m dtt  (Bio-Rad)

 
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    Name:
    Dithiothreitol
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    1 g dithiothreitol DTT reducing agent education use only
    Catalog Number:
    1610610EDU
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    Category:
    pGLO SDS PAGE Extension
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    Structured Review

    Bio-Rad m dtt
    Dithiothreitol
    1 g dithiothreitol DTT reducing agent education use only
    https://www.bioz.com/result/m dtt/product/Bio-Rad
    Average 95 stars, based on 28 article reviews
    Price from $9.99 to $1999.99
    m dtt - by Bioz Stars, 2020-09
    95/100 stars

    Images

    1) Product Images from "Iron-Sulfur (Fe-S) Cluster Assembly"

    Article Title: Iron-Sulfur (Fe-S) Cluster Assembly

    Journal: The Journal of Biological Chemistry

    doi: 10.1074/jbc.M110.127449

    Iron-sulfur cluster transfer from SufBC 2 D to AcnB. Holo-SufBC 2 D complex (0.3 nmol), [Fe-S] ( gray bars ), or [Fe-S] + FADH 2 ( hatched bars ), was co-incubated in 10 μl of 50 m m Tris-HCl, pH 7.6, with ( a ) and without ( b ) 5 m m DTT with apo-AcnB (0.2
    Figure Legend Snippet: Iron-sulfur cluster transfer from SufBC 2 D to AcnB. Holo-SufBC 2 D complex (0.3 nmol), [Fe-S] ( gray bars ), or [Fe-S] + FADH 2 ( hatched bars ), was co-incubated in 10 μl of 50 m m Tris-HCl, pH 7.6, with ( a ) and without ( b ) 5 m m DTT with apo-AcnB (0.2

    Techniques Used: Incubation

    2) Product Images from "The SCAN Domain of ZNF174 Is a Dimer"

    Article Title: The SCAN Domain of ZNF174 Is a Dimer

    Journal: The Journal of biological chemistry

    doi: 10.1074/jbc.M109815200

    Sedimentation equilibrium analysis of the SCAN domain. Sedimentation equilibrium analysis of the recombinant SCAN domain from ZNF174 was performed using a Beckman XL-A Analytical Ultracentrifuge with three different protein concentrations in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, at 20 °C. A , a representative log plot from a sample containing 50 μm (subunit) SCAN centrifuged at 16,000 rpm. Shown with the data are the calculated lines that would result for a protein with a subunit mass of 11.56 kDa and with oligomeric subunit stoichiometries of 1, 2, or 3. B , the residuals from a linear regression of the data shown in A above. C , the calculated subunit stoichiometry for each protein concentration. The values were averaged over three separate acquisitions for each of three different rotor speeds. The error bars represent two standard deviations.
    Figure Legend Snippet: Sedimentation equilibrium analysis of the SCAN domain. Sedimentation equilibrium analysis of the recombinant SCAN domain from ZNF174 was performed using a Beckman XL-A Analytical Ultracentrifuge with three different protein concentrations in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, at 20 °C. A , a representative log plot from a sample containing 50 μm (subunit) SCAN centrifuged at 16,000 rpm. Shown with the data are the calculated lines that would result for a protein with a subunit mass of 11.56 kDa and with oligomeric subunit stoichiometries of 1, 2, or 3. B , the residuals from a linear regression of the data shown in A above. C , the calculated subunit stoichiometry for each protein concentration. The values were averaged over three separate acquisitions for each of three different rotor speeds. The error bars represent two standard deviations.

    Techniques Used: Sedimentation, Recombinant, Protein Concentration

    Purification of recombinant SCAN domain. A , 4 –12% gradient SDS-polyacrylamide gel. Lane 1 , protein standards; lane 2 , supernatant; lane 3 , GST-Sepharose affinity-purified GST-SCAN domain fusion protein before thrombin cleavage; lane 4 , eluate containing SCAN domain after cleavage with thrombin; lane 5 , SCAN domain after cation exchange chromatography; lane 6 , SCAN domain after size exclusion chromatography. B , analytical size exclusion chromatography of the purified SCAN domain. Recombinant purified SCAN domain (225 μm subunit) in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, was applied to an analytical gel filtration column. The column was calibrated under the same conditions with the following protein standards: thyroglobulin, 670,000 Da, 8.9 min; IgG, 158,000 Da, 11.2 min; ovalbumin, 44,000 Da, 12.5 min; myoglobin 17,000 Da, 14.5 min. The indicated positions for monomer, dimer, and trimer were determined from a linear regression of the standards using a subunit molecular mass of 11.56 kDa for the SCAN domain.
    Figure Legend Snippet: Purification of recombinant SCAN domain. A , 4 –12% gradient SDS-polyacrylamide gel. Lane 1 , protein standards; lane 2 , supernatant; lane 3 , GST-Sepharose affinity-purified GST-SCAN domain fusion protein before thrombin cleavage; lane 4 , eluate containing SCAN domain after cleavage with thrombin; lane 5 , SCAN domain after cation exchange chromatography; lane 6 , SCAN domain after size exclusion chromatography. B , analytical size exclusion chromatography of the purified SCAN domain. Recombinant purified SCAN domain (225 μm subunit) in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, was applied to an analytical gel filtration column. The column was calibrated under the same conditions with the following protein standards: thyroglobulin, 670,000 Da, 8.9 min; IgG, 158,000 Da, 11.2 min; ovalbumin, 44,000 Da, 12.5 min; myoglobin 17,000 Da, 14.5 min. The indicated positions for monomer, dimer, and trimer were determined from a linear regression of the standards using a subunit molecular mass of 11.56 kDa for the SCAN domain.

    Techniques Used: Purification, Recombinant, Affinity Purification, Chromatography, Size-exclusion Chromatography, Filtration

    CD spectroscopy of the SCAN domain. CD spectroscopy of the purified SCAN domain was performed in 25 mm phosphate, 200 mm NaCl, 0.2 mm DTT, pH 6.5. A , CD spectrum of the isolated SCAN domain of ZNF174 (25 μm subunit) at 4 °C. B , thermal denaturation of the SCAN domain of ZNF174. The molar ellipticity at 222 nm at increasing temperatures was determined for the SCAN domain at either 5 μm subunit ( closed circles ) or 2 μm subunit ( open circles ).
    Figure Legend Snippet: CD spectroscopy of the SCAN domain. CD spectroscopy of the purified SCAN domain was performed in 25 mm phosphate, 200 mm NaCl, 0.2 mm DTT, pH 6.5. A , CD spectrum of the isolated SCAN domain of ZNF174 (25 μm subunit) at 4 °C. B , thermal denaturation of the SCAN domain of ZNF174. The molar ellipticity at 222 nm at increasing temperatures was determined for the SCAN domain at either 5 μm subunit ( closed circles ) or 2 μm subunit ( open circles ).

    Techniques Used: Spectroscopy, Purification, Isolation

    Related Articles

    Nucleic Acid Electrophoresis:

    Article Title: Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells
    Article Snippet: .. Resolubilised protein samples from cardiomyocytes were incubated in loading buffer and DTT at room temperature (RT) for 10 min. Proteins were separated by SDS-polyacrylamide gel electrophoresis (PAGE) on 4–20% Mini-PROTEAN TGX Precast Gels (Bio-Rad Laboratories) and transferred to low-fluorescence polyvinylidene fluoride (PVDF) membranes (Bio-Rad Laboratories). .. Membranes were blocked with Odyssey blocking buffer (LI-COR Biosciences).

    Filtration:

    Article Title: A Ribosomal Misincorporation of Lys for Arg in Human Triosephosphate Isomerase Expressed in Escherichia coli Gives Rise to Two Protein Populations
    Article Snippet: .. Generally 300 µl of 20 mM triethanolamine, 0.2 mM EDTA, 200 mM NaCl and 1 mM dithiothreitol (pH 7.4) that contained between 25 to 500 µg of protein were applied and eluted with the same buffer. the columns were calibrated with a gel filtration standard (Bio-Rad) containing the following globular protein markers (molecular mass and retention volumes are reported): thyroglobulin (bovine) (669 kDa, 9.8 ml), γ-globulin (bovine) (158 kDa, 12.9 ml), ovalbumin (chicken) (43 kDa, 15.8 ml), myoglobin (horse) (17 kDa, 17.7 ml), and vitamin B12 (1.35 kDa, 21.1 ml). ..

    Purification:

    Article Title: Redox amplification of apoptosis by caspase-dependent cleavage of glutaredoxin 1 and S-glutathionylation of Fas
    Article Snippet: .. As a control, a portion of the lysate was treated with 50 mM DTT to reduce glutathionylated proteins, and these samples were purified through columns (Micro-BioSpin; Bio-Rad Laboratories) to remove DTT before subsequent IP. .. Alternatively, cells were pretreated with biotinylated glutathione ethyl ester as described previously , and lysates were immunoprecipitated using antibiotin antibody.

    Incubation:

    Article Title: Characterization of SLCO5A1/OATP5A1, a Solute Carrier Transport Protein with Non-Classical Function
    Article Snippet: .. For SDS-urea-PAGE (4–10% acrylamide), the samples were incubated for 10 min at 56°C in SDS-PAGE sample buffer in the absence or presence of 20 mM DTT, and electrophoresed in parallel with a blue-stained molecular-mass marker (Precision Plus Protein All Blue, BioRad, München, Germany). .. To investigate the N-glycosylation state of the proteins, the samples were incubated for 2 h in reducing SDS-PAGE sample buffer with either endoglycosidase H (EndoH) or PNGase F (NEB, Frankfurt/Main, Germany); the PNGase-treated sample was supplemented with 1% (w/v) Nonidet P40 to counteract the SDS-mediated inactivation of PNGaseF.

    Article Title: Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells
    Article Snippet: .. Resolubilised protein samples from cardiomyocytes were incubated in loading buffer and DTT at room temperature (RT) for 10 min. Proteins were separated by SDS-polyacrylamide gel electrophoresis (PAGE) on 4–20% Mini-PROTEAN TGX Precast Gels (Bio-Rad Laboratories) and transferred to low-fluorescence polyvinylidene fluoride (PVDF) membranes (Bio-Rad Laboratories). .. Membranes were blocked with Odyssey blocking buffer (LI-COR Biosciences).

    Polyacrylamide Gel Electrophoresis:

    Article Title: Protein CoAlation: a redox-regulated protein modification by coenzyme A in mammalian cells
    Article Snippet: .. Resolubilised protein samples from cardiomyocytes were incubated in loading buffer and DTT at room temperature (RT) for 10 min. Proteins were separated by SDS-polyacrylamide gel electrophoresis (PAGE) on 4–20% Mini-PROTEAN TGX Precast Gels (Bio-Rad Laboratories) and transferred to low-fluorescence polyvinylidene fluoride (PVDF) membranes (Bio-Rad Laboratories). .. Membranes were blocked with Odyssey blocking buffer (LI-COR Biosciences).

    Marker:

    Article Title: Characterization of SLCO5A1/OATP5A1, a Solute Carrier Transport Protein with Non-Classical Function
    Article Snippet: .. For SDS-urea-PAGE (4–10% acrylamide), the samples were incubated for 10 min at 56°C in SDS-PAGE sample buffer in the absence or presence of 20 mM DTT, and electrophoresed in parallel with a blue-stained molecular-mass marker (Precision Plus Protein All Blue, BioRad, München, Germany). .. To investigate the N-glycosylation state of the proteins, the samples were incubated for 2 h in reducing SDS-PAGE sample buffer with either endoglycosidase H (EndoH) or PNGase F (NEB, Frankfurt/Main, Germany); the PNGase-treated sample was supplemented with 1% (w/v) Nonidet P40 to counteract the SDS-mediated inactivation of PNGaseF.

    Silver Staining:

    Article Title: Apical Surface Expression of Aspartic Protease Plasmepsin 4, a Potential Transmission-blocking Target of the Plasmodium Ookinete *
    Article Snippet: .. Resolved proteins were equilibrated for 15 min in buffer I consisting of 6 m urea, 0.376 m Tris-HCl, pH 9.4, 2% SDS, 2% dithiothreitol and buffer II consisting of 6 m urea, 0.376 m Tris-HCl, pH 9.4, 2% SDS, 3% iodoacetamide and then washed with SDS running buffer and separated with SDS-PAGE using 12.5% Tris-HCl gels in a Protean II apparatus (Bio-Rad) operated at 200 V for 57 min. Mass spectrometry-compatible silver staining (Silverquest silver staining kit, Invitrogen) was used to detect proteins. .. Gel spots were manually excised, digested with trypsin, and submitted for mass spectrometry analysis.

    SDS Page:

    Article Title: Characterization of SLCO5A1/OATP5A1, a Solute Carrier Transport Protein with Non-Classical Function
    Article Snippet: .. For SDS-urea-PAGE (4–10% acrylamide), the samples were incubated for 10 min at 56°C in SDS-PAGE sample buffer in the absence or presence of 20 mM DTT, and electrophoresed in parallel with a blue-stained molecular-mass marker (Precision Plus Protein All Blue, BioRad, München, Germany). .. To investigate the N-glycosylation state of the proteins, the samples were incubated for 2 h in reducing SDS-PAGE sample buffer with either endoglycosidase H (EndoH) or PNGase F (NEB, Frankfurt/Main, Germany); the PNGase-treated sample was supplemented with 1% (w/v) Nonidet P40 to counteract the SDS-mediated inactivation of PNGaseF.

    Article Title: Apical Surface Expression of Aspartic Protease Plasmepsin 4, a Potential Transmission-blocking Target of the Plasmodium Ookinete *
    Article Snippet: .. Resolved proteins were equilibrated for 15 min in buffer I consisting of 6 m urea, 0.376 m Tris-HCl, pH 9.4, 2% SDS, 2% dithiothreitol and buffer II consisting of 6 m urea, 0.376 m Tris-HCl, pH 9.4, 2% SDS, 3% iodoacetamide and then washed with SDS running buffer and separated with SDS-PAGE using 12.5% Tris-HCl gels in a Protean II apparatus (Bio-Rad) operated at 200 V for 57 min. Mass spectrometry-compatible silver staining (Silverquest silver staining kit, Invitrogen) was used to detect proteins. .. Gel spots were manually excised, digested with trypsin, and submitted for mass spectrometry analysis.

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  • 99
    Bio-Rad m dtt
    Iron-sulfur cluster transfer from SufBC 2 D to AcnB. Holo-SufBC 2 D complex (0.3 nmol), [Fe-S] ( gray bars ), or [Fe-S] + FADH 2 ( hatched bars ), was co-incubated in 10 μl of 50 m m Tris-HCl, pH 7.6, with ( a ) and without ( b ) 5 m m <t>DTT</t> with <t>apo-AcnB</t> (0.2
    M Dtt, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/m dtt/product/Bio-Rad
    Average 99 stars, based on 28 article reviews
    Price from $9.99 to $1999.99
    m dtt - by Bioz Stars, 2020-09
    99/100 stars
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    Image Search Results


    Iron-sulfur cluster transfer from SufBC 2 D to AcnB. Holo-SufBC 2 D complex (0.3 nmol), [Fe-S] ( gray bars ), or [Fe-S] + FADH 2 ( hatched bars ), was co-incubated in 10 μl of 50 m m Tris-HCl, pH 7.6, with ( a ) and without ( b ) 5 m m DTT with apo-AcnB (0.2

    Journal: The Journal of Biological Chemistry

    Article Title: Iron-Sulfur (Fe-S) Cluster Assembly

    doi: 10.1074/jbc.M110.127449

    Figure Lengend Snippet: Iron-sulfur cluster transfer from SufBC 2 D to AcnB. Holo-SufBC 2 D complex (0.3 nmol), [Fe-S] ( gray bars ), or [Fe-S] + FADH 2 ( hatched bars ), was co-incubated in 10 μl of 50 m m Tris-HCl, pH 7.6, with ( a ) and without ( b ) 5 m m DTT with apo-AcnB (0.2

    Article Snippet: For the experiment in the absence of DTT during the FeS transfer, apo-aconitase B was first pretreated with 5 m m DTT for 30 min, before desalting the protein solution via a MicroBiospin column (Bio-Rad).

    Techniques: Incubation

    Sedimentation equilibrium analysis of the SCAN domain. Sedimentation equilibrium analysis of the recombinant SCAN domain from ZNF174 was performed using a Beckman XL-A Analytical Ultracentrifuge with three different protein concentrations in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, at 20 °C. A , a representative log plot from a sample containing 50 μm (subunit) SCAN centrifuged at 16,000 rpm. Shown with the data are the calculated lines that would result for a protein with a subunit mass of 11.56 kDa and with oligomeric subunit stoichiometries of 1, 2, or 3. B , the residuals from a linear regression of the data shown in A above. C , the calculated subunit stoichiometry for each protein concentration. The values were averaged over three separate acquisitions for each of three different rotor speeds. The error bars represent two standard deviations.

    Journal: The Journal of biological chemistry

    Article Title: The SCAN Domain of ZNF174 Is a Dimer

    doi: 10.1074/jbc.M109815200

    Figure Lengend Snippet: Sedimentation equilibrium analysis of the SCAN domain. Sedimentation equilibrium analysis of the recombinant SCAN domain from ZNF174 was performed using a Beckman XL-A Analytical Ultracentrifuge with three different protein concentrations in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, at 20 °C. A , a representative log plot from a sample containing 50 μm (subunit) SCAN centrifuged at 16,000 rpm. Shown with the data are the calculated lines that would result for a protein with a subunit mass of 11.56 kDa and with oligomeric subunit stoichiometries of 1, 2, or 3. B , the residuals from a linear regression of the data shown in A above. C , the calculated subunit stoichiometry for each protein concentration. The values were averaged over three separate acquisitions for each of three different rotor speeds. The error bars represent two standard deviations.

    Article Snippet: Recombinant purified SCAN domain (225 μ m subunit) in 25 m m phosphate, 200 m m NaCl, 1 m m DTT, pH 6.5 was applied a Bio-Sil SEC 250-5 analytical gel filtration column (Bio-Rad) at 0.7 ml/min with a back-pressure of 800 p.s.i. using a Biologic HR chromatography system (Bio-Rad).

    Techniques: Sedimentation, Recombinant, Protein Concentration

    Purification of recombinant SCAN domain. A , 4 –12% gradient SDS-polyacrylamide gel. Lane 1 , protein standards; lane 2 , supernatant; lane 3 , GST-Sepharose affinity-purified GST-SCAN domain fusion protein before thrombin cleavage; lane 4 , eluate containing SCAN domain after cleavage with thrombin; lane 5 , SCAN domain after cation exchange chromatography; lane 6 , SCAN domain after size exclusion chromatography. B , analytical size exclusion chromatography of the purified SCAN domain. Recombinant purified SCAN domain (225 μm subunit) in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, was applied to an analytical gel filtration column. The column was calibrated under the same conditions with the following protein standards: thyroglobulin, 670,000 Da, 8.9 min; IgG, 158,000 Da, 11.2 min; ovalbumin, 44,000 Da, 12.5 min; myoglobin 17,000 Da, 14.5 min. The indicated positions for monomer, dimer, and trimer were determined from a linear regression of the standards using a subunit molecular mass of 11.56 kDa for the SCAN domain.

    Journal: The Journal of biological chemistry

    Article Title: The SCAN Domain of ZNF174 Is a Dimer

    doi: 10.1074/jbc.M109815200

    Figure Lengend Snippet: Purification of recombinant SCAN domain. A , 4 –12% gradient SDS-polyacrylamide gel. Lane 1 , protein standards; lane 2 , supernatant; lane 3 , GST-Sepharose affinity-purified GST-SCAN domain fusion protein before thrombin cleavage; lane 4 , eluate containing SCAN domain after cleavage with thrombin; lane 5 , SCAN domain after cation exchange chromatography; lane 6 , SCAN domain after size exclusion chromatography. B , analytical size exclusion chromatography of the purified SCAN domain. Recombinant purified SCAN domain (225 μm subunit) in 25 mm phosphate, 200 mm NaCl, 1 mm DTT, pH 6.5, was applied to an analytical gel filtration column. The column was calibrated under the same conditions with the following protein standards: thyroglobulin, 670,000 Da, 8.9 min; IgG, 158,000 Da, 11.2 min; ovalbumin, 44,000 Da, 12.5 min; myoglobin 17,000 Da, 14.5 min. The indicated positions for monomer, dimer, and trimer were determined from a linear regression of the standards using a subunit molecular mass of 11.56 kDa for the SCAN domain.

    Article Snippet: Recombinant purified SCAN domain (225 μ m subunit) in 25 m m phosphate, 200 m m NaCl, 1 m m DTT, pH 6.5 was applied a Bio-Sil SEC 250-5 analytical gel filtration column (Bio-Rad) at 0.7 ml/min with a back-pressure of 800 p.s.i. using a Biologic HR chromatography system (Bio-Rad).

    Techniques: Purification, Recombinant, Affinity Purification, Chromatography, Size-exclusion Chromatography, Filtration

    CD spectroscopy of the SCAN domain. CD spectroscopy of the purified SCAN domain was performed in 25 mm phosphate, 200 mm NaCl, 0.2 mm DTT, pH 6.5. A , CD spectrum of the isolated SCAN domain of ZNF174 (25 μm subunit) at 4 °C. B , thermal denaturation of the SCAN domain of ZNF174. The molar ellipticity at 222 nm at increasing temperatures was determined for the SCAN domain at either 5 μm subunit ( closed circles ) or 2 μm subunit ( open circles ).

    Journal: The Journal of biological chemistry

    Article Title: The SCAN Domain of ZNF174 Is a Dimer

    doi: 10.1074/jbc.M109815200

    Figure Lengend Snippet: CD spectroscopy of the SCAN domain. CD spectroscopy of the purified SCAN domain was performed in 25 mm phosphate, 200 mm NaCl, 0.2 mm DTT, pH 6.5. A , CD spectrum of the isolated SCAN domain of ZNF174 (25 μm subunit) at 4 °C. B , thermal denaturation of the SCAN domain of ZNF174. The molar ellipticity at 222 nm at increasing temperatures was determined for the SCAN domain at either 5 μm subunit ( closed circles ) or 2 μm subunit ( open circles ).

    Article Snippet: Recombinant purified SCAN domain (225 μ m subunit) in 25 m m phosphate, 200 m m NaCl, 1 m m DTT, pH 6.5 was applied a Bio-Sil SEC 250-5 analytical gel filtration column (Bio-Rad) at 0.7 ml/min with a back-pressure of 800 p.s.i. using a Biologic HR chromatography system (Bio-Rad).

    Techniques: Spectroscopy, Purification, Isolation