m dtt  (Thermo Fisher)


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  • 99
    Name:
    Dithiothreitol DTT
    Description:
    Disufide crosslinks of cystines in proteins can be reduced to cysteine residues by dithiothreitol DTT
    Catalog Number:
    d1532
    Price:
    None
    Applications:
    Cell Analysis|Labeling Thiols|Other Thiol-Reactive Probes|Protein, Peptide & Antibody Labeling|Labeling Chemistry
    Category:
    Lab Reagents and Chemicals
    Buy from Supplier


    Structured Review

    Thermo Fisher m dtt
    Variations in the patterns of inhibition of GSH- or <t>DTT-catalyzed</t> T 4 to T 3 conversion by P135S <t>D2</t> using PTU. A, Competitive inhibition of DTT by PTU at a fixed T 4 concentration (3 μ m ). B, Uncompetitive inhibition of T 4 deiodination catalyzed by
    Disufide crosslinks of cystines in proteins can be reduced to cysteine residues by dithiothreitol DTT
    https://www.bioz.com/result/m dtt/product/Thermo Fisher
    Average 99 stars, based on 29 article reviews
    Price from $9.99 to $1999.99
    m dtt - by Bioz Stars, 2020-09
    99/100 stars

    Images

    1) Product Images from "Substitution of Serine for Proline in the Active Center of Type 2 Iodothyronine Deiodinase Substantially Alters Its in Vitro Biochemical Properties with Dithiothreitol But Not Its Function in Intact Cells"

    Article Title: Substitution of Serine for Proline in the Active Center of Type 2 Iodothyronine Deiodinase Substantially Alters Its in Vitro Biochemical Properties with Dithiothreitol But Not Its Function in Intact Cells

    Journal: Endocrinology

    doi: 10.1210/en.2009-0980

    Variations in the patterns of inhibition of GSH- or DTT-catalyzed T 4 to T 3 conversion by P135S D2 using PTU. A, Competitive inhibition of DTT by PTU at a fixed T 4 concentration (3 μ m ). B, Uncompetitive inhibition of T 4 deiodination catalyzed by
    Figure Legend Snippet: Variations in the patterns of inhibition of GSH- or DTT-catalyzed T 4 to T 3 conversion by P135S D2 using PTU. A, Competitive inhibition of DTT by PTU at a fixed T 4 concentration (3 μ m ). B, Uncompetitive inhibition of T 4 deiodination catalyzed by

    Techniques Used: Inhibition, Concentration Assay

    Lineweaver-Burk plots comparing wt D2 and D2 P135S kinetics with respect to T 4 using DTT or GSH as cofactor. A, Double-reciprocal plot of wt D2 activity using DTT 20 m m as cofactor and varying T 4 concentrations. B, Double-reciprocal plot of wt D2 activity
    Figure Legend Snippet: Lineweaver-Burk plots comparing wt D2 and D2 P135S kinetics with respect to T 4 using DTT or GSH as cofactor. A, Double-reciprocal plot of wt D2 activity using DTT 20 m m as cofactor and varying T 4 concentrations. B, Double-reciprocal plot of wt D2 activity

    Techniques Used: Activity Assay

    2) Product Images from "Polysulfides Link H2S to Protein Thiol Oxidation"

    Article Title: Polysulfides Link H2S to Protein Thiol Oxidation

    Journal: Antioxidants & Redox Signaling

    doi: 10.1089/ars.2012.5041

    Polysulfides inhibit PTEN by sulfane sulfur addition. (A) Recombinant PTEN-WT was prereduced with 20 m M DTT for 10 min, followed by buffer exchange into a nonreducing PTEN assay buffer and exposure to 100 μ M H 2 O 2 or NaHS
    Figure Legend Snippet: Polysulfides inhibit PTEN by sulfane sulfur addition. (A) Recombinant PTEN-WT was prereduced with 20 m M DTT for 10 min, followed by buffer exchange into a nonreducing PTEN assay buffer and exposure to 100 μ M H 2 O 2 or NaHS

    Techniques Used: Recombinant, Buffer Exchange

    3) Product Images from "Polysulfides Link H2S to Protein Thiol Oxidation"

    Article Title: Polysulfides Link H2S to Protein Thiol Oxidation

    Journal: Antioxidants & Redox Signaling

    doi: 10.1089/ars.2012.5041

    Polysulfides inhibit PTEN by sulfane sulfur addition. (A) Recombinant PTEN-WT was prereduced with 20 m M DTT for 10 min, followed by buffer exchange into a nonreducing PTEN assay buffer and exposure to 100 μ M H 2 O 2 or NaHS
    Figure Legend Snippet: Polysulfides inhibit PTEN by sulfane sulfur addition. (A) Recombinant PTEN-WT was prereduced with 20 m M DTT for 10 min, followed by buffer exchange into a nonreducing PTEN assay buffer and exposure to 100 μ M H 2 O 2 or NaHS

    Techniques Used: Recombinant, Buffer Exchange

    Related Articles

    Concentration Assay:

    Article Title: H2O2 dynamics in the malaria parasite Plasmodium falciparum
    Article Snippet: .. Purified recombinant roGFP2-Orp1 and HyPer-3/SypHer proteins were reduced with 5 mM DTT for 10 min and 20 mM DTT for 30 min, respectively, at 4°C, desalinated (ZebaTM Spin Desalting Columns, Thermo Scientific), and diluted in reaction buffer to a final concentration of 5 μ M. A 5-fold drug/redox-active compound dilution (25 μ l) was mixed with 100 μ l of 5 μ M roGFP2-Orp1/HyPer in a 96-well microplate (black, half-area, Greiner Bio-One, Frickenhausen). .. Prior to fluorescence measurements via plate reader, protein concentration and loading time were optimized.

    Incubation:

    Article Title: Neuronal Microtubule-associated Protein 2D Is a Dual A-kinase Anchoring Protein Expressed in Rat Ovarian Granulosa Cells *
    Article Snippet: .. For PKA R subunit immunoprecipitations from ovarian extracts and DEAE fractions, samples (containing 500 –800 μg of protein in ovarian extracts or 1 ml from pooled DEAE fractions collected in the absence of DTT) were incubated with 1 μM dithiobis[succinimidylpropionate] (DSP) (Pierce) in dimethyl sulfoxide for 15 min at room temperature. .. The cross-linking reaction was stopped by adding 1 M Tris-HCl, pH 7.5, to a final concentration of 25 mM and incubating samples at room temperature for 15 min. Antibody (10 μl of anti-MAP2 (Sigma), 25 μl of anti-RI (BD Biosciences), 20 μl of anti-RII (Upstate Biotechnology), 10 μl of anti-HA as a nonimmune (NI) control, 10 μl of anti-RIIβ (BD Biosciences Transduction Laboratories)) and 30 μl of protein A+G-agarose was added and incubated for 4 h at 4 °C.

    Recombinant:

    Article Title: H2O2 dynamics in the malaria parasite Plasmodium falciparum
    Article Snippet: .. Purified recombinant roGFP2-Orp1 and HyPer-3/SypHer proteins were reduced with 5 mM DTT for 10 min and 20 mM DTT for 30 min, respectively, at 4°C, desalinated (ZebaTM Spin Desalting Columns, Thermo Scientific), and diluted in reaction buffer to a final concentration of 5 μ M. A 5-fold drug/redox-active compound dilution (25 μ l) was mixed with 100 μ l of 5 μ M roGFP2-Orp1/HyPer in a 96-well microplate (black, half-area, Greiner Bio-One, Frickenhausen). .. Prior to fluorescence measurements via plate reader, protein concentration and loading time were optimized.

    SDS Page:

    Article Title: Physicochemical properties that control protein aggregation also determine whether a protein is retained or released from necrotic cells
    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). .. After electrophoresis, the gel was stained with InstantBlue protein stain and cut into approximately 2 × 6 mm slices then each slice further cut into 1 mm2 pieces.

    Purification:

    Article Title: H2O2 dynamics in the malaria parasite Plasmodium falciparum
    Article Snippet: .. Purified recombinant roGFP2-Orp1 and HyPer-3/SypHer proteins were reduced with 5 mM DTT for 10 min and 20 mM DTT for 30 min, respectively, at 4°C, desalinated (ZebaTM Spin Desalting Columns, Thermo Scientific), and diluted in reaction buffer to a final concentration of 5 μ M. A 5-fold drug/redox-active compound dilution (25 μ l) was mixed with 100 μ l of 5 μ M roGFP2-Orp1/HyPer in a 96-well microplate (black, half-area, Greiner Bio-One, Frickenhausen). .. Prior to fluorescence measurements via plate reader, protein concentration and loading time were optimized.

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  • 99
    Thermo Fisher m dithiothreitol
    Redox potential of the MetAP2 disulfide bond. A , the labeling of fully reduced MetAP2 by the biotin-linked maleimide, MPB, was used to calculate the ratio of reduced to oxidized enzyme as a function of the ratio of reduced (DTT red ) to oxidized (DTT ox ) <t>dithiothreitol.</t> Biotin incorporation was measured by SDS-PAGE and blotting with streptavidin-peroxidase. B , plot of the ratio of reduced to oxidized MetAP2 as a function of the ratio of reduced to oxidized DTT. The solid line . The calculated equilibrium constant is 0.028 (95% confidence interval: 0.012–0.044). From the Nernst equation, the standard redox potential of the Cys 228 -Cys 448 disulfide is −261 mV. Data points and error bars , mean ± S.E. of three independent experiments. C , the initial rate of hydrolysis of Met-Gly-Pro-AMC by fully oxidized or reduced MetAP2 was used to calculate the ratio of reduced to oxidized enzyme as a function of the ratio of reduced (Trx red ) to oxidized (Trx ox ) thioredoxin. The solid line . The calculated equilibrium constant is 0.740 (95% confidence interval: 0.600–0.688), which equates to a standard redox potential of −266 mV for the Cys 228 -Cys 448 disulfide bond. Data points and error bars , mean ± S.E. of three independent experiments.
    M Dithiothreitol, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 94 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/m dithiothreitol/product/Thermo Fisher
    Average 99 stars, based on 94 article reviews
    Price from $9.99 to $1999.99
    m dithiothreitol - by Bioz Stars, 2020-09
    99/100 stars
      Buy from Supplier

    Image Search Results


    Redox potential of the MetAP2 disulfide bond. A , the labeling of fully reduced MetAP2 by the biotin-linked maleimide, MPB, was used to calculate the ratio of reduced to oxidized enzyme as a function of the ratio of reduced (DTT red ) to oxidized (DTT ox ) dithiothreitol. Biotin incorporation was measured by SDS-PAGE and blotting with streptavidin-peroxidase. B , plot of the ratio of reduced to oxidized MetAP2 as a function of the ratio of reduced to oxidized DTT. The solid line . The calculated equilibrium constant is 0.028 (95% confidence interval: 0.012–0.044). From the Nernst equation, the standard redox potential of the Cys 228 -Cys 448 disulfide is −261 mV. Data points and error bars , mean ± S.E. of three independent experiments. C , the initial rate of hydrolysis of Met-Gly-Pro-AMC by fully oxidized or reduced MetAP2 was used to calculate the ratio of reduced to oxidized enzyme as a function of the ratio of reduced (Trx red ) to oxidized (Trx ox ) thioredoxin. The solid line . The calculated equilibrium constant is 0.740 (95% confidence interval: 0.600–0.688), which equates to a standard redox potential of −266 mV for the Cys 228 -Cys 448 disulfide bond. Data points and error bars , mean ± S.E. of three independent experiments.

    Journal: The Journal of Biological Chemistry

    Article Title: Redox Regulation of Methionine Aminopeptidase 2 Activity *

    doi: 10.1074/jbc.M114.554253

    Figure Lengend Snippet: Redox potential of the MetAP2 disulfide bond. A , the labeling of fully reduced MetAP2 by the biotin-linked maleimide, MPB, was used to calculate the ratio of reduced to oxidized enzyme as a function of the ratio of reduced (DTT red ) to oxidized (DTT ox ) dithiothreitol. Biotin incorporation was measured by SDS-PAGE and blotting with streptavidin-peroxidase. B , plot of the ratio of reduced to oxidized MetAP2 as a function of the ratio of reduced to oxidized DTT. The solid line . The calculated equilibrium constant is 0.028 (95% confidence interval: 0.012–0.044). From the Nernst equation, the standard redox potential of the Cys 228 -Cys 448 disulfide is −261 mV. Data points and error bars , mean ± S.E. of three independent experiments. C , the initial rate of hydrolysis of Met-Gly-Pro-AMC by fully oxidized or reduced MetAP2 was used to calculate the ratio of reduced to oxidized enzyme as a function of the ratio of reduced (Trx red ) to oxidized (Trx ox ) thioredoxin. The solid line . The calculated equilibrium constant is 0.740 (95% confidence interval: 0.600–0.688), which equates to a standard redox potential of −266 mV for the Cys 228 -Cys 448 disulfide bond. Data points and error bars , mean ± S.E. of three independent experiments.

    Article Snippet: Just before use, the active site disulfide bond of the oxidoreductase was reduced with 50 m m dithiothreitol and 50 m m tris-(2-carboxyethyl)phosphine (TCEP) for 1 h at 25 °C, and the reducing agents were removed by two passes through Zeba spin desalting columns equilibrated with phosphate-buffered saline (Thermo Scientific).

    Techniques: Labeling, SDS Page

    Polysulfides inhibit PTEN by sulfane sulfur addition. (A) Recombinant PTEN-WT was prereduced with 20 m M DTT for 10 min, followed by buffer exchange into a nonreducing PTEN assay buffer and exposure to 100 μ M H 2 O 2 or NaHS

    Journal: Antioxidants & Redox Signaling

    Article Title: Polysulfides Link H2S to Protein Thiol Oxidation

    doi: 10.1089/ars.2012.5041

    Figure Lengend Snippet: Polysulfides inhibit PTEN by sulfane sulfur addition. (A) Recombinant PTEN-WT was prereduced with 20 m M DTT for 10 min, followed by buffer exchange into a nonreducing PTEN assay buffer and exposure to 100 μ M H 2 O 2 or NaHS

    Article Snippet: Typically, roGFP2-His was prereduced with 20 m M DTT for 10 min before the experiment, and passed through gel filtration columns (Thermo Scientific) pre-equilibrated with the roGFP2 assay buffer to remove DTT immediately before the start of the assay.

    Techniques: Recombinant, Buffer Exchange