klenow dna polymerase Search Results


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  • 99
    New England Biolabs klenow dna polymerase
    The principle of PE-PCR for bacterial <t>DNA</t> amplification and detection. A fusion probe is designed with the sequences at the 3′-end corresponding to the bacterial genomic sequences and a non-bacterial tag sequence at the 5′-end. The reaction is initiated by annealing the fusion probe to the template bacterial DNA after heat-denaturing at 95°C for 5 min (Step 1 and 2). An enzyme mix (EK mix) of exo I and <t>Klenow</t> DNA polymerase is then added into the reaction mixture and incubated at 37°C for 2 h (Step 3a and 3b). Following heat-inactivation of EK mix at 80°C for 20 min (Step 3c), a forward primer (non-bac-F) corresponding to the non-bacterial sequence of the fusion probe and a reverse primer (bac-R) targeting bacterial genomic sequence downstream of the fusion probe are used for PCR amplification of the primer extension product (Step 4). In this setting, only template bacterial DNA but not the endogenous contaminated bacterial DNA is amplified (Step 5).
    Klenow Dna Polymerase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1388 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher klenow dna polymerase
    The principle of PE-PCR for bacterial <t>DNA</t> amplification and detection. A fusion probe is designed with the sequences at the 3′-end corresponding to the bacterial genomic sequences and a non-bacterial tag sequence at the 5′-end. The reaction is initiated by annealing the fusion probe to the template bacterial DNA after heat-denaturing at 95°C for 5 min (Step 1 and 2). An enzyme mix (EK mix) of exo I and <t>Klenow</t> DNA polymerase is then added into the reaction mixture and incubated at 37°C for 2 h (Step 3a and 3b). Following heat-inactivation of EK mix at 80°C for 20 min (Step 3c), a forward primer (non-bac-F) corresponding to the non-bacterial sequence of the fusion probe and a reverse primer (bac-R) targeting bacterial genomic sequence downstream of the fusion probe are used for PCR amplification of the primer extension product (Step 4). In this setting, only template bacterial DNA but not the endogenous contaminated bacterial DNA is amplified (Step 5).
    Klenow Dna Polymerase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 413 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore klenow dna polymerase
    The principle of PE-PCR for bacterial <t>DNA</t> amplification and detection. A fusion probe is designed with the sequences at the 3′-end corresponding to the bacterial genomic sequences and a non-bacterial tag sequence at the 5′-end. The reaction is initiated by annealing the fusion probe to the template bacterial DNA after heat-denaturing at 95°C for 5 min (Step 1 and 2). An enzyme mix (EK mix) of exo I and <t>Klenow</t> DNA polymerase is then added into the reaction mixture and incubated at 37°C for 2 h (Step 3a and 3b). Following heat-inactivation of EK mix at 80°C for 20 min (Step 3c), a forward primer (non-bac-F) corresponding to the non-bacterial sequence of the fusion probe and a reverse primer (bac-R) targeting bacterial genomic sequence downstream of the fusion probe are used for PCR amplification of the primer extension product (Step 4). In this setting, only template bacterial DNA but not the endogenous contaminated bacterial DNA is amplified (Step 5).
    Klenow Dna Polymerase, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore dna polymerase alpha
    Loss of E2F1 attenuates <t>DNA</t> repair. A , comet assay expressed as average tail moment on E2F1 +/+ and E2F1 -/- MEFs untreated ( left-hand graph , control), after incubation for 1 h in medium containing 50 μg/ml MMS ( middle graph, 0 h ), and after incubation for 1 h in medium containing 50 μg/ml MMS followed by recovery with incubation in fresh drug-free medium for 2 h ( right-hand graph, R ). Experiments were performed in duplicate, and measurement of mean tail moment was from 50 cells/slide from 15-20 randomly selected fields representing the whole area of each slide. Statistical analysis was performed using unpaired two-tailed t test on comet tail moments that were determined using Comet Assay II software (Perceptive Instruments; Suffolk, UK). Error bars , S.D. from separate experiments. B , indirect immunofluorescence microscopy on XRCC1 immunostaining ( top ), DNA polymerase I-mediated FITC-dUTP labeling assay ( middle ), and 4′,6-diamidino-2-phenylindole ( DAPI ) staining ( bottom ) performed on E2F1 -/- and E2F1 +/+ MEFs untreated ( C ), after incubation for 1 h in medium containing 50 μg/ml MMS ( 0 h panels ), and after incubation for 1 h in medium containing 50 μg/ml MMS followed by recovery with incubation in fresh drug-free medium for 6 h ( R panels ). C , percentage of apoptosis as determined by Annexin V staining and flow cytometry 48 h after infection of the indicated cells with adenovirus expressing wild-type E2F1 ( Adeno-E2F1 ) or adenovirus expressing GFP ( Adeno-control ). Error bars , S.D. of triplicate experiments and statistical analysis performed using Student's unpaired two-tailed t test.
    Dna Polymerase Alpha, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Roche dna polymerase klenow
    Loss of E2F1 attenuates <t>DNA</t> repair. A , comet assay expressed as average tail moment on E2F1 +/+ and E2F1 -/- MEFs untreated ( left-hand graph , control), after incubation for 1 h in medium containing 50 μg/ml MMS ( middle graph, 0 h ), and after incubation for 1 h in medium containing 50 μg/ml MMS followed by recovery with incubation in fresh drug-free medium for 2 h ( right-hand graph, R ). Experiments were performed in duplicate, and measurement of mean tail moment was from 50 cells/slide from 15-20 randomly selected fields representing the whole area of each slide. Statistical analysis was performed using unpaired two-tailed t test on comet tail moments that were determined using Comet Assay II software (Perceptive Instruments; Suffolk, UK). Error bars , S.D. from separate experiments. B , indirect immunofluorescence microscopy on XRCC1 immunostaining ( top ), DNA polymerase I-mediated FITC-dUTP labeling assay ( middle ), and 4′,6-diamidino-2-phenylindole ( DAPI ) staining ( bottom ) performed on E2F1 -/- and E2F1 +/+ MEFs untreated ( C ), after incubation for 1 h in medium containing 50 μg/ml MMS ( 0 h panels ), and after incubation for 1 h in medium containing 50 μg/ml MMS followed by recovery with incubation in fresh drug-free medium for 6 h ( R panels ). C , percentage of apoptosis as determined by Annexin V staining and flow cytometry 48 h after infection of the indicated cells with adenovirus expressing wild-type E2F1 ( Adeno-E2F1 ) or adenovirus expressing GFP ( Adeno-control ). Error bars , S.D. of triplicate experiments and statistical analysis performed using Student's unpaired two-tailed t test.
    Dna Polymerase Klenow, supplied by Roche, used in various techniques. Bioz Stars score: 91/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Becton Dickinson klenow dna polymerase
    Loss of E2F1 attenuates <t>DNA</t> repair. A , comet assay expressed as average tail moment on E2F1 +/+ and E2F1 -/- MEFs untreated ( left-hand graph , control), after incubation for 1 h in medium containing 50 μg/ml MMS ( middle graph, 0 h ), and after incubation for 1 h in medium containing 50 μg/ml MMS followed by recovery with incubation in fresh drug-free medium for 2 h ( right-hand graph, R ). Experiments were performed in duplicate, and measurement of mean tail moment was from 50 cells/slide from 15-20 randomly selected fields representing the whole area of each slide. Statistical analysis was performed using unpaired two-tailed t test on comet tail moments that were determined using Comet Assay II software (Perceptive Instruments; Suffolk, UK). Error bars , S.D. from separate experiments. B , indirect immunofluorescence microscopy on XRCC1 immunostaining ( top ), DNA polymerase I-mediated FITC-dUTP labeling assay ( middle ), and 4′,6-diamidino-2-phenylindole ( DAPI ) staining ( bottom ) performed on E2F1 -/- and E2F1 +/+ MEFs untreated ( C ), after incubation for 1 h in medium containing 50 μg/ml MMS ( 0 h panels ), and after incubation for 1 h in medium containing 50 μg/ml MMS followed by recovery with incubation in fresh drug-free medium for 6 h ( R panels ). C , percentage of apoptosis as determined by Annexin V staining and flow cytometry 48 h after infection of the indicated cells with adenovirus expressing wild-type E2F1 ( Adeno-E2F1 ) or adenovirus expressing GFP ( Adeno-control ). Error bars , S.D. of triplicate experiments and statistical analysis performed using Student's unpaired two-tailed t test.
    Klenow Dna Polymerase, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Promega klenow dna polymerase
    Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U <t>Klenow</t> <t>DNA</t> polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.
    Klenow Dna Polymerase, supplied by Promega, used in various techniques. Bioz Stars score: 92/100, based on 216 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Illumina Inc klenow dna polymerase
    Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U <t>Klenow</t> <t>DNA</t> polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.
    Klenow Dna Polymerase, supplied by Illumina Inc, used in various techniques. Bioz Stars score: 93/100, based on 411 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare klenow dna polymerase
    Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U <t>Klenow</t> <t>DNA</t> polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.
    Klenow Dna Polymerase, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 92/100, based on 113 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Boehringer Mannheim klenow dna polymerase
    Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U <t>Klenow</t> <t>DNA</t> polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.
    Klenow Dna Polymerase, supplied by Boehringer Mannheim, used in various techniques. Bioz Stars score: 92/100, based on 42 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    PerkinElmer klenow dna polymerase
    Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U <t>Klenow</t> <t>DNA</t> polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.
    Klenow Dna Polymerase, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 92/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TaKaRa klenow dna polymerase
    Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U <t>Klenow</t> <t>DNA</t> polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.
    Klenow Dna Polymerase, supplied by TaKaRa, used in various techniques. Bioz Stars score: 92/100, based on 45 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Enzymatics klenow dna polymerase
    Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U <t>Klenow</t> <t>DNA</t> polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.
    Klenow Dna Polymerase, supplied by Enzymatics, used in various techniques. Bioz Stars score: 92/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Thermo Fisher klenow exo dna polymerase
    Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U <t>Klenow</t> <t>DNA</t> polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.
    Klenow Exo Dna Polymerase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 89/100, based on 83 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Promega klenow dna polymerase fragment
    Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U <t>Klenow</t> <t>DNA</t> polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.
    Klenow Dna Polymerase Fragment, supplied by Promega, used in various techniques. Bioz Stars score: 88/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Enzymatics klenow exo dna polymerase
    Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U <t>Klenow</t> <t>DNA</t> polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.
    Klenow Exo Dna Polymerase, supplied by Enzymatics, used in various techniques. Bioz Stars score: 88/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Stratagene exo klenow dna polymerase
    Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U <t>Klenow</t> <t>DNA</t> polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.
    Exo Klenow Dna Polymerase, supplied by Stratagene, used in various techniques. Bioz Stars score: 88/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    GE Healthcare klenow dna polymerase fragment
    Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U <t>Klenow</t> <t>DNA</t> polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.
    Klenow Dna Polymerase Fragment, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 88/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    The principle of PE-PCR for bacterial DNA amplification and detection. A fusion probe is designed with the sequences at the 3′-end corresponding to the bacterial genomic sequences and a non-bacterial tag sequence at the 5′-end. The reaction is initiated by annealing the fusion probe to the template bacterial DNA after heat-denaturing at 95°C for 5 min (Step 1 and 2). An enzyme mix (EK mix) of exo I and Klenow DNA polymerase is then added into the reaction mixture and incubated at 37°C for 2 h (Step 3a and 3b). Following heat-inactivation of EK mix at 80°C for 20 min (Step 3c), a forward primer (non-bac-F) corresponding to the non-bacterial sequence of the fusion probe and a reverse primer (bac-R) targeting bacterial genomic sequence downstream of the fusion probe are used for PCR amplification of the primer extension product (Step 4). In this setting, only template bacterial DNA but not the endogenous contaminated bacterial DNA is amplified (Step 5).

    Journal: PLoS ONE

    Article Title: An Efficient Strategy for Broad-Range Detection of Low Abundance Bacteria without DNA Decontamination of PCR Reagents

    doi: 10.1371/journal.pone.0020303

    Figure Lengend Snippet: The principle of PE-PCR for bacterial DNA amplification and detection. A fusion probe is designed with the sequences at the 3′-end corresponding to the bacterial genomic sequences and a non-bacterial tag sequence at the 5′-end. The reaction is initiated by annealing the fusion probe to the template bacterial DNA after heat-denaturing at 95°C for 5 min (Step 1 and 2). An enzyme mix (EK mix) of exo I and Klenow DNA polymerase is then added into the reaction mixture and incubated at 37°C for 2 h (Step 3a and 3b). Following heat-inactivation of EK mix at 80°C for 20 min (Step 3c), a forward primer (non-bac-F) corresponding to the non-bacterial sequence of the fusion probe and a reverse primer (bac-R) targeting bacterial genomic sequence downstream of the fusion probe are used for PCR amplification of the primer extension product (Step 4). In this setting, only template bacterial DNA but not the endogenous contaminated bacterial DNA is amplified (Step 5).

    Article Snippet: Materials The exo I and Klenow DNA polymerase were purchased from New England Biolab (Ipswich, MA).

    Techniques: Polymerase Chain Reaction, Amplification, Genomic Sequencing, Sequencing, Incubation, BAC Assay

    Loss of E2F1 attenuates DNA repair. A , comet assay expressed as average tail moment on E2F1 +/+ and E2F1 -/- MEFs untreated ( left-hand graph , control), after incubation for 1 h in medium containing 50 μg/ml MMS ( middle graph, 0 h ), and after incubation for 1 h in medium containing 50 μg/ml MMS followed by recovery with incubation in fresh drug-free medium for 2 h ( right-hand graph, R ). Experiments were performed in duplicate, and measurement of mean tail moment was from 50 cells/slide from 15-20 randomly selected fields representing the whole area of each slide. Statistical analysis was performed using unpaired two-tailed t test on comet tail moments that were determined using Comet Assay II software (Perceptive Instruments; Suffolk, UK). Error bars , S.D. from separate experiments. B , indirect immunofluorescence microscopy on XRCC1 immunostaining ( top ), DNA polymerase I-mediated FITC-dUTP labeling assay ( middle ), and 4′,6-diamidino-2-phenylindole ( DAPI ) staining ( bottom ) performed on E2F1 -/- and E2F1 +/+ MEFs untreated ( C ), after incubation for 1 h in medium containing 50 μg/ml MMS ( 0 h panels ), and after incubation for 1 h in medium containing 50 μg/ml MMS followed by recovery with incubation in fresh drug-free medium for 6 h ( R panels ). C , percentage of apoptosis as determined by Annexin V staining and flow cytometry 48 h after infection of the indicated cells with adenovirus expressing wild-type E2F1 ( Adeno-E2F1 ) or adenovirus expressing GFP ( Adeno-control ). Error bars , S.D. of triplicate experiments and statistical analysis performed using Student's unpaired two-tailed t test.

    Journal: The Journal of Biological Chemistry

    Article Title: E2F1 Regulates the Base Excision Repair Gene XRCC1 and Promotes DNA Repair *

    doi: 10.1074/jbc.M710296200

    Figure Lengend Snippet: Loss of E2F1 attenuates DNA repair. A , comet assay expressed as average tail moment on E2F1 +/+ and E2F1 -/- MEFs untreated ( left-hand graph , control), after incubation for 1 h in medium containing 50 μg/ml MMS ( middle graph, 0 h ), and after incubation for 1 h in medium containing 50 μg/ml MMS followed by recovery with incubation in fresh drug-free medium for 2 h ( right-hand graph, R ). Experiments were performed in duplicate, and measurement of mean tail moment was from 50 cells/slide from 15-20 randomly selected fields representing the whole area of each slide. Statistical analysis was performed using unpaired two-tailed t test on comet tail moments that were determined using Comet Assay II software (Perceptive Instruments; Suffolk, UK). Error bars , S.D. from separate experiments. B , indirect immunofluorescence microscopy on XRCC1 immunostaining ( top ), DNA polymerase I-mediated FITC-dUTP labeling assay ( middle ), and 4′,6-diamidino-2-phenylindole ( DAPI ) staining ( bottom ) performed on E2F1 -/- and E2F1 +/+ MEFs untreated ( C ), after incubation for 1 h in medium containing 50 μg/ml MMS ( 0 h panels ), and after incubation for 1 h in medium containing 50 μg/ml MMS followed by recovery with incubation in fresh drug-free medium for 6 h ( R panels ). C , percentage of apoptosis as determined by Annexin V staining and flow cytometry 48 h after infection of the indicated cells with adenovirus expressing wild-type E2F1 ( Adeno-E2F1 ) or adenovirus expressing GFP ( Adeno-control ). Error bars , S.D. of triplicate experiments and statistical analysis performed using Student's unpaired two-tailed t test.

    Article Snippet: Cells were rinsed in phosphate-buffered saline, permeabilized with 1% Triton X-100 for 20 min, and then incubated in a moist air chamber at 37 °C for 90 min in a labeling mixture containing 10 μ m each dGTP, dATP, and dCTP and 7 μ m dTTP, 3 μ m FITC-dUTP, 20 units/ml Escherichia coli DNA polymerase I (Sigma) in reaction buffer containing 5 m m MgCl2 , 10 m m 2-mercaptoethanol, and 20 μg/ml bovine serum albumin.

    Techniques: Single Cell Gel Electrophoresis, Incubation, Two Tailed Test, Software, Immunofluorescence, Microscopy, Immunostaining, Labeling, Staining, Flow Cytometry, Cytometry, Infection, Expressing

    Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U Klenow DNA polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.

    Journal: BioMed Research International

    Article Title: Heparin and Liver Heparan Sulfate Can Rescue Hepatoma Cells from Topotecan Action

    doi: 10.1155/2014/765794

    Figure Lengend Snippet: Differences of topoisomerase I plasmid cleavage activity trapped by TpT in liver samples and in hepatoma cells (representative image of three independent experiments). pBR322 plasmid was linearized and end-labeled with 5 μ Ci α 32 P ATP by using 20 U Klenow DNA polymerase. To remove the labeling from one end, the linearized plasmid was digested with Hind III restriction endonuclease. Ten microgram 0.35 M NaCI nuclear extracts of HepG2, Hep3B, and human HCC specimens were incubated with 8000 cpm linearized plasmid in the absence or presence of 100 and 200 μ M topotecan. Lanes 1: cleavage reaction without topotecan, lane 2: cleavage reaction with 100 μ M topotecan, and lane 3: cleavage reaction with 200 μ M topotecan. The activity of Hep3B extract was much lower than that of HepG2 and human Iiver cancer.

    Article Snippet: Hind III and Klenow DNA polymerase enzymes were obtained from Promega (Madison, USA).

    Techniques: Plasmid Preparation, Activity Assay, Labeling, Incubation