2 oh datp  (Jena Bioscience)


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    Name:
    dATP Solution
    Description:

    Catalog Number:
    NU-1001-10ML
    Price:
    525.1
    Category:
    Molecular Biology
    Size:
    10 ml
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    Structured Review

    Jena Bioscience 2 oh datp
    Template base and oxidized nucleotide-dependent comparison of ligation failure. Plots show template base-dependent changes in the products of 5'-adenylation for the substrates C gap , G gap , and T gap ( a ), A gap and A nick ( b ), oxidized nucleotide and template base-dependent changes in the products of 5'-adenylation for 8-oxodATP ( c ) and <t>2-OH-dATP</t> ( d ) for the substrates A gap , C gap , G gap and T gap . Time-dependent changes in ligation products are presented in Supplementary Fig. 1b–d . The data represent mean values with the s.d. from three independent experiments.

    https://www.bioz.com/result/2 oh datp/product/Jena Bioscience
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    2 oh datp - by Bioz Stars, 2021-09
    93/100 stars

    Images

    1) Product Images from "Oxidized nucleotide insertion by pol β confounds ligation during base excision repair"

    Article Title: Oxidized nucleotide insertion by pol β confounds ligation during base excision repair

    Journal: Nature Communications

    doi: 10.1038/ncomms14045

    Template base and oxidized nucleotide-dependent comparison of ligation failure. Plots show template base-dependent changes in the products of 5'-adenylation for the substrates C gap , G gap , and T gap ( a ), A gap and A nick ( b ), oxidized nucleotide and template base-dependent changes in the products of 5'-adenylation for 8-oxodATP ( c ) and 2-OH-dATP ( d ) for the substrates A gap , C gap , G gap and T gap . Time-dependent changes in ligation products are presented in Supplementary Fig. 1b–d . The data represent mean values with the s.d. from three independent experiments.
    Figure Legend Snippet: Template base and oxidized nucleotide-dependent comparison of ligation failure. Plots show template base-dependent changes in the products of 5'-adenylation for the substrates C gap , G gap , and T gap ( a ), A gap and A nick ( b ), oxidized nucleotide and template base-dependent changes in the products of 5'-adenylation for 8-oxodATP ( c ) and 2-OH-dATP ( d ) for the substrates A gap , C gap , G gap and T gap . Time-dependent changes in ligation products are presented in Supplementary Fig. 1b–d . The data represent mean values with the s.d. from three independent experiments.

    Techniques Used: Ligation

    2) Product Images from "Stereospecific targeting of MTH1 by (S)-crizotinib as anticancer strategy"

    Article Title: Stereospecific targeting of MTH1 by (S)-crizotinib as anticancer strategy

    Journal: Nature

    doi: 10.1038/nature13194

    MTH1 is the target of SCH51344 a , Representation of the chemical proteomic workflow. b , Sructures of SCH51344 ( 1 ) and the probe used for affinity purification ( 2 ). c , Results from MS-based proteomic affinity purification experiment using SAINT and competition analysis. Data shown are based on two independent experiments for each condition (n = 2/condition), and each replicate was analysed in two technical replicates. d , ITC data for MTH1 with SCH51344. The measured K d was 49 nM (n = 1). e , SCH51344 inhibits hydrolysis of the MTH1 substrates dGTP, 8-oxo-dGTP, and 2-OH-dATP, respectively. Data are shown for two technical replicates ± SEM and representative for at least duplicate experiments (n ≥ 2). f , Silencing of MTH1 by siRNA impairs colony formation of KRAS-positive SW480 (top) and DLD1 (bottom) cells. Data shown as mean ± SEM and images are representative for triplicate experiments (n = 3) (P
    Figure Legend Snippet: MTH1 is the target of SCH51344 a , Representation of the chemical proteomic workflow. b , Sructures of SCH51344 ( 1 ) and the probe used for affinity purification ( 2 ). c , Results from MS-based proteomic affinity purification experiment using SAINT and competition analysis. Data shown are based on two independent experiments for each condition (n = 2/condition), and each replicate was analysed in two technical replicates. d , ITC data for MTH1 with SCH51344. The measured K d was 49 nM (n = 1). e , SCH51344 inhibits hydrolysis of the MTH1 substrates dGTP, 8-oxo-dGTP, and 2-OH-dATP, respectively. Data are shown for two technical replicates ± SEM and representative for at least duplicate experiments (n ≥ 2). f , Silencing of MTH1 by siRNA impairs colony formation of KRAS-positive SW480 (top) and DLD1 (bottom) cells. Data shown as mean ± SEM and images are representative for triplicate experiments (n = 3) (P

    Techniques Used: Affinity Purification, Mass Spectrometry

    3) Product Images from "Proteomic profiling of small-molecule inhibitors reveals dispensability of MTH1 for cancer cell survival"

    Article Title: Proteomic profiling of small-molecule inhibitors reveals dispensability of MTH1 for cancer cell survival

    Journal: Scientific Reports

    doi: 10.1038/srep26521

    Identification of purine-based MTH1 inhibitors by chemical array screening. ( a ) Representative fluorescent image of the chemical arrays (left) and magnified image of the area in a white square (right). Spot of NPD15095 is indicated by a white arrow. ( b ) Chemical structures of purine-based MTH1 inhibitors. ( c ) Effects of NPD15095 (15095), NPD7155 (7155), NPD9948 (9948), and NPD8880 (8880) on the catalytic activity of MTH1. 8-oxo-dGTP and 2-OH-dATP were used as substrates. Data are shown as mean ± s.d. from three independent experiments.
    Figure Legend Snippet: Identification of purine-based MTH1 inhibitors by chemical array screening. ( a ) Representative fluorescent image of the chemical arrays (left) and magnified image of the area in a white square (right). Spot of NPD15095 is indicated by a white arrow. ( b ) Chemical structures of purine-based MTH1 inhibitors. ( c ) Effects of NPD15095 (15095), NPD7155 (7155), NPD9948 (9948), and NPD8880 (8880) on the catalytic activity of MTH1. 8-oxo-dGTP and 2-OH-dATP were used as substrates. Data are shown as mean ± s.d. from three independent experiments.

    Techniques Used: Activity Assay

    4) Product Images from "Oxidized dNTPs and the OGG1 and MUTYH DNA glycosylases combine to induce CAG/CTG repeat instability"

    Article Title: Oxidized dNTPs and the OGG1 and MUTYH DNA glycosylases combine to induce CAG/CTG repeat instability

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkw170

    Incorporation of 8-oxodGMP and 2-OH-dAMP in TNR sequences. ( A and B ) Incorporation of dGMP and 8-oxodGMP opposite cytosine. ( A ) The primer/template sequence and representative gels are shown. Primer/template substrate (160 nM) (S1/T1) was incubated with POL β and increasing concentration of 8-oxodGTP or dGTP at 37°C for 1 h (0–30 μM and 0–3 μM, respectively). M is the DNA substrate without enzyme. Reaction products were separated by 20% denaturing PAGE at 500 V for 2.5 h. Bands were visualized by fluorescence emission by Typhoon scanner and the analysis of the band intensities was performed by ImageJ software. ( B ) Percentage of incorporated dNMP plotted as a function of added dNTPs. Data were fitted by Kaleidagraph software to evaluate kinetics parameters. ( C and D ) Incorporation of 8-oxodGMP and dTMP opposite adenine. Primer/template sequences is S2/T1 (Supplementary Table S1). Experimental conditions and analyses were as described above. The concentration range of 8-oxodGTP and dTTP was 0–2 μM and 0–1 μM, respectively. ( E – F ) Incorporation of 2-OH-dAMP and dAMP in CAG/CTG repeat sequence. ( E ) Primer/template sequence is S3/T2 (Supplementary Table S1); ( F ) Primer/template duplex (160 nM) was incubated with POL β (0.1U) in 10 μl reaction buffer in the absence of dNTP (lane 1), after addition of 2-OH-dATP (lane 2), dGTP and 2-OH-dATP (lane 3); 2-OH-dATP, dGTP and dCTP (lane 4), dATP (lane 5); dATP and dGTP (lane 6), dATP, dGTP and dCTP (lane 7). All nucleotide triphosphates were at 10 μM final concentration. Reaction products were separated by 15% denaturing PAGE and image acquisition and analysis was performed as described before.
    Figure Legend Snippet: Incorporation of 8-oxodGMP and 2-OH-dAMP in TNR sequences. ( A and B ) Incorporation of dGMP and 8-oxodGMP opposite cytosine. ( A ) The primer/template sequence and representative gels are shown. Primer/template substrate (160 nM) (S1/T1) was incubated with POL β and increasing concentration of 8-oxodGTP or dGTP at 37°C for 1 h (0–30 μM and 0–3 μM, respectively). M is the DNA substrate without enzyme. Reaction products were separated by 20% denaturing PAGE at 500 V for 2.5 h. Bands were visualized by fluorescence emission by Typhoon scanner and the analysis of the band intensities was performed by ImageJ software. ( B ) Percentage of incorporated dNMP plotted as a function of added dNTPs. Data were fitted by Kaleidagraph software to evaluate kinetics parameters. ( C and D ) Incorporation of 8-oxodGMP and dTMP opposite adenine. Primer/template sequences is S2/T1 (Supplementary Table S1). Experimental conditions and analyses were as described above. The concentration range of 8-oxodGTP and dTTP was 0–2 μM and 0–1 μM, respectively. ( E – F ) Incorporation of 2-OH-dAMP and dAMP in CAG/CTG repeat sequence. ( E ) Primer/template sequence is S3/T2 (Supplementary Table S1); ( F ) Primer/template duplex (160 nM) was incubated with POL β (0.1U) in 10 μl reaction buffer in the absence of dNTP (lane 1), after addition of 2-OH-dATP (lane 2), dGTP and 2-OH-dATP (lane 3); 2-OH-dATP, dGTP and dCTP (lane 4), dATP (lane 5); dATP and dGTP (lane 6), dATP, dGTP and dCTP (lane 7). All nucleotide triphosphates were at 10 μM final concentration. Reaction products were separated by 15% denaturing PAGE and image acquisition and analysis was performed as described before.

    Techniques Used: Sequencing, Incubation, Concentration Assay, Polyacrylamide Gel Electrophoresis, Fluorescence, Software, CTG Assay

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    Positron Emission Tomography:

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    Protein Extraction:

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    Jena Bioscience 2 oh datp
    Template base and oxidized nucleotide-dependent comparison of ligation failure. Plots show template base-dependent changes in the products of 5'-adenylation for the substrates C gap , G gap , and T gap ( a ), A gap and A nick ( b ), oxidized nucleotide and template base-dependent changes in the products of 5'-adenylation for 8-oxodATP ( c ) and <t>2-OH-dATP</t> ( d ) for the substrates A gap , C gap , G gap and T gap . Time-dependent changes in ligation products are presented in Supplementary Fig. 1b–d . The data represent mean values with the s.d. from three independent experiments.
    2 Oh Datp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/2 oh datp/product/Jena Bioscience
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    2 oh datp - by Bioz Stars, 2021-09
    93/100 stars
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    Image Search Results


    Template base and oxidized nucleotide-dependent comparison of ligation failure. Plots show template base-dependent changes in the products of 5'-adenylation for the substrates C gap , G gap , and T gap ( a ), A gap and A nick ( b ), oxidized nucleotide and template base-dependent changes in the products of 5'-adenylation for 8-oxodATP ( c ) and 2-OH-dATP ( d ) for the substrates A gap , C gap , G gap and T gap . Time-dependent changes in ligation products are presented in Supplementary Fig. 1b–d . The data represent mean values with the s.d. from three independent experiments.

    Journal: Nature Communications

    Article Title: Oxidized nucleotide insertion by pol β confounds ligation during base excision repair

    doi: 10.1038/ncomms14045

    Figure Lengend Snippet: Template base and oxidized nucleotide-dependent comparison of ligation failure. Plots show template base-dependent changes in the products of 5'-adenylation for the substrates C gap , G gap , and T gap ( a ), A gap and A nick ( b ), oxidized nucleotide and template base-dependent changes in the products of 5'-adenylation for 8-oxodATP ( c ) and 2-OH-dATP ( d ) for the substrates A gap , C gap , G gap and T gap . Time-dependent changes in ligation products are presented in Supplementary Fig. 1b–d . The data represent mean values with the s.d. from three independent experiments.

    Article Snippet: The reaction mixture in a final volume of 10 μl contained 50 mM Tris(HCl), pH 7.5, 100 mM KCl, 10 mM MgCl2 , 1 mM ATP, 100 μg ml−1 BSA, 10% glycerol, 1 mM DTT and 200 μM of an oxidized base nucleotide (8-oxodGTP (Jena Bioscience), 2-OH-dATP (Jena Bioscience) or 8-oxodATP (TriLink Biotechnologies)) or a normal base nucleotide (dGTP, dTTP, dATP, or dTTP (NEB)).

    Techniques: Ligation

    MTH1 is the target of SCH51344 a , Representation of the chemical proteomic workflow. b , Sructures of SCH51344 ( 1 ) and the probe used for affinity purification ( 2 ). c , Results from MS-based proteomic affinity purification experiment using SAINT and competition analysis. Data shown are based on two independent experiments for each condition (n = 2/condition), and each replicate was analysed in two technical replicates. d , ITC data for MTH1 with SCH51344. The measured K d was 49 nM (n = 1). e , SCH51344 inhibits hydrolysis of the MTH1 substrates dGTP, 8-oxo-dGTP, and 2-OH-dATP, respectively. Data are shown for two technical replicates ± SEM and representative for at least duplicate experiments (n ≥ 2). f , Silencing of MTH1 by siRNA impairs colony formation of KRAS-positive SW480 (top) and DLD1 (bottom) cells. Data shown as mean ± SEM and images are representative for triplicate experiments (n = 3) (P

    Journal: Nature

    Article Title: Stereospecific targeting of MTH1 by (S)-crizotinib as anticancer strategy

    doi: 10.1038/nature13194

    Figure Lengend Snippet: MTH1 is the target of SCH51344 a , Representation of the chemical proteomic workflow. b , Sructures of SCH51344 ( 1 ) and the probe used for affinity purification ( 2 ). c , Results from MS-based proteomic affinity purification experiment using SAINT and competition analysis. Data shown are based on two independent experiments for each condition (n = 2/condition), and each replicate was analysed in two technical replicates. d , ITC data for MTH1 with SCH51344. The measured K d was 49 nM (n = 1). e , SCH51344 inhibits hydrolysis of the MTH1 substrates dGTP, 8-oxo-dGTP, and 2-OH-dATP, respectively. Data are shown for two technical replicates ± SEM and representative for at least duplicate experiments (n ≥ 2). f , Silencing of MTH1 by siRNA impairs colony formation of KRAS-positive SW480 (top) and DLD1 (bottom) cells. Data shown as mean ± SEM and images are representative for triplicate experiments (n = 3) (P

    Article Snippet: After addition of the substrate dGTP (Fermentas, final concentration 100 μM), 8-oxo-dGTP (TriLink Biotechnologies, final concentration 13.2 μM), or 2-OH-dATP (Jena Bioscience, final concentration 8.3 μM) the generation of pyrophosphate (PPi) as a result of nucleotide triphosphate hydrolysis by MTH1 was monitored over a time course of 15 min using the PPiLight Inorganic Pyrophosphate Assay kit (Lonza Rockland).

    Techniques: Affinity Purification, Mass Spectrometry

    Identification of purine-based MTH1 inhibitors by chemical array screening. ( a ) Representative fluorescent image of the chemical arrays (left) and magnified image of the area in a white square (right). Spot of NPD15095 is indicated by a white arrow. ( b ) Chemical structures of purine-based MTH1 inhibitors. ( c ) Effects of NPD15095 (15095), NPD7155 (7155), NPD9948 (9948), and NPD8880 (8880) on the catalytic activity of MTH1. 8-oxo-dGTP and 2-OH-dATP were used as substrates. Data are shown as mean ± s.d. from three independent experiments.

    Journal: Scientific Reports

    Article Title: Proteomic profiling of small-molecule inhibitors reveals dispensability of MTH1 for cancer cell survival

    doi: 10.1038/srep26521

    Figure Lengend Snippet: Identification of purine-based MTH1 inhibitors by chemical array screening. ( a ) Representative fluorescent image of the chemical arrays (left) and magnified image of the area in a white square (right). Spot of NPD15095 is indicated by a white arrow. ( b ) Chemical structures of purine-based MTH1 inhibitors. ( c ) Effects of NPD15095 (15095), NPD7155 (7155), NPD9948 (9948), and NPD8880 (8880) on the catalytic activity of MTH1. 8-oxo-dGTP and 2-OH-dATP were used as substrates. Data are shown as mean ± s.d. from three independent experiments.

    Article Snippet: After addition of the mixed reagent from the PPiLight Inorganic Pyrophosphate Assay kit (Lonza Rockland), either 8-oxo-dGTP (13.2 μM; TriLink BioTechnologies) or 2-OH-dATP (8.3 μM; Jena Bioscience) was added as a substrate to initiate the enzymatic reaction.

    Techniques: Activity Assay

    Incorporation of 8-oxodGMP and 2-OH-dAMP in TNR sequences. ( A and B ) Incorporation of dGMP and 8-oxodGMP opposite cytosine. ( A ) The primer/template sequence and representative gels are shown. Primer/template substrate (160 nM) (S1/T1) was incubated with POL β and increasing concentration of 8-oxodGTP or dGTP at 37°C for 1 h (0–30 μM and 0–3 μM, respectively). M is the DNA substrate without enzyme. Reaction products were separated by 20% denaturing PAGE at 500 V for 2.5 h. Bands were visualized by fluorescence emission by Typhoon scanner and the analysis of the band intensities was performed by ImageJ software. ( B ) Percentage of incorporated dNMP plotted as a function of added dNTPs. Data were fitted by Kaleidagraph software to evaluate kinetics parameters. ( C and D ) Incorporation of 8-oxodGMP and dTMP opposite adenine. Primer/template sequences is S2/T1 (Supplementary Table S1). Experimental conditions and analyses were as described above. The concentration range of 8-oxodGTP and dTTP was 0–2 μM and 0–1 μM, respectively. ( E – F ) Incorporation of 2-OH-dAMP and dAMP in CAG/CTG repeat sequence. ( E ) Primer/template sequence is S3/T2 (Supplementary Table S1); ( F ) Primer/template duplex (160 nM) was incubated with POL β (0.1U) in 10 μl reaction buffer in the absence of dNTP (lane 1), after addition of 2-OH-dATP (lane 2), dGTP and 2-OH-dATP (lane 3); 2-OH-dATP, dGTP and dCTP (lane 4), dATP (lane 5); dATP and dGTP (lane 6), dATP, dGTP and dCTP (lane 7). All nucleotide triphosphates were at 10 μM final concentration. Reaction products were separated by 15% denaturing PAGE and image acquisition and analysis was performed as described before.

    Journal: Nucleic Acids Research

    Article Title: Oxidized dNTPs and the OGG1 and MUTYH DNA glycosylases combine to induce CAG/CTG repeat instability

    doi: 10.1093/nar/gkw170

    Figure Lengend Snippet: Incorporation of 8-oxodGMP and 2-OH-dAMP in TNR sequences. ( A and B ) Incorporation of dGMP and 8-oxodGMP opposite cytosine. ( A ) The primer/template sequence and representative gels are shown. Primer/template substrate (160 nM) (S1/T1) was incubated with POL β and increasing concentration of 8-oxodGTP or dGTP at 37°C for 1 h (0–30 μM and 0–3 μM, respectively). M is the DNA substrate without enzyme. Reaction products were separated by 20% denaturing PAGE at 500 V for 2.5 h. Bands were visualized by fluorescence emission by Typhoon scanner and the analysis of the band intensities was performed by ImageJ software. ( B ) Percentage of incorporated dNMP plotted as a function of added dNTPs. Data were fitted by Kaleidagraph software to evaluate kinetics parameters. ( C and D ) Incorporation of 8-oxodGMP and dTMP opposite adenine. Primer/template sequences is S2/T1 (Supplementary Table S1). Experimental conditions and analyses were as described above. The concentration range of 8-oxodGTP and dTTP was 0–2 μM and 0–1 μM, respectively. ( E – F ) Incorporation of 2-OH-dAMP and dAMP in CAG/CTG repeat sequence. ( E ) Primer/template sequence is S3/T2 (Supplementary Table S1); ( F ) Primer/template duplex (160 nM) was incubated with POL β (0.1U) in 10 μl reaction buffer in the absence of dNTP (lane 1), after addition of 2-OH-dATP (lane 2), dGTP and 2-OH-dATP (lane 3); 2-OH-dATP, dGTP and dCTP (lane 4), dATP (lane 5); dATP and dGTP (lane 6), dATP, dGTP and dCTP (lane 7). All nucleotide triphosphates were at 10 μM final concentration. Reaction products were separated by 15% denaturing PAGE and image acquisition and analysis was performed as described before.

    Article Snippet: Reagents 8-oxodGTP was obtained from TriLink (TriLink BioTechnologies, San Diego, CA 92121, USA), dNTPs were from Sigma (Sigma-Aldrich, Corporate Offices St. Louis, MO 63103, USA) and 2-OH-dATP was purchased from Jena (Jena Bioscience GmbH 07749 Jena, DE).

    Techniques: Sequencing, Incubation, Concentration Assay, Polyacrylamide Gel Electrophoresis, Fluorescence, Software, CTG Assay