glyceraldehyde 3 phosphate dehydrogenase gapdh Millipore Search Results


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  • 95
    Millipore glyceraldehyde 3 phosphate dehydrogenase gapdh
    Effects of ethanol and androgenization on profibrotic gene expression. Quantitative Real-Time PCR analysis of Interleukin-6 (IL-6) (black bar) and collagen Type 3 (COL3α1) (striped bar) gene expression in control (Ctrl), androgenized (Andro) and Andro + estrogen (Andro + E2) animals maintained on control Lieber-DeCarli (C-LDC) or ethanol-LDC (E-LDC) diet. Gene expression was normalized to <t>glyceraldehyde-3-phosphate</t> dehydrogenase <t>(GAPDH).</t> Data are presented as mean values ± SEM. *P
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    Merck KGaA glyceraldehyde 3 phosphate dehydrogenase gapdh
    Effects of ethanol and androgenization on profibrotic gene expression. Quantitative Real-Time PCR analysis of Interleukin-6 (IL-6) (black bar) and collagen Type 3 (COL3α1) (striped bar) gene expression in control (Ctrl), androgenized (Andro) and Andro + estrogen (Andro + E2) animals maintained on control Lieber-DeCarli (C-LDC) or ethanol-LDC (E-LDC) diet. Gene expression was normalized to <t>glyceraldehyde-3-phosphate</t> dehydrogenase <t>(GAPDH).</t> Data are presented as mean values ± SEM. *P
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    95
    Millipore gapdh
    VP4 is concentrated along the nuclear envelope. (A) Cos7 cells were transiently transfected with either empty vector (−) or VP4 (+) in the presence of the tetracycline repressor. Tetracycline was added for the indicated times. Whole-cell lysates were immunoblotted with antisera against myc to detect VP4 or the loading control <t>GAPDH.</t> (B) Confocal immunofluorescence microscopy localization of VP4 in Cos7 cells was determined after 6 h of induction. Samples were labeled with myc (VP4-myc), ERp57, <t>emerin,</t> or lamin antisera and stained with either Hoechst or DAPI (DAPI, 4′,6-diamidino-2-phenylindole) as indicated. A fraction of the VP4-expressing cells displayed profound nuclear envelope disruption, as displayed in the lamin lower panel. Bars, 10 μm.
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    Millipore internal control glyceraldehyde 3 phosphate dehydrogenase gapdh
    VP4 is concentrated along the nuclear envelope. (A) Cos7 cells were transiently transfected with either empty vector (−) or VP4 (+) in the presence of the tetracycline repressor. Tetracycline was added for the indicated times. Whole-cell lysates were immunoblotted with antisera against myc to detect VP4 or the loading control <t>GAPDH.</t> (B) Confocal immunofluorescence microscopy localization of VP4 in Cos7 cells was determined after 6 h of induction. Samples were labeled with myc (VP4-myc), ERp57, <t>emerin,</t> or lamin antisera and stained with either Hoechst or DAPI (DAPI, 4′,6-diamidino-2-phenylindole) as indicated. A fraction of the VP4-expressing cells displayed profound nuclear envelope disruption, as displayed in the lamin lower panel. Bars, 10 μm.
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    95
    Merck KGaA glyceraldehyde 3 phosphate dehydrogenase
    VP4 is concentrated along the nuclear envelope. (A) Cos7 cells were transiently transfected with either empty vector (−) or VP4 (+) in the presence of the tetracycline repressor. Tetracycline was added for the indicated times. Whole-cell lysates were immunoblotted with antisera against myc to detect VP4 or the loading control <t>GAPDH.</t> (B) Confocal immunofluorescence microscopy localization of VP4 in Cos7 cells was determined after 6 h of induction. Samples were labeled with myc (VP4-myc), ERp57, <t>emerin,</t> or lamin antisera and stained with either Hoechst or DAPI (DAPI, 4′,6-diamidino-2-phenylindole) as indicated. A fraction of the VP4-expressing cells displayed profound nuclear envelope disruption, as displayed in the lamin lower panel. Bars, 10 μm.
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    Merck KGaA monoclonal anti glyceraldehyde 3 phosphate dehydrogenase gapdh
    VP4 is concentrated along the nuclear envelope. (A) Cos7 cells were transiently transfected with either empty vector (−) or VP4 (+) in the presence of the tetracycline repressor. Tetracycline was added for the indicated times. Whole-cell lysates were immunoblotted with antisera against myc to detect VP4 or the loading control <t>GAPDH.</t> (B) Confocal immunofluorescence microscopy localization of VP4 in Cos7 cells was determined after 6 h of induction. Samples were labeled with myc (VP4-myc), ERp57, <t>emerin,</t> or lamin antisera and stained with either Hoechst or DAPI (DAPI, 4′,6-diamidino-2-phenylindole) as indicated. A fraction of the VP4-expressing cells displayed profound nuclear envelope disruption, as displayed in the lamin lower panel. Bars, 10 μm.
    Monoclonal Anti Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 88/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore mouse anti glyceraldehyde 3 phosphate dehydrogenase gapdh
    Expression of TMEM106B in different cell types. ( A ) Cell lysates from HEK293T, NSC-34 and BV-2 were loaded and blotted with anti-TMEM106B and anti-glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> antibodies. ( B ) TMEM106B forms homodimers. FLAG-tagged
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    Millipore anti glyceraldehyde 3 phosphate dehydrogenase gapdh peroxidase
    Expression of TMEM106B in different cell types. ( A ) Cell lysates from HEK293T, NSC-34 and BV-2 were loaded and blotted with anti-TMEM106B and anti-glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> antibodies. ( B ) TMEM106B forms homodimers. FLAG-tagged
    Anti Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh Peroxidase, supplied by Millipore, used in various techniques. Bioz Stars score: 76/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore anti acetyl glyceraldehyde 3 phosphate dehydrogenase gapdh
    Expression of TMEM106B in different cell types. ( A ) Cell lysates from HEK293T, NSC-34 and BV-2 were loaded and blotted with anti-TMEM106B and anti-glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> antibodies. ( B ) TMEM106B forms homodimers. FLAG-tagged
    Anti Acetyl Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Millipore, used in various techniques. Bioz Stars score: 80/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Millipore rabbit anti glyceraldehyde 3 phosphate dehydrogenase gapdh
    Spinal Tyr1472 and Ser1303 phosphorylation of N-methyl-D-aspartate (NMDA) receptor NR2B subunit at day 28 after spinal cord injury (SCI) in wild type (WT) and sigma-1 receptor (σ1R) knockout (KO) mice. ( A ) Quantification and representative immunoblots of total NR2B, pS1303NR2B and glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH).</t> ( B ) Quantification and representative immunoblots of total NR2B, pY1472NR2B and GAPDH. a–b: groups not sharing a letter are significantly different, p
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    Merck KGaA glyceraldehyde 3 phosphate dehydrogenase gapdh abs16
    Spinal Tyr1472 and Ser1303 phosphorylation of N-methyl-D-aspartate (NMDA) receptor NR2B subunit at day 28 after spinal cord injury (SCI) in wild type (WT) and sigma-1 receptor (σ1R) knockout (KO) mice. ( A ) Quantification and representative immunoblots of total NR2B, pS1303NR2B and glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH).</t> ( B ) Quantification and representative immunoblots of total NR2B, pY1472NR2B and GAPDH. a–b: groups not sharing a letter are significantly different, p
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    Millipore cardiac glyceraldehyde 3 phosphate dehydrogenase gapdh
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
    Cardiac Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh, supplied by Millipore, used in various techniques. Bioz Stars score: 79/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore monoclonal anti glyceraldehyde 3 phosphate dehydrogenase gapdh 1 100 000 millipore
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
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    Millipore human polyclonal glyceraldehyde 3 phosphate dehydrogenase gapdh
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
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    Millipore primary mouse glyceraldehyde 3 phosphate dehydrogenase gapdh antibody
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
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    Millipore anti glyceraldehyde 3 phosphate dehydrogenase gapdh polyclonal antibodies
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
    Anti Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh Polyclonal Antibodies, supplied by Millipore, used in various techniques. Bioz Stars score: 82/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore recombinant glyceraldehyde 3 phosphate dehydrogenase gapdh
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
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    86
    Merck KGaA reference protein glyceraldehyde 3 phosphate dehydrogenase
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
    Reference Protein Glyceraldehyde 3 Phosphate Dehydrogenase, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 86/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Millipore mouse monoclonal glyceraldehyde 3 phosphate dehydrogenase gapdh 1 1000
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
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    Millipore glyceraldehyde 3 phosphate dehydrogenase gapdh expression
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
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    Millipore rabbit polyclonal anti glyceraldehyde 3 phosphate dehydrogenase antibody gapdh
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
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    Millipore mouse anti glyceraldehyde 3 phosphate dehydrogenase anti gapdh 6c5
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
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    Millipore g mouse glyceraldehyde 3 phosphate dehydrogenase gapdh mouse monoclonal
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
    G Mouse Glyceraldehyde 3 Phosphate Dehydrogenase Gapdh Mouse Monoclonal, supplied by Millipore, used in various techniques. Bioz Stars score: 77/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Becton Dickinson glyceraldehyde 3 phosphate dehydrogenase
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
    Glyceraldehyde 3 Phosphate Dehydrogenase, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 95/100, based on 70 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Santa Cruz Biotechnology glyceraldehyde 3 phosphate dehydrogenase
    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase <t>(GAPDH)</t> as an internal control.
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    Millipore human erythrocyte gapdh
    Extracellular (secreted) <t>GAPDH</t> bound to E-cadherin. ( A ) MKN-7 cells were cultured with human erythrocyte GAPDH at 5 U/mL for 1 day. The cells were fixed under nonpermeabilizing conditions, stained with the indicated antibodies and analyzed by confocal microscopy. Scale bar is 50 μm. ( B ) Cell membranes of MKN-7 cells were incubated with <t>FLAG-tagged</t> human recombinant wtGAPDH or human erythrocyte GAPDH. The immunoprecipitates generated with the indicated antibodies were analyzed by Western blotting with anti-E-cadherin antibody. ( C ) Human erythrocyte GAPDH was added to a human recombinant E-cadherin-coated plate. GAPDH bound to the plate was detected by Western blot. ( D ) MKN-7 and MKN-74 cells were cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. The mTOR-p70S6K pathway was analyzed by Western blot. ( E ) MKN-7 cells were transfected with control siRNA or E-cadherin siRNA for 3 days and then further cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. E-cadherin and phosphorylated RPS6 were analyzed by Western blotting.
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    Merck KGaA mouse anti glyceraldehyde 3 phosphate dehydrogenase gapdh monoclonal antibody
    Extracellular (secreted) <t>GAPDH</t> bound to E-cadherin. ( A ) MKN-7 cells were cultured with human erythrocyte GAPDH at 5 U/mL for 1 day. The cells were fixed under nonpermeabilizing conditions, stained with the indicated antibodies and analyzed by confocal microscopy. Scale bar is 50 μm. ( B ) Cell membranes of MKN-7 cells were incubated with <t>FLAG-tagged</t> human recombinant wtGAPDH or human erythrocyte GAPDH. The immunoprecipitates generated with the indicated antibodies were analyzed by Western blotting with anti-E-cadherin antibody. ( C ) Human erythrocyte GAPDH was added to a human recombinant E-cadherin-coated plate. GAPDH bound to the plate was detected by Western blot. ( D ) MKN-7 and MKN-74 cells were cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. The mTOR-p70S6K pathway was analyzed by Western blot. ( E ) MKN-7 cells were transfected with control siRNA or E-cadherin siRNA for 3 days and then further cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. E-cadherin and phosphorylated RPS6 were analyzed by Western blotting.
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    Millipore rabbit anti human glyceraldehyde 3 phosphate dehydrogenase gapdh ab
    Extracellular (secreted) <t>GAPDH</t> bound to E-cadherin. ( A ) MKN-7 cells were cultured with human erythrocyte GAPDH at 5 U/mL for 1 day. The cells were fixed under nonpermeabilizing conditions, stained with the indicated antibodies and analyzed by confocal microscopy. Scale bar is 50 μm. ( B ) Cell membranes of MKN-7 cells were incubated with <t>FLAG-tagged</t> human recombinant wtGAPDH or human erythrocyte GAPDH. The immunoprecipitates generated with the indicated antibodies were analyzed by Western blotting with anti-E-cadherin antibody. ( C ) Human erythrocyte GAPDH was added to a human recombinant E-cadherin-coated plate. GAPDH bound to the plate was detected by Western blot. ( D ) MKN-7 and MKN-74 cells were cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. The mTOR-p70S6K pathway was analyzed by Western blot. ( E ) MKN-7 cells were transfected with control siRNA or E-cadherin siRNA for 3 days and then further cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. E-cadherin and phosphorylated RPS6 were analyzed by Western blotting.
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    Millipore mouse monoclonal anti glyceraldehyde 3 phosphate dehydrogenase gapdh antibody 374
    Extracellular (secreted) <t>GAPDH</t> bound to E-cadherin. ( A ) MKN-7 cells were cultured with human erythrocyte GAPDH at 5 U/mL for 1 day. The cells were fixed under nonpermeabilizing conditions, stained with the indicated antibodies and analyzed by confocal microscopy. Scale bar is 50 μm. ( B ) Cell membranes of MKN-7 cells were incubated with <t>FLAG-tagged</t> human recombinant wtGAPDH or human erythrocyte GAPDH. The immunoprecipitates generated with the indicated antibodies were analyzed by Western blotting with anti-E-cadherin antibody. ( C ) Human erythrocyte GAPDH was added to a human recombinant E-cadherin-coated plate. GAPDH bound to the plate was detected by Western blot. ( D ) MKN-7 and MKN-74 cells were cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. The mTOR-p70S6K pathway was analyzed by Western blot. ( E ) MKN-7 cells were transfected with control siRNA or E-cadherin siRNA for 3 days and then further cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. E-cadherin and phosphorylated RPS6 were analyzed by Western blotting.
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    Millipore anti glyceraldehyde 3 phosphate dehydrogenase
    Extracellular (secreted) <t>GAPDH</t> bound to E-cadherin. ( A ) MKN-7 cells were cultured with human erythrocyte GAPDH at 5 U/mL for 1 day. The cells were fixed under nonpermeabilizing conditions, stained with the indicated antibodies and analyzed by confocal microscopy. Scale bar is 50 μm. ( B ) Cell membranes of MKN-7 cells were incubated with <t>FLAG-tagged</t> human recombinant wtGAPDH or human erythrocyte GAPDH. The immunoprecipitates generated with the indicated antibodies were analyzed by Western blotting with anti-E-cadherin antibody. ( C ) Human erythrocyte GAPDH was added to a human recombinant E-cadherin-coated plate. GAPDH bound to the plate was detected by Western blot. ( D ) MKN-7 and MKN-74 cells were cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. The mTOR-p70S6K pathway was analyzed by Western blot. ( E ) MKN-7 cells were transfected with control siRNA or E-cadherin siRNA for 3 days and then further cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. E-cadherin and phosphorylated RPS6 were analyzed by Western blotting.
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    Image Search Results


    Effects of ethanol and androgenization on profibrotic gene expression. Quantitative Real-Time PCR analysis of Interleukin-6 (IL-6) (black bar) and collagen Type 3 (COL3α1) (striped bar) gene expression in control (Ctrl), androgenized (Andro) and Andro + estrogen (Andro + E2) animals maintained on control Lieber-DeCarli (C-LDC) or ethanol-LDC (E-LDC) diet. Gene expression was normalized to glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Data are presented as mean values ± SEM. *P

    Journal: PLoS ONE

    Article Title: Neonatal Androgenization Exacerbates Alcohol-Induced Liver Injury in Adult Rats, an Effect Abrogated by Estrogen

    doi: 10.1371/journal.pone.0029463

    Figure Lengend Snippet: Effects of ethanol and androgenization on profibrotic gene expression. Quantitative Real-Time PCR analysis of Interleukin-6 (IL-6) (black bar) and collagen Type 3 (COL3α1) (striped bar) gene expression in control (Ctrl), androgenized (Andro) and Andro + estrogen (Andro + E2) animals maintained on control Lieber-DeCarli (C-LDC) or ethanol-LDC (E-LDC) diet. Gene expression was normalized to glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Data are presented as mean values ± SEM. *P

    Article Snippet: For Western blot analyses, antibodies against cytochrome P450 2E1 (CYP2E1), cytochrome P450 1A2 (CYP1A2) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were purchased from Millipore (Billerica, MA).

    Techniques: Expressing, Real-time Polymerase Chain Reaction

    VP4 is concentrated along the nuclear envelope. (A) Cos7 cells were transiently transfected with either empty vector (−) or VP4 (+) in the presence of the tetracycline repressor. Tetracycline was added for the indicated times. Whole-cell lysates were immunoblotted with antisera against myc to detect VP4 or the loading control GAPDH. (B) Confocal immunofluorescence microscopy localization of VP4 in Cos7 cells was determined after 6 h of induction. Samples were labeled with myc (VP4-myc), ERp57, emerin, or lamin antisera and stained with either Hoechst or DAPI (DAPI, 4′,6-diamidino-2-phenylindole) as indicated. A fraction of the VP4-expressing cells displayed profound nuclear envelope disruption, as displayed in the lamin lower panel. Bars, 10 μm.

    Journal: Journal of Virology

    Article Title: The Simian Virus 40 Late Viral Protein VP4 Disrupts the Nuclear Envelope for Viral Release

    doi: 10.1128/JVI.07047-11

    Figure Lengend Snippet: VP4 is concentrated along the nuclear envelope. (A) Cos7 cells were transiently transfected with either empty vector (−) or VP4 (+) in the presence of the tetracycline repressor. Tetracycline was added for the indicated times. Whole-cell lysates were immunoblotted with antisera against myc to detect VP4 or the loading control GAPDH. (B) Confocal immunofluorescence microscopy localization of VP4 in Cos7 cells was determined after 6 h of induction. Samples were labeled with myc (VP4-myc), ERp57, emerin, or lamin antisera and stained with either Hoechst or DAPI (DAPI, 4′,6-diamidino-2-phenylindole) as indicated. A fraction of the VP4-expressing cells displayed profound nuclear envelope disruption, as displayed in the lamin lower panel. Bars, 10 μm.

    Article Snippet: The following antibodies were obtained as indicated: myc, lamin A/C, and emerin (Cell Signaling, Danvers, MA); GAPDH (glyceraldehyde-3-phosphate dehydrogenase; Millipore, Billerica, MA); VP1 and VP2/3 (Abcam, Cambridge, MA; VP2/3 was also obtained from A. Oppenheim, Jerusalem, Israel); calnexin (Enzo Life Sciences Inc., Ann Arbor, MI); large T antigen (LT; Merck KGaA, Darmstadt, Germany); and glutathione S -transferase (GST; Abmart, Arlington, MA).

    Techniques: Transfection, Plasmid Preparation, Immunofluorescence, Microscopy, Labeling, Staining, Expressing

    Expression of TMEM106B in different cell types. ( A ) Cell lysates from HEK293T, NSC-34 and BV-2 were loaded and blotted with anti-TMEM106B and anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibodies. ( B ) TMEM106B forms homodimers. FLAG-tagged

    Journal: Human Molecular Genetics

    Article Title: The frontotemporal lobar degeneration risk factor, TMEM106B, regulates lysosomal morphology and function

    doi: 10.1093/hmg/dds475

    Figure Lengend Snippet: Expression of TMEM106B in different cell types. ( A ) Cell lysates from HEK293T, NSC-34 and BV-2 were loaded and blotted with anti-TMEM106B and anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibodies. ( B ) TMEM106B forms homodimers. FLAG-tagged

    Article Snippet: The following antibodies were used in the study: sheep anti-mouse PGRN antibodies, goat anti-human PGRN antibodies and goat anti-mouse sortilin from R & D systems; mouse anti-myc (9E10) and anti-FLAG (M2) antibodies from Sigma-Aldrich; mouse anti-LAMP1 and EEA1 antibodies from BD biosciences; rabbit anti-EGFR, rabbit anti-phospho-Erk1/2 and rabbit anti-cleaved caspase 3 antibodies from Cell Signaling; rat anti-mouse LAMP1 (1D4B) antibodies from BioLegend; rabbit anti-TDP 43 antibodies from Proteintech; and mouse anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibodies from Millipore.

    Techniques: Expressing

    Modified microparticles can deliver functional peroxisome proliferator-activated receptor-γ (PPARγ) to target cells. THP-1 cells were cultured for 24 h with no microparticles (No MP) or Meg-01 culture-derived green fluorescent protein (GFP)-positive microparticles (GFP MP) or PPARγ-overexpressing microparticles (PPARγ MP), in the presence of 0, 10, 100 or 1000 nM rosiglitazone alone (A), or with 10 μM GW9662 (B). Quantitative real-time PCR of mRNA was performed, and starting quantities of fatty acid-binding protein 4 (FABP4) were normalized to glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and then subtracted from the value for the 0 nM concentration of each microparticle treatment group. Values were compared by use of two-way ANOVA and the Bonferroni post test. * P

    Journal: Journal of thrombosis and haemostasis : JTH

    Article Title: A novel method for overexpression of peroxisome proliferator-activated receptor-? in megakaryocyte and platelet microparticles achieves transcellular signaling

    doi: 10.1111/jth.12017

    Figure Lengend Snippet: Modified microparticles can deliver functional peroxisome proliferator-activated receptor-γ (PPARγ) to target cells. THP-1 cells were cultured for 24 h with no microparticles (No MP) or Meg-01 culture-derived green fluorescent protein (GFP)-positive microparticles (GFP MP) or PPARγ-overexpressing microparticles (PPARγ MP), in the presence of 0, 10, 100 or 1000 nM rosiglitazone alone (A), or with 10 μM GW9662 (B). Quantitative real-time PCR of mRNA was performed, and starting quantities of fatty acid-binding protein 4 (FABP4) were normalized to glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and then subtracted from the value for the 0 nM concentration of each microparticle treatment group. Values were compared by use of two-way ANOVA and the Bonferroni post test. * P

    Article Snippet: The primary antibodies used for this work were as follows: rabbit anti-human peroxisome proliferator-activated receptor-γ (PPARγ) (Cell Signaling Technology, Boston, MA, USA), mouse anti-Flag (Clonetech Laboratories, Mountain View, CA, USA), mouse anti-human actin, and mouse anti-human glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (Calbiochem, Darmstadt, Germany).

    Techniques: Modification, Functional Assay, Cell Culture, Derivative Assay, Real-time Polymerase Chain Reaction, Binding Assay, Concentration Assay

    Protein quantity and quality of buffered ethanol 70% (BE70) fixative. (A) Amount of protein extracted from each condition was measured using the bicinchoninic acid (BCA) Protein Assay Kit. The protein extraction yield was expressed as the mean of three replicated samples (mean ± SD). (B) Protein integrity of different fixative solutions was assessed by western blotting. Proteins extracted from different fixative solutions were separated by 4% to 12% reducing sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE), electroblotted to nitrocellulose membrane, and probed with anti-aquaporin 1 (AQP1; 1:1000). (C) Western blotting by anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibody. Relative GAPDH signal of each entity was normalized to neutral-buffered formalin (NBF). Abbreviations: E, 70% ethanol.

    Journal: Journal of Histochemistry and Cytochemistry

    Article Title: A Buffered Alcohol-Based Fixative for Histomorphologic and Molecular Applications

    doi: 10.1369/0022155416649579

    Figure Lengend Snippet: Protein quantity and quality of buffered ethanol 70% (BE70) fixative. (A) Amount of protein extracted from each condition was measured using the bicinchoninic acid (BCA) Protein Assay Kit. The protein extraction yield was expressed as the mean of three replicated samples (mean ± SD). (B) Protein integrity of different fixative solutions was assessed by western blotting. Proteins extracted from different fixative solutions were separated by 4% to 12% reducing sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE), electroblotted to nitrocellulose membrane, and probed with anti-aquaporin 1 (AQP1; 1:1000). (C) Western blotting by anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibody. Relative GAPDH signal of each entity was normalized to neutral-buffered formalin (NBF). Abbreviations: E, 70% ethanol.

    Article Snippet: The membranes were blocked with 5% nonfat dry milk in Tris-buffered saline with Tween (TBST; 50 mM Tris, pH 7.5, 150 mM NaCl, and 0.05% Tween-20) for 1 hr, washed, and incubated overnight at 4C in TBST with rabbit anti-AQP1 polyclonal antibody (Cat. No. sc-20810; dilution 1:100; Santa Cruz Biotechnology, Dallas, TA) and mouse anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) monoclonal antibody (clone 6C5; dilution 1:3000; Calbiochem, Gibbstown, NJ).

    Techniques: BIA-KA, Protein Extraction, Western Blot, Polyacrylamide Gel Electrophoresis, SDS Page

    Spinal Tyr1472 and Ser1303 phosphorylation of N-methyl-D-aspartate (NMDA) receptor NR2B subunit at day 28 after spinal cord injury (SCI) in wild type (WT) and sigma-1 receptor (σ1R) knockout (KO) mice. ( A ) Quantification and representative immunoblots of total NR2B, pS1303NR2B and glyceraldehyde 3-phosphate dehydrogenase (GAPDH). ( B ) Quantification and representative immunoblots of total NR2B, pY1472NR2B and GAPDH. a–b: groups not sharing a letter are significantly different, p

    Journal: Scientific Reports

    Article Title: Critical role of sigma-1 receptors in central neuropathic pain-related behaviours after mild spinal cord injury in mice

    doi: 10.1038/s41598-018-22217-9

    Figure Lengend Snippet: Spinal Tyr1472 and Ser1303 phosphorylation of N-methyl-D-aspartate (NMDA) receptor NR2B subunit at day 28 after spinal cord injury (SCI) in wild type (WT) and sigma-1 receptor (σ1R) knockout (KO) mice. ( A ) Quantification and representative immunoblots of total NR2B, pS1303NR2B and glyceraldehyde 3-phosphate dehydrogenase (GAPDH). ( B ) Quantification and representative immunoblots of total NR2B, pY1472NR2B and GAPDH. a–b: groups not sharing a letter are significantly different, p

    Article Snippet: To ensure equal protein loading, rabbit anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibody (1:40,000, Sigma-Aldrich Quimica S.A.) was used as a loading control.

    Techniques: Knock-Out, Mouse Assay, Western Blot

    Spinal ERK1/2 phosphorylation (pERK) expression at day 28 after spinal cord injury (SCI) in wild type (WT) and sigma-1 receptor (σ1R) knockout (KO) mice. Quantification and representative immunoblots of total ERK, pERK and glyceraldehyde 3-phosphate dehydrogenase (GAPDH). Protein expressions were normalized to GAPDH and data is presented as a percentage respect to WT naïve or KO naïve mice (mean ± standard error of the mean; n = 5–6). a–b: groups not sharing a letter are significantly different, p

    Journal: Scientific Reports

    Article Title: Critical role of sigma-1 receptors in central neuropathic pain-related behaviours after mild spinal cord injury in mice

    doi: 10.1038/s41598-018-22217-9

    Figure Lengend Snippet: Spinal ERK1/2 phosphorylation (pERK) expression at day 28 after spinal cord injury (SCI) in wild type (WT) and sigma-1 receptor (σ1R) knockout (KO) mice. Quantification and representative immunoblots of total ERK, pERK and glyceraldehyde 3-phosphate dehydrogenase (GAPDH). Protein expressions were normalized to GAPDH and data is presented as a percentage respect to WT naïve or KO naïve mice (mean ± standard error of the mean; n = 5–6). a–b: groups not sharing a letter are significantly different, p

    Article Snippet: To ensure equal protein loading, rabbit anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibody (1:40,000, Sigma-Aldrich Quimica S.A.) was used as a loading control.

    Techniques: Expressing, Knock-Out, Mouse Assay, Western Blot

    Spinal inflammatory cytokines (tumour necrosis factor [TNF]-α and interleukin[IL]-1β) expression at day 28 after spinal cord injury (SCI) in wild type (WT) and sigma-1 receptor knockout (KO). ( A ) Quantification and representative immunoblots of TNF-α and glyceraldehyde 3-phosphate dehydrogenase (GAPDH). a–b: groups not sharing a letter are significantly different, p

    Journal: Scientific Reports

    Article Title: Critical role of sigma-1 receptors in central neuropathic pain-related behaviours after mild spinal cord injury in mice

    doi: 10.1038/s41598-018-22217-9

    Figure Lengend Snippet: Spinal inflammatory cytokines (tumour necrosis factor [TNF]-α and interleukin[IL]-1β) expression at day 28 after spinal cord injury (SCI) in wild type (WT) and sigma-1 receptor knockout (KO). ( A ) Quantification and representative immunoblots of TNF-α and glyceraldehyde 3-phosphate dehydrogenase (GAPDH). a–b: groups not sharing a letter are significantly different, p

    Article Snippet: To ensure equal protein loading, rabbit anti-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) antibody (1:40,000, Sigma-Aldrich Quimica S.A.) was used as a loading control.

    Techniques: Expressing, Knock-Out, Western Blot

    Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an internal control.

    Journal: PPAR Research

    Article Title: HDAC Inhibition Modulates Cardiac PPARs and Fatty Acid Metabolism in Diabetic Cardiomyopathy

    doi: 10.1155/2016/5938740

    Figure Lengend Snippet: Cardiac fatty acid metabolic proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Representative immunoblots and average data of (a) ratio of phosphorylated 5′ adenosine monophosphate-activated protein kinase 2 α (pAMPK2 α ) to total AMPK2 α , (b) peroxisome proliferator-activated receptor- (PPAR-) γ coactivator- (PGC-) 1 α , (c) phosphorylated acetyl coenzyme A carboxylase (pACC), (d) cluster of differentiation 36 (CD36), (e) diacylglycerol acyltransferase 1 (DGAT1), and (f) DGAT2 from control ( n = 4), DM ( n = 4), and DM + MPT0E014 ( n = 4) rats. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an internal control.

    Article Snippet: Targeted bands were normalized to cardiac glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (Sigma-Aldrich) to confirm equal protein loading.

    Techniques: Western Blot, Pyrolysis Gas Chromatography

    Cardiac peroxisome proliferator-activated receptor (PPAR) proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Cardiac PPAR- α and PPAR- δ protein expressions significantly decreased in DM ( n = 4) compared to control ( n = 4) and DM + MPT0E014 ( n = 4) rats. Cardiac PPAR- γ protein expressions were enhanced in DM ( n = 4) compared to control ( n = 4) and DM + MPT0E014 ( n = 4) rats. Representative immunoblots and average data of (a) PPAR- α , (b) PPAR- γ , and (c) PPAR- δ in different groups. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an internal control.

    Journal: PPAR Research

    Article Title: HDAC Inhibition Modulates Cardiac PPARs and Fatty Acid Metabolism in Diabetic Cardiomyopathy

    doi: 10.1155/2016/5938740

    Figure Lengend Snippet: Cardiac peroxisome proliferator-activated receptor (PPAR) proteins in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Cardiac PPAR- α and PPAR- δ protein expressions significantly decreased in DM ( n = 4) compared to control ( n = 4) and DM + MPT0E014 ( n = 4) rats. Cardiac PPAR- γ protein expressions were enhanced in DM ( n = 4) compared to control ( n = 4) and DM + MPT0E014 ( n = 4) rats. Representative immunoblots and average data of (a) PPAR- α , (b) PPAR- γ , and (c) PPAR- δ in different groups. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an internal control.

    Article Snippet: Targeted bands were normalized to cardiac glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (Sigma-Aldrich) to confirm equal protein loading.

    Techniques: Western Blot

    Cardiac inflammatory proteins and ratio of phosphorylated Akt to total Akt in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Cardiac tumor necrosis factor- (TNF-) α and interleukin- (IL-) 6 protein levels were significantly higher in DM rats ( n = 4) compared to control ( n = 4) and DM + MPT0E014 ( n = 4) rats. Representative immunoblots and average data of (a) TNF- α , (b) IL-6, and (c) ratio of pAkt to total Akt in different groups. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an internal control.

    Journal: PPAR Research

    Article Title: HDAC Inhibition Modulates Cardiac PPARs and Fatty Acid Metabolism in Diabetic Cardiomyopathy

    doi: 10.1155/2016/5938740

    Figure Lengend Snippet: Cardiac inflammatory proteins and ratio of phosphorylated Akt to total Akt in control, diabetes mellitus (DM), and MPT0E014-treated DM (DM + MPT0E014) rats. Cardiac tumor necrosis factor- (TNF-) α and interleukin- (IL-) 6 protein levels were significantly higher in DM rats ( n = 4) compared to control ( n = 4) and DM + MPT0E014 ( n = 4) rats. Representative immunoblots and average data of (a) TNF- α , (b) IL-6, and (c) ratio of pAkt to total Akt in different groups. Densitometry was normalized to glyceraldehyde 3-phosphate dehydrogenase (GAPDH) as an internal control.

    Article Snippet: Targeted bands were normalized to cardiac glyceraldehyde 3-phosphate dehydrogenase (GAPDH) (Sigma-Aldrich) to confirm equal protein loading.

    Techniques: Western Blot

    Extracellular (secreted) GAPDH bound to E-cadherin. ( A ) MKN-7 cells were cultured with human erythrocyte GAPDH at 5 U/mL for 1 day. The cells were fixed under nonpermeabilizing conditions, stained with the indicated antibodies and analyzed by confocal microscopy. Scale bar is 50 μm. ( B ) Cell membranes of MKN-7 cells were incubated with FLAG-tagged human recombinant wtGAPDH or human erythrocyte GAPDH. The immunoprecipitates generated with the indicated antibodies were analyzed by Western blotting with anti-E-cadherin antibody. ( C ) Human erythrocyte GAPDH was added to a human recombinant E-cadherin-coated plate. GAPDH bound to the plate was detected by Western blot. ( D ) MKN-7 and MKN-74 cells were cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. The mTOR-p70S6K pathway was analyzed by Western blot. ( E ) MKN-7 cells were transfected with control siRNA or E-cadherin siRNA for 3 days and then further cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. E-cadherin and phosphorylated RPS6 were analyzed by Western blotting.

    Journal: PLoS ONE

    Article Title: Stromal Cells Positively and Negatively Modulate the Growth of Cancer Cells: Stimulation via the PGE2-TNFα-IL-6 Pathway and Inhibition via Secreted GAPDH-E-Cadherin Interaction

    doi: 10.1371/journal.pone.0119415

    Figure Lengend Snippet: Extracellular (secreted) GAPDH bound to E-cadherin. ( A ) MKN-7 cells were cultured with human erythrocyte GAPDH at 5 U/mL for 1 day. The cells were fixed under nonpermeabilizing conditions, stained with the indicated antibodies and analyzed by confocal microscopy. Scale bar is 50 μm. ( B ) Cell membranes of MKN-7 cells were incubated with FLAG-tagged human recombinant wtGAPDH or human erythrocyte GAPDH. The immunoprecipitates generated with the indicated antibodies were analyzed by Western blotting with anti-E-cadherin antibody. ( C ) Human erythrocyte GAPDH was added to a human recombinant E-cadherin-coated plate. GAPDH bound to the plate was detected by Western blot. ( D ) MKN-7 and MKN-74 cells were cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. The mTOR-p70S6K pathway was analyzed by Western blot. ( E ) MKN-7 cells were transfected with control siRNA or E-cadherin siRNA for 3 days and then further cultured with human erythrocyte GAPDH at 5 U/mL or anti-E-cadherin antibody at 1 μg/mL for 1 day. E-cadherin and phosphorylated RPS6 were analyzed by Western blotting.

    Article Snippet: Anti-vimentin (V2258), anti- SM-α-actin (A2547), anti-α-tubulin (T9026), anti-phospho-(tyr705)-STAT3 (SAB4300033), anti-RPL-18A (HPA055259), and anti-FLAG M2 (F3165) antibodies, rabbit muscle GAPDH (G2267) and human erythrocyte GAPDH (G6019) were purchased from Sigma.

    Techniques: Cell Culture, Staining, Confocal Microscopy, Incubation, Recombinant, Generated, Western Blot, Transfection