glyceraldehyde 3 phosphate dehydrogenase gapdh Thermo Fisher Search Results


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  • 90
    Thermo Fisher gapdh monoclonal antibody
    CS improves liver health and treats cholestasis in Pemt –/– mice. Pemt +/+ and Pemt –/– mice were fed the HFD for 6 weeks and either continued on the HFD or the CSHFD for an additional 6 weeks. (A) Plasma BA concentration. (B) Hepatic TG, (C) PC, (D) PE, and (E) PC:PE ratio. Values are means ± SEM (n = 6 per group). mRNA expression of hepatic genes involved in (F) inflammation, (G) fibrosis, and (H) oxidative stress. Values are means ± SEM (n = 5 per group). (I) Hepatic <t>BSEP,</t> CHOP, and Bip and quantification relative to the amount of <t>GAPDH.</t> Values are means ± SEM (n = 6 per group); two‐way ANOVA followed by Fisher’s LSD post‐hoc test. Values that do not share a letter are significantly different ( P
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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.
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 2819 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher glyceraldehyde 3 phosphate dehydrogenase gapdh mrnas
    Analysis of NRAGE expression in the liver tissues. (A) NRAGE <t>mRNA</t> levels did not differ significantly between non-cancerous liver tissues of patients with and without cirrhosis. (B) NRAGE mRNA levels were significantly elevated in the HCC tissues compared with the corresponding non-cancerous liver tissues. (C) Two representative cases demonstrating strong immunoreactivity of NRAGE specific to the HCC tissues (magnification: Left, ×200; right, ×100; and inset, ×400). (D) Analysis of the correlation between NRAGE and AATF mRNA levels in the HCC tissues. HCC, hepatocellular carcinoma; NRAGE, neurotrophin receptor-interacting melanoma antigen-encoding protein; <t>GAPDH,</t> <t>glyceraldehyde-3-phosphate</t> dehydrogenase; N, normal; T, tumor; AATF, apoptosis-antagonizing transcription factor.
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh Mrnas, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 87/100, based on 44 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher taqman glyceraldehyde 3 phosphate dehydrogenase gapdh
    Amplification curve of realtime quantitative polymerase chain reaction (PCR) for thymidylate synthase (TS) mRNA and <t>glyceraldehyde-3-phosphate</t> dehydrogenase <t>(GAPDH).</t> FAM dye and JOE dye were used for TS mRNA and GAPDH, respectively. One cycle of reverse transcription (stage 1, 42℃ 5 minutes; stage 2, 95℃ 10 seconds) and 40 cycles of PCR reaction (stage 3, 95℃ 5 seconds; 60℃ 30 seconds) were performed for real-time quantitative PCR. Blue lines and yellow lines indicate TS mRNA and GAPDH, respectively. All tested extracted RNAs were drawn in the figure together.
    Taqman Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 82/100, based on 22 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher gapdh glyceraldehyde 3 phosphate dehydrogenase primers
    Atorvastatin inhibits tumour necrosis factor (TNF)-α-mediated matrix metalloproteinase 9 (MMP-9) production via the mitogen-activated protein/extracellular-regulated kinase (MEK/ERK) pathway. (a) Mouse vascular smooth muscle cells (MOVAS) cells were cultured with TNF-α and atorvastatin for 6 h, total RNA isolated, and cDNA synthesized. Real-time reverse transcription–polymerase chain reaction was performed and relative quantities of MMP-9 were expressed as a ratio against the housekeeping gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH).</t> (b) MOVAS cells were incubated with atorvastatin and TNF-α. Total protein was extracted and Western blot analysis was performed using antibodies specific for phospho-ERK 1/2 (in panel b) or antibodies specific for phospho-nuclear factor (NF)-κB (c). (d) Similar conditions to those in (a) but U0126, a MEK 1/2 inhibitor, was used instead of atorvastatin. All data presented represent at least three independent experiments. *** P
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    Thermo Fisher endogenous glyceraldehyde 3 phosphate dehydrogenase gapdh
    Atorvastatin inhibits tumour necrosis factor (TNF)-α-mediated matrix metalloproteinase 9 (MMP-9) production via the mitogen-activated protein/extracellular-regulated kinase (MEK/ERK) pathway. (a) Mouse vascular smooth muscle cells (MOVAS) cells were cultured with TNF-α and atorvastatin for 6 h, total RNA isolated, and cDNA synthesized. Real-time reverse transcription–polymerase chain reaction was performed and relative quantities of MMP-9 were expressed as a ratio against the housekeeping gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH).</t> (b) MOVAS cells were incubated with atorvastatin and TNF-α. Total protein was extracted and Western blot analysis was performed using antibodies specific for phospho-ERK 1/2 (in panel b) or antibodies specific for phospho-nuclear factor (NF)-κB (c). (d) Similar conditions to those in (a) but U0126, a MEK 1/2 inhibitor, was used instead of atorvastatin. All data presented represent at least three independent experiments. *** P
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    Thermo Fisher glyceraldehyde 3 phosphate dehydrogenase gapdh probes
    Atorvastatin inhibits tumour necrosis factor (TNF)-α-mediated matrix metalloproteinase 9 (MMP-9) production via the mitogen-activated protein/extracellular-regulated kinase (MEK/ERK) pathway. (a) Mouse vascular smooth muscle cells (MOVAS) cells were cultured with TNF-α and atorvastatin for 6 h, total RNA isolated, and cDNA synthesized. Real-time reverse transcription–polymerase chain reaction was performed and relative quantities of MMP-9 were expressed as a ratio against the housekeeping gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH).</t> (b) MOVAS cells were incubated with atorvastatin and TNF-α. Total protein was extracted and Western blot analysis was performed using antibodies specific for phospho-ERK 1/2 (in panel b) or antibodies specific for phospho-nuclear factor (NF)-κB (c). (d) Similar conditions to those in (a) but U0126, a MEK 1/2 inhibitor, was used instead of atorvastatin. All data presented represent at least three independent experiments. *** P
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh Probes, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 80/100, based on 19 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher glyceraldehyde 3 phosphate dehydrogenase gapdh decatemplate
    Atorvastatin inhibits tumour necrosis factor (TNF)-α-mediated matrix metalloproteinase 9 (MMP-9) production via the mitogen-activated protein/extracellular-regulated kinase (MEK/ERK) pathway. (a) Mouse vascular smooth muscle cells (MOVAS) cells were cultured with TNF-α and atorvastatin for 6 h, total RNA isolated, and cDNA synthesized. Real-time reverse transcription–polymerase chain reaction was performed and relative quantities of MMP-9 were expressed as a ratio against the housekeeping gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH).</t> (b) MOVAS cells were incubated with atorvastatin and TNF-α. Total protein was extracted and Western blot analysis was performed using antibodies specific for phospho-ERK 1/2 (in panel b) or antibodies specific for phospho-nuclear factor (NF)-κB (c). (d) Similar conditions to those in (a) but U0126, a MEK 1/2 inhibitor, was used instead of atorvastatin. All data presented represent at least three independent experiments. *** P
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    Thermo Fisher control glyceraldehyde 3 phosphate dehydrogenase gapdh
    Atorvastatin inhibits tumour necrosis factor (TNF)-α-mediated matrix metalloproteinase 9 (MMP-9) production via the mitogen-activated protein/extracellular-regulated kinase (MEK/ERK) pathway. (a) Mouse vascular smooth muscle cells (MOVAS) cells were cultured with TNF-α and atorvastatin for 6 h, total RNA isolated, and cDNA synthesized. Real-time reverse transcription–polymerase chain reaction was performed and relative quantities of MMP-9 were expressed as a ratio against the housekeeping gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH).</t> (b) MOVAS cells were incubated with atorvastatin and TNF-α. Total protein was extracted and Western blot analysis was performed using antibodies specific for phospho-ERK 1/2 (in panel b) or antibodies specific for phospho-nuclear factor (NF)-κB (c). (d) Similar conditions to those in (a) but U0126, a MEK 1/2 inhibitor, was used instead of atorvastatin. All data presented represent at least three independent experiments. *** P
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    Thermo Fisher endogenous control glyceraldehyde 3 phosphate dehydrogenase gapdh
    Collagen I induces matrix metalloproteinase (MMP)-2 expression through discoidin domain receptor (DDR)2, but not DDR1 in normal human lung fibroblasts (NHLFs) . NHLFs were reverse transfected with negative control small interfering (si)RNA, and DDR2-specific and DDR1-specific siRNA using lipofectamine RNAiMAX. At 48 h after transfection, NHLFs were serum-starved for 24 h and incubated with collagen I (25 μg/mL) or vehicle (acetic acid, 0.1 M) for 16 h. Total RNA was isolated, reverse transcribed and real-time quantitative PCR was performed using the TaqMan system with specific primers and TaqMan probes for human, MMP-2 (A) , and glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH).</t> The expression changes (fold increase) were calculated relative to unstimulated control cells after normalizing with GAPDH. Results are representative of mean fold increase ± SD of three independent experiments performed in triplicate (n = 9, * P
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    Thermo Fisher glyceraldehyde 3 phosphate dehydrogenase gapdh gene
    Collagen I induces matrix metalloproteinase (MMP)-2 expression through discoidin domain receptor (DDR)2, but not DDR1 in normal human lung fibroblasts (NHLFs) . NHLFs were reverse transfected with negative control small interfering (si)RNA, and DDR2-specific and DDR1-specific siRNA using lipofectamine RNAiMAX. At 48 h after transfection, NHLFs were serum-starved for 24 h and incubated with collagen I (25 μg/mL) or vehicle (acetic acid, 0.1 M) for 16 h. Total RNA was isolated, reverse transcribed and real-time quantitative PCR was performed using the TaqMan system with specific primers and TaqMan probes for human, MMP-2 (A) , and glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH).</t> The expression changes (fold increase) were calculated relative to unstimulated control cells after normalizing with GAPDH. Results are representative of mean fold increase ± SD of three independent experiments performed in triplicate (n = 9, * P
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    Thermo Fisher human glyceraldehyde 3 phosphate dehydrogenase gapdh
    Collagen I induces matrix metalloproteinase (MMP)-2 expression through discoidin domain receptor (DDR)2, but not DDR1 in normal human lung fibroblasts (NHLFs) . NHLFs were reverse transfected with negative control small interfering (si)RNA, and DDR2-specific and DDR1-specific siRNA using lipofectamine RNAiMAX. At 48 h after transfection, NHLFs were serum-starved for 24 h and incubated with collagen I (25 μg/mL) or vehicle (acetic acid, 0.1 M) for 16 h. Total RNA was isolated, reverse transcribed and real-time quantitative PCR was performed using the TaqMan system with specific primers and TaqMan probes for human, MMP-2 (A) , and glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH).</t> The expression changes (fold increase) were calculated relative to unstimulated control cells after normalizing with GAPDH. Results are representative of mean fold increase ± SD of three independent experiments performed in triplicate (n = 9, * P
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    Thermo Fisher glyceraldehyde 3 phosphate dehydrogenase gapdh sirna
    Bioluminescent SCLC cell lines respond to <t>GAPDH</t> depletion. DMS-53 luc+ and DMS-114 luc+ cells were treated with siRNAs against the housekeeping gene, GAPDH. GAPDH levels after knockdown were measured using quantitative RT-PCR. Approximately 91% and 97% knockdown was achieved for DMS-53 luc+ and DMS-114 luc+ cells, respectively ( A, B ). Negative controls included untreated cells (“Untreated”) and cells treated with a negative control <t>siRNA</t> provided by the manufacturer (“Negative Control siRNA”, Applied Biosystems). Cell viability upon GAPDH silencing was measured using luciferase assays ( C,D ). Points represent mean values and error bars represent standard error of means (n = 3 for quantitative RT-PCR, n = 4 for luciferase assays).
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    Thermo Fisher glyceraldehyde 3 phosphate dehydrogenase gapdh taqman reagents
    Bioluminescent SCLC cell lines respond to <t>GAPDH</t> depletion. DMS-53 luc+ and DMS-114 luc+ cells were treated with siRNAs against the housekeeping gene, GAPDH. GAPDH levels after knockdown were measured using quantitative RT-PCR. Approximately 91% and 97% knockdown was achieved for DMS-53 luc+ and DMS-114 luc+ cells, respectively ( A, B ). Negative controls included untreated cells (“Untreated”) and cells treated with a negative control <t>siRNA</t> provided by the manufacturer (“Negative Control siRNA”, Applied Biosystems). Cell viability upon GAPDH silencing was measured using luciferase assays ( C,D ). Points represent mean values and error bars represent standard error of means (n = 3 for quantitative RT-PCR, n = 4 for luciferase assays).
    Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh Taqman Reagents, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher glyceraldehyde 3 phosphate dehydrogenase
    Low-level MeHg induces genes regulating mitochondrial biogenesis via miR-25. ( a ) qPCR analysis of mature miR-30d, miR-1285, and miR-25 expression levels performed on RNA extracted from ihNPCs treated with 0 nM, 10 nM and 50 nM MeHg; ( b ) A representative Western blot of p53 expression in ihNPCs. Cells were transfected with 50 nM of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1 for 48 h; ( c ) Western blot analysis of p53 expression performed in 10 nM-treated ihNPCs after transient transfection of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression has been used as a loading control and a representative figure of three independent experiments has been shown. Results of gray value analysis are also reported (left part); ( d – f ) qPCR analysis of TFAM, PCG-α and p53R2 expression performed in 10 nM-treated ihNPCs after transient transfection of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1. All experiments were repeated three times (technical triplicates) with biological triplicates ( n  = 3). Bar graphs show mean ± SEM (*  p
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    Thermo Fisher ptri glyceraldehyde 3 phosphate dehydrogenase gapdh plasmid
    Low-level MeHg induces genes regulating mitochondrial biogenesis via miR-25. ( a ) qPCR analysis of mature miR-30d, miR-1285, and miR-25 expression levels performed on RNA extracted from ihNPCs treated with 0 nM, 10 nM and 50 nM MeHg; ( b ) A representative Western blot of p53 expression in ihNPCs. Cells were transfected with 50 nM of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1 for 48 h; ( c ) Western blot analysis of p53 expression performed in 10 nM-treated ihNPCs after transient transfection of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression has been used as a loading control and a representative figure of three independent experiments has been shown. Results of gray value analysis are also reported (left part); ( d – f ) qPCR analysis of TFAM, PCG-α and p53R2 expression performed in 10 nM-treated ihNPCs after transient transfection of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1. All experiments were repeated three times (technical triplicates) with biological triplicates ( n  = 3). Bar graphs show mean ± SEM (*  p
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    Thermo Fisher control human glyceraldehyde 3 phosphate dehydrogenase gapdh
    Low-level MeHg induces genes regulating mitochondrial biogenesis via miR-25. ( a ) qPCR analysis of mature miR-30d, miR-1285, and miR-25 expression levels performed on RNA extracted from ihNPCs treated with 0 nM, 10 nM and 50 nM MeHg; ( b ) A representative Western blot of p53 expression in ihNPCs. Cells were transfected with 50 nM of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1 for 48 h; ( c ) Western blot analysis of p53 expression performed in 10 nM-treated ihNPCs after transient transfection of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression has been used as a loading control and a representative figure of three independent experiments has been shown. Results of gray value analysis are also reported (left part); ( d – f ) qPCR analysis of TFAM, PCG-α and p53R2 expression performed in 10 nM-treated ihNPCs after transient transfection of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1. All experiments were repeated three times (technical triplicates) with biological triplicates ( n  = 3). Bar graphs show mean ± SEM (*  p
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    Thermo Fisher rat glyceraldehyde 3 phosphate dehydrogenase gapdh primers
    Low-level MeHg induces genes regulating mitochondrial biogenesis via miR-25. ( a ) qPCR analysis of mature miR-30d, miR-1285, and miR-25 expression levels performed on RNA extracted from ihNPCs treated with 0 nM, 10 nM and 50 nM MeHg; ( b ) A representative Western blot of p53 expression in ihNPCs. Cells were transfected with 50 nM of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1 for 48 h; ( c ) Western blot analysis of p53 expression performed in 10 nM-treated ihNPCs after transient transfection of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression has been used as a loading control and a representative figure of three independent experiments has been shown. Results of gray value analysis are also reported (left part); ( d – f ) qPCR analysis of TFAM, PCG-α and p53R2 expression performed in 10 nM-treated ihNPCs after transient transfection of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1. All experiments were repeated three times (technical triplicates) with biological triplicates ( n  = 3). Bar graphs show mean ± SEM (*  p
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    Thermo Fisher control gene glyceraldehyde 3 phosphate dehydrogenase gapdh
    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
    Control Gene Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 80/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
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    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
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    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
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    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
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    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
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    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
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    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
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    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.
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    Proteomic analysis and mechanotransduction protein expression of ascending aortas in WT and mLMNA + mice. (A) : Proteomic analysis of the ascending aortas in wild type (WT) and mLMNA + mice. This two-dimensional (2-D) gel image shows protein expression in the ascending aortas of WT (green) and mLMNA + (red) mice at 12 months. Yellow spots indicate commonly expressed proteins. The image suggests relatively greater expression of cytoskeleton (myosin regulatory light polypeptide 9, destrin, cytochrome b-c1 complex, actins) and mechanotransduction-related (vimentin, vinculin, transgelin) proteins in WT relative to mLMNA + mice, and relatively greater expression in mitochondrial enzymes and extracellular matrix components in mLMNA + mice relative to WT mice. A complete list of proteins can be found in (B) . (C) : Mechanotransduction protein levels in the ascending aorta of 12-month-old WT and mLMNA + mice. When vinculin, transgelin and vimentin bands were normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH),</t> the quantity of each protein was reduced in LMNA + mice compared with WT. The level of vimentin was the most significantly reduced.
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    Correlation between relative levels of Onchocerca volvulus genome and RAR-α relative expression levels. <t>GAPDH</t> indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Ovol2 and RAR relative levels for the control sample have been adjusted to 1 and are highlighted in green.
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    BVDV infection and tunicamycin treatment decrease intracellular GSH levels in MDBK cells. (A) Northern blot analysis of BVDV-infected MDBK cells harvested at the indicated times postinfection and probed with a radiolabeled <t>cDNA</t> probe from the human GCLC gene. The Northern blots were stripped and probed with a radiolabeled RNA probe specific for the mouse <t>GAPDH</t> gene. 5M and 30M, 5 and 30 h post-mock infection, respectively. (B) Intracellular levels of GSH were measured in BVDV-infected MDBK cell lysates. The GSH levels were normalized to total protein content in the cell lysates. (C) GSH levels were measured in mock-infected or BVDV-infected MDBK cells harvested at 24 h postinfection (h.p.i.). In separate cultures, MDBK cells were treated with 1 μg of tunicamycin (TUN) or irradiated with 40 μJ of UV light (218 nm). GSH levels were normalized to total protein content in the cell extracts.
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    BVDV infection and tunicamycin treatment decrease intracellular GSH levels in MDBK cells. (A) Northern blot analysis of BVDV-infected MDBK cells harvested at the indicated times postinfection and probed with a radiolabeled <t>cDNA</t> probe from the human GCLC gene. The Northern blots were stripped and probed with a radiolabeled RNA probe specific for the mouse <t>GAPDH</t> gene. 5M and 30M, 5 and 30 h post-mock infection, respectively. (B) Intracellular levels of GSH were measured in BVDV-infected MDBK cell lysates. The GSH levels were normalized to total protein content in the cell lysates. (C) GSH levels were measured in mock-infected or BVDV-infected MDBK cells harvested at 24 h postinfection (h.p.i.). In separate cultures, MDBK cells were treated with 1 μg of tunicamycin (TUN) or irradiated with 40 μJ of UV light (218 nm). GSH levels were normalized to total protein content in the cell extracts.
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    BVDV infection and tunicamycin treatment decrease intracellular GSH levels in MDBK cells. (A) Northern blot analysis of BVDV-infected MDBK cells harvested at the indicated times postinfection and probed with a radiolabeled <t>cDNA</t> probe from the human GCLC gene. The Northern blots were stripped and probed with a radiolabeled RNA probe specific for the mouse <t>GAPDH</t> gene. 5M and 30M, 5 and 30 h post-mock infection, respectively. (B) Intracellular levels of GSH were measured in BVDV-infected MDBK cell lysates. The GSH levels were normalized to total protein content in the cell lysates. (C) GSH levels were measured in mock-infected or BVDV-infected MDBK cells harvested at 24 h postinfection (h.p.i.). In separate cultures, MDBK cells were treated with 1 μg of tunicamycin (TUN) or irradiated with 40 μJ of UV light (218 nm). GSH levels were normalized to total protein content in the cell extracts.
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    Image Search Results


    CS improves liver health and treats cholestasis in Pemt –/– mice. Pemt +/+ and Pemt –/– mice were fed the HFD for 6 weeks and either continued on the HFD or the CSHFD for an additional 6 weeks. (A) Plasma BA concentration. (B) Hepatic TG, (C) PC, (D) PE, and (E) PC:PE ratio. Values are means ± SEM (n = 6 per group). mRNA expression of hepatic genes involved in (F) inflammation, (G) fibrosis, and (H) oxidative stress. Values are means ± SEM (n = 5 per group). (I) Hepatic BSEP, CHOP, and Bip and quantification relative to the amount of GAPDH. Values are means ± SEM (n = 6 per group); two‐way ANOVA followed by Fisher’s LSD post‐hoc test. Values that do not share a letter are significantly different ( P

    Journal: Hepatology Communications

    Article Title: Impaired Hepatic Phosphatidylcholine Synthesis Leads to Cholestasis in Mice Challenged With a High‐Fat Diet

    doi: 10.1002/hep4.1302

    Figure Lengend Snippet: CS improves liver health and treats cholestasis in Pemt –/– mice. Pemt +/+ and Pemt –/– mice were fed the HFD for 6 weeks and either continued on the HFD or the CSHFD for an additional 6 weeks. (A) Plasma BA concentration. (B) Hepatic TG, (C) PC, (D) PE, and (E) PC:PE ratio. Values are means ± SEM (n = 6 per group). mRNA expression of hepatic genes involved in (F) inflammation, (G) fibrosis, and (H) oxidative stress. Values are means ± SEM (n = 5 per group). (I) Hepatic BSEP, CHOP, and Bip and quantification relative to the amount of GAPDH. Values are means ± SEM (n = 6 per group); two‐way ANOVA followed by Fisher’s LSD post‐hoc test. Values that do not share a letter are significantly different ( P

    Article Snippet: Membranes were probed with CCAAT/‐enhancer‐binding protein homologous protein (CHOP; catalog No. 2895; Cell Signaling, Beverly, MA), binding immunoglobulin protein (BiP)/78 kDa glucose‐regulated protein (GRP78) (catalog No. 3183; Cell Signaling), BSEP (catalog No. PB9414; Boster), glyceraldehyde 3‐phosphate dehydrogenase (GAPDH; catalog No. AM4300; Ambion), and tubulin (catalog No. T6199; Sigma‐Aldrich).

    Techniques: Mouse Assay, Concentration Assay, Expressing

    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

    Analysis of NRAGE expression in the liver tissues. (A) NRAGE mRNA levels did not differ significantly between non-cancerous liver tissues of patients with and without cirrhosis. (B) NRAGE mRNA levels were significantly elevated in the HCC tissues compared with the corresponding non-cancerous liver tissues. (C) Two representative cases demonstrating strong immunoreactivity of NRAGE specific to the HCC tissues (magnification: Left, ×200; right, ×100; and inset, ×400). (D) Analysis of the correlation between NRAGE and AATF mRNA levels in the HCC tissues. HCC, hepatocellular carcinoma; NRAGE, neurotrophin receptor-interacting melanoma antigen-encoding protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; N, normal; T, tumor; AATF, apoptosis-antagonizing transcription factor.

    Journal: Oncology Letters

    Article Title: NRAGE promotes the malignant phenotype of hepatocellular carcinoma

    doi: 10.3892/ol.2016.4120

    Figure Lengend Snippet: Analysis of NRAGE expression in the liver tissues. (A) NRAGE mRNA levels did not differ significantly between non-cancerous liver tissues of patients with and without cirrhosis. (B) NRAGE mRNA levels were significantly elevated in the HCC tissues compared with the corresponding non-cancerous liver tissues. (C) Two representative cases demonstrating strong immunoreactivity of NRAGE specific to the HCC tissues (magnification: Left, ×200; right, ×100; and inset, ×400). (D) Analysis of the correlation between NRAGE and AATF mRNA levels in the HCC tissues. HCC, hepatocellular carcinoma; NRAGE, neurotrophin receptor-interacting melanoma antigen-encoding protein; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; N, normal; T, tumor; AATF, apoptosis-antagonizing transcription factor.

    Article Snippet: RT-qPCR was performed using the SYBR® Green PCR Core Reagents kit (Applied Biosystems; Thermo Fisher Scientific, Inc.) and specific primers for NRAGE (Hokkaido System Science Co., Ltd., Tokyo, Japan) as follows: One cycle at 95°C for 10 min, 40 cycles at 95°C for 5 sec and 60°C for 30 sec. For standardization, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) mRNA (TaqMan GAPDH Control Reagents; Applied Biosystems; Thermo Fisher Scientific, Inc.) was quantified in each sample.

    Techniques: Expressing

    Amplification curve of realtime quantitative polymerase chain reaction (PCR) for thymidylate synthase (TS) mRNA and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). FAM dye and JOE dye were used for TS mRNA and GAPDH, respectively. One cycle of reverse transcription (stage 1, 42℃ 5 minutes; stage 2, 95℃ 10 seconds) and 40 cycles of PCR reaction (stage 3, 95℃ 5 seconds; 60℃ 30 seconds) were performed for real-time quantitative PCR. Blue lines and yellow lines indicate TS mRNA and GAPDH, respectively. All tested extracted RNAs were drawn in the figure together.

    Journal: Journal of the Korean Surgical Society

    Article Title: A practical approach for assessing chemosensitivity in colorectal cancer cell lines by comparative analysis of cell viability and thymidylate synthase mRNA expression

    doi: 10.4174/jkss.2012.82.1.28

    Figure Lengend Snippet: Amplification curve of realtime quantitative polymerase chain reaction (PCR) for thymidylate synthase (TS) mRNA and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). FAM dye and JOE dye were used for TS mRNA and GAPDH, respectively. One cycle of reverse transcription (stage 1, 42℃ 5 minutes; stage 2, 95℃ 10 seconds) and 40 cycles of PCR reaction (stage 3, 95℃ 5 seconds; 60℃ 30 seconds) were performed for real-time quantitative PCR. Blue lines and yellow lines indicate TS mRNA and GAPDH, respectively. All tested extracted RNAs were drawn in the figure together.

    Article Snippet: TaqMan glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (Applied Biosystems) was used as an internal control.

    Techniques: Amplification, Real-time Polymerase Chain Reaction, Polymerase Chain Reaction

    Atorvastatin inhibits tumour necrosis factor (TNF)-α-mediated matrix metalloproteinase 9 (MMP-9) production via the mitogen-activated protein/extracellular-regulated kinase (MEK/ERK) pathway. (a) Mouse vascular smooth muscle cells (MOVAS) cells were cultured with TNF-α and atorvastatin for 6 h, total RNA isolated, and cDNA synthesized. Real-time reverse transcription–polymerase chain reaction was performed and relative quantities of MMP-9 were expressed as a ratio against the housekeeping gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH). (b) MOVAS cells were incubated with atorvastatin and TNF-α. Total protein was extracted and Western blot analysis was performed using antibodies specific for phospho-ERK 1/2 (in panel b) or antibodies specific for phospho-nuclear factor (NF)-κB (c). (d) Similar conditions to those in (a) but U0126, a MEK 1/2 inhibitor, was used instead of atorvastatin. All data presented represent at least three independent experiments. *** P

    Journal: Clinical and Experimental Immunology

    Article Title: The role of atorvastatin in regulating the immune response leading to vascular damage in a model of Kawasaki disease

    doi: 10.1111/j.1365-2249.2011.04331.x

    Figure Lengend Snippet: Atorvastatin inhibits tumour necrosis factor (TNF)-α-mediated matrix metalloproteinase 9 (MMP-9) production via the mitogen-activated protein/extracellular-regulated kinase (MEK/ERK) pathway. (a) Mouse vascular smooth muscle cells (MOVAS) cells were cultured with TNF-α and atorvastatin for 6 h, total RNA isolated, and cDNA synthesized. Real-time reverse transcription–polymerase chain reaction was performed and relative quantities of MMP-9 were expressed as a ratio against the housekeeping gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH). (b) MOVAS cells were incubated with atorvastatin and TNF-α. Total protein was extracted and Western blot analysis was performed using antibodies specific for phospho-ERK 1/2 (in panel b) or antibodies specific for phospho-nuclear factor (NF)-κB (c). (d) Similar conditions to those in (a) but U0126, a MEK 1/2 inhibitor, was used instead of atorvastatin. All data presented represent at least three independent experiments. *** P

    Article Snippet: Complementary DNA (cDNA) was synthesized using the GeneAmp RNA PCR kit and murine leukaemia virus reverse transcriptase (Applied Biosystems, Foster City, CA, USA). cDNA was then amplified by real-time RT–PCR following the manufacturer's protocol with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) primers and probe (Applied Biosystems) and the MMP-9 primers and probe set (Assays-on-Demand; Applied Biosystems) in an ABI PRISM 7900 Sequence Detection System (Applied Biosystems).

    Techniques: Cell Culture, Isolation, Synthesized, Reverse Transcription Polymerase Chain Reaction, Incubation, Western Blot

    Collagen I induces matrix metalloproteinase (MMP)-2 expression through discoidin domain receptor (DDR)2, but not DDR1 in normal human lung fibroblasts (NHLFs) . NHLFs were reverse transfected with negative control small interfering (si)RNA, and DDR2-specific and DDR1-specific siRNA using lipofectamine RNAiMAX. At 48 h after transfection, NHLFs were serum-starved for 24 h and incubated with collagen I (25 μg/mL) or vehicle (acetic acid, 0.1 M) for 16 h. Total RNA was isolated, reverse transcribed and real-time quantitative PCR was performed using the TaqMan system with specific primers and TaqMan probes for human, MMP-2 (A) , and glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The expression changes (fold increase) were calculated relative to unstimulated control cells after normalizing with GAPDH. Results are representative of mean fold increase ± SD of three independent experiments performed in triplicate (n = 9, * P

    Journal: Fibrogenesis & Tissue Repair

    Article Title: Discoidin domain receptors regulate the migration of primary human lung fibroblasts through collagen matrices

    doi: 10.1186/1755-1536-5-3

    Figure Lengend Snippet: Collagen I induces matrix metalloproteinase (MMP)-2 expression through discoidin domain receptor (DDR)2, but not DDR1 in normal human lung fibroblasts (NHLFs) . NHLFs were reverse transfected with negative control small interfering (si)RNA, and DDR2-specific and DDR1-specific siRNA using lipofectamine RNAiMAX. At 48 h after transfection, NHLFs were serum-starved for 24 h and incubated with collagen I (25 μg/mL) or vehicle (acetic acid, 0.1 M) for 16 h. Total RNA was isolated, reverse transcribed and real-time quantitative PCR was performed using the TaqMan system with specific primers and TaqMan probes for human, MMP-2 (A) , and glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The expression changes (fold increase) were calculated relative to unstimulated control cells after normalizing with GAPDH. Results are representative of mean fold increase ± SD of three independent experiments performed in triplicate (n = 9, * P

    Article Snippet: PCR was performed by denaturation at 95°C for 20 s, followed by 40 cycles of 95°C for 1 s and 60°C for 20 s. The expression changes (fold increase) were calculated relative to unstimulated control cells using the crossing points of the log linear portion of the amplification curve after normalizing with glyceraldehyde 3-phosphate dehydrogenase (GAPDH) endogenous control (VIC/MGB) (Life Technologies, Paisley, UK).

    Techniques: Expressing, Transfection, Negative Control, Incubation, Isolation, Real-time Polymerase Chain Reaction

    Bioluminescent SCLC cell lines respond to GAPDH depletion. DMS-53 luc+ and DMS-114 luc+ cells were treated with siRNAs against the housekeeping gene, GAPDH. GAPDH levels after knockdown were measured using quantitative RT-PCR. Approximately 91% and 97% knockdown was achieved for DMS-53 luc+ and DMS-114 luc+ cells, respectively ( A, B ). Negative controls included untreated cells (“Untreated”) and cells treated with a negative control siRNA provided by the manufacturer (“Negative Control siRNA”, Applied Biosystems). Cell viability upon GAPDH silencing was measured using luciferase assays ( C,D ). Points represent mean values and error bars represent standard error of means (n = 3 for quantitative RT-PCR, n = 4 for luciferase assays).

    Journal: PLoS ONE

    Article Title: Bioluminescence-Based High-Throughput Screen Identifies Pharmacological Agents That Target Neurotransmitter Signaling in Small Cell Lung Carcinoma

    doi: 10.1371/journal.pone.0024132

    Figure Lengend Snippet: Bioluminescent SCLC cell lines respond to GAPDH depletion. DMS-53 luc+ and DMS-114 luc+ cells were treated with siRNAs against the housekeeping gene, GAPDH. GAPDH levels after knockdown were measured using quantitative RT-PCR. Approximately 91% and 97% knockdown was achieved for DMS-53 luc+ and DMS-114 luc+ cells, respectively ( A, B ). Negative controls included untreated cells (“Untreated”) and cells treated with a negative control siRNA provided by the manufacturer (“Negative Control siRNA”, Applied Biosystems). Cell viability upon GAPDH silencing was measured using luciferase assays ( C,D ). Points represent mean values and error bars represent standard error of means (n = 3 for quantitative RT-PCR, n = 4 for luciferase assays).

    Article Snippet: Cells were transfected with 5–10 nM of a Silencer Select Negative Control #1 or glyceraldehyde 3-phosphate dehydrogenase (GAPDH) siRNA (Applied Biosystems) using Lipofectamine 2000 (Invitrogen) in Opti-MEM (Invitrogen).

    Techniques: Quantitative RT-PCR, Negative Control, Luciferase

    Low-level MeHg induces genes regulating mitochondrial biogenesis via miR-25. ( a ) qPCR analysis of mature miR-30d, miR-1285, and miR-25 expression levels performed on RNA extracted from ihNPCs treated with 0 nM, 10 nM and 50 nM MeHg; ( b ) A representative Western blot of p53 expression in ihNPCs. Cells were transfected with 50 nM of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1 for 48 h; ( c ) Western blot analysis of p53 expression performed in 10 nM-treated ihNPCs after transient transfection of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression has been used as a loading control and a representative figure of three independent experiments has been shown. Results of gray value analysis are also reported (left part); ( d – f ) qPCR analysis of TFAM, PCG-α and p53R2 expression performed in 10 nM-treated ihNPCs after transient transfection of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1. All experiments were repeated three times (technical triplicates) with biological triplicates ( n  = 3). Bar graphs show mean ± SEM (*  p

    Journal: International Journal of Molecular Sciences

    Article Title: Low-Dose Methylmercury-Induced Genes Regulate Mitochondrial Biogenesis via miR-25 in Immortalized Human Embryonic Neural Progenitor Cells

    doi: 10.3390/ijms17122058

    Figure Lengend Snippet: Low-level MeHg induces genes regulating mitochondrial biogenesis via miR-25. ( a ) qPCR analysis of mature miR-30d, miR-1285, and miR-25 expression levels performed on RNA extracted from ihNPCs treated with 0 nM, 10 nM and 50 nM MeHg; ( b ) A representative Western blot of p53 expression in ihNPCs. Cells were transfected with 50 nM of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1 for 48 h; ( c ) Western blot analysis of p53 expression performed in 10 nM-treated ihNPCs after transient transfection of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein expression has been used as a loading control and a representative figure of three independent experiments has been shown. Results of gray value analysis are also reported (left part); ( d – f ) qPCR analysis of TFAM, PCG-α and p53R2 expression performed in 10 nM-treated ihNPCs after transient transfection of miR-25 mimics, miR-mimic negative control#1, miR-25 inhibitor and miR-inhibitor negative control#1. All experiments were repeated three times (technical triplicates) with biological triplicates ( n = 3). Bar graphs show mean ± SEM (* p

    Article Snippet: The membrane was blocked with 5% skim milk for 1 h at room temperature and then incubated with primary antibodies to p53 and glyceraldehyde 3-phosphate dehydrogenase (GAPDH; Life Technology, Carlsbad, CA, USA) at 4 °C for 24 h. On the following day, the membrane was washed with 0.1% Tween-20 in Tris-buffered saline (TBS-T) and then incubated with horseradish peroxidase (HRP)-conjugated secondary antibody (anti-mouse) (Life Technology) for 1 h. The membrane was reacted with enhanced chemiluminescent (ECL) solution (ThermoFisher, Carlsbad, CA, USA), and LAS-3000 mini (Fujifilm, Tokyo, Japan) chemiluminescence detection device was used to visualize the labels.

    Techniques: Real-time Polymerase Chain Reaction, Expressing, Western Blot, Transfection, Negative Control

    LncRNA- SNHG7  is a direct transcriptional target of c-Myc. (A, B) MCF-7 and MDA-MB-231 cells were transduced with sh-ctrl or sh-c-Myc lentivirus, pCDH or pCDH-c-Myc lentivirus. Western blot analysis of c-Myc and β-actin. LncRNA- SNHG7  level was assessed by quantitative RT-PCR. (C) Schematic illustration of the consensus c-Myc binding sites in lncRNA- SNHG7  gene promoter. The wild-type and mutant binding sites are shown in the open boxes. The corresponding pGL3-based luciferase reporter constructs generated are shown. (D, E) MCF-7 were transduced with sh-ctrl or sh-c-Myc lentivirus, pCDH or pCDH-c-Myc lentivirus followed by transfection with the indicated pGL3-based luciferase reporter constructs. The reporter activity was measured 24 hours post-transfection, and plotted after normalizing with the Renilla luciferase activity. Western blot analysis of c-Myc and β-actin. (F) MCF-7 cells lysates were analyzed by ChIP assay using anti-c-Myc or IgG rabbit antibody. The ChIP products were amplified by semi-quantitative RT-PCR. (G) Correlation analyses conducted between c-Myc and lncRNA- SNHG7  in breast cancers (n = 50 biologically independent samples). Pearson correlation coefficients ( r ) and  p -values. Data were presented as mean ± standard deviation. lncRNA = long non-coding RNA; sh = short hairpin; RT-PCR = real-time polymerase chain reaction; NS = not significant; GAPDH = glyceraldehyde 3-phosphate dehydrogenase; IgG = immunoglobulin G. * p

    Journal: Journal of Breast Cancer

    Article Title: c-Myc-Induced Long Non-Coding RNA Small Nucleolar RNA Host Gene 7 Regulates Glycolysis in Breast Cancer

    doi: 10.4048/jbc.2019.22.e54

    Figure Lengend Snippet: LncRNA- SNHG7 is a direct transcriptional target of c-Myc. (A, B) MCF-7 and MDA-MB-231 cells were transduced with sh-ctrl or sh-c-Myc lentivirus, pCDH or pCDH-c-Myc lentivirus. Western blot analysis of c-Myc and β-actin. LncRNA- SNHG7 level was assessed by quantitative RT-PCR. (C) Schematic illustration of the consensus c-Myc binding sites in lncRNA- SNHG7 gene promoter. The wild-type and mutant binding sites are shown in the open boxes. The corresponding pGL3-based luciferase reporter constructs generated are shown. (D, E) MCF-7 were transduced with sh-ctrl or sh-c-Myc lentivirus, pCDH or pCDH-c-Myc lentivirus followed by transfection with the indicated pGL3-based luciferase reporter constructs. The reporter activity was measured 24 hours post-transfection, and plotted after normalizing with the Renilla luciferase activity. Western blot analysis of c-Myc and β-actin. (F) MCF-7 cells lysates were analyzed by ChIP assay using anti-c-Myc or IgG rabbit antibody. The ChIP products were amplified by semi-quantitative RT-PCR. (G) Correlation analyses conducted between c-Myc and lncRNA- SNHG7 in breast cancers (n = 50 biologically independent samples). Pearson correlation coefficients ( r ) and p -values. Data were presented as mean ± standard deviation. lncRNA = long non-coding RNA; sh = short hairpin; RT-PCR = real-time polymerase chain reaction; NS = not significant; GAPDH = glyceraldehyde 3-phosphate dehydrogenase; IgG = immunoglobulin G. * p

    Article Snippet: Primary antibodies used in the current study were: anti-HK2 (Thermo Fisher), anti-GPI (Thermo Fisher), anti-PFKL (Thermo Fisher), anti-ALDB (Thermo Fisher), anti-TPI1 (Sigma Aldrich), anti-PGK1 (Thermo Fisher), anti-PGAM1 (Sigma Aldrich), anti-ENO1 (Sigma Aldrich), anti-PKM2 (Sigma Aldrich), anti-lactate dehydrogenase A (LDHA; Thermo Fisher), anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH; Thermo Fisher), and anti-β actin (Sigma Aldrich).

    Techniques: Multiple Displacement Amplification, Transduction, Western Blot, Quantitative RT-PCR, Binding Assay, Mutagenesis, Luciferase, Construct, Generated, Transfection, Activity Assay, Chromatin Immunoprecipitation, Amplification, Standard Deviation, Reverse Transcription Polymerase Chain Reaction, Real-time Polymerase Chain Reaction

    Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH) were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.

    Journal: Breast Cancer Research : BCR

    Article Title: Large isoform of MRJ (DNAJB6) reduces malignant activity of breast cancer

    doi: 10.1186/bcr1874

    Figure Lengend Snippet: Confirmation of changes in level of secreted proteins. (a) The changes in the secreted proteome of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) expressor observed by mass spectrometry were confirmed by Western blot analysis. Serum-free medium from equal number of MDA-MB-435 parent (P), vector (V), MRJ(L) expressors (M) or MDA-MB-231 vector (V), and MRJ(L) expressors (M) was probed for presence of osteopontin (SPP1), osteonectin (SPARC), VGF nerve growth factor inducible (VGF), and zinc binding α 2 -glycoprotein 1 (AZGP1). Equal amount of total protein extract (20 μg) of the same cells was probed for the level of KiSS1 (melanoma metastasis suppressor); simultaneously, the expression of MRJ(L) was confirmed. β-Actin was used to verify equal loading of the lysate. Apparent molecular weights of the proteins detected are given in parenthesis: VGF (90 kDa), SPP1 (62 kDa), AZGP1 (47 kDa), SPARC (40 kDa), nucleophosmin (NPM1; 37 kDa), MRJ(L) (38 kDa), and KiSS1 (15 kDa). (b) Real-time quantitative RT-PCR analysis was performed using RNA from the MDA-MB-435-vector and MDA-MB-435-MRJ(L) expressor. The PCR primers and probes for KiSS1, NPM1, AZGP1, SPARC, SPP1, and VGF and endorse control gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH) were used. The reaction was performed for up to 40 cycles in triplicate. The gene expression Δ CT values of mRNAs from each sample were calculated by normalizing with internal control GAPDH. The fold change is represented as 2 -ΔΔCT . Real-time quantitative RT-PCR analysis was performed on the experimental mRNAs in triplicate and the experiment was repeated once from an independent passage.

    Article Snippet: The PCR primers and probes for KiSS1, nucleophosmin (NPM1), osteonectin (SPARC), osteopontin (SPP1), zinc binding α2 -glycoprotein 1 (AZGP1) and VGF nerve growth factor inducible (VGF), and endorse control gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH) were purchased from Applied Biosystems Inc. Quantative RT-PCR was performed on an ABI 7500 HT instrument (Applied Biosystems, Foster City, CA, USA).

    Techniques: Mass Spectrometry, Western Blot, Multiple Displacement Amplification, Plasmid Preparation, Binding Assay, Expressing, Quantitative RT-PCR, Polymerase Chain Reaction

    Expression of MRJ in breast cancer cell lines and tissues. (a) Expression of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) is significantly lower in various breast cancer cell lines as compared with that observed in RNA from normal breast. Real-time quantitative RT-PCR was used to assess expression of MRJ(L) relative to endorse control gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The data are represented as fold change in the abundance of the MRJ(L) transcripts using commercially available normal breast RNA as a calibrator. Each reaction was carried out in triplicate, and the experiment was repeated once with RNA from the same cell lines at a different passage. The error bars represent the standard error. (b) Expression of MRJ isoforms in various breast cancer cell lines. An equal amount of protein lysate (20 μg) was resolved on SDS-PAGE and immunoblotted for levels of MRJ isoforms. Equal loading was confirmed by comparable β-actin signal. (c) Tissue microarray staining for MRJ. A breast carcinoma progression array (CC08-00-001; developed by Cybrdi Inc.) was stained by 1:100 dilution (10 μg/ml) of DNAJB6 monoclonal antibody. Mouse IgG 1 was used for the isotype background control. Photomicrographs were taken in the area of most intense and diffuse staining for MRJ. The photomicrographs are representative images showing staining patterns of MRJ. Panel 1 corresponds to cystic hyperplasia, and panel 2 corresponds to infiltrating ductal carcinoma grade III.

    Journal: Breast Cancer Research : BCR

    Article Title: Large isoform of MRJ (DNAJB6) reduces malignant activity of breast cancer

    doi: 10.1186/bcr1874

    Figure Lengend Snippet: Expression of MRJ in breast cancer cell lines and tissues. (a) Expression of mammalian relative of DnaJ (MRJ) long isoform (MRJ [L]) is significantly lower in various breast cancer cell lines as compared with that observed in RNA from normal breast. Real-time quantitative RT-PCR was used to assess expression of MRJ(L) relative to endorse control gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH). The data are represented as fold change in the abundance of the MRJ(L) transcripts using commercially available normal breast RNA as a calibrator. Each reaction was carried out in triplicate, and the experiment was repeated once with RNA from the same cell lines at a different passage. The error bars represent the standard error. (b) Expression of MRJ isoforms in various breast cancer cell lines. An equal amount of protein lysate (20 μg) was resolved on SDS-PAGE and immunoblotted for levels of MRJ isoforms. Equal loading was confirmed by comparable β-actin signal. (c) Tissue microarray staining for MRJ. A breast carcinoma progression array (CC08-00-001; developed by Cybrdi Inc.) was stained by 1:100 dilution (10 μg/ml) of DNAJB6 monoclonal antibody. Mouse IgG 1 was used for the isotype background control. Photomicrographs were taken in the area of most intense and diffuse staining for MRJ. The photomicrographs are representative images showing staining patterns of MRJ. Panel 1 corresponds to cystic hyperplasia, and panel 2 corresponds to infiltrating ductal carcinoma grade III.

    Article Snippet: The PCR primers and probes for KiSS1, nucleophosmin (NPM1), osteonectin (SPARC), osteopontin (SPP1), zinc binding α2 -glycoprotein 1 (AZGP1) and VGF nerve growth factor inducible (VGF), and endorse control gene glyceraldehyde 3-phosphate dehydrogenase (GAPDH) were purchased from Applied Biosystems Inc. Quantative RT-PCR was performed on an ABI 7500 HT instrument (Applied Biosystems, Foster City, CA, USA).

    Techniques: Expressing, Quantitative RT-PCR, SDS Page, Microarray, Staining

    Proteomic analysis and mechanotransduction protein expression of ascending aortas in WT and mLMNA + mice. (A) : Proteomic analysis of the ascending aortas in wild type (WT) and mLMNA + mice. This two-dimensional (2-D) gel image shows protein expression in the ascending aortas of WT (green) and mLMNA + (red) mice at 12 months. Yellow spots indicate commonly expressed proteins. The image suggests relatively greater expression of cytoskeleton (myosin regulatory light polypeptide 9, destrin, cytochrome b-c1 complex, actins) and mechanotransduction-related (vimentin, vinculin, transgelin) proteins in WT relative to mLMNA + mice, and relatively greater expression in mitochondrial enzymes and extracellular matrix components in mLMNA + mice relative to WT mice. A complete list of proteins can be found in (B) . (C) : Mechanotransduction protein levels in the ascending aorta of 12-month-old WT and mLMNA + mice. When vinculin, transgelin and vimentin bands were normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH), the quantity of each protein was reduced in LMNA + mice compared with WT. The level of vimentin was the most significantly reduced.

    Journal: Stem Cell Research & Therapy

    Article Title: Shear stress-induced mechanotransduction protein deregulation and vasculopathy in a mouse model of progeria

    doi: 10.1186/scrt429

    Figure Lengend Snippet: Proteomic analysis and mechanotransduction protein expression of ascending aortas in WT and mLMNA + mice. (A) : Proteomic analysis of the ascending aortas in wild type (WT) and mLMNA + mice. This two-dimensional (2-D) gel image shows protein expression in the ascending aortas of WT (green) and mLMNA + (red) mice at 12 months. Yellow spots indicate commonly expressed proteins. The image suggests relatively greater expression of cytoskeleton (myosin regulatory light polypeptide 9, destrin, cytochrome b-c1 complex, actins) and mechanotransduction-related (vimentin, vinculin, transgelin) proteins in WT relative to mLMNA + mice, and relatively greater expression in mitochondrial enzymes and extracellular matrix components in mLMNA + mice relative to WT mice. A complete list of proteins can be found in (B) . (C) : Mechanotransduction protein levels in the ascending aorta of 12-month-old WT and mLMNA + mice. When vinculin, transgelin and vimentin bands were normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH), the quantity of each protein was reduced in LMNA + mice compared with WT. The level of vimentin was the most significantly reduced.

    Article Snippet: Primary antibodies included rabbit anti-transgelin (1:1,000), mouse anti-vinculin (1:200), rabbit anti-vimentin (1:500), (Abcam, Cambridge, MA, USA) and mouse anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (1:5,000, Ambion, Austin, TX, USA).

    Techniques: Expressing, Mouse Assay

    Western blot analysis of vimentin in the ascending and descending aortas. (A) Vimentin expression was investigated by Western blot in 2-, 6- and 12-month-old wild type (WT) and mLMNA + mice. Blots were performed in triplicate and total vimentin intensity of the four isomer bands was normalized with glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and the ratio indicated. At two months, vimentin was expressed at a similar level in WT and mLMNA + ascending aortas. However, vimentin expression was reduced by 30% at 6 months and by 60% at 12 months in mLMNA + ascending aortas. The 12-month descending aortas showed no difference between WT and mLMNA + mice. (B) When the expression bands of SMαA in the ascending aortas of six-month-old WT and mLMNA + mice were normalized to GAPDH, they were similar (ratio = 1.0:0.9). (* P

    Journal: Stem Cell Research & Therapy

    Article Title: Shear stress-induced mechanotransduction protein deregulation and vasculopathy in a mouse model of progeria

    doi: 10.1186/scrt429

    Figure Lengend Snippet: Western blot analysis of vimentin in the ascending and descending aortas. (A) Vimentin expression was investigated by Western blot in 2-, 6- and 12-month-old wild type (WT) and mLMNA + mice. Blots were performed in triplicate and total vimentin intensity of the four isomer bands was normalized with glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and the ratio indicated. At two months, vimentin was expressed at a similar level in WT and mLMNA + ascending aortas. However, vimentin expression was reduced by 30% at 6 months and by 60% at 12 months in mLMNA + ascending aortas. The 12-month descending aortas showed no difference between WT and mLMNA + mice. (B) When the expression bands of SMαA in the ascending aortas of six-month-old WT and mLMNA + mice were normalized to GAPDH, they were similar (ratio = 1.0:0.9). (* P

    Article Snippet: Primary antibodies included rabbit anti-transgelin (1:1,000), mouse anti-vinculin (1:200), rabbit anti-vimentin (1:500), (Abcam, Cambridge, MA, USA) and mouse anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (1:5,000, Ambion, Austin, TX, USA).

    Techniques: Western Blot, Expressing, Mouse Assay

    Epigenetic silencing of GATA6 through the activation of STAT3 suppresses expression of trefoil factors (TFF) 1 and 2 in gastric cancer: ( A ) Relative expression levels of GATA6 in immortalized gastric epithelial cells (GES) and gastric cancer cell lines as determined by RT-PCR; ( B ) Methylation level of the GATA6 promoter in gastric cancer cell lines, as determined by bisulfite pyrosequencing. Relative expression levels of ( C ) TFF1 and ( D ) TFF2 in the same gastric cancer cell lines, as determined by RT-PCR; ( E ) Western blot analysis showing the protein levels of STAT3 and phosphorylated STAT3 (pSTAT3) in AGS gastric cancer cells treated with various quantities of STAT3 inhibitor rhodium(III) complex 6 (RHD6). The protein level of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was used as a loading control. Relative expression levels of GATA6 , TFF1 , and TFF2 in ( F ) MKN45, ( G ) MKN28, and ( H ) AGS gastric cancer cells treated with dimethyl sulfoxide (DMSO) or 2.5 μm of RHD6. (*** p

    Journal: International Journal of Molecular Sciences

    Article Title: Aberrant JAK/STAT Signaling Suppresses TFF1 and TFF2 through Epigenetic Silencing of GATA6 in Gastric Cancer

    doi: 10.3390/ijms17091467

    Figure Lengend Snippet: Epigenetic silencing of GATA6 through the activation of STAT3 suppresses expression of trefoil factors (TFF) 1 and 2 in gastric cancer: ( A ) Relative expression levels of GATA6 in immortalized gastric epithelial cells (GES) and gastric cancer cell lines as determined by RT-PCR; ( B ) Methylation level of the GATA6 promoter in gastric cancer cell lines, as determined by bisulfite pyrosequencing. Relative expression levels of ( C ) TFF1 and ( D ) TFF2 in the same gastric cancer cell lines, as determined by RT-PCR; ( E ) Western blot analysis showing the protein levels of STAT3 and phosphorylated STAT3 (pSTAT3) in AGS gastric cancer cells treated with various quantities of STAT3 inhibitor rhodium(III) complex 6 (RHD6). The protein level of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was used as a loading control. Relative expression levels of GATA6 , TFF1 , and TFF2 in ( F ) MKN45, ( G ) MKN28, and ( H ) AGS gastric cancer cells treated with dimethyl sulfoxide (DMSO) or 2.5 μm of RHD6. (*** p

    Article Snippet: The membrane was then incubated overnight at 4 °C with primary antibodies, rabbit anti-pSTAT3 (1:1000, Cell Signaling, Beverly, MA, USA), mouse anti-STAT3 (1:1000, Cell Signaling), rabbit anti-GATA6 (1:1000, Abcam, Cambridge, UK), rabbit anti-TFF1 (1:1000, Abcam), mouse anti-TFF2 (1:1000, Abcam) or mouse anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibodies (1:1000, Thermo Fisher Scientific, Rockford, IL, USA), as diluted in 1× phosphate-buffered saline with Tween (PBST).

    Techniques: Activation Assay, Expressing, Reverse Transcription Polymerase Chain Reaction, Methylation, Western Blot

    Correlation between relative levels of Onchocerca volvulus genome and RAR-α relative expression levels. GAPDH indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Ovol2 and RAR relative levels for the control sample have been adjusted to 1 and are highlighted in green.

    Journal: Infectious Diseases

    Article Title: Retinoid Expression in Onchocercal Skin Disease: Pilot Study

    doi: 10.1177/1178633617731741

    Figure Lengend Snippet: Correlation between relative levels of Onchocerca volvulus genome and RAR-α relative expression levels. GAPDH indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Ovol2 and RAR relative levels for the control sample have been adjusted to 1 and are highlighted in green.

    Article Snippet: Quantitative polymerase chain reaction and data analysis A target-specific TaqMan assay for O volvulus genomic sequence, for RAR-α transcripts, and for the genomic sequence of human glyceraldehyde 3-phosphate dehydrogenase (GAPDH) gene, was obtained from Applied Biosystems Inc. (ABI).

    Techniques: Expressing

    Fold expression of RAR-α relative to control sample (normalized with expression levels of GAPDH). GAPDH indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Uncolored bars indicate that no average Ct was obtained for the retinoic acid receptor (RAR) and/or GAPDH assay for that sample. Retinoic acid receptor expression levels for the control sample have been adjusted to 1 and are highlighted in green.

    Journal: Infectious Diseases

    Article Title: Retinoid Expression in Onchocercal Skin Disease: Pilot Study

    doi: 10.1177/1178633617731741

    Figure Lengend Snippet: Fold expression of RAR-α relative to control sample (normalized with expression levels of GAPDH). GAPDH indicates glyceraldehyde 3-phosphate dehydrogenase; RAR-α, retinoic acid receptor-α. (+) or (−) tags after sample IDs designate their association with positive and negative sample groups, respectively. Uncolored bars indicate that no average Ct was obtained for the retinoic acid receptor (RAR) and/or GAPDH assay for that sample. Retinoic acid receptor expression levels for the control sample have been adjusted to 1 and are highlighted in green.

    Article Snippet: Quantitative polymerase chain reaction and data analysis A target-specific TaqMan assay for O volvulus genomic sequence, for RAR-α transcripts, and for the genomic sequence of human glyceraldehyde 3-phosphate dehydrogenase (GAPDH) gene, was obtained from Applied Biosystems Inc. (ABI).

    Techniques: Expressing

    BVDV infection and tunicamycin treatment decrease intracellular GSH levels in MDBK cells. (A) Northern blot analysis of BVDV-infected MDBK cells harvested at the indicated times postinfection and probed with a radiolabeled cDNA probe from the human GCLC gene. The Northern blots were stripped and probed with a radiolabeled RNA probe specific for the mouse GAPDH gene. 5M and 30M, 5 and 30 h post-mock infection, respectively. (B) Intracellular levels of GSH were measured in BVDV-infected MDBK cell lysates. The GSH levels were normalized to total protein content in the cell lysates. (C) GSH levels were measured in mock-infected or BVDV-infected MDBK cells harvested at 24 h postinfection (h.p.i.). In separate cultures, MDBK cells were treated with 1 μg of tunicamycin (TUN) or irradiated with 40 μJ of UV light (218 nm). GSH levels were normalized to total protein content in the cell extracts.

    Journal: Journal of Virology

    Article Title: Replication of a Cytopathic Strain of Bovine Viral Diarrhea Virus Activates PERK and Induces Endoplasmic Reticulum Stress-Mediated Apoptosis of MDBK Cells

    doi: 10.1128/JVI.76.19.9588-9599.2002

    Figure Lengend Snippet: BVDV infection and tunicamycin treatment decrease intracellular GSH levels in MDBK cells. (A) Northern blot analysis of BVDV-infected MDBK cells harvested at the indicated times postinfection and probed with a radiolabeled cDNA probe from the human GCLC gene. The Northern blots were stripped and probed with a radiolabeled RNA probe specific for the mouse GAPDH gene. 5M and 30M, 5 and 30 h post-mock infection, respectively. (B) Intracellular levels of GSH were measured in BVDV-infected MDBK cell lysates. The GSH levels were normalized to total protein content in the cell lysates. (C) GSH levels were measured in mock-infected or BVDV-infected MDBK cells harvested at 24 h postinfection (h.p.i.). In separate cultures, MDBK cells were treated with 1 μg of tunicamycin (TUN) or irradiated with 40 μJ of UV light (218 nm). GSH levels were normalized to total protein content in the cell extracts.

    Article Snippet: The plasmid containing the mouse glyceraldehyde-3-phosphate dehydrogenase (GAPDH) cDNA was purchased from Ambion, Inc., Austin, Tex.

    Techniques: Infection, Northern Blot, Irradiation