buffer 4  (New England Biolabs)


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    Structured Review

    New England Biolabs buffer 4
    Buffer 4, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/buffer 4/product/New England Biolabs
    Average 90 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
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    90/100 stars

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    Polymerase Chain Reaction:

    Article Title: Aerobic degradation of dichlorinated dibenzo-p-dioxin and dichlorinated dibenzofuran by bacteria strains obtained from tropical contaminated soil.
    Article Snippet: .. Bacterial diversity and aerobic catabolic competence of dioxin-degrading bacterial strains isolated from a polluted soil in the tropics were explored. .. Bacterial diversity and aerobic catabolic competence of dioxin-degrading bacterial strains isolated from a polluted soil in the tropics were explored.

    Concentration Assay:

    Article Title: 5-Hydroxymethylcytosine as a clinical biomarker: Fluorescence-based assay for high-throughput epigenetic quantification in human tissues.
    Article Snippet: .. 5-hmC labeling 5-hmC residues were fluorescently labeled via a two-step chemoenzymatic reaction.7,13,27,28 In each reaction tube, 1 μg of genomic DNA was mixed with 3 μl of 10× buffer 4 (New England Biolabs, Ipswich, MA), uridine diphosphate-6-azideglucose (UDP-6-N3-Glu) 29 to a final concentration of 45 μM, 2 μl (20 units) of T4 phage β-glucosyltransferase (T4-BGT, New England Biolabs) and ultrapure water to a final volume of 30 μl. .. The reaction mixture was incubated overnight at 37 C. The following day, Dibenzocyclooctyl (DBCO)-PEG4-5/6TAMRA (Jena Bioscience, Jena, Germany) was added to a final concentration of 150 μM, and the reaction was incubated overnight at 37 C. The labeled DNA samples were purified from excess fluorophores using Oligo Clean Concentrator columns (Zymo research), according to manufacturer’s recommendations, with three washing steps for optimal results.

    Labeling:

    Article Title: 5-Hydroxymethylcytosine as a clinical biomarker: Fluorescence-based assay for high-throughput epigenetic quantification in human tissues.
    Article Snippet: .. 5-hmC labeling 5-hmC residues were fluorescently labeled via a two-step chemoenzymatic reaction.7,13,27,28 In each reaction tube, 1 μg of genomic DNA was mixed with 3 μl of 10× buffer 4 (New England Biolabs, Ipswich, MA), uridine diphosphate-6-azideglucose (UDP-6-N3-Glu) 29 to a final concentration of 45 μM, 2 μl (20 units) of T4 phage β-glucosyltransferase (T4-BGT, New England Biolabs) and ultrapure water to a final volume of 30 μl. .. The reaction mixture was incubated overnight at 37 C. The following day, Dibenzocyclooctyl (DBCO)-PEG4-5/6TAMRA (Jena Bioscience, Jena, Germany) was added to a final concentration of 150 μM, and the reaction was incubated overnight at 37 C. The labeled DNA samples were purified from excess fluorophores using Oligo Clean Concentrator columns (Zymo research), according to manufacturer’s recommendations, with three washing steps for optimal results.

    Purification:

    Article Title: Aerobic degradation of dichlorinated dibenzo-p-dioxin and dichlorinated dibenzofuran by bacteria strains obtained from tropical contaminated soil.
    Article Snippet: .. Bacterial diversity and aerobic catabolic competence of dioxin-degrading bacterial strains isolated from a polluted soil in the tropics were explored. .. Bacterial diversity and aerobic catabolic competence of dioxin-degrading bacterial strains isolated from a polluted soil in the tropics were explored.

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  • 96
    New England Biolabs t4 rna ligase buffer
    DSSS protocol workflow. ( A ) Fragmentation. RNA is fragmented to sizes in the range of 60–200 nt. ( B ) Dephosphorylation. 5′ phosphates are removed from RNA by treatment with alkaline phosphatase. ( C ) 3′ adapter ligation. Dephosphorylated 200-nt-long RNA fragments are selected by urea-PAGE. The 3′ adapter is ligated to the 3′ ends using <t>T4</t> RNA ligase I. ( D ) Rephosphorylation. Fragments are rephosphorylated by treatment with T4 polynucleotide kinase as preparation for the next ligation step. ( E ) 5′ adapter ligation, preceded by removal of the nonligated 3′adapter by urea-PAGE size selection. ( F ) Reverse transcription (RT) and amplification of library. Molecules with 5′ and 3′ adapters were selected by urea-PAGE. First strand cDNA synthesis and PCR amplification were carried out with the indicated primers. ( G ) Sequencing.
    T4 Rna Ligase Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 96/100, based on 35 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    New England Biolabs methyltransferase buffer
    Single-Molecule Detection of CMG Pausing at a Lagging-Strand <t>Methyltransferase</t> Block (A) Schematic representation of experimental approach used in single-molecule DNA unwinding assays. (B) Images of a sample field of view showing accumulation of EGFP-RPA fluorescence signal at different time points from the addition of EGFP-RPA into the chamber. (C) Example unwinding traces of DNA substrates without a protein barrier. Traces exhibit a signal drop upon completion of unwinding due to dissociation of the leading-strand template (depicted in A). (D) Distribution of average fork rates measured in fully unwound substrates without MH (black) and after bypassing MH Lag (blue). Number of molecules are n(-MH) = 199, n(MH Lag after pause) = 20. (E) Sample unwinding traces of DNA substrates modified with MH Lag . Pausing observed at 800 bp is highlighted with gray rectangle. (F) Distribution of pause durations observed in molecules exhibiting a pausing event (n = 109). The solid line is a fit to a single exponential. See also Figure S6 .
    Methyltransferase Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 94/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    New England Biolabs ck2 buffer
    Phosphorylation of PACSIN 1 at serine 358 by <t>CK2.</t> A , scheme of PACSIN 1 represents its domain structure and location of Ser 358 . B , recombinant wild-type PACSIN 1 ( P1 wt ) and PACSIN 1 S358A ( P1 S358A ) were purified as GST fusion proteins, and GST was removed by proteolytic cleavage. The proteins were incubated with CK2 and [γ- 32 P]ATP for 20 min and analyzed by SDS-PAGE. The SDS-polyacrylamide gel was stained with Coomassie Brilliant Blue, dried, and exposed to an x-ray film. C , recombinant proteins including GST and an unrelated mutant PACSIN 1 T25A ( P1 T25A ) as controls were incubated with (+) or without (−) CK2, resolved by native PAGE, and immunoblotted with antibodies specific for PACSIN 1 or PACSIN 1 pS358. D , for kinetic analysis wild-type PACSIN 1 (P1 wt) was incubated with CK2 for the indicated time periods, separated by native PAGE and immunoblotted ( WB ) for PACSIN 1.
    Ck2 Buffer, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    New England Biolabs supercoiled 3 h puc19 plasmid dna
    Comparison of <t>pUC19</t> L <t>DNA</t> exposed to the same number (~2 × 10 11 ) of 125 IEH and 123 IEH decays per μ g DNA: (−) and (+) indicate absence and presence of radioiodinated ligand, respectively.
    Supercoiled 3 H Puc19 Plasmid Dna, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    DSSS protocol workflow. ( A ) Fragmentation. RNA is fragmented to sizes in the range of 60–200 nt. ( B ) Dephosphorylation. 5′ phosphates are removed from RNA by treatment with alkaline phosphatase. ( C ) 3′ adapter ligation. Dephosphorylated 200-nt-long RNA fragments are selected by urea-PAGE. The 3′ adapter is ligated to the 3′ ends using T4 RNA ligase I. ( D ) Rephosphorylation. Fragments are rephosphorylated by treatment with T4 polynucleotide kinase as preparation for the next ligation step. ( E ) 5′ adapter ligation, preceded by removal of the nonligated 3′adapter by urea-PAGE size selection. ( F ) Reverse transcription (RT) and amplification of library. Molecules with 5′ and 3′ adapters were selected by urea-PAGE. First strand cDNA synthesis and PCR amplification were carried out with the indicated primers. ( G ) Sequencing.

    Journal: Genome Research

    Article Title: Strand-specific deep sequencing of the transcriptome

    doi: 10.1101/gr.094318.109

    Figure Lengend Snippet: DSSS protocol workflow. ( A ) Fragmentation. RNA is fragmented to sizes in the range of 60–200 nt. ( B ) Dephosphorylation. 5′ phosphates are removed from RNA by treatment with alkaline phosphatase. ( C ) 3′ adapter ligation. Dephosphorylated 200-nt-long RNA fragments are selected by urea-PAGE. The 3′ adapter is ligated to the 3′ ends using T4 RNA ligase I. ( D ) Rephosphorylation. Fragments are rephosphorylated by treatment with T4 polynucleotide kinase as preparation for the next ligation step. ( E ) 5′ adapter ligation, preceded by removal of the nonligated 3′adapter by urea-PAGE size selection. ( F ) Reverse transcription (RT) and amplification of library. Molecules with 5′ and 3′ adapters were selected by urea-PAGE. First strand cDNA synthesis and PCR amplification were carried out with the indicated primers. ( G ) Sequencing.

    Article Snippet: We incubated the following reaction mixture for 30 min at 37°C: 10 μL of sample, 1 μL of 10× T4 RNA ligase buffer (as fresh ATP supply), 10 U of polynucleotide kinase (New England BioLabs), 3 μL of RNase free water.

    Techniques: De-Phosphorylation Assay, Ligation, Polyacrylamide Gel Electrophoresis, Selection, Amplification, Polymerase Chain Reaction, Sequencing

    Single-Molecule Detection of CMG Pausing at a Lagging-Strand Methyltransferase Block (A) Schematic representation of experimental approach used in single-molecule DNA unwinding assays. (B) Images of a sample field of view showing accumulation of EGFP-RPA fluorescence signal at different time points from the addition of EGFP-RPA into the chamber. (C) Example unwinding traces of DNA substrates without a protein barrier. Traces exhibit a signal drop upon completion of unwinding due to dissociation of the leading-strand template (depicted in A). (D) Distribution of average fork rates measured in fully unwound substrates without MH (black) and after bypassing MH Lag (blue). Number of molecules are n(-MH) = 199, n(MH Lag after pause) = 20. (E) Sample unwinding traces of DNA substrates modified with MH Lag . Pausing observed at 800 bp is highlighted with gray rectangle. (F) Distribution of pause durations observed in molecules exhibiting a pausing event (n = 109). The solid line is a fit to a single exponential. See also Figure S6 .

    Journal: Cell Reports

    Article Title: Dynamics of the Eukaryotic Replicative Helicase at Lagging-Strand Protein Barriers Support the Steric Exclusion Model

    doi: 10.1016/j.celrep.2019.01.086

    Figure Lengend Snippet: Single-Molecule Detection of CMG Pausing at a Lagging-Strand Methyltransferase Block (A) Schematic representation of experimental approach used in single-molecule DNA unwinding assays. (B) Images of a sample field of view showing accumulation of EGFP-RPA fluorescence signal at different time points from the addition of EGFP-RPA into the chamber. (C) Example unwinding traces of DNA substrates without a protein barrier. Traces exhibit a signal drop upon completion of unwinding due to dissociation of the leading-strand template (depicted in A). (D) Distribution of average fork rates measured in fully unwound substrates without MH (black) and after bypassing MH Lag (blue). Number of molecules are n(-MH) = 199, n(MH Lag after pause) = 20. (E) Sample unwinding traces of DNA substrates modified with MH Lag . Pausing observed at 800 bp is highlighted with gray rectangle. (F) Distribution of pause durations observed in molecules exhibiting a pausing event (n = 109). The solid line is a fit to a single exponential. See also Figure S6 .

    Article Snippet: 5FdC-modified fork templates were mixed with HpaII methyltransferase (M.HpaII) in 1:4 DNA to protein molar ratio in methyltransferase buffer (50 mM Tris-HCl, pH 7.5, 0.5 mM 2-mercaptoethanol (β-ME), 10 mM EDTA, NEB) supplemented with 100 μM S-adenosylmethionine (NEB), and incubated at 37°C for 3 hours.

    Techniques: Blocking Assay, Recombinase Polymerase Amplification, Fluorescence, Modification

    Phosphorylation of PACSIN 1 at serine 358 by CK2. A , scheme of PACSIN 1 represents its domain structure and location of Ser 358 . B , recombinant wild-type PACSIN 1 ( P1 wt ) and PACSIN 1 S358A ( P1 S358A ) were purified as GST fusion proteins, and GST was removed by proteolytic cleavage. The proteins were incubated with CK2 and [γ- 32 P]ATP for 20 min and analyzed by SDS-PAGE. The SDS-polyacrylamide gel was stained with Coomassie Brilliant Blue, dried, and exposed to an x-ray film. C , recombinant proteins including GST and an unrelated mutant PACSIN 1 T25A ( P1 T25A ) as controls were incubated with (+) or without (−) CK2, resolved by native PAGE, and immunoblotted with antibodies specific for PACSIN 1 or PACSIN 1 pS358. D , for kinetic analysis wild-type PACSIN 1 (P1 wt) was incubated with CK2 for the indicated time periods, separated by native PAGE and immunoblotted ( WB ) for PACSIN 1.

    Journal: The Journal of Biological Chemistry

    Article Title: Casein Kinase 2 Phosphorylation of Protein Kinase C and Casein Kinase 2 Substrate in Neurons (PACSIN) 1 Protein Regulates Neuronal Spine Formation *

    doi: 10.1074/jbc.M113.461293

    Figure Lengend Snippet: Phosphorylation of PACSIN 1 at serine 358 by CK2. A , scheme of PACSIN 1 represents its domain structure and location of Ser 358 . B , recombinant wild-type PACSIN 1 ( P1 wt ) and PACSIN 1 S358A ( P1 S358A ) were purified as GST fusion proteins, and GST was removed by proteolytic cleavage. The proteins were incubated with CK2 and [γ- 32 P]ATP for 20 min and analyzed by SDS-PAGE. The SDS-polyacrylamide gel was stained with Coomassie Brilliant Blue, dried, and exposed to an x-ray film. C , recombinant proteins including GST and an unrelated mutant PACSIN 1 T25A ( P1 T25A ) as controls were incubated with (+) or without (−) CK2, resolved by native PAGE, and immunoblotted with antibodies specific for PACSIN 1 or PACSIN 1 pS358. D , for kinetic analysis wild-type PACSIN 1 (P1 wt) was incubated with CK2 for the indicated time periods, separated by native PAGE and immunoblotted ( WB ) for PACSIN 1.

    Article Snippet: Samples of recombinant proteins (0.5 μg) were incubated at 30 °C for the indicated time periods in CK2 buffer (20 m m Tris, pH 7.5, 50 m m KCl, 10 m m MgCl2 with 200 μ m ATP (or 125 μ m ATP + 0.2 megabecquerel of [γ-32 P]ATP)) and 250 units of CK2 (New England Biolabs).

    Techniques: Recombinant, Purification, Incubation, SDS Page, Staining, Mutagenesis, Clear Native PAGE, Western Blot

    Reduced spine formation in the presence of the PACSIN 1 S358A mutant or after CK2 inhibition. A , rat hippocampal neurons were transfected with either PACSIN 1 wt ( left ). the mutant protein S358A ( right ) or the mutant protein S358D (data not shown) in combination with EGFP to visualize spines ( upper panel ). Enlargements of three dendrite segments of neurons transfected with either PACSIN 1 wt ( left ) or S358A mutant ( right ) are shown. Fewer spines can be detected in neurons expressing PACSIN 1 S358A ( lower panel ). B , quantification of two independent experiments. For each group five dendrites were counted on each of 12 cells, n = 60 dendrites; **, p

    Journal: The Journal of Biological Chemistry

    Article Title: Casein Kinase 2 Phosphorylation of Protein Kinase C and Casein Kinase 2 Substrate in Neurons (PACSIN) 1 Protein Regulates Neuronal Spine Formation *

    doi: 10.1074/jbc.M113.461293

    Figure Lengend Snippet: Reduced spine formation in the presence of the PACSIN 1 S358A mutant or after CK2 inhibition. A , rat hippocampal neurons were transfected with either PACSIN 1 wt ( left ). the mutant protein S358A ( right ) or the mutant protein S358D (data not shown) in combination with EGFP to visualize spines ( upper panel ). Enlargements of three dendrite segments of neurons transfected with either PACSIN 1 wt ( left ) or S358A mutant ( right ) are shown. Fewer spines can be detected in neurons expressing PACSIN 1 S358A ( lower panel ). B , quantification of two independent experiments. For each group five dendrites were counted on each of 12 cells, n = 60 dendrites; **, p

    Article Snippet: Samples of recombinant proteins (0.5 μg) were incubated at 30 °C for the indicated time periods in CK2 buffer (20 m m Tris, pH 7.5, 50 m m KCl, 10 m m MgCl2 with 200 μ m ATP (or 125 μ m ATP + 0.2 megabecquerel of [γ-32 P]ATP)) and 250 units of CK2 (New England Biolabs).

    Techniques: Mutagenesis, Inhibition, Transfection, Expressing

    Model of the mechanism by which PACSIN 1 affects spine formation. A , in the absence of BDNF, overexpression of PACSIN 1 S358A or inhibition of CK2 supports a stable Rac1-NADRIN-PACSIN 1 complex which leads to Rac1 GTP hydrolysis. B , in the presence of BDNF higher levels of activated CK2 phosphorylate PACSIN 1 at Ser 358 which causes a destabilization of the protein complex. This leads to higher concentrations of Rac1 GTP which induces spine formation. TrkB , tropomyosin-related kinase B.

    Journal: The Journal of Biological Chemistry

    Article Title: Casein Kinase 2 Phosphorylation of Protein Kinase C and Casein Kinase 2 Substrate in Neurons (PACSIN) 1 Protein Regulates Neuronal Spine Formation *

    doi: 10.1074/jbc.M113.461293

    Figure Lengend Snippet: Model of the mechanism by which PACSIN 1 affects spine formation. A , in the absence of BDNF, overexpression of PACSIN 1 S358A or inhibition of CK2 supports a stable Rac1-NADRIN-PACSIN 1 complex which leads to Rac1 GTP hydrolysis. B , in the presence of BDNF higher levels of activated CK2 phosphorylate PACSIN 1 at Ser 358 which causes a destabilization of the protein complex. This leads to higher concentrations of Rac1 GTP which induces spine formation. TrkB , tropomyosin-related kinase B.

    Article Snippet: Samples of recombinant proteins (0.5 μg) were incubated at 30 °C for the indicated time periods in CK2 buffer (20 m m Tris, pH 7.5, 50 m m KCl, 10 m m MgCl2 with 200 μ m ATP (or 125 μ m ATP + 0.2 megabecquerel of [γ-32 P]ATP)) and 250 units of CK2 (New England Biolabs).

    Techniques: Over Expression, Inhibition

    Comparison of pUC19 L DNA exposed to the same number (~2 × 10 11 ) of 125 IEH and 123 IEH decays per μ g DNA: (−) and (+) indicate absence and presence of radioiodinated ligand, respectively.

    Journal: International journal of radiation biology

    Article Title: DNA double-strand breaks induced by decay of 123I-labeled Hoechst 33342: Role of DNA topology

    doi: 10.1080/09553000802512568

    Figure Lengend Snippet: Comparison of pUC19 L DNA exposed to the same number (~2 × 10 11 ) of 125 IEH and 123 IEH decays per μ g DNA: (−) and (+) indicate absence and presence of radioiodinated ligand, respectively.

    Article Snippet: Supercoiled 3 H-pUC19 plasmid DNA (100 μ g in 134 μ l 1X PBS, pH 7.4) was digested with EcoRI (1,000 units, 50 μ l) in EcoRI buffer (1×, 500 μ l, New England Biolabs Inc, Beverly MA, USA) for 16 h at 37°C.

    Techniques:

    Quantitative analysis of DNA strand breaks in supercoiled 3 H-pUC19 DNA

    Journal: International journal of radiation biology

    Article Title: DNA double-strand breaks induced by decay of 123I-labeled Hoechst 33342: Role of DNA topology

    doi: 10.1080/09553000802512568

    Figure Lengend Snippet: Quantitative analysis of DNA strand breaks in supercoiled 3 H-pUC19 DNA

    Article Snippet: Supercoiled 3 H-pUC19 plasmid DNA (100 μ g in 134 μ l 1X PBS, pH 7.4) was digested with EcoRI (1,000 units, 50 μ l) in EcoRI buffer (1×, 500 μ l, New England Biolabs Inc, Beverly MA, USA) for 16 h at 37°C.

    Techniques:

    Quantitative analysis of data from agarose gel electrophoresis assessing disappearance of SC 3 H-pUC19 plasmid DNA (A) and appearance of L DNA (B), indicator of DSB formation, as function of accumulated 123 I decays.

    Journal: International journal of radiation biology

    Article Title: DNA double-strand breaks induced by decay of 123I-labeled Hoechst 33342: Role of DNA topology

    doi: 10.1080/09553000802512568

    Figure Lengend Snippet: Quantitative analysis of data from agarose gel electrophoresis assessing disappearance of SC 3 H-pUC19 plasmid DNA (A) and appearance of L DNA (B), indicator of DSB formation, as function of accumulated 123 I decays.

    Article Snippet: Supercoiled 3 H-pUC19 plasmid DNA (100 μ g in 134 μ l 1X PBS, pH 7.4) was digested with EcoRI (1,000 units, 50 μ l) in EcoRI buffer (1×, 500 μ l, New England Biolabs Inc, Beverly MA, USA) for 16 h at 37°C.

    Techniques: Agarose Gel Electrophoresis, Plasmid Preparation

    Agarose gel analysis of L form of 3 H-pUC19 plasmid DNA incubated with 123 IEH at 4°C in PBS (pH 7.4): lane 1, control (no 123 IEH); lane 2, 4.6 × 10 12 decays/ml; lane 3, 8.1 × 10 12 decays/ml; lane 4, 11.5 × 10 12 decays/ml;

    Journal: International journal of radiation biology

    Article Title: DNA double-strand breaks induced by decay of 123I-labeled Hoechst 33342: Role of DNA topology

    doi: 10.1080/09553000802512568

    Figure Lengend Snippet: Agarose gel analysis of L form of 3 H-pUC19 plasmid DNA incubated with 123 IEH at 4°C in PBS (pH 7.4): lane 1, control (no 123 IEH); lane 2, 4.6 × 10 12 decays/ml; lane 3, 8.1 × 10 12 decays/ml; lane 4, 11.5 × 10 12 decays/ml;

    Article Snippet: Supercoiled 3 H-pUC19 plasmid DNA (100 μ g in 134 μ l 1X PBS, pH 7.4) was digested with EcoRI (1,000 units, 50 μ l) in EcoRI buffer (1×, 500 μ l, New England Biolabs Inc, Beverly MA, USA) for 16 h at 37°C.

    Techniques: Agarose Gel Electrophoresis, Plasmid Preparation, Incubation

    Quantitative analysis of data obtained from agarose gel electrophoresis indicating disappearance of L 3 H-pUC19 plasmid DNA after exposure to 123 IEH (●). Error bars are the standard deviation of the mean for three independent experiments. Dotted

    Journal: International journal of radiation biology

    Article Title: DNA double-strand breaks induced by decay of 123I-labeled Hoechst 33342: Role of DNA topology

    doi: 10.1080/09553000802512568

    Figure Lengend Snippet: Quantitative analysis of data obtained from agarose gel electrophoresis indicating disappearance of L 3 H-pUC19 plasmid DNA after exposure to 123 IEH (●). Error bars are the standard deviation of the mean for three independent experiments. Dotted

    Article Snippet: Supercoiled 3 H-pUC19 plasmid DNA (100 μ g in 134 μ l 1X PBS, pH 7.4) was digested with EcoRI (1,000 units, 50 μ l) in EcoRI buffer (1×, 500 μ l, New England Biolabs Inc, Beverly MA, USA) for 16 h at 37°C.

    Techniques: Agarose Gel Electrophoresis, Plasmid Preparation, Standard Deviation

    Agarose gel analysis of SC 3 H-pUC19 plasmid DNA incubated with 123 IEH at 4°C in PBS (pH 7.4): lane 1, control (no 123 IEH); lane 2 9.7 × 10 12 decays/ml; lane 3, 13.7 × 10 12 decays/ml; lane 4, 23.5 × 10 12 decays/ml; lane

    Journal: International journal of radiation biology

    Article Title: DNA double-strand breaks induced by decay of 123I-labeled Hoechst 33342: Role of DNA topology

    doi: 10.1080/09553000802512568

    Figure Lengend Snippet: Agarose gel analysis of SC 3 H-pUC19 plasmid DNA incubated with 123 IEH at 4°C in PBS (pH 7.4): lane 1, control (no 123 IEH); lane 2 9.7 × 10 12 decays/ml; lane 3, 13.7 × 10 12 decays/ml; lane 4, 23.5 × 10 12 decays/ml; lane

    Article Snippet: Supercoiled 3 H-pUC19 plasmid DNA (100 μ g in 134 μ l 1X PBS, pH 7.4) was digested with EcoRI (1,000 units, 50 μ l) in EcoRI buffer (1×, 500 μ l, New England Biolabs Inc, Beverly MA, USA) for 16 h at 37°C.

    Techniques: Agarose Gel Electrophoresis, Plasmid Preparation, Incubation