dtt Thermo Fisher Search Results


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  • 99
    Thermo Fisher dithiotreitol dtt
    NCC is the main form of injury-induced protein aggregation. ( a – d ) Jurkat cells were treated with vehicle (uninjured), etoposide, staurosporine or Fas ligand for 24 h. ( a ) Triton-soluble and -insoluble proteins were isolated and subjected to SDS-PAGE under reducing conditions followed by immunoblot analysis. Results are representative of n = 3–6 independent experiments. ( b ) Triton-soluble and -insoluble proteins were isolated and subjected to SDS-PAGE in the presence/absence of <t>dithiothreitol</t> (DTT) followed by immunoblot analysis. Results are representative of n = 2–3 independent experiments. ( c ) Cells were fixed, subjected to immunofluorescence and imaged by super-resolution microscopy with xy- resolution of 70 nm. Shown are representative x , y micrographs, where the bottom two rows are magnified micrographs taken from the boxed areas in the top two rows. Staurosporine-induced necrosis causes NCC-proteins (α-tubulin, EF2 and MCM7) to relocate into aberrant and distinct structures. Arrows indicate EF2 deposits that exhibit little-to-no staining for tubulin or MCM7. Arrowheads indicate MCM7 deposits that exhibit little-to-no staining for tubulin or EF2. Note, the procedure used to stain oxidized thiols was not compatible with the sample preparation for super-resolution microscopy. ( d ) Cells were fixed and subjected to immunofluorescence with maleimide co-staining for oxidized thiols. Shown are representative x,y confocal micrographs. Staurosporine-induced necrosis leads to nuclear breakdown and a marked increase in oxidized thiols that colocalize with aberrantly deposited NCC-proteins (3PDGH, GAPDH, MCM7, EF1, EF2 and α-tubulin).
    Dithiotreitol Dtt, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 193 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher dtt
    The NPXY motif and GULP are required for internalization of Jedi-1. Time course for internalization of Jedi-1-GFP (A) or Jedi-1-GFP APXA mutant (B) after addition of microspheres. HeLa cells were transfected with wild-type or APXA mutant Jedi-1-GFP. Surface proteins were biotinylated with EZ-Link Sulfo-NHS-SS-Biotin at 4°C and then exposed to fluorescent microspheres and warmed to 37°C for the time indicated. The <t>biotinylation</t> of surface proteins was then reversed using the reducing agent <t>DTT.</t> The cells were lysed, and internalized, biotinylated Jedi-1 or mutant Jedi-1 was pulled down with avidin-conjugated agarose beads and detected by immunoblotting with a GFP antibody. Total levels of Jedi-1 are shown in lysates ( n = 3). (C) Control MEFs or MEFs with GULP knocked down (MEF psiGULP) were transfected with Jedi-GFP. The cells were then exposed to microspheres or left untreated for 90 min, and the internalized Jedi-1 was detected as in A and B. Levels of Jedi-1–GFP and GULP are shown in the lysates.
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    95
    Thermo Fisher m dtt
    The NPXY motif and GULP are required for internalization of Jedi-1. Time course for internalization of Jedi-1-GFP (A) or Jedi-1-GFP APXA mutant (B) after addition of microspheres. HeLa cells were transfected with wild-type or APXA mutant Jedi-1-GFP. Surface proteins were biotinylated with EZ-Link Sulfo-NHS-SS-Biotin at 4°C and then exposed to fluorescent microspheres and warmed to 37°C for the time indicated. The <t>biotinylation</t> of surface proteins was then reversed using the reducing agent <t>DTT.</t> The cells were lysed, and internalized, biotinylated Jedi-1 or mutant Jedi-1 was pulled down with avidin-conjugated agarose beads and detected by immunoblotting with a GFP antibody. Total levels of Jedi-1 are shown in lysates ( n = 3). (C) Control MEFs or MEFs with GULP knocked down (MEF psiGULP) were transfected with Jedi-GFP. The cells were then exposed to microspheres or left untreated for 90 min, and the internalized Jedi-1 was detected as in A and B. Levels of Jedi-1–GFP and GULP are shown in the lysates.
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    99
    Thermo Fisher ultrapure dithiothreitol dtt
    Determination of the relative Cu(I)-binding affinity of de-coppering drugs in competition with Cu 1 Cox17. Fractional occupancy of Cu(I)-binding sites in Cox17 at different concentrations of PA ( a ), TR ( b ), <t>BAL</t> ( c ), DMS ( d ) and TTM ( e ) in a metal competition experiment. Conditions: Cox17 1 μM; 20 mM ammonium acetate, pH = 7.3, <t>DTT</t> 50 μM; T = 25 °C. Results of duplicate experiments are presented with different symbols. The solid line shows the fitting curve with hyperbolic equation (y = P1*(1 − [x/(P2 + x)]) + P3), where P2 = C 50 .
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    Thermo Fisher sds loading buffer
    Determination of the relative Cu(I)-binding affinity of de-coppering drugs in competition with Cu 1 Cox17. Fractional occupancy of Cu(I)-binding sites in Cox17 at different concentrations of PA ( a ), TR ( b ), <t>BAL</t> ( c ), DMS ( d ) and TTM ( e ) in a metal competition experiment. Conditions: Cox17 1 μM; 20 mM ammonium acetate, pH = 7.3, <t>DTT</t> 50 μM; T = 25 °C. Results of duplicate experiments are presented with different symbols. The solid line shows the fitting curve with hyperbolic equation (y = P1*(1 − [x/(P2 + x)]) + P3), where P2 = C 50 .
    Sds Loading Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1823 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher 1m dithiothreitol dtt
    Determination of the relative Cu(I)-binding affinity of de-coppering drugs in competition with Cu 1 Cox17. Fractional occupancy of Cu(I)-binding sites in Cox17 at different concentrations of PA ( a ), TR ( b ), <t>BAL</t> ( c ), DMS ( d ) and TTM ( e ) in a metal competition experiment. Conditions: Cox17 1 μM; 20 mM ammonium acetate, pH = 7.3, <t>DTT</t> 50 μM; T = 25 °C. Results of duplicate experiments are presented with different symbols. The solid line shows the fitting curve with hyperbolic equation (y = P1*(1 − [x/(P2 + x)]) + P3), where P2 = C 50 .
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    91
    Thermo Fisher dithiothreitol dtt 200 mm solution in water
    Determination of the relative Cu(I)-binding affinity of de-coppering drugs in competition with Cu 1 Cox17. Fractional occupancy of Cu(I)-binding sites in Cox17 at different concentrations of PA ( a ), TR ( b ), <t>BAL</t> ( c ), DMS ( d ) and TTM ( e ) in a metal competition experiment. Conditions: Cox17 1 μM; 20 mM ammonium acetate, pH = 7.3, <t>DTT</t> 50 μM; T = 25 °C. Results of duplicate experiments are presented with different symbols. The solid line shows the fitting curve with hyperbolic equation (y = P1*(1 − [x/(P2 + x)]) + P3), where P2 = C 50 .
    Dithiothreitol Dtt 200 Mm Solution In Water, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher 1x dtt
    Determination of the relative Cu(I)-binding affinity of de-coppering drugs in competition with Cu 1 Cox17. Fractional occupancy of Cu(I)-binding sites in Cox17 at different concentrations of PA ( a ), TR ( b ), <t>BAL</t> ( c ), DMS ( d ) and TTM ( e ) in a metal competition experiment. Conditions: Cox17 1 μM; 20 mM ammonium acetate, pH = 7.3, <t>DTT</t> 50 μM; T = 25 °C. Results of duplicate experiments are presented with different symbols. The solid line shows the fitting curve with hyperbolic equation (y = P1*(1 − [x/(P2 + x)]) + P3), where P2 = C 50 .
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    94
    Thermo Fisher 10x dtt
    Determination of the relative Cu(I)-binding affinity of de-coppering drugs in competition with Cu 1 Cox17. Fractional occupancy of Cu(I)-binding sites in Cox17 at different concentrations of PA ( a ), TR ( b ), <t>BAL</t> ( c ), DMS ( d ) and TTM ( e ) in a metal competition experiment. Conditions: Cox17 1 μM; 20 mM ammonium acetate, pH = 7.3, <t>DTT</t> 50 μM; T = 25 °C. Results of duplicate experiments are presented with different symbols. The solid line shows the fitting curve with hyperbolic equation (y = P1*(1 − [x/(P2 + x)]) + P3), where P2 = C 50 .
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    87
    Thermo Fisher dtt stock
    RP-HPLC profiles for the H3 <t>rHA</t> proteins. Each H3 rHA was analyzed in duplicate. Representative chromatograms from the day 0 and 28 time points are provided. rHAs were incubated with 25 mM <t>DTT</t> for at least 30 minutes prior to analysis. ~25 μg of each rHA was injected onto a Poros R1 column and an acetonitrile gradient applied.
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    86
    Thermo Fisher sonication dtt
    RP-HPLC profiles for the H3 <t>rHA</t> proteins. Each H3 rHA was analyzed in duplicate. Representative chromatograms from the day 0 and 28 time points are provided. rHAs were incubated with 25 mM <t>DTT</t> for at least 30 minutes prior to analysis. ~25 μg of each rHA was injected onto a Poros R1 column and an acetonitrile gradient applied.
    Sonication Dtt, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Thermo Fisher dtt reducing buffer
    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled <t>DTT,</t> <t>LDS</t> and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.
    Dtt Reducing Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 87/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher nupage buffer dtt
    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled <t>DTT,</t> <t>LDS</t> and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.
    Nupage Buffer Dtt, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Fisher Scientific dtt
    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled <t>DTT,</t> <t>LDS</t> and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.
    Dtt, supplied by Fisher Scientific, used in various techniques. Bioz Stars score: 95/100, based on 401 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher dtt reducing reagent
    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled <t>DTT,</t> <t>LDS</t> and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.
    Dtt Reducing Reagent, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    97
    Thermo Fisher 1 4 dithiothreitol
    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled <t>DTT,</t> <t>LDS</t> and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.
    1 4 Dithiothreitol, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 97/100, based on 39 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    87
    Thermo Fisher dtt data
    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled <t>DTT,</t> <t>LDS</t> and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.
    Dtt Data, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 87/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Thermo Fisher fresh dtt
    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled <t>DTT,</t> <t>LDS</t> and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.
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    91
    Thermo Fisher 1x nupage buffer dtt
    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled <t>DTT,</t> <t>LDS</t> and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.
    1x Nupage Buffer Dtt, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Thermo Fisher nr dtt
    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled <t>DTT,</t> <t>LDS</t> and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.
    Nr Dtt, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 86/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher nupage dtt
    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled <t>DTT,</t> <t>LDS</t> and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.
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    84
    Thermo Fisher 100 mm dithiothreitol
    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled <t>DTT,</t> <t>LDS</t> and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.
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    Thermo Fisher prepared dtt
    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled <t>DTT,</t> <t>LDS</t> and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.
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    Thermo Fisher dye dtt
    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled <t>DTT,</t> <t>LDS</t> and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.
    Dye Dtt, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 92/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    NCC is the main form of injury-induced protein aggregation. ( a – d ) Jurkat cells were treated with vehicle (uninjured), etoposide, staurosporine or Fas ligand for 24 h. ( a ) Triton-soluble and -insoluble proteins were isolated and subjected to SDS-PAGE under reducing conditions followed by immunoblot analysis. Results are representative of n = 3–6 independent experiments. ( b ) Triton-soluble and -insoluble proteins were isolated and subjected to SDS-PAGE in the presence/absence of dithiothreitol (DTT) followed by immunoblot analysis. Results are representative of n = 2–3 independent experiments. ( c ) Cells were fixed, subjected to immunofluorescence and imaged by super-resolution microscopy with xy- resolution of 70 nm. Shown are representative x , y micrographs, where the bottom two rows are magnified micrographs taken from the boxed areas in the top two rows. Staurosporine-induced necrosis causes NCC-proteins (α-tubulin, EF2 and MCM7) to relocate into aberrant and distinct structures. Arrows indicate EF2 deposits that exhibit little-to-no staining for tubulin or MCM7. Arrowheads indicate MCM7 deposits that exhibit little-to-no staining for tubulin or EF2. Note, the procedure used to stain oxidized thiols was not compatible with the sample preparation for super-resolution microscopy. ( d ) Cells were fixed and subjected to immunofluorescence with maleimide co-staining for oxidized thiols. Shown are representative x,y confocal micrographs. Staurosporine-induced necrosis leads to nuclear breakdown and a marked increase in oxidized thiols that colocalize with aberrantly deposited NCC-proteins (3PDGH, GAPDH, MCM7, EF1, EF2 and α-tubulin).

    Journal: Open Biology

    Article Title: Physicochemical properties that control protein aggregation also determine whether a protein is retained or released from necrotic cells

    doi: 10.1098/rsob.160098

    Figure Lengend Snippet: NCC is the main form of injury-induced protein aggregation. ( a – d ) Jurkat cells were treated with vehicle (uninjured), etoposide, staurosporine or Fas ligand for 24 h. ( a ) Triton-soluble and -insoluble proteins were isolated and subjected to SDS-PAGE under reducing conditions followed by immunoblot analysis. Results are representative of n = 3–6 independent experiments. ( b ) Triton-soluble and -insoluble proteins were isolated and subjected to SDS-PAGE in the presence/absence of dithiothreitol (DTT) followed by immunoblot analysis. Results are representative of n = 2–3 independent experiments. ( c ) Cells were fixed, subjected to immunofluorescence and imaged by super-resolution microscopy with xy- resolution of 70 nm. Shown are representative x , y micrographs, where the bottom two rows are magnified micrographs taken from the boxed areas in the top two rows. Staurosporine-induced necrosis causes NCC-proteins (α-tubulin, EF2 and MCM7) to relocate into aberrant and distinct structures. Arrows indicate EF2 deposits that exhibit little-to-no staining for tubulin or MCM7. Arrowheads indicate MCM7 deposits that exhibit little-to-no staining for tubulin or EF2. Note, the procedure used to stain oxidized thiols was not compatible with the sample preparation for super-resolution microscopy. ( d ) Cells were fixed and subjected to immunofluorescence with maleimide co-staining for oxidized thiols. Shown are representative x,y confocal micrographs. Staurosporine-induced necrosis leads to nuclear breakdown and a marked increase in oxidized thiols that colocalize with aberrantly deposited NCC-proteins (3PDGH, GAPDH, MCM7, EF1, EF2 and α-tubulin).

    Article Snippet: SDS-PAGE for tryptic digestion Samples were boiled in 2% SDS-loading buffer with dithiothreitol and subjected to SDS-PAGE using a NuPAGE Novex Bis-Tris Mini gel (4–12%) with NuPAGE MOPS SDS-Running buffer supplemented with 1× NuPAGE antioxidant (Life Technologies).

    Techniques: Isolation, SDS Page, Immunofluorescence, Microscopy, Staining, Sample Prep

    The NPXY motif and GULP are required for internalization of Jedi-1. Time course for internalization of Jedi-1-GFP (A) or Jedi-1-GFP APXA mutant (B) after addition of microspheres. HeLa cells were transfected with wild-type or APXA mutant Jedi-1-GFP. Surface proteins were biotinylated with EZ-Link Sulfo-NHS-SS-Biotin at 4°C and then exposed to fluorescent microspheres and warmed to 37°C for the time indicated. The biotinylation of surface proteins was then reversed using the reducing agent DTT. The cells were lysed, and internalized, biotinylated Jedi-1 or mutant Jedi-1 was pulled down with avidin-conjugated agarose beads and detected by immunoblotting with a GFP antibody. Total levels of Jedi-1 are shown in lysates ( n = 3). (C) Control MEFs or MEFs with GULP knocked down (MEF psiGULP) were transfected with Jedi-GFP. The cells were then exposed to microspheres or left untreated for 90 min, and the internalized Jedi-1 was detected as in A and B. Levels of Jedi-1–GFP and GULP are shown in the lysates.

    Journal: Molecular Biology of the Cell

    Article Title: The adaptor protein GULP promotes Jedi-1–mediated phagocytosis through a clathrin-dependent mechanism

    doi: 10.1091/mbc.E13-11-0658

    Figure Lengend Snippet: The NPXY motif and GULP are required for internalization of Jedi-1. Time course for internalization of Jedi-1-GFP (A) or Jedi-1-GFP APXA mutant (B) after addition of microspheres. HeLa cells were transfected with wild-type or APXA mutant Jedi-1-GFP. Surface proteins were biotinylated with EZ-Link Sulfo-NHS-SS-Biotin at 4°C and then exposed to fluorescent microspheres and warmed to 37°C for the time indicated. The biotinylation of surface proteins was then reversed using the reducing agent DTT. The cells were lysed, and internalized, biotinylated Jedi-1 or mutant Jedi-1 was pulled down with avidin-conjugated agarose beads and detected by immunoblotting with a GFP antibody. Total levels of Jedi-1 are shown in lysates ( n = 3). (C) Control MEFs or MEFs with GULP knocked down (MEF psiGULP) were transfected with Jedi-GFP. The cells were then exposed to microspheres or left untreated for 90 min, and the internalized Jedi-1 was detected as in A and B. Levels of Jedi-1–GFP and GULP are shown in the lysates.

    Article Snippet: The biotinylation of surface proteins was reversed using 50 mM DTT at various time points after stimulation with 2-μm carboxylate-modified latex beads (Invitrogen).

    Techniques: Mutagenesis, Transfection, Avidin-Biotin Assay

    The reducing agent dithiothreitol (DTT) causes large voltage offsets in Ag/AgCl electrodes. Summary of the voltage offsets produced by 1 mM DTT. Two wire purities of 99.9 and 99.99% silver were examined. As in , bare wire ( A ), which simulates the

    Journal: American Journal of Physiology - Cell Physiology

    Article Title: Redox artifacts in electrophysiological recordings

    doi: 10.1152/ajpcell.00318.2012

    Figure Lengend Snippet: The reducing agent dithiothreitol (DTT) causes large voltage offsets in Ag/AgCl electrodes. Summary of the voltage offsets produced by 1 mM DTT. Two wire purities of 99.9 and 99.99% silver were examined. As in , bare wire ( A ), which simulates the

    Article Snippet: Tris-2-carboxyethly-phosphine (TCEP) and dithiothreitol (DTT) were obtained from Pierce.

    Techniques: Produced

    Inhibition of the proteasome activity leads to the detection of GFP-bZIP60u on the ER. Seedlings (7-days-old) of transgenic Arabidopsis plants harbouring the construct 60pro:GFP-bZIP60 were pretreated with DMSO (0.2% v/v) or MG132 (100 mM) during 18 hours. Then seedlings were treated with DMSO (0.2% v/v) (A-D), DMSO (0.2% v/v) plus DTT (2 mM) (E-H), MG132 (100 μM) (I-L) or MG132 (100 μM) plus DTT (2 mM) (M-P) during 3 hours. All treatments were performed in 0.5x MS phytagel plates supplemented with the chemicals mentioned above at the indicated concentrations. After treatment, seedlings were stained with ER-Tracker Blue-White DPX (1 μM) during 45 minutes, rinsed and stained with FM 4–64 (5 μM) during additional 5 minutes at room temperature. Finally, roots were analyzed by confocal microscopy. Scale bar equals 5 μm. Images are representative of three independent experiments. (Q) Immunoblot analysis of total protein extracts obtained from bzip60 / 60pro:GFP-bZIP60 transgenic Arabidopsis seedlings (7-days-old) treated with DMSO (0.2% v/v), MG132 (100 μM) or MG132 (100 μM) plus DTT (2 mM) as mentioned above, using a polyclonal antibody against GFP. bzip60 mutant seedlings were used as control. Anti-PEPC antibody was used as loading control. Data are representative of three independent experiments. (R) CE-LIF analysis of RT-PCR products obtained from total RNA extracted from roots of bzip60 mutant or bzip60 / 60pro:GFP-bZIP60 transgenic Arabidopsis plants (7-days-old) treated with DMSO (0.2% v/v), DMSO (0.2% v/v) plus DTT (2 mM), MG132 (100 μM) or MG132 (100 μM) plus DTT (2 mM) as described above. Spherograms peaks, corresponding to the unspliced form of bZIP60 (U) and spliced form (S), are depicted. Asterisks indicate the detection of a third peak only present in DTT treated samples. Data are representative of three independent experiments.

    Journal: PLoS ONE

    Article Title: The Dynamic of the Splicing of bZIP60 and the Proteins Encoded by the Spliced and Unspliced mRNAs Reveals Some Unique Features during the Activation of UPR in Arabidopsis thaliana

    doi: 10.1371/journal.pone.0122936

    Figure Lengend Snippet: Inhibition of the proteasome activity leads to the detection of GFP-bZIP60u on the ER. Seedlings (7-days-old) of transgenic Arabidopsis plants harbouring the construct 60pro:GFP-bZIP60 were pretreated with DMSO (0.2% v/v) or MG132 (100 mM) during 18 hours. Then seedlings were treated with DMSO (0.2% v/v) (A-D), DMSO (0.2% v/v) plus DTT (2 mM) (E-H), MG132 (100 μM) (I-L) or MG132 (100 μM) plus DTT (2 mM) (M-P) during 3 hours. All treatments were performed in 0.5x MS phytagel plates supplemented with the chemicals mentioned above at the indicated concentrations. After treatment, seedlings were stained with ER-Tracker Blue-White DPX (1 μM) during 45 minutes, rinsed and stained with FM 4–64 (5 μM) during additional 5 minutes at room temperature. Finally, roots were analyzed by confocal microscopy. Scale bar equals 5 μm. Images are representative of three independent experiments. (Q) Immunoblot analysis of total protein extracts obtained from bzip60 / 60pro:GFP-bZIP60 transgenic Arabidopsis seedlings (7-days-old) treated with DMSO (0.2% v/v), MG132 (100 μM) or MG132 (100 μM) plus DTT (2 mM) as mentioned above, using a polyclonal antibody against GFP. bzip60 mutant seedlings were used as control. Anti-PEPC antibody was used as loading control. Data are representative of three independent experiments. (R) CE-LIF analysis of RT-PCR products obtained from total RNA extracted from roots of bzip60 mutant or bzip60 / 60pro:GFP-bZIP60 transgenic Arabidopsis plants (7-days-old) treated with DMSO (0.2% v/v), DMSO (0.2% v/v) plus DTT (2 mM), MG132 (100 μM) or MG132 (100 μM) plus DTT (2 mM) as described above. Spherograms peaks, corresponding to the unspliced form of bZIP60 (U) and spliced form (S), are depicted. Asterisks indicate the detection of a third peak only present in DTT treated samples. Data are representative of three independent experiments.

    Article Snippet: For subcellular imaging, seedlings of 7 days-old treated with DMSO, DMSO plus DTT, MG132 or MG132 plus DTT were stained with ER-Tracker Blue-White DPX dye (Molecular Probes, Life Technologies) diluted on liquid MS media during 45 minutes, rinsed on liquid MS media and stained with FM 4–64 dye (Molecular Probes, Life Technologies) during 5 minutes; at room temperature.

    Techniques: Inhibition, Activity Assay, Transgenic Assay, Construct, Mass Spectrometry, Staining, Confocal Microscopy, Mutagenesis, Reverse Transcription Polymerase Chain Reaction

    Determination of the relative Cu(I)-binding affinity of de-coppering drugs in competition with Cu 1 Cox17. Fractional occupancy of Cu(I)-binding sites in Cox17 at different concentrations of PA ( a ), TR ( b ), BAL ( c ), DMS ( d ) and TTM ( e ) in a metal competition experiment. Conditions: Cox17 1 μM; 20 mM ammonium acetate, pH = 7.3, DTT 50 μM; T = 25 °C. Results of duplicate experiments are presented with different symbols. The solid line shows the fitting curve with hyperbolic equation (y = P1*(1 − [x/(P2 + x)]) + P3), where P2 = C 50 .

    Journal: Scientific Reports

    Article Title: Copper(I)-binding properties of de-coppering drugs for the treatment of Wilson disease. α-Lipoic acid as a potential anti-copper agent

    doi: 10.1038/s41598-018-19873-2

    Figure Lengend Snippet: Determination of the relative Cu(I)-binding affinity of de-coppering drugs in competition with Cu 1 Cox17. Fractional occupancy of Cu(I)-binding sites in Cox17 at different concentrations of PA ( a ), TR ( b ), BAL ( c ), DMS ( d ) and TTM ( e ) in a metal competition experiment. Conditions: Cox17 1 μM; 20 mM ammonium acetate, pH = 7.3, DTT 50 μM; T = 25 °C. Results of duplicate experiments are presented with different symbols. The solid line shows the fitting curve with hyperbolic equation (y = P1*(1 − [x/(P2 + x)]) + P3), where P2 = C 50 .

    Article Snippet: Reagents Chemical reagents: PA, TR, BAL, DMS, LA, ammonium TTM, diethylammonium DETC were purchased from Sigma-Aldrich, DTT (ultrapure) from USB Corporation, DLA from Santa Cruz Biotechnology.

    Techniques: Binding Assay

    Determination of the relative Cu(I)-binding affinity of TTM and DETC in competition with Cu 10 MT. ESI-MS spectra of Cu 10 MT in the presence of 1 μM–20 μM TTM ( a ) and 0.1–7 mM DETC ( c ). Conditions: MT 3 μM; 20 mM ammonium acetate, pH = 7.3, DTT 10 mM; T = 25 °C. Ions with a charge state + 5 are shown; numbers on the peaks denote the metal stoichiometry of the complex. Number of asterisks denotes number of TTM molecules in the complex. Fractional occupancy of Cu(I)-binding sites in MT at different concentrations of TTM ( b ) and DETC ( d ) in a metal competition experiment. Results of duplicate experiments are presented with different symbols. The solid line shows the fitting curve with Hill equation (y = START + (END − START) * x^n / (K^n + x^n)), where K = C 50 .

    Journal: Scientific Reports

    Article Title: Copper(I)-binding properties of de-coppering drugs for the treatment of Wilson disease. α-Lipoic acid as a potential anti-copper agent

    doi: 10.1038/s41598-018-19873-2

    Figure Lengend Snippet: Determination of the relative Cu(I)-binding affinity of TTM and DETC in competition with Cu 10 MT. ESI-MS spectra of Cu 10 MT in the presence of 1 μM–20 μM TTM ( a ) and 0.1–7 mM DETC ( c ). Conditions: MT 3 μM; 20 mM ammonium acetate, pH = 7.3, DTT 10 mM; T = 25 °C. Ions with a charge state + 5 are shown; numbers on the peaks denote the metal stoichiometry of the complex. Number of asterisks denotes number of TTM molecules in the complex. Fractional occupancy of Cu(I)-binding sites in MT at different concentrations of TTM ( b ) and DETC ( d ) in a metal competition experiment. Results of duplicate experiments are presented with different symbols. The solid line shows the fitting curve with Hill equation (y = START + (END − START) * x^n / (K^n + x^n)), where K = C 50 .

    Article Snippet: Reagents Chemical reagents: PA, TR, BAL, DMS, LA, ammonium TTM, diethylammonium DETC were purchased from Sigma-Aldrich, DTT (ultrapure) from USB Corporation, DLA from Santa Cruz Biotechnology.

    Techniques: Binding Assay, Mass Spectrometry

    RP-HPLC profiles for the H3 rHA proteins. Each H3 rHA was analyzed in duplicate. Representative chromatograms from the day 0 and 28 time points are provided. rHAs were incubated with 25 mM DTT for at least 30 minutes prior to analysis. ~25 μg of each rHA was injected onto a Poros R1 column and an acetonitrile gradient applied.

    Journal: BMC Biotechnology

    Article Title: Modifications of cysteine residues in the transmembrane and cytoplasmic domains of a recombinant hemagglutinin protein prevent cross-linked multimer formation and potency loss

    doi: 10.1186/s12896-014-0111-y

    Figure Lengend Snippet: RP-HPLC profiles for the H3 rHA proteins. Each H3 rHA was analyzed in duplicate. Representative chromatograms from the day 0 and 28 time points are provided. rHAs were incubated with 25 mM DTT for at least 30 minutes prior to analysis. ~25 μg of each rHA was injected onto a Poros R1 column and an acetonitrile gradient applied.

    Article Snippet: For reducing conditions, a final concentration of 100 mM DTT was added to the Laemmli-rHA solution using a 500 mM DTT stock (Pierce, product# 20291, lot# ND170603) and incubated in a 100°C heat block for 3–5 min prior to loading on to the gel.

    Techniques: High Performance Liquid Chromatography, Incubation, Injection

    Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled DTT, LDS and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.

    Journal: Colloids and Surfaces. B, Biointerfaces

    Article Title: What interactions drive the salivary mucosal pellicle formation?

    doi: 10.1016/j.colsurfb.2014.05.020

    Figure Lengend Snippet: Gels following CBB and PAS staining (WMS only) of WMS and PS pellicle formations on hydrophobic particles from different subjects. Lanes: saliva pre (1), saliva post (2), water wash 1 (3), water wash 2 (4), SDS 1 (5), SDS 2 (6) and boiled DTT, LDS and water (7). Boxes highlight clear differences in binding ± TGM. The box highlighted by the arrow indicates an effect only seen in 50% of the samples. It shows what appear to be a possible cross-linked proteins, perhaps statherin and histatin bound higher due to crosslinking.

    Article Snippet: All samples were prepared with 0.5 M DTT reducing buffer (1:10) (Invitrogen) and LDS sample buffer (1:4) (Invitrogen) and boiled for 3 min. 15 μl of sample was then loaded onto a lane of a 4–12% Bis-Tris gel (Invitrogen) and all samples were run according to manufacturer's instructions in MES-SDS running buffer.

    Techniques: Staining, Binding Assay