tris-glycine gel Search Results


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  • 95
    Millipore tris glycine buffer
    Effect of CTAB on the dilution of <t>SDS–BSA</t> complex. The inset shows the fluorescence profile of the protein after subtracting the background SDS fluorescence. Conditions: 15 m M SDS, 1× <t>Tris–glycine</t> buffer at 8.6 pH, 5× sypro
    Tris Glycine Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 95/100, based on 219 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher tris glycine protein gels
    Effect of CTAB on the dilution of <t>SDS–BSA</t> complex. The inset shows the fluorescence profile of the protein after subtracting the background SDS fluorescence. Conditions: 15 m M SDS, 1× <t>Tris–glycine</t> buffer at 8.6 pH, 5× sypro
    Tris Glycine Protein Gels, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 84 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad tris glycine gels
    Effect of AO-11 and AO-15 on the in vitro polymerization of the Aβ 42 peptide. (A) Image of Aβ 42 incubated for 0 or 24 hours in the presence of DMSO, or for 24 hours in the presence of 50 μM AO-11 or AO-15. A small aliquot was applied to formvar/carbon-coated copper grids and stained with 4% (w/v) aqueous uranyl acetate grids for EM analysis. The images are representative of at least three independent experiments. (B) Western blot analysis of <t>SDS-PAGE</t> performed on parallel samples used in A. A sample of each Aβ 42 reaction (calculated to be 10 μg) was separated on a 4–20% <t>Tris-Glycine</t> SDS-PAGE gel and probed with monoclonal anti-Aβ antibody (6E10).
    Tris Glycine Gels, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 1155 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher tris glycine gel
    RNAP containing βG1249D generates holoenzyme with AsiA/σD581BpA, but is defective in generating the crosslink with β’. ( A ) Native <t>Tris-glycine</t> gel. Solutions were assembled with the indicated components. The positions of AsiA, RNAP core, AsiA-RNAP holoenzyme, and σD581BpA are marked. (The bands that migrate faster than AsiA seen in lane 1 are trace contaminants present in the σD581BpA preparation.) ( B ) SDS-PAGE gel showing the products obtained after <t>photocrosslinking.</t> Arrow points to the crosslink between σD581BpA and β’ 80 HRGVICEK 87 identified in Figure 3 .
    Tris Glycine Gel, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 3809 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher tris glycine gels
    Protein profile of NL4-3 and NL4-3/ΔRT virions. Virions purified by ultracentrifugation were used to extract proteins and separated in a gradient 4-12% <t>Tris-Glycine</t> gel. An <t>anti-p24</t> monoclonal antibody was used to study the processing profile of Gag in NL4-3/ΔRT and NL4-3 virions. There is a weaker processing of Gag in NL4-3/ΔRT virions, represented by an increase in p55- gag and MA-CA p41 forms in detriment of CA p24. At the same, an increase in intermediate forms is also shown in NL4-3/ΔRT virions.
    Tris Glycine Gels, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 5559 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher precise tris glycine gels
    Protein profile of NL4-3 and NL4-3/ΔRT virions. Virions purified by ultracentrifugation were used to extract proteins and separated in a gradient 4-12% <t>Tris-Glycine</t> gel. An <t>anti-p24</t> monoclonal antibody was used to study the processing profile of Gag in NL4-3/ΔRT and NL4-3 virions. There is a weaker processing of Gag in NL4-3/ΔRT virions, represented by an increase in p55- gag and MA-CA p41 forms in detriment of CA p24. At the same, an increase in intermediate forms is also shown in NL4-3/ΔRT virions.
    Precise Tris Glycine Gels, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Lonza tris glycine gels
    Protein profile of NL4-3 and NL4-3/ΔRT virions. Virions purified by ultracentrifugation were used to extract proteins and separated in a gradient 4-12% <t>Tris-Glycine</t> gel. An <t>anti-p24</t> monoclonal antibody was used to study the processing profile of Gag in NL4-3/ΔRT and NL4-3 virions. There is a weaker processing of Gag in NL4-3/ΔRT virions, represented by an increase in p55- gag and MA-CA p41 forms in detriment of CA p24. At the same, an increase in intermediate forms is also shown in NL4-3/ΔRT virions.
    Tris Glycine Gels, supplied by Lonza, used in various techniques. Bioz Stars score: 95/100, based on 146 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Bio-Rad tris glycine gel
    Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% <t>Tris-glycine</t> gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 <t>kDa</t> (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p
    Tris Glycine Gel, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 966 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    GenScript tris glycine gel
    Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% <t>Tris-glycine</t> gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 <t>kDa</t> (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p
    Tris Glycine Gel, supplied by GenScript, used in various techniques. Bioz Stars score: 95/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Cambrex tris glycine gels
    Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% <t>Tris-glycine</t> gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 <t>kDa</t> (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p
    Tris Glycine Gels, supplied by Cambrex, used in various techniques. Bioz Stars score: 91/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Becton Dickinson tris glycine gel
    Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% <t>Tris-glycine</t> gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 <t>kDa</t> (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p
    Tris Glycine Gel, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 91/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Cambrex tris glycine gel
    Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% <t>Tris-glycine</t> gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 <t>kDa</t> (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p
    Tris Glycine Gel, supplied by Cambrex, used in various techniques. Bioz Stars score: 91/100, based on 40 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    NuSep tris glycine gel
    Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% <t>Tris-glycine</t> gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 <t>kDa</t> (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p
    Tris Glycine Gel, supplied by NuSep, used in various techniques. Bioz Stars score: 91/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Millipore tris glycine gels
    Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% <t>Tris-glycine</t> gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 <t>kDa</t> (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p
    Tris Glycine Gels, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 398 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Lonza tris glycine gel
    Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% <t>Tris-glycine</t> gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 <t>kDa</t> (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p
    Tris Glycine Gel, supplied by Lonza, used in various techniques. Bioz Stars score: 91/100, based on 50 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    NuSep tris glycine gels
    Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% <t>Tris-glycine</t> gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 <t>kDa</t> (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p
    Tris Glycine Gels, supplied by NuSep, used in various techniques. Bioz Stars score: 91/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Beyotime tris glycine gels
    Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% <t>Tris-glycine</t> gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 <t>kDa</t> (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p
    Tris Glycine Gels, supplied by Beyotime, used in various techniques. Bioz Stars score: 91/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Koma Biotech tris glycine gel
    Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% <t>Tris-glycine</t> gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 <t>kDa</t> (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p
    Tris Glycine Gel, supplied by Koma Biotech, used in various techniques. Bioz Stars score: 91/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher tris glycine gradient gels
    Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% <t>Tris-glycine</t> gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 <t>kDa</t> (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p
    Tris Glycine Gradient Gels, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 479 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Thermo Fisher tris glycine precast gel
    Western blot analysis of the expression of the R. rickettsii signal peptidase I in E. coli strain IT41. Total proteins from the E. coli cells carrying pTrcHisRR4 or pTrcHisC plasmids, separated on 4 to 12% <t>Tris-glycine</t> precast gel, <t>1×</t> Tris-glycine-SDS running buffer, transferred to polyvinylidene difluoride membrane was probed with His-Tag monoclonal antibodies by using a WesternBreeze chromogenic immunodetection kit. Lane 1, total proteins from E. coli IT41/pTrcHisRR4; lane 2, total proteins from E. coli IT41/pTrcHisC; and lane 3, total proteins from E. coli IT41. Lane M, Bio-Rad Kaleidoscope prestained markers (carbonic anhydrase, 39.7 kDa; soybean trypsin inhibitor, 32.1 kDa).
    Tris Glycine Precast Gel, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 87/100, based on 74 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Thermo Fisher tris glycine denaturing gel
    Western blot analysis of the expression of the R. rickettsii signal peptidase I in E. coli strain IT41. Total proteins from the E. coli cells carrying pTrcHisRR4 or pTrcHisC plasmids, separated on 4 to 12% <t>Tris-glycine</t> precast gel, <t>1×</t> Tris-glycine-SDS running buffer, transferred to polyvinylidene difluoride membrane was probed with His-Tag monoclonal antibodies by using a WesternBreeze chromogenic immunodetection kit. Lane 1, total proteins from E. coli IT41/pTrcHisRR4; lane 2, total proteins from E. coli IT41/pTrcHisC; and lane 3, total proteins from E. coli IT41. Lane M, Bio-Rad Kaleidoscope prestained markers (carbonic anhydrase, 39.7 kDa; soybean trypsin inhibitor, 32.1 kDa).
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    Thermo Fisher acrylamide tris glycine gel
    Western blot analysis of the expression of the R. rickettsii signal peptidase I in E. coli strain IT41. Total proteins from the E. coli cells carrying pTrcHisRR4 or pTrcHisC plasmids, separated on 4 to 12% <t>Tris-glycine</t> precast gel, <t>1×</t> Tris-glycine-SDS running buffer, transferred to polyvinylidene difluoride membrane was probed with His-Tag monoclonal antibodies by using a WesternBreeze chromogenic immunodetection kit. Lane 1, total proteins from E. coli IT41/pTrcHisRR4; lane 2, total proteins from E. coli IT41/pTrcHisC; and lane 3, total proteins from E. coli IT41. Lane M, Bio-Rad Kaleidoscope prestained markers (carbonic anhydrase, 39.7 kDa; soybean trypsin inhibitor, 32.1 kDa).
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    Thermo Fisher gradient tris glycine gel
    Western blot analysis of the expression of the R. rickettsii signal peptidase I in E. coli strain IT41. Total proteins from the E. coli cells carrying pTrcHisRR4 or pTrcHisC plasmids, separated on 4 to 12% <t>Tris-glycine</t> precast gel, <t>1×</t> Tris-glycine-SDS running buffer, transferred to polyvinylidene difluoride membrane was probed with His-Tag monoclonal antibodies by using a WesternBreeze chromogenic immunodetection kit. Lane 1, total proteins from E. coli IT41/pTrcHisRR4; lane 2, total proteins from E. coli IT41/pTrcHisC; and lane 3, total proteins from E. coli IT41. Lane M, Bio-Rad Kaleidoscope prestained markers (carbonic anhydrase, 39.7 kDa; soybean trypsin inhibitor, 32.1 kDa).
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    Bio-Rad gradient tris glycine gel
    Western blot analysis of the expression of the R. rickettsii signal peptidase I in E. coli strain IT41. Total proteins from the E. coli cells carrying pTrcHisRR4 or pTrcHisC plasmids, separated on 4 to 12% <t>Tris-glycine</t> precast gel, <t>1×</t> Tris-glycine-SDS running buffer, transferred to polyvinylidene difluoride membrane was probed with His-Tag monoclonal antibodies by using a WesternBreeze chromogenic immunodetection kit. Lane 1, total proteins from E. coli IT41/pTrcHisRR4; lane 2, total proteins from E. coli IT41/pTrcHisC; and lane 3, total proteins from E. coli IT41. Lane M, Bio-Rad Kaleidoscope prestained markers (carbonic anhydrase, 39.7 kDa; soybean trypsin inhibitor, 32.1 kDa).
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    NuSep tris glycine gradient gel
    Western blot analysis of the expression of the R. rickettsii signal peptidase I in E. coli strain IT41. Total proteins from the E. coli cells carrying pTrcHisRR4 or pTrcHisC plasmids, separated on 4 to 12% <t>Tris-glycine</t> precast gel, <t>1×</t> Tris-glycine-SDS running buffer, transferred to polyvinylidene difluoride membrane was probed with His-Tag monoclonal antibodies by using a WesternBreeze chromogenic immunodetection kit. Lane 1, total proteins from E. coli IT41/pTrcHisRR4; lane 2, total proteins from E. coli IT41/pTrcHisC; and lane 3, total proteins from E. coli IT41. Lane M, Bio-Rad Kaleidoscope prestained markers (carbonic anhydrase, 39.7 kDa; soybean trypsin inhibitor, 32.1 kDa).
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    Lonza gradient tris glycine gels
    Western blot analysis of the expression of the R. rickettsii signal peptidase I in E. coli strain IT41. Total proteins from the E. coli cells carrying pTrcHisRR4 or pTrcHisC plasmids, separated on 4 to 12% <t>Tris-glycine</t> precast gel, <t>1×</t> Tris-glycine-SDS running buffer, transferred to polyvinylidene difluoride membrane was probed with His-Tag monoclonal antibodies by using a WesternBreeze chromogenic immunodetection kit. Lane 1, total proteins from E. coli IT41/pTrcHisRR4; lane 2, total proteins from E. coli IT41/pTrcHisC; and lane 3, total proteins from E. coli IT41. Lane M, Bio-Rad Kaleidoscope prestained markers (carbonic anhydrase, 39.7 kDa; soybean trypsin inhibitor, 32.1 kDa).
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    Thermo Fisher tris glycine nupage gel
    Western blot analysis of the expression of the R. rickettsii signal peptidase I in E. coli strain IT41. Total proteins from the E. coli cells carrying pTrcHisRR4 or pTrcHisC plasmids, separated on 4 to 12% <t>Tris-glycine</t> precast gel, <t>1×</t> Tris-glycine-SDS running buffer, transferred to polyvinylidene difluoride membrane was probed with His-Tag monoclonal antibodies by using a WesternBreeze chromogenic immunodetection kit. Lane 1, total proteins from E. coli IT41/pTrcHisRR4; lane 2, total proteins from E. coli IT41/pTrcHisC; and lane 3, total proteins from E. coli IT41. Lane M, Bio-Rad Kaleidoscope prestained markers (carbonic anhydrase, 39.7 kDa; soybean trypsin inhibitor, 32.1 kDa).
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    Cambrex tris glycine precast gel
    Western blot analysis of the expression of the R. rickettsii signal peptidase I in E. coli strain IT41. Total proteins from the E. coli cells carrying pTrcHisRR4 or pTrcHisC plasmids, separated on 4 to 12% <t>Tris-glycine</t> precast gel, <t>1×</t> Tris-glycine-SDS running buffer, transferred to polyvinylidene difluoride membrane was probed with His-Tag monoclonal antibodies by using a WesternBreeze chromogenic immunodetection kit. Lane 1, total proteins from E. coli IT41/pTrcHisRR4; lane 2, total proteins from E. coli IT41/pTrcHisC; and lane 3, total proteins from E. coli IT41. Lane M, Bio-Rad Kaleidoscope prestained markers (carbonic anhydrase, 39.7 kDa; soybean trypsin inhibitor, 32.1 kDa).
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    Fisher Scientific precast tris glycine gels
    Western blot analysis of the expression of the R. rickettsii signal peptidase I in E. coli strain IT41. Total proteins from the E. coli cells carrying pTrcHisRR4 or pTrcHisC plasmids, separated on 4 to 12% <t>Tris-glycine</t> precast gel, <t>1×</t> Tris-glycine-SDS running buffer, transferred to polyvinylidene difluoride membrane was probed with His-Tag monoclonal antibodies by using a WesternBreeze chromogenic immunodetection kit. Lane 1, total proteins from E. coli IT41/pTrcHisRR4; lane 2, total proteins from E. coli IT41/pTrcHisC; and lane 3, total proteins from E. coli IT41. Lane M, Bio-Rad Kaleidoscope prestained markers (carbonic anhydrase, 39.7 kDa; soybean trypsin inhibitor, 32.1 kDa).
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    Bio-Rad tris glycine precast gel
    Western blot analysis of the expression of the R. rickettsii signal peptidase I in E. coli strain IT41. Total proteins from the E. coli cells carrying pTrcHisRR4 or pTrcHisC plasmids, separated on 4 to 12% <t>Tris-glycine</t> precast gel, <t>1×</t> Tris-glycine-SDS running buffer, transferred to polyvinylidene difluoride membrane was probed with His-Tag monoclonal antibodies by using a WesternBreeze chromogenic immunodetection kit. Lane 1, total proteins from E. coli IT41/pTrcHisRR4; lane 2, total proteins from E. coli IT41/pTrcHisC; and lane 3, total proteins from E. coli IT41. Lane M, Bio-Rad Kaleidoscope prestained markers (carbonic anhydrase, 39.7 kDa; soybean trypsin inhibitor, 32.1 kDa).
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    Image Search Results


    Effect of CTAB on the dilution of SDS–BSA complex. The inset shows the fluorescence profile of the protein after subtracting the background SDS fluorescence. Conditions: 15 m M SDS, 1× Tris–glycine buffer at 8.6 pH, 5× sypro

    Journal: Protein Science : A Publication of the Protein Society

    Article Title: Dilution of protein-surfactant complexes: A fluorescence study

    doi: 10.1002/pro.2313

    Figure Lengend Snippet: Effect of CTAB on the dilution of SDS–BSA complex. The inset shows the fluorescence profile of the protein after subtracting the background SDS fluorescence. Conditions: 15 m M SDS, 1× Tris–glycine buffer at 8.6 pH, 5× sypro

    Article Snippet: Bovine serum albumin (BSA, 66 kDa), beta-galactosidase from E. coli (betagal, 465 kDa), carbonic anhydrase from bovine erythrocytes (CA, 28 kDa), sodium dodecyl sulfate (SDS), hexadecyl trimethyl ammonium bromide (CTAB), beta-mercaptoethanol (DTT), and Tris–Glycine buffer were obtained from Sigma (St. Louis, MO).

    Techniques: Fluorescence

    Effect of protein concentration on the dilution of SDS–BSA complex. The inset shows the fluorescence profile of the protein after subtracting the background SDS fluorescence. Conditions: 15 m M SDS, 1× Tris–glycine buffer at 8.6

    Journal: Protein Science : A Publication of the Protein Society

    Article Title: Dilution of protein-surfactant complexes: A fluorescence study

    doi: 10.1002/pro.2313

    Figure Lengend Snippet: Effect of protein concentration on the dilution of SDS–BSA complex. The inset shows the fluorescence profile of the protein after subtracting the background SDS fluorescence. Conditions: 15 m M SDS, 1× Tris–glycine buffer at 8.6

    Article Snippet: Bovine serum albumin (BSA, 66 kDa), beta-galactosidase from E. coli (betagal, 465 kDa), carbonic anhydrase from bovine erythrocytes (CA, 28 kDa), sodium dodecyl sulfate (SDS), hexadecyl trimethyl ammonium bromide (CTAB), beta-mercaptoethanol (DTT), and Tris–Glycine buffer were obtained from Sigma (St. Louis, MO).

    Techniques: Protein Concentration, Fluorescence

    Effect of AO-11 and AO-15 on the in vitro polymerization of the Aβ 42 peptide. (A) Image of Aβ 42 incubated for 0 or 24 hours in the presence of DMSO, or for 24 hours in the presence of 50 μM AO-11 or AO-15. A small aliquot was applied to formvar/carbon-coated copper grids and stained with 4% (w/v) aqueous uranyl acetate grids for EM analysis. The images are representative of at least three independent experiments. (B) Western blot analysis of SDS-PAGE performed on parallel samples used in A. A sample of each Aβ 42 reaction (calculated to be 10 μg) was separated on a 4–20% Tris-Glycine SDS-PAGE gel and probed with monoclonal anti-Aβ antibody (6E10).

    Journal: Disease Models & Mechanisms

    Article Title: Development and validation of a yeast high-throughput screen for inhibitors of A?42 oligomerization

    doi: 10.1242/dmm.007963

    Figure Lengend Snippet: Effect of AO-11 and AO-15 on the in vitro polymerization of the Aβ 42 peptide. (A) Image of Aβ 42 incubated for 0 or 24 hours in the presence of DMSO, or for 24 hours in the presence of 50 μM AO-11 or AO-15. A small aliquot was applied to formvar/carbon-coated copper grids and stained with 4% (w/v) aqueous uranyl acetate grids for EM analysis. The images are representative of at least three independent experiments. (B) Western blot analysis of SDS-PAGE performed on parallel samples used in A. A sample of each Aβ 42 reaction (calculated to be 10 μg) was separated on a 4–20% Tris-Glycine SDS-PAGE gel and probed with monoclonal anti-Aβ antibody (6E10).

    Article Snippet: For SDS-PAGE, lysates of late logarithmic cells grown at 30°C in 5 ml +Ade with 50 μM CuSO4 and DMSO or a compound were treated with 1% SDS for 7 minutes at room temperature, resolved on 7.5% Tris-Glycine gels (0% SDS, Bio-Rad) in 0.1% SDS containing Laemmli running buffer and transferred to a PVDF membrane (Bio-Rad) in Laemmli buffer with 0.1% SDS and 15% methanol.

    Techniques: In Vitro, Incubation, Staining, Western Blot, SDS Page

    Aβ-MRF aggregates into SDS-stable low-n oligomers in yeast. (A) Detection of Aβ-MRF by western blot analysis. Cells expressing Aβ-MRF or Aβm2-MRF were grown in the presence of DMSO control, or inhibitor candidates (100 μM of AO-11 or AO-15). The lysates were treated with SDS (1%) or without SDS for 7 minutes at room temperature and resolved with SDS-PAGE in which 0.1% SDS was included in the running buffer. Equal expression of Aβ-MRF was confirmed with boiled lysates in the presence of SDS (2%) and β-mercaptoethanol (BME). The prediction of the dimer and trimer Aβ-MRF migration position was based on the migration of the Aβ-MRF monomer (calculated molecular mass 73.7 kDa), which migrated at 95 kDa on PAGE. (B) Detection of SDS-stable Aβ-MRF assemblies. After SDS-PAGE separation of the fusion protein in lysates not treated with SDS, the gel portions marked with rectangles (1 and 2 in A), were excised, equilibrated in SDS sample buffer containing 1% SDS for 7 minutes at room temperature, loaded and resolved on a second SDS-PAGE. (C) Detection of native Aβ-MRF assemblies using blue native PAGE. Yeast lysates were prepared under non-denaturing conditions, treated with, or without, BME (0.8%) and boiled (+) or not boiled (–) before loading on a 3–12% Novex Bis-Tris blue native gel. Marked sizes in kDa were bands of NativeMark protein standards (IgM hexamer, 1236; IgM pentamer, 1048 kDa). Aβ-MRF or Aβm2-MRF were detected in A–C with anti-Sup35-RF antibodies. Each western blot shown is representative of at least three independent trials.

    Journal: Disease Models & Mechanisms

    Article Title: Development and validation of a yeast high-throughput screen for inhibitors of A?42 oligomerization

    doi: 10.1242/dmm.007963

    Figure Lengend Snippet: Aβ-MRF aggregates into SDS-stable low-n oligomers in yeast. (A) Detection of Aβ-MRF by western blot analysis. Cells expressing Aβ-MRF or Aβm2-MRF were grown in the presence of DMSO control, or inhibitor candidates (100 μM of AO-11 or AO-15). The lysates were treated with SDS (1%) or without SDS for 7 minutes at room temperature and resolved with SDS-PAGE in which 0.1% SDS was included in the running buffer. Equal expression of Aβ-MRF was confirmed with boiled lysates in the presence of SDS (2%) and β-mercaptoethanol (BME). The prediction of the dimer and trimer Aβ-MRF migration position was based on the migration of the Aβ-MRF monomer (calculated molecular mass 73.7 kDa), which migrated at 95 kDa on PAGE. (B) Detection of SDS-stable Aβ-MRF assemblies. After SDS-PAGE separation of the fusion protein in lysates not treated with SDS, the gel portions marked with rectangles (1 and 2 in A), were excised, equilibrated in SDS sample buffer containing 1% SDS for 7 minutes at room temperature, loaded and resolved on a second SDS-PAGE. (C) Detection of native Aβ-MRF assemblies using blue native PAGE. Yeast lysates were prepared under non-denaturing conditions, treated with, or without, BME (0.8%) and boiled (+) or not boiled (–) before loading on a 3–12% Novex Bis-Tris blue native gel. Marked sizes in kDa were bands of NativeMark protein standards (IgM hexamer, 1236; IgM pentamer, 1048 kDa). Aβ-MRF or Aβm2-MRF were detected in A–C with anti-Sup35-RF antibodies. Each western blot shown is representative of at least three independent trials.

    Article Snippet: For SDS-PAGE, lysates of late logarithmic cells grown at 30°C in 5 ml +Ade with 50 μM CuSO4 and DMSO or a compound were treated with 1% SDS for 7 minutes at room temperature, resolved on 7.5% Tris-Glycine gels (0% SDS, Bio-Rad) in 0.1% SDS containing Laemmli running buffer and transferred to a PVDF membrane (Bio-Rad) in Laemmli buffer with 0.1% SDS and 15% methanol.

    Techniques: Western Blot, Expressing, SDS Page, Migration, Polyacrylamide Gel Electrophoresis, Blue Native PAGE

    RNAP containing βG1249D generates holoenzyme with AsiA/σD581BpA, but is defective in generating the crosslink with β’. ( A ) Native Tris-glycine gel. Solutions were assembled with the indicated components. The positions of AsiA, RNAP core, AsiA-RNAP holoenzyme, and σD581BpA are marked. (The bands that migrate faster than AsiA seen in lane 1 are trace contaminants present in the σD581BpA preparation.) ( B ) SDS-PAGE gel showing the products obtained after photocrosslinking. Arrow points to the crosslink between σD581BpA and β’ 80 HRGVICEK 87 identified in Figure 3 .

    Journal: Nucleic Acids Research

    Article Title: Visualizing the phage T4 activated transcription complex of DNA and E. coli RNA polymerase

    doi: 10.1093/nar/gkw656

    Figure Lengend Snippet: RNAP containing βG1249D generates holoenzyme with AsiA/σD581BpA, but is defective in generating the crosslink with β’. ( A ) Native Tris-glycine gel. Solutions were assembled with the indicated components. The positions of AsiA, RNAP core, AsiA-RNAP holoenzyme, and σD581BpA are marked. (The bands that migrate faster than AsiA seen in lane 1 are trace contaminants present in the σD581BpA preparation.) ( B ) SDS-PAGE gel showing the products obtained after photocrosslinking. Arrow points to the crosslink between σD581BpA and β’ 80 HRGVICEK 87 identified in Figure 3 .

    Article Snippet: A 20 μl aliquot was used for photocrosslinking, and a 5 μl aliquot was applied to a 4–12% Tris-glycine gel (Invitrogen/Thermo Fisher) run in 1× Native Tris-glycine buffer (Invitrogen/Thermo Fisher) and stained in Gel Code (Thermo Fisher) as described ( ).

    Techniques: SDS Page

    Kinase assays demonstrate that p38 MAPK directly phosphorylates NHE1 at a site(s) between amino acids 703 and 793. The numbering system used corresponds to the rabbit NHE1 sequence. (A) Protein lysates from FL5.12A cells cultured with or without IL-3 for 2 h were immunoprecipitated with either an antibody specific for phospho-p38 MAPK (p38) or an antibody specific for the motif, p-TP, and the ability of these kinases to phosphorylated the WT NHE-GST fusion protein was evaluated by an in-gel kinase assay as described in Materials and Methods. Only p38 phosphorylated the WT NHE-GST fusion protein, an activity which increased 1.8-fold during IL-3 withdrawal (left panel). Protein lysates from FL5.12A cells were also immunoprecipitated with c-Jun fusion beads to capture JNK, which was tested in an in vitro kinase assay for its ability to phosphorylate the WT NHEGST fusion protein. Unlike p38 MAPK, JNK did not phosphorylate NHE (right panel). (B) Protein lysates extracted from anisomycin-activated FL5.12A cells were immunoprecipitated with antibody to phospho-p38 MAPK and a kinase assay performed as described in Materials and Methods using the WT NHE-GST fusion protein and seven mutant NHE-GST fusion proteins as substrates. GST alone was included as a negative control. (C) The results of the kinase assay from panel B are summarized in table form. In addition, phospho-p38 MAPK did not phosphorylate NHE-GST fusion proteins containing amino acids 635 to 663. Possible phosphorylation sites by p38 MAPK on NHE are located in the region from amino acids 703 to 743, which excludes the proposed p90RSK phosphorylation site (Serine 703, numbering from human NHE1 sequence). (D) FL5.12A cells, cultured without IL-3 for 0, 1, 2, and 3 h or treated with anisomycin (+), were lysed, and the precleared protein extracts were immunoprecipitated with the A7 antibody specific for NHE1 and then run on an 8% Tris-glycine SDS gel and analyzed by Western blotting with the p-TP-specific antibody (left panel). The same blots were then reprobed with a commercially available anti-NHE1 antibody (right panel). NHE1 did not contain an activated p-TP motif. (E) Mass spectrometry analysis, as described in Materials and Methods, identified four sites at Thr 717, Ser 722, Ser 725, and Ser 728 as in vitro targets for p38 MAPK activity. Phosphorylation of one or more of these sites by p38 MAPK modulates alkalinization mediated by NHE during trophic factor withdrawal.

    Journal: Molecular and Cellular Biology

    Article Title: Trophic Factor Withdrawal: p38 Mitogen-Activated Protein Kinase Activates NHE1, Which Induces Intracellular Alkalinization

    doi: 10.1128/MCB.21.22.7545-7557.2001

    Figure Lengend Snippet: Kinase assays demonstrate that p38 MAPK directly phosphorylates NHE1 at a site(s) between amino acids 703 and 793. The numbering system used corresponds to the rabbit NHE1 sequence. (A) Protein lysates from FL5.12A cells cultured with or without IL-3 for 2 h were immunoprecipitated with either an antibody specific for phospho-p38 MAPK (p38) or an antibody specific for the motif, p-TP, and the ability of these kinases to phosphorylated the WT NHE-GST fusion protein was evaluated by an in-gel kinase assay as described in Materials and Methods. Only p38 phosphorylated the WT NHE-GST fusion protein, an activity which increased 1.8-fold during IL-3 withdrawal (left panel). Protein lysates from FL5.12A cells were also immunoprecipitated with c-Jun fusion beads to capture JNK, which was tested in an in vitro kinase assay for its ability to phosphorylate the WT NHEGST fusion protein. Unlike p38 MAPK, JNK did not phosphorylate NHE (right panel). (B) Protein lysates extracted from anisomycin-activated FL5.12A cells were immunoprecipitated with antibody to phospho-p38 MAPK and a kinase assay performed as described in Materials and Methods using the WT NHE-GST fusion protein and seven mutant NHE-GST fusion proteins as substrates. GST alone was included as a negative control. (C) The results of the kinase assay from panel B are summarized in table form. In addition, phospho-p38 MAPK did not phosphorylate NHE-GST fusion proteins containing amino acids 635 to 663. Possible phosphorylation sites by p38 MAPK on NHE are located in the region from amino acids 703 to 743, which excludes the proposed p90RSK phosphorylation site (Serine 703, numbering from human NHE1 sequence). (D) FL5.12A cells, cultured without IL-3 for 0, 1, 2, and 3 h or treated with anisomycin (+), were lysed, and the precleared protein extracts were immunoprecipitated with the A7 antibody specific for NHE1 and then run on an 8% Tris-glycine SDS gel and analyzed by Western blotting with the p-TP-specific antibody (left panel). The same blots were then reprobed with a commercially available anti-NHE1 antibody (right panel). NHE1 did not contain an activated p-TP motif. (E) Mass spectrometry analysis, as described in Materials and Methods, identified four sites at Thr 717, Ser 722, Ser 725, and Ser 728 as in vitro targets for p38 MAPK activity. Phosphorylation of one or more of these sites by p38 MAPK modulates alkalinization mediated by NHE during trophic factor withdrawal.

    Article Snippet: The immunoprecipitates were washed in RIPA buffer, run on a 10% Tris-glycine SDS gel (Invitrogen), and blotted for p38 MAPK (Santa Cruz) as previously described.

    Techniques: Sequencing, Cell Culture, Immunoprecipitation, Kinase Assay, Activity Assay, In Vitro, Mutagenesis, Negative Control, SDS-Gel, Western Blot, Mass Spectrometry

    Protein profile of NL4-3 and NL4-3/ΔRT virions. Virions purified by ultracentrifugation were used to extract proteins and separated in a gradient 4-12% Tris-Glycine gel. An anti-p24 monoclonal antibody was used to study the processing profile of Gag in NL4-3/ΔRT and NL4-3 virions. There is a weaker processing of Gag in NL4-3/ΔRT virions, represented by an increase in p55- gag and MA-CA p41 forms in detriment of CA p24. At the same, an increase in intermediate forms is also shown in NL4-3/ΔRT virions.

    Journal: PLoS ONE

    Article Title: Generation and Characterization of a Defective HIV-1 Virus as an Immunogen for a Therapeutic Vaccine

    doi: 10.1371/journal.pone.0048848

    Figure Lengend Snippet: Protein profile of NL4-3 and NL4-3/ΔRT virions. Virions purified by ultracentrifugation were used to extract proteins and separated in a gradient 4-12% Tris-Glycine gel. An anti-p24 monoclonal antibody was used to study the processing profile of Gag in NL4-3/ΔRT and NL4-3 virions. There is a weaker processing of Gag in NL4-3/ΔRT virions, represented by an increase in p55- gag and MA-CA p41 forms in detriment of CA p24. At the same, an increase in intermediate forms is also shown in NL4-3/ΔRT virions.

    Article Snippet: For Western blot (WB) 200 ng of the different extracts quantified by Ag p24 were mixed with Laemmli buffer and resolved in pre-cast 4–12% Tris-Glycine gels (Novex® 4–12% Tris-Glycine Mini Gel; Invitrogen).

    Techniques: Purification

    Kinase assays demonstrate that p38 MAPK directly phosphorylates NHE1 at a site(s) between amino acids 703 and 793. The numbering system used corresponds to the rabbit NHE1 sequence. (A) Protein lysates from FL5.12A cells cultured with or without IL-3 for 2 h were immunoprecipitated with either an antibody specific for phospho-p38 MAPK (p38) or an antibody specific for the motif, p-TP, and the ability of these kinases to phosphorylated the WT NHE-GST fusion protein was evaluated by an in-gel kinase assay as described in Materials and Methods. Only p38 phosphorylated the WT NHE-GST fusion protein, an activity which increased 1.8-fold during IL-3 withdrawal (left panel). Protein lysates from FL5.12A cells were also immunoprecipitated with c-Jun fusion beads to capture JNK, which was tested in an in vitro kinase assay for its ability to phosphorylate the WT NHEGST fusion protein. Unlike p38 MAPK, JNK did not phosphorylate NHE (right panel). (B) Protein lysates extracted from anisomycin-activated FL5.12A cells were immunoprecipitated with antibody to phospho-p38 MAPK and a kinase assay performed as described in Materials and Methods using the WT NHE-GST fusion protein and seven mutant NHE-GST fusion proteins as substrates. GST alone was included as a negative control. (C) The results of the kinase assay from panel B are summarized in table form. In addition, phospho-p38 MAPK did not phosphorylate NHE-GST fusion proteins containing amino acids 635 to 663. Possible phosphorylation sites by p38 MAPK on NHE are located in the region from amino acids 703 to 743, which excludes the proposed p90RSK phosphorylation site (Serine 703, numbering from human NHE1 sequence). (D) FL5.12A cells, cultured without IL-3 for 0, 1, 2, and 3 h or treated with anisomycin (+), were lysed, and the precleared protein extracts were immunoprecipitated with the A7 antibody specific for NHE1 and then run on an 8% Tris-glycine SDS gel and analyzed by Western blotting with the p-TP-specific antibody (left panel). The same blots were then reprobed with a commercially available anti-NHE1 antibody (right panel). NHE1 did not contain an activated p-TP motif. (E) Mass spectrometry analysis, as described in Materials and Methods, identified four sites at Thr 717, Ser 722, Ser 725, and Ser 728 as in vitro targets for p38 MAPK activity. Phosphorylation of one or more of these sites by p38 MAPK modulates alkalinization mediated by NHE during trophic factor withdrawal.

    Journal: Molecular and Cellular Biology

    Article Title: Trophic Factor Withdrawal: p38 Mitogen-Activated Protein Kinase Activates NHE1, Which Induces Intracellular Alkalinization

    doi: 10.1128/MCB.21.22.7545-7557.2001

    Figure Lengend Snippet: Kinase assays demonstrate that p38 MAPK directly phosphorylates NHE1 at a site(s) between amino acids 703 and 793. The numbering system used corresponds to the rabbit NHE1 sequence. (A) Protein lysates from FL5.12A cells cultured with or without IL-3 for 2 h were immunoprecipitated with either an antibody specific for phospho-p38 MAPK (p38) or an antibody specific for the motif, p-TP, and the ability of these kinases to phosphorylated the WT NHE-GST fusion protein was evaluated by an in-gel kinase assay as described in Materials and Methods. Only p38 phosphorylated the WT NHE-GST fusion protein, an activity which increased 1.8-fold during IL-3 withdrawal (left panel). Protein lysates from FL5.12A cells were also immunoprecipitated with c-Jun fusion beads to capture JNK, which was tested in an in vitro kinase assay for its ability to phosphorylate the WT NHEGST fusion protein. Unlike p38 MAPK, JNK did not phosphorylate NHE (right panel). (B) Protein lysates extracted from anisomycin-activated FL5.12A cells were immunoprecipitated with antibody to phospho-p38 MAPK and a kinase assay performed as described in Materials and Methods using the WT NHE-GST fusion protein and seven mutant NHE-GST fusion proteins as substrates. GST alone was included as a negative control. (C) The results of the kinase assay from panel B are summarized in table form. In addition, phospho-p38 MAPK did not phosphorylate NHE-GST fusion proteins containing amino acids 635 to 663. Possible phosphorylation sites by p38 MAPK on NHE are located in the region from amino acids 703 to 743, which excludes the proposed p90RSK phosphorylation site (Serine 703, numbering from human NHE1 sequence). (D) FL5.12A cells, cultured without IL-3 for 0, 1, 2, and 3 h or treated with anisomycin (+), were lysed, and the precleared protein extracts were immunoprecipitated with the A7 antibody specific for NHE1 and then run on an 8% Tris-glycine SDS gel and analyzed by Western blotting with the p-TP-specific antibody (left panel). The same blots were then reprobed with a commercially available anti-NHE1 antibody (right panel). NHE1 did not contain an activated p-TP motif. (E) Mass spectrometry analysis, as described in Materials and Methods, identified four sites at Thr 717, Ser 722, Ser 725, and Ser 728 as in vitro targets for p38 MAPK activity. Phosphorylation of one or more of these sites by p38 MAPK modulates alkalinization mediated by NHE during trophic factor withdrawal.

    Article Snippet: After extensive washing of beads, the recovered protein was analyzed by SDS-polyacrylamide gel electrophoresis on 8% Tris-glycine SDS gels (Invitrogen).

    Techniques: Sequencing, Cell Culture, Immunoprecipitation, Kinase Assay, Activity Assay, In Vitro, Mutagenesis, Negative Control, SDS-Gel, Western Blot, Mass Spectrometry

    Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% Tris-glycine gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 kDa (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p

    Journal: CNS neuroscience & therapeutics

    Article Title: Anthoxanthin polyphenols attenuate Aβ oligomer-induced neuronal responses associated with Alzheimer's disease

    doi: 10.1111/cns.12659

    Figure Lengend Snippet: Hydroxylated anthoxanthins alter Aβ oligomer size distribution Oligomers were prepared from Aβ 1-42 (15 μM) in the absence (CONT, control) or presence of 150 μM anthoxanthins flavone (FLA), apigenin (API), luteolin (LUT), kaempferol (KAE), or quercetin (QUE) by dilution from DMSO into 12 mM phosphate (pH 7.4) containing 1 μM NaCl. Following oligomerization (30 min, 25°C), oligomers were stabilized via addition of Tween-20 (0.1%), resolved by SDS-PAGE on either a 4-20% Tris-glycine gel (panel A) or a 16.5% Tris-tricine gel (panel D), transferred to nitrocellulose membrane, and probed with 6E10 antibody. Images are representative of 3-5 independent experiments. Using volumetric analysis in conjunction with the 4-20% Tris-glycine gel images (panel A), oligomer species within size ranges of 100-250 kDa (panel B) and 25-100 kDa (panel C) were quantified. Using band intensity analysis in conjunction with the 16.5% Tris-tricine gel images (panel D), tetramer (panel E), trimer (panel G), and monomer (panel F) species were quantified. Reported results are normalized to the control, shown as a dashed line with a value of 1 and representing no change. Error bars indicate SEM, n=3-5. *p

    Article Snippet: For oligomers 25-250 kDa in size, stabilized oligomers were separated on a 4-20% Tris-glycine gel (Bio-rad, Hercules, CA); for monomer, trimer, and tetramer, stabilized oligomers were separated on a 16.5% Tris-tricine gel (Bio-rad).

    Techniques: SDS Page

    Western blot analysis of the expression of the R. rickettsii signal peptidase I in E. coli strain IT41. Total proteins from the E. coli cells carrying pTrcHisRR4 or pTrcHisC plasmids, separated on 4 to 12% Tris-glycine precast gel, 1× Tris-glycine-SDS running buffer, transferred to polyvinylidene difluoride membrane was probed with His-Tag monoclonal antibodies by using a WesternBreeze chromogenic immunodetection kit. Lane 1, total proteins from E. coli IT41/pTrcHisRR4; lane 2, total proteins from E. coli IT41/pTrcHisC; and lane 3, total proteins from E. coli IT41. Lane M, Bio-Rad Kaleidoscope prestained markers (carbonic anhydrase, 39.7 kDa; soybean trypsin inhibitor, 32.1 kDa).

    Journal: Journal of Bacteriology

    Article Title: Molecular and Functional Analysis of the lepB Gene, Encoding a Type I Signal Peptidase from Rickettsia rickettsii and Rickettsia typhi

    doi: 10.1128/JB.185.15.4578-4584.2003

    Figure Lengend Snippet: Western blot analysis of the expression of the R. rickettsii signal peptidase I in E. coli strain IT41. Total proteins from the E. coli cells carrying pTrcHisRR4 or pTrcHisC plasmids, separated on 4 to 12% Tris-glycine precast gel, 1× Tris-glycine-SDS running buffer, transferred to polyvinylidene difluoride membrane was probed with His-Tag monoclonal antibodies by using a WesternBreeze chromogenic immunodetection kit. Lane 1, total proteins from E. coli IT41/pTrcHisRR4; lane 2, total proteins from E. coli IT41/pTrcHisC; and lane 3, total proteins from E. coli IT41. Lane M, Bio-Rad Kaleidoscope prestained markers (carbonic anhydrase, 39.7 kDa; soybean trypsin inhibitor, 32.1 kDa).

    Article Snippet: Cell suspensions were mixed with equal volumes of 2× Tris-glycine-sodium dodecyl sulfate (SDS) sample buffer (Invitrogen Life Technologies) and boiled at 100°C for 5 min. Total cell proteins were separated on 4 to 12% Tris-glycine precast gel (Invitrogen Life Technologies) by using 1× Tris-glycine-SDS running buffer (Bio-Rad, Hercules, Calif.).

    Techniques: Western Blot, Expressing, Immunodetection