated with primary antibody, anti-nuclear factor (NF)-κB (catalog number: #8242, 1:1,000; Cell Signaling Technologies, Danvers, MA, USA), anti-p-NF-κB p65 (catalog number: #3033, 1:1,000; Cell Signaling Technologies), or anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH, catalog number: #5174, 1:1,000; Cell Signaling Technologies) at 4°C overnight.

    Techniques: Mouse Assay, Western Blot

    Increasing GLUT1 expression increases trans-plasma membrane electron transport (tPMET). ( a ) Western blot analysis confirms effective lipofectamine transfection. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was utilized as the loading control. N = 3 ( b ) Western blot quantification demonstrates that the transfected samples have a ~30% increase in GLUT1 expression. N = 3/group, * p

    Journal: Antioxidants

    Article Title: Trans-Plasma Membrane Electron Transport and Ascorbate Efflux by Skeletal Muscle

    doi: 10.3390/antiox6040089

    Figure Lengend Snippet: Increasing GLUT1 expression increases trans-plasma membrane electron transport (tPMET). ( a ) Western blot analysis confirms effective lipofectamine transfection. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was utilized as the loading control. N = 3 ( b ) Western blot quantification demonstrates that the transfected samples have a ~30% increase in GLUT1 expression. N = 3/group, * p

    Article Snippet: Following initial imaging, membranes were washed with TBST and incubated with HRP-conjugated antibodies against glyceraldehyde 3-phosphate dehydrogenase (GAPDH-HRP) (Cell Signaling Technology, Danvers, MA, USA).

    Techniques: Expressing, Western Blot, Transfection

    TGF-β1 promotes phosphorylation of Smad2 linker region in human VSMCs. VSMCs were stimulated for 0.5, 1 and 2 h with TGF-β1 (2 ng/ml), harvested and total protein was extracted. Proteins were resolved by 10% SDS-PAGE and then transferred to PVDF membrane. Membranes were incubated with anti-phospho-Smad2 (Ser245/250/255) (1:1000) and then followed by incubation with peroxidase labeled anti-rabbit IgG (1:10000) and ECL detection. Anti-GAPDH was used as loading control. Normalized data in each case are shown as mean ± SEM from three independent experiments and statistical significance was determined by One-way ANOVA followed by least significant difference post-hoc analysis. * p

    Journal: Journal of Cell Communication and Signaling

    Article Title: Transforming growth factor–β1 mediated CHST11 and CHSY1 mRNA expression is ROS dependent in vascular smooth muscle cells

    doi: 10.1007/s12079-018-0495-x

    Figure Lengend Snippet: TGF-β1 promotes phosphorylation of Smad2 linker region in human VSMCs. VSMCs were stimulated for 0.5, 1 and 2 h with TGF-β1 (2 ng/ml), harvested and total protein was extracted. Proteins were resolved by 10% SDS-PAGE and then transferred to PVDF membrane. Membranes were incubated with anti-phospho-Smad2 (Ser245/250/255) (1:1000) and then followed by incubation with peroxidase labeled anti-rabbit IgG (1:10000) and ECL detection. Anti-GAPDH was used as loading control. Normalized data in each case are shown as mean ± SEM from three independent experiments and statistical significance was determined by One-way ANOVA followed by least significant difference post-hoc analysis. * p

    Article Snippet: Human recombinant transforming growth factor-β, anti-phospho-Smad2 (Ser245/250/255), anti-phospho-p38-MAPK (Thr180/Tyr182), anti-phospho-ERK (1/2) (Thr202/Tyr204), anti-rabbit immunoglobulin-G (IgG)-horseradish peroxidase (HRP) and Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) rabbit monoclonal IgG antibody were purchased from Cell Signalling Technology (Beverly, MA, USA).

    Techniques: SDS Page, Incubation, Labeling

    TGF-β mediated MAPK (ERK and p38) phosphorylation is Nox-dependent signalling in human VSMCs. VSMCs were pre-incubated with DPI (20 μM) and apocynin (20 μM) for 30 min before being treated with TGF-β (2 ng/ml) for 5 min. Membranes were incubated with a Anti-phospho-ERK (1/2) (Thr202/Tyr204) (1:4000) followed by followed by peroxidase labeled anti-rabbit IgG (1:2000). b Anti-phospho-p38-MAPK (Thr180/Tyr182) (1:1000) followed by followed by peroxidase labeled anti-rabbit IgG (1:2000) and ECL detection. Anti-GAPDH was as loading control. Normalized data in each case are shown as mean ± SEM from three independent experiments and statistical significance was determined by One-way ANOVA followed by least significant difference post-hoc analysis. ** p ˂0.01 compared with untreated control, # p ˂0.05 and ## p ˂0.01 compared with TGF-β

    Journal: Journal of Cell Communication and Signaling

    Article Title: Transforming growth factor–β1 mediated CHST11 and CHSY1 mRNA expression is ROS dependent in vascular smooth muscle cells

    doi: 10.1007/s12079-018-0495-x

    Figure Lengend Snippet: TGF-β mediated MAPK (ERK and p38) phosphorylation is Nox-dependent signalling in human VSMCs. VSMCs were pre-incubated with DPI (20 μM) and apocynin (20 μM) for 30 min before being treated with TGF-β (2 ng/ml) for 5 min. Membranes were incubated with a Anti-phospho-ERK (1/2) (Thr202/Tyr204) (1:4000) followed by followed by peroxidase labeled anti-rabbit IgG (1:2000). b Anti-phospho-p38-MAPK (Thr180/Tyr182) (1:1000) followed by followed by peroxidase labeled anti-rabbit IgG (1:2000) and ECL detection. Anti-GAPDH was as loading control. Normalized data in each case are shown as mean ± SEM from three independent experiments and statistical significance was determined by One-way ANOVA followed by least significant difference post-hoc analysis. ** p ˂0.01 compared with untreated control, # p ˂0.05 and ## p ˂0.01 compared with TGF-β

    Article Snippet: Human recombinant transforming growth factor-β, anti-phospho-Smad2 (Ser245/250/255), anti-phospho-p38-MAPK (Thr180/Tyr182), anti-phospho-ERK (1/2) (Thr202/Tyr204), anti-rabbit immunoglobulin-G (IgG)-horseradish peroxidase (HRP) and Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) rabbit monoclonal IgG antibody were purchased from Cell Signalling Technology (Beverly, MA, USA).

    Techniques: Incubation, Labeling

    Nox-dependent signalling regulates TGFBR1/Alk-5 mediated Smad2 linker region phosphorylation in human VSMCs. a VSMCs were treated with TGF-β1 (2 ng/ml) for 30 min in the presence and absence of the TGFBR1 antagonist, SB431542 (SB) (10 μM) and the Nox inhibitor, DPI (1–20 μM) b VSMCs were treated with TGF-β1 (2 ng/ml) for 30 min in the presence and absence of the Nox inhibitor, apocynin (1 and 10 μM). Membranes were incubated with anti-phospho-Smad2 (Ser245/250/255) (1:1000) followed with peroxidase labeled anti-rabbit IgG (1:10000) and ECL detection. Anti-GAPDH was as loading control. Normalised data in each case are shown as mean ± SEM from three independent experiments and statistical significance was determined by One-way ANOVA followed by least significant difference post-hoc analysis. * p

    Journal: Journal of Cell Communication and Signaling

    Article Title: Transforming growth factor–β1 mediated CHST11 and CHSY1 mRNA expression is ROS dependent in vascular smooth muscle cells

    doi: 10.1007/s12079-018-0495-x

    Figure Lengend Snippet: Nox-dependent signalling regulates TGFBR1/Alk-5 mediated Smad2 linker region phosphorylation in human VSMCs. a VSMCs were treated with TGF-β1 (2 ng/ml) for 30 min in the presence and absence of the TGFBR1 antagonist, SB431542 (SB) (10 μM) and the Nox inhibitor, DPI (1–20 μM) b VSMCs were treated with TGF-β1 (2 ng/ml) for 30 min in the presence and absence of the Nox inhibitor, apocynin (1 and 10 μM). Membranes were incubated with anti-phospho-Smad2 (Ser245/250/255) (1:1000) followed with peroxidase labeled anti-rabbit IgG (1:10000) and ECL detection. Anti-GAPDH was as loading control. Normalised data in each case are shown as mean ± SEM from three independent experiments and statistical significance was determined by One-way ANOVA followed by least significant difference post-hoc analysis. * p

    Article Snippet: Human recombinant transforming growth factor-β, anti-phospho-Smad2 (Ser245/250/255), anti-phospho-p38-MAPK (Thr180/Tyr182), anti-phospho-ERK (1/2) (Thr202/Tyr204), anti-rabbit immunoglobulin-G (IgG)-horseradish peroxidase (HRP) and Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) rabbit monoclonal IgG antibody were purchased from Cell Signalling Technology (Beverly, MA, USA).

    Techniques: Incubation, Labeling