dtt Thermo Fisher Search Results


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  • 90
    Thermo Fisher dithiothreitol
    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).
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    90
    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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    90
    Thermo Fisher dtt ultrapure
    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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    95
    Thermo Fisher m 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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    80
    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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    80
    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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    80
    Thermo Fisher dithiothrectol
    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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    78
    Thermo Fisher dithiothreatol
    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 .
    Dithiothreatol, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 78/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    83
    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.
    Dtt Stock, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 83/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    Thermo Fisher nupage buffer 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.
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    80
    Thermo Fisher ultra pure 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.
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    79
    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: 79/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    Thermo Fisher sonication 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.
    Sonication Dtt, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 79/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    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: 77/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    79
    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: 79/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    82
    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: 82/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    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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    83
    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.
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    90
    Thermo Fisher nupage lds sample 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.
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    78
    Thermo Fisher dtt pt7cfe1 chis vector
    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 thermofisher 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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    Thermo Fisher lds dtt 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.
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    Thermo Fisher dtt solution
    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 sds dtt gel
    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 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.
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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

    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