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  • 95
    Millipore glyceraldehyde 3 phosphate dehydrogenase gapdh
    Reverse transcription-polymerase chain reaction analysis. Expression profile of (A) Pax-2, (B) Oct-4 and (C) <t>GAPDH</t> in the isolated kidney-derived stem cells. The reactions were run in triplicate. PAX-2, paired box 2; Oct-4, octamer-binding transcription factor 4; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 1099 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Trevigen glyceraldehyde 3 phosphate dehydrogenase gapdh
    Treatment with LFN for 2 d led to a dose-dependent decrease in ASCL1 and CgA. <t>GAPDH,</t> glyceraldehyde 3-phosphate dehydrogenase.
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Trevigen, used in various techniques. Bioz Stars score: 94/100, based on 75 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Covance glyceraldehyde 3 phosphate dehydrogenase gapdh
    Treatment with LFN for 2 d led to a dose-dependent decrease in ASCL1 and CgA. <t>GAPDH,</t> glyceraldehyde 3-phosphate dehydrogenase.
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Covance, used in various techniques. Bioz Stars score: 90/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Proteintech glyceraldehyde 3 phosphate dehydrogenase gapdh
    Effects of DACT1 on β-catenin in myocardial cells. Effect of DACT1 overexpression on β-catenin concentration A) and distribution B) in H9C2 and HL-1 cells. C) Correlation between DACT1 and β-catenin expression in the myocardial tissues of patients with valvular heart disease. D) Colocation of DACT1 and β-catenin in the myocardial cells. H9C2 and HL-1 cells were overexpressed with the two isoforms of the DACT1 coding sequence, and then immunofluorescence was used to detect the DACT1 (DACT1-V1 or DACT1-V2) (OriGene) and β-catenin (CST) location. The secondary antibody Alexa Fluor 647 was used for DACT1 detection and Alexa Fluor 568 for β-catenin. The ZEN (Zeiss) software was used for further analysis. Alexa Fluor 647 was represented by the green color and Alexa Fluor 568 by the red color, while channel 488 was closed to avoid interference. DACT1=dishevelled binding antagonist of beta catenin 1; DAPI=2-(4-amidinophenyl)-6-indolecarbamidine dihydrochloride; <t>GAPDH=glyceraldehyde-3-phosphate</t> dehydrogenase
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    TaKaRa glyceraldehyde 3 phosphate dehydrogenase gapdh
    Effect of exogenous SIRT1 on the extracellular matrix metabolism of nucleus pulposus cells . mRNA expression of (a) aggrecan , (b) Sox9 and (c) collagen type 2 following treatment with recombinant human silent mating type information regulator 2 homolog 1 (rhSIRT1). Data were obtained from 11 patients (six lumbar spinal stenosis and lumbar disc herniation patients, and five idiopathic scoliosis patients). <t>GAPDH,</t> glyceraldehyde 3-phosphate dehydrogenase.
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    Thermo Fisher glyceraldehyde 3 phosphate dehydrogenase gapdh
    Comparison of RNase expression and HIV inhibition in T h 17-polarized cells with those in T h 0-polarized cells. (A) Representative flow cytometry plots depicting IL-17 expression among T h 0-polarized, CCR6 − cells and T h 17-polarized, CCR6 + cells. SSC, side scatter. (B) Box plot showing differential gene expression between T h 0- and T h 17-polarized cells. Total RNA from T h 0- or T h 17-polarized cells was analyzed by using microarrays. Relative levels of gene expression in T h 17-polarized cells and T h 0-polarized cells are shown. (C) Thirty micrograms of total protein from cell lysates of CCR6 − , T h 0-polarized and CCR6 + , T h 17-polarized CD4 T cells from three donors was denatured and separated according to size by SDS-PAGE, transferred to a PVDF membrane, and then probed for the indicated RNase expression with anti-RNase antibodies. The loading control was glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH).</t> (D) T h 0- and T h 17-polarized CD4 T cells were infected with HIV IIIB , washed, and then resuspended in medium containing the indicated RNases. Percent inhibition was calculated from the percentage of p24 + cells, as measured by flow cytometry.
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    Santa Cruz Biotechnology glyceraldehyde 3 phosphate dehydrogenase gapdh
    Atorvastatin effect on the expression of smooth muscle actin. <t>GAPDH:</t> <t>Glyceraldehyde-3-phosphate</t> dehydrogenase; SMA: Smooth muscle actin.
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 1768 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    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
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    Eurofins 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
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    Bioworld Antibodies 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
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    Valiant 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
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    GeneTex glyceraldehyde 3 phosphate dehydrogenase gapdh
    CD44v9 expression in ESCC cells induced to undergo EMT. (A) Morphological features of TE6 cells. (B) Western blot analysis of CD44v9, E‐cadherin, and vimentin in TE6 cells. TGF‐β converted TE6 cells to a spindle‐like mesenchymal morphology. The expression of E‐cadherin was decreased, and the expression of vimentin and CD44v9 was increased, by TGF‐β stimulation. In contrast, cell morphology and the expression of CD44v9, E‐cadherin, and vimentin were not changed in cells transfected with siCD44v9. ESCC, esophageal squamous cell carcinoma; EMT, epithelial‐mesenchymal transition; <t>GAPDH,</t> glyceraldehyde 3‐phosphate dehydrogenase; TGF‐β, transforming growth factor‐β
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    Agilent technologies glyceraldehyde 3 phosphate dehydrogenase gapdh
    CD44v9 expression in ESCC cells induced to undergo EMT. (A) Morphological features of TE6 cells. (B) Western blot analysis of CD44v9, E‐cadherin, and vimentin in TE6 cells. TGF‐β converted TE6 cells to a spindle‐like mesenchymal morphology. The expression of E‐cadherin was decreased, and the expression of vimentin and CD44v9 was increased, by TGF‐β stimulation. In contrast, cell morphology and the expression of CD44v9, E‐cadherin, and vimentin were not changed in cells transfected with siCD44v9. ESCC, esophageal squamous cell carcinoma; EMT, epithelial‐mesenchymal transition; <t>GAPDH,</t> glyceraldehyde 3‐phosphate dehydrogenase; TGF‐β, transforming growth factor‐β
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    Elim Bio glyceraldehyde 3 phosphate dehydrogenase gapdh
    CD44v9 expression in ESCC cells induced to undergo EMT. (A) Morphological features of TE6 cells. (B) Western blot analysis of CD44v9, E‐cadherin, and vimentin in TE6 cells. TGF‐β converted TE6 cells to a spindle‐like mesenchymal morphology. The expression of E‐cadherin was decreased, and the expression of vimentin and CD44v9 was increased, by TGF‐β stimulation. In contrast, cell morphology and the expression of CD44v9, E‐cadherin, and vimentin were not changed in cells transfected with siCD44v9. ESCC, esophageal squamous cell carcinoma; EMT, epithelial‐mesenchymal transition; <t>GAPDH,</t> glyceraldehyde 3‐phosphate dehydrogenase; TGF‐β, transforming growth factor‐β
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    Sangon Biotech glyceraldehyde 3 phosphate dehydrogenase gapdh
    Efficient differentiation of mesenchymal stem cells (MSCs) from human induced pluripotent stem cells (iPSCs) and characterization of iMSCs-Exo. (A) Phase-contrast image of long-term cultured iPSC clone before differentiation (i), intermediate phase of induced iPSCs (ii), and iMSCs (iii). (B) Quantitative reverse-transcriptase polymerase chain reaction analysis of the expression level of pluripotent genes (Nanog, Oct4, and Msx1) in iPSCs during differentiation (i) and in iPSCs and iMSCs (ii). (C) Flow cytometric analysis of mesenchymal positive markers, such as CD29, CD44, CD73, CD90, CD105, and CD146, and negative markers, such as CD34, CD45, CD133, and HLA-DR. Black histograms represent the isotype controls, and the red solid peak represents the marker indicated. (D) Multi-differentiation potential of iMSCs. (i) Alizarin Red staining of osteogenic mineralization (day 14). (ii) Oil Red O staining of small lipid droplets (day 21). (iii) Toluidine Blue staining of cartilaginous extracellular matrix (day 21). (E) Morphology of iMSCs-Exo under transmission electron microscopy. (F) Western blotting analysis of exosomal CD63, CD81, and CD9 protein in iMSCs and iMSCs-Exo. The culture medium served as the control. <t>GAPDH,</t> glyceraldehyde 3-phosphate dehydrogenase; iMSC, induced pluripotent stem cell-derived mesenchymal stem cell; iMSCs-Exo, exosomes derived from induced pluripotent stem cell-derived mesenchymal stem cells.
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    Bioneer Corporation glyceraldehyde 3 phosphate dehydrogenase gapdh
    Inhibition of iNOS expression by TSG in LPS-stimulated RAW 264.7 macrophages. RAW 264.7 cells were pretreated with the indicated concentrations of TSG for 1 h and then stimulated by LPS (100 ng/ml) for 24 h. (A) mRNA and (B) protein expression levels of iNOS were determined by reverse transcription-polymerase chain reaction and western blot analysis, and <t>GAPDH</t> and actin were used as internal controls, respectively. LPS, lipopolysaccharide; TSG, total saponins extracted from ginseng; iNOS, inducible nitric oxide synthase; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.
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    R&D Systems glyceraldehyde 3 phosphate dehydrogenase gapdh
    Inhibition of iNOS expression by TSG in LPS-stimulated RAW 264.7 macrophages. RAW 264.7 cells were pretreated with the indicated concentrations of TSG for 1 h and then stimulated by LPS (100 ng/ml) for 24 h. (A) mRNA and (B) protein expression levels of iNOS were determined by reverse transcription-polymerase chain reaction and western blot analysis, and <t>GAPDH</t> and actin were used as internal controls, respectively. LPS, lipopolysaccharide; TSG, total saponins extracted from ginseng; iNOS, inducible nitric oxide synthase; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.
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    rdi research diagnostics glyceraldehyde 3 phosphate dehydrogenase gapdh
    Inhibition of iNOS expression by TSG in LPS-stimulated RAW 264.7 macrophages. RAW 264.7 cells were pretreated with the indicated concentrations of TSG for 1 h and then stimulated by LPS (100 ng/ml) for 24 h. (A) mRNA and (B) protein expression levels of iNOS were determined by reverse transcription-polymerase chain reaction and western blot analysis, and <t>GAPDH</t> and actin were used as internal controls, respectively. LPS, lipopolysaccharide; TSG, total saponins extracted from ginseng; iNOS, inducible nitric oxide synthase; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.
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    Meridian Life Science glyceraldehyde 3 phosphate dehydrogenase gapdh
    Inhibition of iNOS expression by TSG in LPS-stimulated RAW 264.7 macrophages. RAW 264.7 cells were pretreated with the indicated concentrations of TSG for 1 h and then stimulated by LPS (100 ng/ml) for 24 h. (A) mRNA and (B) protein expression levels of iNOS were determined by reverse transcription-polymerase chain reaction and western blot analysis, and <t>GAPDH</t> and actin were used as internal controls, respectively. LPS, lipopolysaccharide; TSG, total saponins extracted from ginseng; iNOS, inducible nitric oxide synthase; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.
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    Stratagene glyceraldehyde 3 phosphate dehydrogenase gapdh
    Levels of trk A mRNA in the developing retina. The graph ( A ) shows the relative levels of trk A mRNA in the chicken retina during development. The levels were measured using RNase protection assay on total RNA prepared from retinas of the indicated ages, and a representative gel is illustrated in B . Ten micrograms of total RNA of each age was analyzed in the assay, and as an internal standard, a probe for chicken <t>glyceraldehyde-3-phosphate</t> dehydrogenase <t>(GAPDH)</t> was used. Analysis of protected RNA fragments was made on a denaturing polyacrylamide gel, which was exposed to screens, and scanned by a PhosphorImager. E, embryonic day; P, postnatal day; st, Hamburger and Hamilton stage.
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    Abmart glyceraldehyde 3 phosphate dehydrogenase gapdh
    Levels of trk A mRNA in the developing retina. The graph ( A ) shows the relative levels of trk A mRNA in the chicken retina during development. The levels were measured using RNase protection assay on total RNA prepared from retinas of the indicated ages, and a representative gel is illustrated in B . Ten micrograms of total RNA of each age was analyzed in the assay, and as an internal standard, a probe for chicken <t>glyceraldehyde-3-phosphate</t> dehydrogenase <t>(GAPDH)</t> was used. Analysis of protected RNA fragments was made on a denaturing polyacrylamide gel, which was exposed to screens, and scanned by a PhosphorImager. E, embryonic day; P, postnatal day; st, Hamburger and Hamilton stage.
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    ProMab glyceraldehyde 3 phosphate dehydrogenase gapdh
    Levels of trk A mRNA in the developing retina. The graph ( A ) shows the relative levels of trk A mRNA in the chicken retina during development. The levels were measured using RNase protection assay on total RNA prepared from retinas of the indicated ages, and a representative gel is illustrated in B . Ten micrograms of total RNA of each age was analyzed in the assay, and as an internal standard, a probe for chicken <t>glyceraldehyde-3-phosphate</t> dehydrogenase <t>(GAPDH)</t> was used. Analysis of protected RNA fragments was made on a denaturing polyacrylamide gel, which was exposed to screens, and scanned by a PhosphorImager. E, embryonic day; P, postnatal day; st, Hamburger and Hamilton stage.
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    Trinity Biotech glyceraldehyde 3 phosphate dehydrogenase gapdh
    Levels of trk A mRNA in the developing retina. The graph ( A ) shows the relative levels of trk A mRNA in the chicken retina during development. The levels were measured using RNase protection assay on total RNA prepared from retinas of the indicated ages, and a representative gel is illustrated in B . Ten micrograms of total RNA of each age was analyzed in the assay, and as an internal standard, a probe for chicken <t>glyceraldehyde-3-phosphate</t> dehydrogenase <t>(GAPDH)</t> was used. Analysis of protected RNA fragments was made on a denaturing polyacrylamide gel, which was exposed to screens, and scanned by a PhosphorImager. E, embryonic day; P, postnatal day; st, Hamburger and Hamilton stage.
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    Abfrontier glyceraldehyde 3 phosphate dehydrogenase gapdh
    The effect of esculetin on the expression of cell cycle arrest- and apoptosis-related proteins in human malignant melanoma. (A) The G361 cells were incubated with esculetin (20, 40, and 80 μg/mL) or without for 48 hours. The cell lysates were determined using Western blot analysis with antibodies against p27, p21, and cyclin D1. Equal loading protein was confirmed using <t>glyceraldehyde-3-phosphate</t> de-hydrogenase <t>(GAPDH).</t> (B) The G361 cells were treated with esculetin (0, 20, 40, and 80 μg/mL) for 48 hours. The cell lysates were then determined via Western blot analysis with antibodies against procaspase 3, active caspase 3, Bax, and PARP. Equal loading protein was confirmed using GAPDH. The values were measured using Image J densitometry, and the data were expressed as a representative of two or three independent experiments.
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    Merck KGaA glyceraldehyde 3 phosphate dehydrogenase gapdh
    The effect of esculetin on the expression of cell cycle arrest- and apoptosis-related proteins in human malignant melanoma. (A) The G361 cells were incubated with esculetin (20, 40, and 80 μg/mL) or without for 48 hours. The cell lysates were determined using Western blot analysis with antibodies against p27, p21, and cyclin D1. Equal loading protein was confirmed using <t>glyceraldehyde-3-phosphate</t> de-hydrogenase <t>(GAPDH).</t> (B) The G361 cells were treated with esculetin (0, 20, 40, and 80 μg/mL) for 48 hours. The cell lysates were then determined via Western blot analysis with antibodies against procaspase 3, active caspase 3, Bax, and PARP. Equal loading protein was confirmed using GAPDH. The values were measured using Image J densitometry, and the data were expressed as a representative of two or three independent experiments.
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 94/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Abcam glyceraldehyde 3 phosphate dehydrogenase gapdh
    Western blot analysis of FOXM1 protein expression in noncancerous and tumor tissues. ( a ) Bands of FOXM1 and glyceraldehyde 3‐phosphate dehydrogenase <t>(GAPDH)</t> and ( b ) quantitative analysis of FOXM1/GAPDH in noncancerous and tumor tissues.
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Abcam, used in various techniques. Bioz Stars score: 95/100, based on 1068 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Pharmingen glyceraldehyde 3 phosphate dehydrogenase gapdh
    Western blot analysis of FOXM1 protein expression in noncancerous and tumor tissues. ( a ) Bands of FOXM1 and glyceraldehyde 3‐phosphate dehydrogenase <t>(GAPDH)</t> and ( b ) quantitative analysis of FOXM1/GAPDH in noncancerous and tumor tissues.
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Pharmingen, used in various techniques. Bioz Stars score: 90/100, based on 49 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Bio-Rad glyceraldehyde 3 phosphate dehydrogenase gapdh
    Increased mRNA Levels of Peroxiredoxin and Thioredoxin Families in Eight Cancer Tissues Compared with Normal Tissues . Cancer Survey qRT-PCR array was used to determine the transcript levels of Prx I-VI, Trx1, and Trx2 in breast, colon, kidney, liver, lung, ovary, prostate, and thyroid cancers. Samples in each of the eight cancer groups in the set of arrays consisted of three samples of normal tissue and nine samples of cancer tissues (cancer, phases I-IV) from different individuals. Data were analyzed using the comparative C T method with the values normalized to <t>GAPDH</t> levels. The y-axis represents the increase in the induction fold of the mRNA level of cancer tissue compared with the data from three samples of normal tissue. Error bar displays the range of standard error. Figure in inset is a scatter plot with individual values of the induction fold for Prx I depicted by each dot, the mean induction fold depicted by the longer horizontal line, and standard error depicted by the error bars (shorter horizontal lines) above and below the mean line. Clinicopathological information for each patient was provided by the supplier. Abbreviations: GAPDH, glyceraldehyde 3-phosphate dehydrogenase; mRNA, messenger RNA; Prx, peroxiredoxin; qRT-PCR, quantitative real-time polymerase chain reaction; Trx, thioredoxin.
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    Bio Basic Canada glyceraldehyde 3 phosphate dehydrogenase gapdh
    Increased mRNA Levels of Peroxiredoxin and Thioredoxin Families in Eight Cancer Tissues Compared with Normal Tissues . Cancer Survey qRT-PCR array was used to determine the transcript levels of Prx I-VI, Trx1, and Trx2 in breast, colon, kidney, liver, lung, ovary, prostate, and thyroid cancers. Samples in each of the eight cancer groups in the set of arrays consisted of three samples of normal tissue and nine samples of cancer tissues (cancer, phases I-IV) from different individuals. Data were analyzed using the comparative C T method with the values normalized to <t>GAPDH</t> levels. The y-axis represents the increase in the induction fold of the mRNA level of cancer tissue compared with the data from three samples of normal tissue. Error bar displays the range of standard error. Figure in inset is a scatter plot with individual values of the induction fold for Prx I depicted by each dot, the mean induction fold depicted by the longer horizontal line, and standard error depicted by the error bars (shorter horizontal lines) above and below the mean line. Clinicopathological information for each patient was provided by the supplier. Abbreviations: GAPDH, glyceraldehyde 3-phosphate dehydrogenase; mRNA, messenger RNA; Prx, peroxiredoxin; qRT-PCR, quantitative real-time polymerase chain reaction; Trx, thioredoxin.
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    HyTest glyceraldehyde 3 phosphate dehydrogenase gapdh
    Increased mRNA Levels of Peroxiredoxin and Thioredoxin Families in Eight Cancer Tissues Compared with Normal Tissues . Cancer Survey qRT-PCR array was used to determine the transcript levels of Prx I-VI, Trx1, and Trx2 in breast, colon, kidney, liver, lung, ovary, prostate, and thyroid cancers. Samples in each of the eight cancer groups in the set of arrays consisted of three samples of normal tissue and nine samples of cancer tissues (cancer, phases I-IV) from different individuals. Data were analyzed using the comparative C T method with the values normalized to <t>GAPDH</t> levels. The y-axis represents the increase in the induction fold of the mRNA level of cancer tissue compared with the data from three samples of normal tissue. Error bar displays the range of standard error. Figure in inset is a scatter plot with individual values of the induction fold for Prx I depicted by each dot, the mean induction fold depicted by the longer horizontal line, and standard error depicted by the error bars (shorter horizontal lines) above and below the mean line. Clinicopathological information for each patient was provided by the supplier. Abbreviations: GAPDH, glyceraldehyde 3-phosphate dehydrogenase; mRNA, messenger RNA; Prx, peroxiredoxin; qRT-PCR, quantitative real-time polymerase chain reaction; Trx, thioredoxin.
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    OriGene glyceraldehyde 3 phosphate dehydrogenase gapdh
    BRCA1 CpG hypermethylation associates with constitutively active AHR in triple negative breast cancers (TNBC) cells. ( A ) Representative Western blot images comparing immunocomplexes of AHR and internal standard glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> in HCC38 and UACC3199 cells. ( B ) Data from methylation-specific PCR (MSP) comparing BRCA1 and ESR1 CpG methylation in HCC38 and MCF7 cells. ( C ) Bands represent immunocomplexes for BRCA1, estrogen receptor (ER)α, AHR, and internal standard GAPDH in MCF7 and HCC38 cells. ( D ) Comparison of AHR mRNA expression in HCC38 and MCF7 cells. ( E ) Expression of AHR targets CYP1A1 and CYP1B1 in HCC38 and MCF7 cells. ( F ) CYP1A1 and CYP1B1 expression in HCC38 cells treated with the AHR antagonist CH-223191. Bars represent sample means ± SEM from ≥3 biological replicates from individual experiments. VEH: vehicle-treated control. Asterisks indicate significant differences (*, p
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    Image Search Results


    Reverse transcription-polymerase chain reaction analysis. Expression profile of (A) Pax-2, (B) Oct-4 and (C) GAPDH in the isolated kidney-derived stem cells. The reactions were run in triplicate. PAX-2, paired box 2; Oct-4, octamer-binding transcription factor 4; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Journal: Experimental and Therapeutic Medicine

    Article Title: Identification and isolation of kidney-derived stem cells from transgenic rats with diphtheria toxin-induced kidney damage

    doi: 10.3892/etm.2016.3516

    Figure Lengend Snippet: Reverse transcription-polymerase chain reaction analysis. Expression profile of (A) Pax-2, (B) Oct-4 and (C) GAPDH in the isolated kidney-derived stem cells. The reactions were run in triplicate. PAX-2, paired box 2; Oct-4, octamer-binding transcription factor 4; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Article Snippet: PCR was performed on 1 µl cDNA using the following primers: Oct-4, forward 5′-CTGTAACCGGCGCCAGAA-3′ and reverse 5′-TGCATGGGAGAGCCCAGA-3′ (Sigma-Aldrich); Pax-2, the SABiosciences RT2 PCR primer set (LOC293992; Qiagen Sciences, LLC); and glyceraldehyde-3-phosphate dehydrogenase (GAPDH), forward 5′-TGGAGAGGCCTGCCAAGTA-3′ and reverse 5′-AAGAGTGGGAGTTGCTGTTG-3′ (Sigma-Aldrich).

    Techniques: Reverse Transcription Polymerase Chain Reaction, Expressing, Isolation, Derivative Assay, Binding Assay

    Treatment with LFN for 2 d led to a dose-dependent decrease in ASCL1 and CgA. GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Journal: The Journal of surgical research

    Article Title: Leflunomide suppresses growth in human medullary thyroid cancer cells

    doi: 10.1016/j.jss.2013.05.089

    Figure Lengend Snippet: Treatment with LFN for 2 d led to a dose-dependent decrease in ASCL1 and CgA. GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Article Snippet: The following primary antibody dilutions were used: 1:1000 for ASCL1 (BD Pharmingen, San Diego, CA), CgA (Invitrogen, Carlsbad, CA), and 1:10,000 for glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (Trevigen, Gaithersburg, MD).

    Techniques:

    Long-term treatment with LFN led to a dose-dependent decrease in ASCL-1 and CgA. (A) Four-day LFN treatment. (B) Six-day LFN treatment. GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Journal: The Journal of surgical research

    Article Title: Leflunomide suppresses growth in human medullary thyroid cancer cells

    doi: 10.1016/j.jss.2013.05.089

    Figure Lengend Snippet: Long-term treatment with LFN led to a dose-dependent decrease in ASCL-1 and CgA. (A) Four-day LFN treatment. (B) Six-day LFN treatment. GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Article Snippet: The following primary antibody dilutions were used: 1:1000 for ASCL1 (BD Pharmingen, San Diego, CA), CgA (Invitrogen, Carlsbad, CA), and 1:10,000 for glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (Trevigen, Gaithersburg, MD).

    Techniques:

    Effects of DACT1 on β-catenin in myocardial cells. Effect of DACT1 overexpression on β-catenin concentration A) and distribution B) in H9C2 and HL-1 cells. C) Correlation between DACT1 and β-catenin expression in the myocardial tissues of patients with valvular heart disease. D) Colocation of DACT1 and β-catenin in the myocardial cells. H9C2 and HL-1 cells were overexpressed with the two isoforms of the DACT1 coding sequence, and then immunofluorescence was used to detect the DACT1 (DACT1-V1 or DACT1-V2) (OriGene) and β-catenin (CST) location. The secondary antibody Alexa Fluor 647 was used for DACT1 detection and Alexa Fluor 568 for β-catenin. The ZEN (Zeiss) software was used for further analysis. Alexa Fluor 647 was represented by the green color and Alexa Fluor 568 by the red color, while channel 488 was closed to avoid interference. DACT1=dishevelled binding antagonist of beta catenin 1; DAPI=2-(4-amidinophenyl)-6-indolecarbamidine dihydrochloride; GAPDH=glyceraldehyde-3-phosphate dehydrogenase

    Journal: Brazilian Journal of Cardiovascular Surgery

    Article Title: DACT1 Involvement in the Cytoskeletal Arrangement of Cardiomyocytes in Atrial Fibrillation by Regulating Cx43

    doi: 10.21470/1678-9741-2019-0033

    Figure Lengend Snippet: Effects of DACT1 on β-catenin in myocardial cells. Effect of DACT1 overexpression on β-catenin concentration A) and distribution B) in H9C2 and HL-1 cells. C) Correlation between DACT1 and β-catenin expression in the myocardial tissues of patients with valvular heart disease. D) Colocation of DACT1 and β-catenin in the myocardial cells. H9C2 and HL-1 cells were overexpressed with the two isoforms of the DACT1 coding sequence, and then immunofluorescence was used to detect the DACT1 (DACT1-V1 or DACT1-V2) (OriGene) and β-catenin (CST) location. The secondary antibody Alexa Fluor 647 was used for DACT1 detection and Alexa Fluor 568 for β-catenin. The ZEN (Zeiss) software was used for further analysis. Alexa Fluor 647 was represented by the green color and Alexa Fluor 568 by the red color, while channel 488 was closed to avoid interference. DACT1=dishevelled binding antagonist of beta catenin 1; DAPI=2-(4-amidinophenyl)-6-indolecarbamidine dihydrochloride; GAPDH=glyceraldehyde-3-phosphate dehydrogenase

    Article Snippet: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (Proteintech) or β-actin (Wuhan GoodBio Tech.

    Techniques: Over Expression, Concentration Assay, Expressing, Sequencing, Immunofluorescence, Software, Binding Assay

    The effect of DACT1 on Cx43 in myocardial cells. The effect of DACT1 overexpression on Cx43 concentration A) and distribution B) in H9C2 and HL-1 cells. C) Cx43 expression in the myocardial tissues of patients with valvular heart disease. DACT1=dishevelled binding antagonist of beta catenin 1; GAPDH=glyceraldehyde-3-phosphate dehydrogenase

    Journal: Brazilian Journal of Cardiovascular Surgery

    Article Title: DACT1 Involvement in the Cytoskeletal Arrangement of Cardiomyocytes in Atrial Fibrillation by Regulating Cx43

    doi: 10.21470/1678-9741-2019-0033

    Figure Lengend Snippet: The effect of DACT1 on Cx43 in myocardial cells. The effect of DACT1 overexpression on Cx43 concentration A) and distribution B) in H9C2 and HL-1 cells. C) Cx43 expression in the myocardial tissues of patients with valvular heart disease. DACT1=dishevelled binding antagonist of beta catenin 1; GAPDH=glyceraldehyde-3-phosphate dehydrogenase

    Article Snippet: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (Proteintech) or β-actin (Wuhan GoodBio Tech.

    Techniques: Over Expression, Concentration Assay, Expressing, Binding Assay

    Effect of exogenous SIRT1 on the extracellular matrix metabolism of nucleus pulposus cells . mRNA expression of (a) aggrecan , (b) Sox9 and (c) collagen type 2 following treatment with recombinant human silent mating type information regulator 2 homolog 1 (rhSIRT1). Data were obtained from 11 patients (six lumbar spinal stenosis and lumbar disc herniation patients, and five idiopathic scoliosis patients). GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Journal: Arthritis Research & Therapy

    Article Title: Expression of silent mating type information regulator 2 homolog 1 and its role in human intervertebral disc cell homeostasis

    doi: 10.1186/ar3533

    Figure Lengend Snippet: Effect of exogenous SIRT1 on the extracellular matrix metabolism of nucleus pulposus cells . mRNA expression of (a) aggrecan , (b) Sox9 and (c) collagen type 2 following treatment with recombinant human silent mating type information regulator 2 homolog 1 (rhSIRT1). Data were obtained from 11 patients (six lumbar spinal stenosis and lumbar disc herniation patients, and five idiopathic scoliosis patients). GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Article Snippet: Predesigned primers were used for SIRT1, aggrecan (HA069617; Takarabio), Sox9 (HA117773; Takarabio), collagen type 2 (HA098861; Takarabio), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH ) (HA067812; Takarabio).

    Techniques: Expressing, Recombinant

    SIRT1 mRNA and protein expression in nucleus pulposus cells . (a) Silent mating type information regulator 2 homolog 1 ( SIRT1 ) mRNA expression in human nucleus pulposus (NP) cells. Results of RT-PCR on NP cells derived from disc tissues of patients with lumbar spinal stenosis, lumbar disc herniation and idiopathic scoliosis are shown. (b) SIRT1 protein distribution in NP cells. Immunohistochemical staining of NP cells for β-actin (A) and SIRT1 (B) (images are merged in C ). Bars = 15 μm. GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Journal: Arthritis Research & Therapy

    Article Title: Expression of silent mating type information regulator 2 homolog 1 and its role in human intervertebral disc cell homeostasis

    doi: 10.1186/ar3533

    Figure Lengend Snippet: SIRT1 mRNA and protein expression in nucleus pulposus cells . (a) Silent mating type information regulator 2 homolog 1 ( SIRT1 ) mRNA expression in human nucleus pulposus (NP) cells. Results of RT-PCR on NP cells derived from disc tissues of patients with lumbar spinal stenosis, lumbar disc herniation and idiopathic scoliosis are shown. (b) SIRT1 protein distribution in NP cells. Immunohistochemical staining of NP cells for β-actin (A) and SIRT1 (B) (images are merged in C ). Bars = 15 μm. GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Article Snippet: Predesigned primers were used for SIRT1, aggrecan (HA069617; Takarabio), Sox9 (HA117773; Takarabio), collagen type 2 (HA098861; Takarabio), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH ) (HA067812; Takarabio).

    Techniques: Expressing, Reverse Transcription Polymerase Chain Reaction, Derivative Assay, Immunohistochemistry, Staining

    Comparison of RNase expression and HIV inhibition in T h 17-polarized cells with those in T h 0-polarized cells. (A) Representative flow cytometry plots depicting IL-17 expression among T h 0-polarized, CCR6 − cells and T h 17-polarized, CCR6 + cells. SSC, side scatter. (B) Box plot showing differential gene expression between T h 0- and T h 17-polarized cells. Total RNA from T h 0- or T h 17-polarized cells was analyzed by using microarrays. Relative levels of gene expression in T h 17-polarized cells and T h 0-polarized cells are shown. (C) Thirty micrograms of total protein from cell lysates of CCR6 − , T h 0-polarized and CCR6 + , T h 17-polarized CD4 T cells from three donors was denatured and separated according to size by SDS-PAGE, transferred to a PVDF membrane, and then probed for the indicated RNase expression with anti-RNase antibodies. The loading control was glyceraldehyde 3-phosphate dehydrogenase (GAPDH). (D) T h 0- and T h 17-polarized CD4 T cells were infected with HIV IIIB , washed, and then resuspended in medium containing the indicated RNases. Percent inhibition was calculated from the percentage of p24 + cells, as measured by flow cytometry.

    Journal: Journal of Virology

    Article Title: Human Th17 Cells Lack HIV-Inhibitory RNases and Are Highly Permissive to Productive HIV Infection

    doi: 10.1128/JVI.02869-15

    Figure Lengend Snippet: Comparison of RNase expression and HIV inhibition in T h 17-polarized cells with those in T h 0-polarized cells. (A) Representative flow cytometry plots depicting IL-17 expression among T h 0-polarized, CCR6 − cells and T h 17-polarized, CCR6 + cells. SSC, side scatter. (B) Box plot showing differential gene expression between T h 0- and T h 17-polarized cells. Total RNA from T h 0- or T h 17-polarized cells was analyzed by using microarrays. Relative levels of gene expression in T h 17-polarized cells and T h 0-polarized cells are shown. (C) Thirty micrograms of total protein from cell lysates of CCR6 − , T h 0-polarized and CCR6 + , T h 17-polarized CD4 T cells from three donors was denatured and separated according to size by SDS-PAGE, transferred to a PVDF membrane, and then probed for the indicated RNase expression with anti-RNase antibodies. The loading control was glyceraldehyde 3-phosphate dehydrogenase (GAPDH). (D) T h 0- and T h 17-polarized CD4 T cells were infected with HIV IIIB , washed, and then resuspended in medium containing the indicated RNases. Percent inhibition was calculated from the percentage of p24 + cells, as measured by flow cytometry.

    Article Snippet: As a loading control, blots were also probed with an HRP-conjugated antibody to glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (ThermoFisher Scientific Inc., Rockville, MD).

    Techniques: Expressing, Inhibition, Flow Cytometry, Cytometry, SDS Page, Infection

    Atorvastatin effect on the expression of smooth muscle actin. GAPDH: Glyceraldehyde-3-phosphate dehydrogenase; SMA: Smooth muscle actin.

    Journal: World Journal of Gastroenterology : WJG

    Article Title: Atorvastatin and rosuvastatin do not prevent thioacetamide induced liver cirrhosis in rats

    doi: 10.3748/wjg.v19.i2.241

    Figure Lengend Snippet: Atorvastatin effect on the expression of smooth muscle actin. GAPDH: Glyceraldehyde-3-phosphate dehydrogenase; SMA: Smooth muscle actin.

    Article Snippet: Equal amounts of total protein-were separated in 4%-12% bis-tris (BT) gels (NuPAGE, Gibco-BRL Life Technologies, Grand Island, NY), blotted onto Hybond C extra membranes, blocked overnight in 5% milk, and incubated with antibodies against α smooth muscle actin (αSMA), glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (Santa Cruz Biotechnology, Santa Cruz, CA, United States) and then incubated with horseradish peroxidase-conjugated secondary antibody.

    Techniques: Expressing

    Effects of a combination of rapamycin (RP) and mycophenolic acid (MPA) on tumor necrosis factor (TNF)-α-induced expression of pro-inflammatory genes in HaCaT cells. HaCaT cells were pre-incubated for 24 h and then stimulated with TNF-α (20 ng/ml) after a 1 h pretreatment with RP, MPA, or a combination of the two drugs for 6 h. Pro-inflammatory gene expression was analyzed by reverse transcription-polymerase chain reaction (RT-PCR) using specific primers. The experiment was repeated independently at least three times. IL: interleukin, GAPDH: glyceraldehyde 3-phosphate dehydrogenase.

    Journal: Annals of Dermatology

    Article Title: Synergistic Inhibition of Tumor Necrosis Factor-Alpha-Stimulated Pro-Inflammatory Cytokine Expression in HaCaT Cells by a Combination of Rapamycin and Mycophenolic Acid

    doi: 10.5021/ad.2015.27.1.32

    Figure Lengend Snippet: Effects of a combination of rapamycin (RP) and mycophenolic acid (MPA) on tumor necrosis factor (TNF)-α-induced expression of pro-inflammatory genes in HaCaT cells. HaCaT cells were pre-incubated for 24 h and then stimulated with TNF-α (20 ng/ml) after a 1 h pretreatment with RP, MPA, or a combination of the two drugs for 6 h. Pro-inflammatory gene expression was analyzed by reverse transcription-polymerase chain reaction (RT-PCR) using specific primers. The experiment was repeated independently at least three times. IL: interleukin, GAPDH: glyceraldehyde 3-phosphate dehydrogenase.

    Article Snippet: Antibodies specific to ICAM-1, phospho-extracellular signal-related kinases (ERK), phospho-IκBα, and lamin B were purchased from Cell Signaling Technology (Beverly, MA, USA). phosphor-c-Jun N-terminal kinases (JNK) and Phosphor-p38, and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibodies were purchased from Santa Cruz Biotechnology Inc. (Santa Cruz, CA, USA), and inducible nitric oxide synthase (iNOS) antibodies were obtained from BD Bioscience (San Jose, CA, USA).

    Techniques: Expressing, Incubation, Reverse Transcription Polymerase Chain Reaction

    Melittin attenuates the expression of pro-inflammatory cytokine in obstructed kidneys. ( A ) Immunohistochemical staining shows that melittin inhibits the expressions of tumor necrosis factor (TNF)-α and interleukin (IL)-1β in kidneys at 7 days after unilateral ureteral obstruction (UUO) surgery. Immunohistochemical staining was used to evaluate the extent of pro-inflammatory cytokines, which was subsequently quantified. ( B , C ) Western blot analysis and Reverse transcription-polymerase chain reaction (RT-PCR) results show that melittin suppresses the protein and mRNA expressions of TNF-α and IL-1β in UUO kidneys. Glyceraldehyde-3-phosphate-dehydrogenase (GAPDH) levels were analyzed as an internal control. −: not treated, +: treated. These are representative images from each study group. Magnification: 400×. The results are expressed as means ± SE of three independent determinations. * p

    Journal: Molecules

    Article Title: The Protective Effect of Melittin on Renal Fibrosis in an Animal Model of Unilateral Ureteral Obstruction

    doi: 10.3390/molecules21091137

    Figure Lengend Snippet: Melittin attenuates the expression of pro-inflammatory cytokine in obstructed kidneys. ( A ) Immunohistochemical staining shows that melittin inhibits the expressions of tumor necrosis factor (TNF)-α and interleukin (IL)-1β in kidneys at 7 days after unilateral ureteral obstruction (UUO) surgery. Immunohistochemical staining was used to evaluate the extent of pro-inflammatory cytokines, which was subsequently quantified. ( B , C ) Western blot analysis and Reverse transcription-polymerase chain reaction (RT-PCR) results show that melittin suppresses the protein and mRNA expressions of TNF-α and IL-1β in UUO kidneys. Glyceraldehyde-3-phosphate-dehydrogenase (GAPDH) levels were analyzed as an internal control. −: not treated, +: treated. These are representative images from each study group. Magnification: 400×. The results are expressed as means ± SE of three independent determinations. * p

    Article Snippet: The primary antibodies used in this study were as follows: anti-TNF-α, anti-fibronectin, anti-α-SMA (Abcam), anti-TGF-β1 (R & D Systems), anti-IL-1β, anti-collagen type I, and anti-glyceraldehyde-3-phosphate-dehydrogenase (GAPDH) (Santa Cruz Biotechnology).

    Techniques: Expressing, Immunohistochemistry, Staining, Western Blot, Reverse Transcription Polymerase Chain Reaction

    Cyclic AMP sponge is able to bind cAMP in vitro. (A) NCM460 cell lysates immunoprecipitated (IP) using Sp-2-AEA-cAMPS-Agarose beads (Sp-cAMPS): lanes 1–3: input, 4–6: IP, 4: untransfected, 5: mut -NES-cAMP sponge, 6: NES-cAMP sponge. (B) cAMP competitive assay, HeLa cell lysates, lanes 1–3: input, 4–14: IP, 4–8: untranfected, 9: mut -NES-cAMP sponge, 10–14: NES-cAMP sponge, lanes 8 and 14: beads only. Loading control: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH).

    Journal: PLoS ONE

    Article Title: "cAMP Sponge": A Buffer for Cyclic Adenosine 3?, 5?-Monophosphate

    doi: 10.1371/journal.pone.0007649

    Figure Lengend Snippet: Cyclic AMP sponge is able to bind cAMP in vitro. (A) NCM460 cell lysates immunoprecipitated (IP) using Sp-2-AEA-cAMPS-Agarose beads (Sp-cAMPS): lanes 1–3: input, 4–6: IP, 4: untransfected, 5: mut -NES-cAMP sponge, 6: NES-cAMP sponge. (B) cAMP competitive assay, HeLa cell lysates, lanes 1–3: input, 4–14: IP, 4–8: untranfected, 9: mut -NES-cAMP sponge, 10–14: NES-cAMP sponge, lanes 8 and 14: beads only. Loading control: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH).

    Article Snippet: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) antibody (1∶2000; Santa Cruz) was used as a loading control for the total cell lysates and to detect protein contamination for the immunoprecipitated proteins.

    Techniques: In Vitro, Immunoprecipitation

    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

    CD44v9 expression in ESCC cells induced to undergo EMT. (A) Morphological features of TE6 cells. (B) Western blot analysis of CD44v9, E‐cadherin, and vimentin in TE6 cells. TGF‐β converted TE6 cells to a spindle‐like mesenchymal morphology. The expression of E‐cadherin was decreased, and the expression of vimentin and CD44v9 was increased, by TGF‐β stimulation. In contrast, cell morphology and the expression of CD44v9, E‐cadherin, and vimentin were not changed in cells transfected with siCD44v9. ESCC, esophageal squamous cell carcinoma; EMT, epithelial‐mesenchymal transition; GAPDH, glyceraldehyde 3‐phosphate dehydrogenase; TGF‐β, transforming growth factor‐β

    Journal: Cancer Medicine

    Article Title: CD44v9 is associated with epithelial‐mesenchymal transition and poor outcomes in esophageal squamous cell carcinoma, et al. CD44v9 is associated with epithelial‐mesenchymal transition and poor outcomes in esophageal squamous cell carcinoma

    doi: 10.1002/cam4.1874

    Figure Lengend Snippet: CD44v9 expression in ESCC cells induced to undergo EMT. (A) Morphological features of TE6 cells. (B) Western blot analysis of CD44v9, E‐cadherin, and vimentin in TE6 cells. TGF‐β converted TE6 cells to a spindle‐like mesenchymal morphology. The expression of E‐cadherin was decreased, and the expression of vimentin and CD44v9 was increased, by TGF‐β stimulation. In contrast, cell morphology and the expression of CD44v9, E‐cadherin, and vimentin were not changed in cells transfected with siCD44v9. ESCC, esophageal squamous cell carcinoma; EMT, epithelial‐mesenchymal transition; GAPDH, glyceraldehyde 3‐phosphate dehydrogenase; TGF‐β, transforming growth factor‐β

    Article Snippet: The primary antibodies used were as follows: anti‐CD44v9 (LKG‐M001, 1:1000 dilution; COSMO BIO LTD), glyceraldehyde 3‐phosphate dehydrogenase (GAPDH) (GTX100118, 1:1000 dilution; GeneTex Inc, Irvine, CA, USA), anti‐E‐cadherin (24E10, 1:1000 dilution; Cell Signaling Technology Japan, Tokyo, Japan), and anti‐vimentin (D21H3, 1:1000 dilution; Cell Signaling Technology Japan).

    Techniques: Expressing, Western Blot, Transfection

    Efficient differentiation of mesenchymal stem cells (MSCs) from human induced pluripotent stem cells (iPSCs) and characterization of iMSCs-Exo. (A) Phase-contrast image of long-term cultured iPSC clone before differentiation (i), intermediate phase of induced iPSCs (ii), and iMSCs (iii). (B) Quantitative reverse-transcriptase polymerase chain reaction analysis of the expression level of pluripotent genes (Nanog, Oct4, and Msx1) in iPSCs during differentiation (i) and in iPSCs and iMSCs (ii). (C) Flow cytometric analysis of mesenchymal positive markers, such as CD29, CD44, CD73, CD90, CD105, and CD146, and negative markers, such as CD34, CD45, CD133, and HLA-DR. Black histograms represent the isotype controls, and the red solid peak represents the marker indicated. (D) Multi-differentiation potential of iMSCs. (i) Alizarin Red staining of osteogenic mineralization (day 14). (ii) Oil Red O staining of small lipid droplets (day 21). (iii) Toluidine Blue staining of cartilaginous extracellular matrix (day 21). (E) Morphology of iMSCs-Exo under transmission electron microscopy. (F) Western blotting analysis of exosomal CD63, CD81, and CD9 protein in iMSCs and iMSCs-Exo. The culture medium served as the control. GAPDH, glyceraldehyde 3-phosphate dehydrogenase; iMSC, induced pluripotent stem cell-derived mesenchymal stem cell; iMSCs-Exo, exosomes derived from induced pluripotent stem cell-derived mesenchymal stem cells.

    Journal: Stem Cell Research & Therapy

    Article Title: Exosomes secreted by human-induced pluripotent stem cell-derived mesenchymal stem cells attenuate limb ischemia by promoting angiogenesis in mice

    doi: 10.1186/scrt546

    Figure Lengend Snippet: Efficient differentiation of mesenchymal stem cells (MSCs) from human induced pluripotent stem cells (iPSCs) and characterization of iMSCs-Exo. (A) Phase-contrast image of long-term cultured iPSC clone before differentiation (i), intermediate phase of induced iPSCs (ii), and iMSCs (iii). (B) Quantitative reverse-transcriptase polymerase chain reaction analysis of the expression level of pluripotent genes (Nanog, Oct4, and Msx1) in iPSCs during differentiation (i) and in iPSCs and iMSCs (ii). (C) Flow cytometric analysis of mesenchymal positive markers, such as CD29, CD44, CD73, CD90, CD105, and CD146, and negative markers, such as CD34, CD45, CD133, and HLA-DR. Black histograms represent the isotype controls, and the red solid peak represents the marker indicated. (D) Multi-differentiation potential of iMSCs. (i) Alizarin Red staining of osteogenic mineralization (day 14). (ii) Oil Red O staining of small lipid droplets (day 21). (iii) Toluidine Blue staining of cartilaginous extracellular matrix (day 21). (E) Morphology of iMSCs-Exo under transmission electron microscopy. (F) Western blotting analysis of exosomal CD63, CD81, and CD9 protein in iMSCs and iMSCs-Exo. The culture medium served as the control. GAPDH, glyceraldehyde 3-phosphate dehydrogenase; iMSC, induced pluripotent stem cell-derived mesenchymal stem cell; iMSCs-Exo, exosomes derived from induced pluripotent stem cell-derived mesenchymal stem cells.

    Article Snippet: The following human primers were used: Nanog, Oct4, Msx1, hypoxia-inducible factor-1α (HIF-1α), vascular endothelial growth factor-A (VEGFA), VEGFB, placental growth factor (PGF), basic fibroblast growth factor (bFGF), transforming growth factor beta 1 (TGFB1), Angiogenin (Angio), VEGF receptor 2 (kinase insert domain receptor, or KDR), bFGF receptor (bFGFR), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (all from Sangon Biotech, Shanghai, China).

    Techniques: Cell Culture, Polymerase Chain Reaction, Expressing, Flow Cytometry, Marker, Staining, Transmission Assay, Electron Microscopy, Western Blot, Derivative Assay

    Inhibition of iNOS expression by TSG in LPS-stimulated RAW 264.7 macrophages. RAW 264.7 cells were pretreated with the indicated concentrations of TSG for 1 h and then stimulated by LPS (100 ng/ml) for 24 h. (A) mRNA and (B) protein expression levels of iNOS were determined by reverse transcription-polymerase chain reaction and western blot analysis, and GAPDH and actin were used as internal controls, respectively. LPS, lipopolysaccharide; TSG, total saponins extracted from ginseng; iNOS, inducible nitric oxide synthase; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Journal: Experimental and Therapeutic Medicine

    Article Title: Anti-inflammatory potential of total saponins derived from the roots of Panax ginseng in lipopolysaccharide-activated RAW 264.7 macrophages

    doi: 10.3892/etm.2015.2965

    Figure Lengend Snippet: Inhibition of iNOS expression by TSG in LPS-stimulated RAW 264.7 macrophages. RAW 264.7 cells were pretreated with the indicated concentrations of TSG for 1 h and then stimulated by LPS (100 ng/ml) for 24 h. (A) mRNA and (B) protein expression levels of iNOS were determined by reverse transcription-polymerase chain reaction and western blot analysis, and GAPDH and actin were used as internal controls, respectively. LPS, lipopolysaccharide; TSG, total saponins extracted from ginseng; iNOS, inducible nitric oxide synthase; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Article Snippet: The PCR primers were as follows: iNOS forward, 5′-ATGTCCGAAGCAAACATCAC-3′ and reverse, 5′-TAATGTCCAGGAAGTAGGTG-3′; IL-1β forward, 5′-GGGCTGCTTCCAAACCTTTG-3′ and reverse, 5′-GCTTGGGATCCACACTCTCC-3′; TNF-α forward, 5′-TCTCATCAGTTCTATGGCCC-3′ and reverse, 5′-GGGAGTAGACAAGGTACAAC-3′; and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) forward, 5′-AGGCCGGTGCTGAGTATGTC-3′ and reverse, 5′-TGCCTGCTTCACCACCTTCT-3′ (Bioneer Corporation).

    Techniques: Inhibition, Expressing, Reverse Transcription Polymerase Chain Reaction, Western Blot

    Inhibition of LPS-induced TNF-α and IL-1β expression by TSG in LPS-stimulated RAW 264.7 macrophages. RAW 264.7 cells were pretreated with various concentrations of TSG for 1 h and then stimulated by LPS (100 ng/ml) for 24 h. (A) mRNA and (B) protein expression levels of TNF-α and IL-1β were determined by performing reverse transcription-polymerase chain reaction (RT-PCR) and western blot analysis, in which GAPDH and actin were used as internal controls, respectively. LPS, lipopolysaccharide; TSG, total saponins extracted from ginseng; TNF-α, tumor necrosis factor-α; IL-1β, interleukin-1β; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Journal: Experimental and Therapeutic Medicine

    Article Title: Anti-inflammatory potential of total saponins derived from the roots of Panax ginseng in lipopolysaccharide-activated RAW 264.7 macrophages

    doi: 10.3892/etm.2015.2965

    Figure Lengend Snippet: Inhibition of LPS-induced TNF-α and IL-1β expression by TSG in LPS-stimulated RAW 264.7 macrophages. RAW 264.7 cells were pretreated with various concentrations of TSG for 1 h and then stimulated by LPS (100 ng/ml) for 24 h. (A) mRNA and (B) protein expression levels of TNF-α and IL-1β were determined by performing reverse transcription-polymerase chain reaction (RT-PCR) and western blot analysis, in which GAPDH and actin were used as internal controls, respectively. LPS, lipopolysaccharide; TSG, total saponins extracted from ginseng; TNF-α, tumor necrosis factor-α; IL-1β, interleukin-1β; GAPDH, glyceraldehyde 3-phosphate dehydrogenase.

    Article Snippet: The PCR primers were as follows: iNOS forward, 5′-ATGTCCGAAGCAAACATCAC-3′ and reverse, 5′-TAATGTCCAGGAAGTAGGTG-3′; IL-1β forward, 5′-GGGCTGCTTCCAAACCTTTG-3′ and reverse, 5′-GCTTGGGATCCACACTCTCC-3′; TNF-α forward, 5′-TCTCATCAGTTCTATGGCCC-3′ and reverse, 5′-GGGAGTAGACAAGGTACAAC-3′; and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) forward, 5′-AGGCCGGTGCTGAGTATGTC-3′ and reverse, 5′-TGCCTGCTTCACCACCTTCT-3′ (Bioneer Corporation).

    Techniques: Inhibition, Expressing, Reverse Transcription Polymerase Chain Reaction, Western Blot

    Levels of trk A mRNA in the developing retina. The graph ( A ) shows the relative levels of trk A mRNA in the chicken retina during development. The levels were measured using RNase protection assay on total RNA prepared from retinas of the indicated ages, and a representative gel is illustrated in B . Ten micrograms of total RNA of each age was analyzed in the assay, and as an internal standard, a probe for chicken glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was used. Analysis of protected RNA fragments was made on a denaturing polyacrylamide gel, which was exposed to screens, and scanned by a PhosphorImager. E, embryonic day; P, postnatal day; st, Hamburger and Hamilton stage.

    Journal: The Journal of comparative neurology

    Article Title: Nerve Growth Factor Receptor TrkA Is Expressed by Horizontal and Amacrine Cells During Chicken Retinal Development

    doi:

    Figure Lengend Snippet: Levels of trk A mRNA in the developing retina. The graph ( A ) shows the relative levels of trk A mRNA in the chicken retina during development. The levels were measured using RNase protection assay on total RNA prepared from retinas of the indicated ages, and a representative gel is illustrated in B . Ten micrograms of total RNA of each age was analyzed in the assay, and as an internal standard, a probe for chicken glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was used. Analysis of protected RNA fragments was made on a denaturing polyacrylamide gel, which was exposed to screens, and scanned by a PhosphorImager. E, embryonic day; P, postnatal day; st, Hamburger and Hamilton stage.

    Article Snippet: The RNase protection assay (RPA) was performed by using the RPAII Ribonuclease Protection Assay Kit (Ambion, Austin, TX). cRNA probes of trk A and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were in vitro transcribed from DNA templates cloned into the pBS SK M13+ and the pBS KS M13+ cloning vectors (Stratagene, La Jolla, CA), respectively.

    Techniques: Rnase Protection Assay

    The effect of esculetin on the expression of cell cycle arrest- and apoptosis-related proteins in human malignant melanoma. (A) The G361 cells were incubated with esculetin (20, 40, and 80 μg/mL) or without for 48 hours. The cell lysates were determined using Western blot analysis with antibodies against p27, p21, and cyclin D1. Equal loading protein was confirmed using glyceraldehyde-3-phosphate de-hydrogenase (GAPDH). (B) The G361 cells were treated with esculetin (0, 20, 40, and 80 μg/mL) for 48 hours. The cell lysates were then determined via Western blot analysis with antibodies against procaspase 3, active caspase 3, Bax, and PARP. Equal loading protein was confirmed using GAPDH. The values were measured using Image J densitometry, and the data were expressed as a representative of two or three independent experiments.

    Journal: Journal of Cancer Prevention

    Article Title: Esculetin, a Coumarin Derivative, Exhibits Anti-proliferative and Pro-apoptotic Activity in G361 Human Malignant Melanoma

    doi: 10.15430/JCP.2015.20.2.106

    Figure Lengend Snippet: The effect of esculetin on the expression of cell cycle arrest- and apoptosis-related proteins in human malignant melanoma. (A) The G361 cells were incubated with esculetin (20, 40, and 80 μg/mL) or without for 48 hours. The cell lysates were determined using Western blot analysis with antibodies against p27, p21, and cyclin D1. Equal loading protein was confirmed using glyceraldehyde-3-phosphate de-hydrogenase (GAPDH). (B) The G361 cells were treated with esculetin (0, 20, 40, and 80 μg/mL) for 48 hours. The cell lysates were then determined via Western blot analysis with antibodies against procaspase 3, active caspase 3, Bax, and PARP. Equal loading protein was confirmed using GAPDH. The values were measured using Image J densitometry, and the data were expressed as a representative of two or three independent experiments.

    Article Snippet: The primary antibodies used in this study were as followings: α-Sp1, α-p27, α-p21, α-cyclinD1 (Santa Cruz Biotechnology Inc., Santa Cruz, CA, USA), α-procaspase 3, α-cleaved caspase 3 (Cell Signaling Technology, Denvers, MA, USA), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (AbFrontier, Seoul, Korea).

    Techniques: Expressing, Incubation, Western Blot

    The effect of esculetin on Sp1 expression in human malignant melanoma. (A) The G361 cells were treated with different concentrations of esculetin (0, 20, 40, and 80 μg/mL) for 48 hours. The cell lysates were separated by SDS PAGE, and then the membranes were transferred from SDS PAGE gels subjected to Western blot analysis for Sp1. An equal loading protein was confirmed using glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The histogram showed the ratio of Sp1 to GAPDH expression, and the results were expressed as the average of a triplicate sample from three independent experiments. The asterisk suggested P

    Journal: Journal of Cancer Prevention

    Article Title: Esculetin, a Coumarin Derivative, Exhibits Anti-proliferative and Pro-apoptotic Activity in G361 Human Malignant Melanoma

    doi: 10.15430/JCP.2015.20.2.106

    Figure Lengend Snippet: The effect of esculetin on Sp1 expression in human malignant melanoma. (A) The G361 cells were treated with different concentrations of esculetin (0, 20, 40, and 80 μg/mL) for 48 hours. The cell lysates were separated by SDS PAGE, and then the membranes were transferred from SDS PAGE gels subjected to Western blot analysis for Sp1. An equal loading protein was confirmed using glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The histogram showed the ratio of Sp1 to GAPDH expression, and the results were expressed as the average of a triplicate sample from three independent experiments. The asterisk suggested P

    Article Snippet: The primary antibodies used in this study were as followings: α-Sp1, α-p27, α-p21, α-cyclinD1 (Santa Cruz Biotechnology Inc., Santa Cruz, CA, USA), α-procaspase 3, α-cleaved caspase 3 (Cell Signaling Technology, Denvers, MA, USA), and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (AbFrontier, Seoul, Korea).

    Techniques: Expressing, SDS Page, Western Blot

    Western blot analysis of FOXM1 protein expression in noncancerous and tumor tissues. ( a ) Bands of FOXM1 and glyceraldehyde 3‐phosphate dehydrogenase (GAPDH) and ( b ) quantitative analysis of FOXM1/GAPDH in noncancerous and tumor tissues.

    Journal: Thoracic Cancer

    Article Title: FOXM1: A potential indicator to predict lymphatic metastatic recurrence in stage IIA esophageal squamous cell carcinoma

    doi: 10.1111/1759-7714.12776

    Figure Lengend Snippet: Western blot analysis of FOXM1 protein expression in noncancerous and tumor tissues. ( a ) Bands of FOXM1 and glyceraldehyde 3‐phosphate dehydrogenase (GAPDH) and ( b ) quantitative analysis of FOXM1/GAPDH in noncancerous and tumor tissues.

    Article Snippet: Membranes were incubated overnight at 4°C with primary antibodies anti‐FOXM1 (1:500) and anti‐glyceraldehyde 3‐phosphate dehydrogenase (GAPDH) (1: 5000; Abcam, Cambridge, MA, USA).

    Techniques: Western Blot, Expressing

    Increased mRNA Levels of Peroxiredoxin and Thioredoxin Families in Eight Cancer Tissues Compared with Normal Tissues . Cancer Survey qRT-PCR array was used to determine the transcript levels of Prx I-VI, Trx1, and Trx2 in breast, colon, kidney, liver, lung, ovary, prostate, and thyroid cancers. Samples in each of the eight cancer groups in the set of arrays consisted of three samples of normal tissue and nine samples of cancer tissues (cancer, phases I-IV) from different individuals. Data were analyzed using the comparative C T method with the values normalized to GAPDH levels. The y-axis represents the increase in the induction fold of the mRNA level of cancer tissue compared with the data from three samples of normal tissue. Error bar displays the range of standard error. Figure in inset is a scatter plot with individual values of the induction fold for Prx I depicted by each dot, the mean induction fold depicted by the longer horizontal line, and standard error depicted by the error bars (shorter horizontal lines) above and below the mean line. Clinicopathological information for each patient was provided by the supplier. Abbreviations: GAPDH, glyceraldehyde 3-phosphate dehydrogenase; mRNA, messenger RNA; Prx, peroxiredoxin; qRT-PCR, quantitative real-time polymerase chain reaction; Trx, thioredoxin.

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Overexpression of peroxiredoxin I and thioredoxin1 in human breast carcinoma

    doi: 10.1186/1756-9966-28-93

    Figure Lengend Snippet: Increased mRNA Levels of Peroxiredoxin and Thioredoxin Families in Eight Cancer Tissues Compared with Normal Tissues . Cancer Survey qRT-PCR array was used to determine the transcript levels of Prx I-VI, Trx1, and Trx2 in breast, colon, kidney, liver, lung, ovary, prostate, and thyroid cancers. Samples in each of the eight cancer groups in the set of arrays consisted of three samples of normal tissue and nine samples of cancer tissues (cancer, phases I-IV) from different individuals. Data were analyzed using the comparative C T method with the values normalized to GAPDH levels. The y-axis represents the increase in the induction fold of the mRNA level of cancer tissue compared with the data from three samples of normal tissue. Error bar displays the range of standard error. Figure in inset is a scatter plot with individual values of the induction fold for Prx I depicted by each dot, the mean induction fold depicted by the longer horizontal line, and standard error depicted by the error bars (shorter horizontal lines) above and below the mean line. Clinicopathological information for each patient was provided by the supplier. Abbreviations: GAPDH, glyceraldehyde 3-phosphate dehydrogenase; mRNA, messenger RNA; Prx, peroxiredoxin; qRT-PCR, quantitative real-time polymerase chain reaction; Trx, thioredoxin.

    Article Snippet: Polymerase chain reaction was performed in 96-well optical plates using the iCycler (Bio-Rad Laboratories, Hercules, CA, USA) with primers specific for Prx I-VI, Trx1, Trx2, β-actin, glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and iQ SYBR Green Supermix (Bio-Rad).

    Techniques: Quantitative RT-PCR, Real-time Polymerase Chain Reaction

    Expression Profiles of Peroxiredoxin I and Thioredoxin1 in 48 Major Human Tissues . The Human Major Tissue qRT-PCR array was used to determine transcript levels of Prx I (Figure 1A) and Trx1 (Figure 1B). For the human tissue array, tissues were selected from 48 individuals of different ethnicity. The y-axis represents the value of pg × 10 4 of DNA determined. Data were abtained using the comparative C T method with the values normalized to GAPDH levels and a standard curve. Details are in the

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Overexpression of peroxiredoxin I and thioredoxin1 in human breast carcinoma

    doi: 10.1186/1756-9966-28-93

    Figure Lengend Snippet: Expression Profiles of Peroxiredoxin I and Thioredoxin1 in 48 Major Human Tissues . The Human Major Tissue qRT-PCR array was used to determine transcript levels of Prx I (Figure 1A) and Trx1 (Figure 1B). For the human tissue array, tissues were selected from 48 individuals of different ethnicity. The y-axis represents the value of pg × 10 4 of DNA determined. Data were abtained using the comparative C T method with the values normalized to GAPDH levels and a standard curve. Details are in the "Materials and Method" section. Abbreviations: GAPDH, glyceraldehyde 3-phosphate dehydrogenase; Prx I, peroxiredoxin I; qRT-PCR, quantitative real-time polymerase chain reaction; Trx1, thioredoxin 1.

    Article Snippet: Polymerase chain reaction was performed in 96-well optical plates using the iCycler (Bio-Rad Laboratories, Hercules, CA, USA) with primers specific for Prx I-VI, Trx1, Trx2, β-actin, glyceraldehyde 3-phosphate dehydrogenase (GAPDH), and iQ SYBR Green Supermix (Bio-Rad).

    Techniques: Expressing, Quantitative RT-PCR, Real-time Polymerase Chain Reaction

    BRCA1 CpG hypermethylation associates with constitutively active AHR in triple negative breast cancers (TNBC) cells. ( A ) Representative Western blot images comparing immunocomplexes of AHR and internal standard glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in HCC38 and UACC3199 cells. ( B ) Data from methylation-specific PCR (MSP) comparing BRCA1 and ESR1 CpG methylation in HCC38 and MCF7 cells. ( C ) Bands represent immunocomplexes for BRCA1, estrogen receptor (ER)α, AHR, and internal standard GAPDH in MCF7 and HCC38 cells. ( D ) Comparison of AHR mRNA expression in HCC38 and MCF7 cells. ( E ) Expression of AHR targets CYP1A1 and CYP1B1 in HCC38 and MCF7 cells. ( F ) CYP1A1 and CYP1B1 expression in HCC38 cells treated with the AHR antagonist CH-223191. Bars represent sample means ± SEM from ≥3 biological replicates from individual experiments. VEH: vehicle-treated control. Asterisks indicate significant differences (*, p

    Journal: Nutrients

    Article Title: Epigenetic Activation of BRCA1 by Genistein In Vivo and Triple Negative Breast Cancer Cells Linked to Antagonism toward Aryl Hydrocarbon Receptor

    doi: 10.3390/nu11112559

    Figure Lengend Snippet: BRCA1 CpG hypermethylation associates with constitutively active AHR in triple negative breast cancers (TNBC) cells. ( A ) Representative Western blot images comparing immunocomplexes of AHR and internal standard glyceraldehyde 3-phosphate dehydrogenase (GAPDH) in HCC38 and UACC3199 cells. ( B ) Data from methylation-specific PCR (MSP) comparing BRCA1 and ESR1 CpG methylation in HCC38 and MCF7 cells. ( C ) Bands represent immunocomplexes for BRCA1, estrogen receptor (ER)α, AHR, and internal standard GAPDH in MCF7 and HCC38 cells. ( D ) Comparison of AHR mRNA expression in HCC38 and MCF7 cells. ( E ) Expression of AHR targets CYP1A1 and CYP1B1 in HCC38 and MCF7 cells. ( F ) CYP1A1 and CYP1B1 expression in HCC38 cells treated with the AHR antagonist CH-223191. Bars represent sample means ± SEM from ≥3 biological replicates from individual experiments. VEH: vehicle-treated control. Asterisks indicate significant differences (*, p

    Article Snippet: Immunoblotting was carried out with antibodies raised against BRCA1 (Boster Bio, Pleasanton, CA, USA; Ref. PB9015), ERα (Santa Cruz, Ref. MC-20), AHR (Santa Cruz Biotechnology Inc, Dallas, TX, USA; Ref. B-11), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (Origene, Rockville, MD, USA; Ref. TA890003).

    Techniques: Western Blot, Methylation, Polymerase Chain Reaction, CpG Methylation Assay, Expressing