exonuclease iii Thermo Fisher Search Results


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  • 98
    New England Biolabs exonuclease iii
    Exonuclease Iii, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 98/100, based on 517 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher exonuclease iii
    Evidence of a covalently linked 5′ TP. (A) <t>DNA-protein</t> complex (lane 1), complex treated with exonuclease <t>III</t> for 15 min (lane 2), complex treated with exonuclease III for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with exonuclease III for 15 min (lane 5), and PK-DNA treated with exonuclease III for 30 min (lane 6). (B) DNA-protein complex (lane 1), complex treated with λ exonuclease for 15 min (lane 2), complex treated with λ exonuclease for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with λ exonuclease for 30 min (lane 5), PK-DNA treated with 0.5 M piperidine (lane 6), PK-DNA treated with piperidine and λ exonuclease for 30 min (lane 7). The amounts used are indicated in Materials and Methods.
    Exonuclease Iii, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 138 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    95
    Thermo Fisher lambda exonuclease iii
    Evidence of a covalently linked 5′ TP. (A) <t>DNA-protein</t> complex (lane 1), complex treated with exonuclease <t>III</t> for 15 min (lane 2), complex treated with exonuclease III for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with exonuclease III for 15 min (lane 5), and PK-DNA treated with exonuclease III for 30 min (lane 6). (B) DNA-protein complex (lane 1), complex treated with λ exonuclease for 15 min (lane 2), complex treated with λ exonuclease for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with λ exonuclease for 30 min (lane 5), PK-DNA treated with 0.5 M piperidine (lane 6), PK-DNA treated with piperidine and λ exonuclease for 30 min (lane 7). The amounts used are indicated in Materials and Methods.
    Lambda Exonuclease Iii, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher exonuclease iii reaction buffer
    Evidence of a covalently linked 5′ TP. (A) <t>DNA-protein</t> complex (lane 1), complex treated with exonuclease <t>III</t> for 15 min (lane 2), complex treated with exonuclease III for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with exonuclease III for 15 min (lane 5), and PK-DNA treated with exonuclease III for 30 min (lane 6). (B) DNA-protein complex (lane 1), complex treated with λ exonuclease for 15 min (lane 2), complex treated with λ exonuclease for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with λ exonuclease for 30 min (lane 5), PK-DNA treated with 0.5 M piperidine (lane 6), PK-DNA treated with piperidine and λ exonuclease for 30 min (lane 7). The amounts used are indicated in Materials and Methods.
    Exonuclease Iii Reaction Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    Thermo Fisher exonucleases iii
    Evidence of a covalently linked 5′ TP. (A) <t>DNA-protein</t> complex (lane 1), complex treated with exonuclease <t>III</t> for 15 min (lane 2), complex treated with exonuclease III for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with exonuclease III for 15 min (lane 5), and PK-DNA treated with exonuclease III for 30 min (lane 6). (B) DNA-protein complex (lane 1), complex treated with λ exonuclease for 15 min (lane 2), complex treated with λ exonuclease for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with λ exonuclease for 30 min (lane 5), PK-DNA treated with 0.5 M piperidine (lane 6), PK-DNA treated with piperidine and λ exonuclease for 30 min (lane 7). The amounts used are indicated in Materials and Methods.
    Exonucleases Iii, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 88/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher superscript iii
    Evidence of a covalently linked 5′ TP. (A) <t>DNA-protein</t> complex (lane 1), complex treated with exonuclease <t>III</t> for 15 min (lane 2), complex treated with exonuclease III for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with exonuclease III for 15 min (lane 5), and PK-DNA treated with exonuclease III for 30 min (lane 6). (B) DNA-protein complex (lane 1), complex treated with λ exonuclease for 15 min (lane 2), complex treated with λ exonuclease for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with λ exonuclease for 30 min (lane 5), PK-DNA treated with 0.5 M piperidine (lane 6), PK-DNA treated with piperidine and λ exonuclease for 30 min (lane 7). The amounts used are indicated in Materials and Methods.
    Superscript Iii, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 44296 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher superscript iii reverse transcriptase
    Evidence of a covalently linked 5′ TP. (A) <t>DNA-protein</t> complex (lane 1), complex treated with exonuclease <t>III</t> for 15 min (lane 2), complex treated with exonuclease III for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with exonuclease III for 15 min (lane 5), and PK-DNA treated with exonuclease III for 30 min (lane 6). (B) DNA-protein complex (lane 1), complex treated with λ exonuclease for 15 min (lane 2), complex treated with λ exonuclease for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with λ exonuclease for 30 min (lane 5), PK-DNA treated with 0.5 M piperidine (lane 6), PK-DNA treated with piperidine and λ exonuclease for 30 min (lane 7). The amounts used are indicated in Materials and Methods.
    Superscript Iii Reverse Transcriptase, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 69294 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher dnase i kit
    Evidence of a covalently linked 5′ TP. (A) <t>DNA-protein</t> complex (lane 1), complex treated with exonuclease <t>III</t> for 15 min (lane 2), complex treated with exonuclease III for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with exonuclease III for 15 min (lane 5), and PK-DNA treated with exonuclease III for 30 min (lane 6). (B) DNA-protein complex (lane 1), complex treated with λ exonuclease for 15 min (lane 2), complex treated with λ exonuclease for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with λ exonuclease for 30 min (lane 5), PK-DNA treated with 0.5 M piperidine (lane 6), PK-DNA treated with piperidine and λ exonuclease for 30 min (lane 7). The amounts used are indicated in Materials and Methods.
    Dnase I Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Thermo Fisher rt reagent kit
    Evidence of a covalently linked 5′ TP. (A) <t>DNA-protein</t> complex (lane 1), complex treated with exonuclease <t>III</t> for 15 min (lane 2), complex treated with exonuclease III for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with exonuclease III for 15 min (lane 5), and PK-DNA treated with exonuclease III for 30 min (lane 6). (B) DNA-protein complex (lane 1), complex treated with λ exonuclease for 15 min (lane 2), complex treated with λ exonuclease for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with λ exonuclease for 30 min (lane 5), PK-DNA treated with 0.5 M piperidine (lane 6), PK-DNA treated with piperidine and λ exonuclease for 30 min (lane 7). The amounts used are indicated in Materials and Methods.
    Rt Reagent Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 157 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher exo iii s1 deletion kit
    Evidence of a covalently linked 5′ TP. (A) <t>DNA-protein</t> complex (lane 1), complex treated with exonuclease <t>III</t> for 15 min (lane 2), complex treated with exonuclease III for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with exonuclease III for 15 min (lane 5), and PK-DNA treated with exonuclease III for 30 min (lane 6). (B) DNA-protein complex (lane 1), complex treated with λ exonuclease for 15 min (lane 2), complex treated with λ exonuclease for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with λ exonuclease for 30 min (lane 5), PK-DNA treated with 0.5 M piperidine (lane 6), PK-DNA treated with piperidine and λ exonuclease for 30 min (lane 7). The amounts used are indicated in Materials and Methods.
    Exo Iii S1 Deletion Kit, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    89
    Thermo Fisher exo iii
    Optimization of experimental conditions: (a) effect of the incubation time of <t>Exo</t> <t>III</t> digestion; (b) effect of Exo III concentration; (c) effect of signal DNA concentration; (d) effect of the incubation temperature; (e) effect of the signal DNA/capture DNA ratio; (f) effect of the pH value. Experimental conditions: 10 nmol/L oligo-1, 40 nmol/L oligo-2, 10 U Exo III, 50 mmol/L K + , and 160 nmol/L NMM. Error bars represent the standard deviation of three independent experiments.
    Exo Iii, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 89/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Thermo Fisher exo iii s1n digestion
    Optimization of experimental conditions: (a) effect of the incubation time of <t>Exo</t> <t>III</t> digestion; (b) effect of Exo III concentration; (c) effect of signal DNA concentration; (d) effect of the incubation temperature; (e) effect of the signal DNA/capture DNA ratio; (f) effect of the pH value. Experimental conditions: 10 nmol/L oligo-1, 40 nmol/L oligo-2, 10 U Exo III, 50 mmol/L K + , and 160 nmol/L NMM. Error bars represent the standard deviation of three independent experiments.
    Exo Iii S1n Digestion, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Evidence of a covalently linked 5′ TP. (A) DNA-protein complex (lane 1), complex treated with exonuclease III for 15 min (lane 2), complex treated with exonuclease III for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with exonuclease III for 15 min (lane 5), and PK-DNA treated with exonuclease III for 30 min (lane 6). (B) DNA-protein complex (lane 1), complex treated with λ exonuclease for 15 min (lane 2), complex treated with λ exonuclease for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with λ exonuclease for 30 min (lane 5), PK-DNA treated with 0.5 M piperidine (lane 6), PK-DNA treated with piperidine and λ exonuclease for 30 min (lane 7). The amounts used are indicated in Materials and Methods.

    Journal: Journal of Bacteriology

    Article Title: Genomic Sequence of C1, the First Streptococcal Phage

    doi: 10.1128/JB.185.11.3325-3332.2003

    Figure Lengend Snippet: Evidence of a covalently linked 5′ TP. (A) DNA-protein complex (lane 1), complex treated with exonuclease III for 15 min (lane 2), complex treated with exonuclease III for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with exonuclease III for 15 min (lane 5), and PK-DNA treated with exonuclease III for 30 min (lane 6). (B) DNA-protein complex (lane 1), complex treated with λ exonuclease for 15 min (lane 2), complex treated with λ exonuclease for 30 min (lane 3), PK-DNA (lane 4), PK-DNA treated with λ exonuclease for 30 min (lane 5), PK-DNA treated with 0.5 M piperidine (lane 6), PK-DNA treated with piperidine and λ exonuclease for 30 min (lane 7). The amounts used are indicated in Materials and Methods.

    Article Snippet: Aliquots (10 μg each) of the DNA-protein complex or protease K-digested DNA (PK-DNA) were treated with either 2 μl (130 U) of exonuclease III or 2 μl (11 U) of lambda exonuclease (both from Gibco/BRL) at 37°C according to the manufacturer's instructions.

    Techniques:

    Southern blot of pQC110 and pQC26-derived DNAs isolated from ZX7 transformants. ( A ) from transformants receiving Dra I-cleaved pQC110 DNA. DNAs were electrophoresed for 13 hr at 40 v in 0.5% agarose gel and probed with 32 P-labled pQC110 DNA (lanes 4 – 17 ). Molecular lengths were calculated relative to Hin dIII-treated bacteriophage λ DNA (lane 1 ), a 1-kb DNA-size ladder (Life Technologies, Inc.) (lane 2 ), or covalently closed circular pQC110 DNA isolated from E. coli (lane 3 ). ( B ) Surviving replicons are linear plasmids. Lanes 4 – 7 (NT) show DNA isolated from 4 randomly selected transformants by proteinase K/SDS treatment. Aliquots of the same DNAs were treated with 100 units exonuclease III (lanes 8 – 11 ) or 10 units λ exonuclease (lanes 12 – 15 ) at 37°C for 4 hr and electrophoresed for 18 hr at 38 v in 0.5 % agarose gel. λ Hin dIII-treated DNA (lane 1 ), 1-kb DNA ladder (lane 2 ), and pQC110 DNA (from E. coli , lane 3 ) are molecular size markers. ( C ) Electrophoresis of pQC110-derived DNAs shown in A after treatment with NaOH and renaturation. Lane designations are as in A . ( D ) Bam HI digestion of pQC110-derived DNAs from A . Lane 1 contains a 1-kb ladder. Lanes 2 – 15 correspond to DNAs in lanes 4 – 17 of A . The 8.5-kb and 5-kb DNA bands discussed in the text are indicated. ( E ) Bam HI digestion of pQC110-derived DNAs following denaturation and renaturation. Lanes 2 – 16 correspond to DNAs in lanes 3 – 17 of A . ( F ) Effect of denaturation on migration of Bam HI fragments containing putative palindrome apices of linear plasmids. Agarose gel analysis of inserts recovered from agarose gel following Bam HI digestion of pQC143–pQC146. The banding position of DNAs dissolved in TE (lanes 2 – 5 ) or analyzed following treatment with NaOH and neutralization is shown in lanes 6 – 9 . ( G ) Endonuclease analysis of Bam HI fragments containing putative palindrome apices. DNAs were digested by the enzymes indicated and electrophoresed for 3 hr at 80 v on 1% agarose gel. Lanes 2, 4, 6, 8 , and lanes 10, 12, 14, 16 correspond to lanes 2 – 5 from F . Lanes 3, 5, 7, 9 , and lanes 11, 13, 15, 17 correspond to lanes 6 – 9 from F . ( H ) Effect of denaturation on migration of Sac I-cleaved pQC26 DNA isolated from four transformants by adding proteinase K/SDS (lanes 3 – 7 ) or NaOH/SDS (lanes 8 – 12 ), and electrophoresed for 20 hr at 36 v in 0.5% agarose gel. Lane 1 (1-kb ladder) and 2 (pQC26, from E. coli ) are markers.

    Journal: Genes & Development

    Article Title: Long palindromes formed in Streptomyces by nonrecombinational intra-strand annealing

    doi:

    Figure Lengend Snippet: Southern blot of pQC110 and pQC26-derived DNAs isolated from ZX7 transformants. ( A ) from transformants receiving Dra I-cleaved pQC110 DNA. DNAs were electrophoresed for 13 hr at 40 v in 0.5% agarose gel and probed with 32 P-labled pQC110 DNA (lanes 4 – 17 ). Molecular lengths were calculated relative to Hin dIII-treated bacteriophage λ DNA (lane 1 ), a 1-kb DNA-size ladder (Life Technologies, Inc.) (lane 2 ), or covalently closed circular pQC110 DNA isolated from E. coli (lane 3 ). ( B ) Surviving replicons are linear plasmids. Lanes 4 – 7 (NT) show DNA isolated from 4 randomly selected transformants by proteinase K/SDS treatment. Aliquots of the same DNAs were treated with 100 units exonuclease III (lanes 8 – 11 ) or 10 units λ exonuclease (lanes 12 – 15 ) at 37°C for 4 hr and electrophoresed for 18 hr at 38 v in 0.5 % agarose gel. λ Hin dIII-treated DNA (lane 1 ), 1-kb DNA ladder (lane 2 ), and pQC110 DNA (from E. coli , lane 3 ) are molecular size markers. ( C ) Electrophoresis of pQC110-derived DNAs shown in A after treatment with NaOH and renaturation. Lane designations are as in A . ( D ) Bam HI digestion of pQC110-derived DNAs from A . Lane 1 contains a 1-kb ladder. Lanes 2 – 15 correspond to DNAs in lanes 4 – 17 of A . The 8.5-kb and 5-kb DNA bands discussed in the text are indicated. ( E ) Bam HI digestion of pQC110-derived DNAs following denaturation and renaturation. Lanes 2 – 16 correspond to DNAs in lanes 3 – 17 of A . ( F ) Effect of denaturation on migration of Bam HI fragments containing putative palindrome apices of linear plasmids. Agarose gel analysis of inserts recovered from agarose gel following Bam HI digestion of pQC143–pQC146. The banding position of DNAs dissolved in TE (lanes 2 – 5 ) or analyzed following treatment with NaOH and neutralization is shown in lanes 6 – 9 . ( G ) Endonuclease analysis of Bam HI fragments containing putative palindrome apices. DNAs were digested by the enzymes indicated and electrophoresed for 3 hr at 80 v on 1% agarose gel. Lanes 2, 4, 6, 8 , and lanes 10, 12, 14, 16 correspond to lanes 2 – 5 from F . Lanes 3, 5, 7, 9 , and lanes 11, 13, 15, 17 correspond to lanes 6 – 9 from F . ( H ) Effect of denaturation on migration of Sac I-cleaved pQC26 DNA isolated from four transformants by adding proteinase K/SDS (lanes 3 – 7 ) or NaOH/SDS (lanes 8 – 12 ), and electrophoresed for 20 hr at 36 v in 0.5% agarose gel. Lane 1 (1-kb ladder) and 2 (pQC26, from E. coli ) are markers.

    Article Snippet: Aliquots of DNA were incubated with 100 units of E. coli exonuclease III or 10 units of bacteriophage λ exonuclease (either purchased from Life Technologies, Inc. or a gift of Drs. Deb Chatterjee and Per Harbury) at 37°C for 1 hr and the completeness of their digestion was confirmed by gel electrophoresis.

    Techniques: Southern Blot, Derivative Assay, Isolation, Agarose Gel Electrophoresis, Electrophoresis, Migration, Neutralization

    Schematic of sequence-specific annealing and 5′–3′ exonuclease-based cleavage of the fluorescent dye-labeled probe. A: Annealing of the primers and the probe to the target sequence. The probe is labeled with a reporter dye, 6-carboxy fluorescein, at the 5′ end and a quencher dye, 6-carboxy-tetramethyl rhodamine, at the 3′ end. When both dyes are attached to the probe, fluorescence emission of the reporter dye is quenched by the quencher dye. B: Extension of the primer and the initiation of cleavage of the probe at its 5′ end by Taq polymerase. C: Release of the probe from the target strand and completion of the new strand synthesis. The separation of the reporter dye from the quencher dye abrogates the quencher effect and results in an increase in the fluorescence signal of the reporter dye.

    Journal: The American Journal of Pathology

    Article Title: Novel 5? Exonuclease-Based Real-Time PCR Assay for the Detection of t(14;18)(q32;q21) in Patients with Follicular Lymphoma

    doi:

    Figure Lengend Snippet: Schematic of sequence-specific annealing and 5′–3′ exonuclease-based cleavage of the fluorescent dye-labeled probe. A: Annealing of the primers and the probe to the target sequence. The probe is labeled with a reporter dye, 6-carboxy fluorescein, at the 5′ end and a quencher dye, 6-carboxy-tetramethyl rhodamine, at the 3′ end. When both dyes are attached to the probe, fluorescence emission of the reporter dye is quenched by the quencher dye. B: Extension of the primer and the initiation of cleavage of the probe at its 5′ end by Taq polymerase. C: Release of the probe from the target strand and completion of the new strand synthesis. The separation of the reporter dye from the quencher dye abrogates the quencher effect and results in an increase in the fluorescence signal of the reporter dye.

    Article Snippet: This assay exploits the 5′–3′ exonuclease activity of Taq polymerase and integrates fluorogenic PCR with a laser-based instrumentation system, the PRISM 7700 Sequence Detector (PE Applied Biosystems, Foster City, CA), to detect and quantitate specific PCR amplicons as the reaction proceeds.

    Techniques: Sequencing, Labeling, Fluorescence

    Model for 5′-CCCCCCCCCCCC A -3′–5′-GGGG T GGGGGGGA-3′ extension. The figure depicts the assumed events during the extension of double-stranded 5′-CCCCCCCCCCCC A -3′–5′-GGGG T GGGGGGGA-3′ oligonucleotide. Polymerase binds the oligonucleotide ( 1 ) and shifts A-nucleotide at the 3′ end of 5′-CCCCCCCCCCCC A -3′ until it is paired with T. A single-stranded template-primer fragment and a loop de novo are then formed as a result of the 3′ end slippage ( 2 ). The primer strand is synthesized complementary to the template sequence; residues incorporated into the primer are marked in red ( 3 ). The enzyme–DNA complex dissociates ( 4 ) and a loop relaxes into a structure with overhang at the 5′ end ( 5 ). The overhang cannot be used as a template for Klenow exo − due to inability to pair A-nucleotide at the 3′ end of the primer with either nucleotide in sequence of the template.

    Journal: Nucleic Acids Research

    Article Title: In vitro synthesis of uniform poly(dG)-poly(dC) by Klenow exo− fragment of polymerase I

    doi: 10.1093/nar/gki178

    Figure Lengend Snippet: Model for 5′-CCCCCCCCCCCC A -3′–5′-GGGG T GGGGGGGA-3′ extension. The figure depicts the assumed events during the extension of double-stranded 5′-CCCCCCCCCCCC A -3′–5′-GGGG T GGGGGGGA-3′ oligonucleotide. Polymerase binds the oligonucleotide ( 1 ) and shifts A-nucleotide at the 3′ end of 5′-CCCCCCCCCCCC A -3′ until it is paired with T. A single-stranded template-primer fragment and a loop de novo are then formed as a result of the 3′ end slippage ( 2 ). The primer strand is synthesized complementary to the template sequence; residues incorporated into the primer are marked in red ( 3 ). The enzyme–DNA complex dissociates ( 4 ) and a loop relaxes into a structure with overhang at the 5′ end ( 5 ). The overhang cannot be used as a template for Klenow exo − due to inability to pair A-nucleotide at the 3′ end of the primer with either nucleotide in sequence of the template.

    Article Snippet: Klenow fragment exonuclease minus of DNA polymerase I, E.coli lacking the 3′→5′ exonuclease activity (Klenow exo− ) was purchased from Fermentas (Lithuania).

    Techniques: Synthesized, Sequencing

    HPLC analysis of products of 5′-CCCCCCCCCCCC A -3′–5′-GGGGTGGGGGGGA-3′ extension. Polymerase extension assay was performed as described in Materials and Methods with 5 μM 5′-CCCCCCCCCCCC A -3′–5′-GGGG T GGGGGGGA-3′ and 10 μg/ml of Klenow exo − at 37°C. The reaction was started by addition of the enzyme and terminated by addition of 10 mM EDTA. Aliquots of 50 μl of sample were withdrawn from the assay mixture before (black curve) and 10 (red curve), and 20 (blue curve) min after the reaction had been started. Oligomers were separated from dGTP and dCTP with TSKgel G-3000 SWXL HPLC column (7.8 × 300 mm) and loaded in 0.1 M KOH onto TSKgel DNA-NPR column (4.6 × 75 mm). Elution was performed using a 20 min linear gradient between 0 and 1 M KCl in 0.1 M KOH at a flow rate of 0.6 ml/min.

    Journal: Nucleic Acids Research

    Article Title: In vitro synthesis of uniform poly(dG)-poly(dC) by Klenow exo− fragment of polymerase I

    doi: 10.1093/nar/gki178

    Figure Lengend Snippet: HPLC analysis of products of 5′-CCCCCCCCCCCC A -3′–5′-GGGGTGGGGGGGA-3′ extension. Polymerase extension assay was performed as described in Materials and Methods with 5 μM 5′-CCCCCCCCCCCC A -3′–5′-GGGG T GGGGGGGA-3′ and 10 μg/ml of Klenow exo − at 37°C. The reaction was started by addition of the enzyme and terminated by addition of 10 mM EDTA. Aliquots of 50 μl of sample were withdrawn from the assay mixture before (black curve) and 10 (red curve), and 20 (blue curve) min after the reaction had been started. Oligomers were separated from dGTP and dCTP with TSKgel G-3000 SWXL HPLC column (7.8 × 300 mm) and loaded in 0.1 M KOH onto TSKgel DNA-NPR column (4.6 × 75 mm). Elution was performed using a 20 min linear gradient between 0 and 1 M KCl in 0.1 M KOH at a flow rate of 0.6 ml/min.

    Article Snippet: Klenow fragment exonuclease minus of DNA polymerase I, E.coli lacking the 3′→5′ exonuclease activity (Klenow exo− ) was purchased from Fermentas (Lithuania).

    Techniques: High Performance Liquid Chromatography, Flow Cytometry

    Optimization of experimental conditions: (a) effect of the incubation time of Exo III digestion; (b) effect of Exo III concentration; (c) effect of signal DNA concentration; (d) effect of the incubation temperature; (e) effect of the signal DNA/capture DNA ratio; (f) effect of the pH value. Experimental conditions: 10 nmol/L oligo-1, 40 nmol/L oligo-2, 10 U Exo III, 50 mmol/L K + , and 160 nmol/L NMM. Error bars represent the standard deviation of three independent experiments.

    Journal: Journal of Analytical Methods in Chemistry

    Article Title: A Sensitive Fluorescence Biosensor for Silver Ions (Ag+) Detection Based on C-Ag+-C Structure and Exonuclease III-Assisted Dual-Recycling Amplification

    doi: 10.1155/2019/3712032

    Figure Lengend Snippet: Optimization of experimental conditions: (a) effect of the incubation time of Exo III digestion; (b) effect of Exo III concentration; (c) effect of signal DNA concentration; (d) effect of the incubation temperature; (e) effect of the signal DNA/capture DNA ratio; (f) effect of the pH value. Experimental conditions: 10 nmol/L oligo-1, 40 nmol/L oligo-2, 10 U Exo III, 50 mmol/L K + , and 160 nmol/L NMM. Error bars represent the standard deviation of three independent experiments.

    Article Snippet: Exo III was purchased from the Thermo Fisher Scientific Inc. (USA).

    Techniques: Incubation, Concentration Assay, Standard Deviation

    Fluorescence spectra (a) and calibration plot (b) for Ag + . Experimental conditions: 10 nmol/L oligo-1, 40 nmol/L oligo-2, 10 U Exo III, 50 mmol/L K + , 160 nmol/L NMM, and 50 min incubation time. Error bars represent the standard deviation of three independent experiments.

    Journal: Journal of Analytical Methods in Chemistry

    Article Title: A Sensitive Fluorescence Biosensor for Silver Ions (Ag+) Detection Based on C-Ag+-C Structure and Exonuclease III-Assisted Dual-Recycling Amplification

    doi: 10.1155/2019/3712032

    Figure Lengend Snippet: Fluorescence spectra (a) and calibration plot (b) for Ag + . Experimental conditions: 10 nmol/L oligo-1, 40 nmol/L oligo-2, 10 U Exo III, 50 mmol/L K + , 160 nmol/L NMM, and 50 min incubation time. Error bars represent the standard deviation of three independent experiments.

    Article Snippet: Exo III was purchased from the Thermo Fisher Scientific Inc. (USA).

    Techniques: Fluorescence, Incubation, Standard Deviation

    Selectivity of the biosensor. Experimental conditions: 10 nmol/L oligo-1, 40 nmol/L oligo-2, 10 U Exo III, 50 mmol/L K + , 160 nmol/L NMM, and 50 min incubation time. The concentration of Ag + was 1.5 nmol/L, and the concentrations of other metal ions were 15 nmol/L. Error bars represent the standard deviation of three independent experiments.

    Journal: Journal of Analytical Methods in Chemistry

    Article Title: A Sensitive Fluorescence Biosensor for Silver Ions (Ag+) Detection Based on C-Ag+-C Structure and Exonuclease III-Assisted Dual-Recycling Amplification

    doi: 10.1155/2019/3712032

    Figure Lengend Snippet: Selectivity of the biosensor. Experimental conditions: 10 nmol/L oligo-1, 40 nmol/L oligo-2, 10 U Exo III, 50 mmol/L K + , 160 nmol/L NMM, and 50 min incubation time. The concentration of Ag + was 1.5 nmol/L, and the concentrations of other metal ions were 15 nmol/L. Error bars represent the standard deviation of three independent experiments.

    Article Snippet: Exo III was purchased from the Thermo Fisher Scientific Inc. (USA).

    Techniques: Incubation, Concentration Assay, Standard Deviation

    Fluorescence emission spectra of different solutions: (a) 10 nmol/L oligo-1 + 1500 pmol/L Ag + ; (b) 40 nmol/L oligo-2 + 1500 pmol/L Ag + ; (c) 10 nmol/L oligo-1 + 40 nmol/L oligo-2; (d) 10 nmol/L oligo-1 + 40 nmol/L oligo-2 + 10 U Exo III; (e) 10 nmol/L oligo-1 + 40 nmol/L oligo-2 + 10 U Exo III + 1500 pmol/L Ag + . Experimental conditions: 50 mmol/L K + and 160 nmol/L NMM.

    Journal: Journal of Analytical Methods in Chemistry

    Article Title: A Sensitive Fluorescence Biosensor for Silver Ions (Ag+) Detection Based on C-Ag+-C Structure and Exonuclease III-Assisted Dual-Recycling Amplification

    doi: 10.1155/2019/3712032

    Figure Lengend Snippet: Fluorescence emission spectra of different solutions: (a) 10 nmol/L oligo-1 + 1500 pmol/L Ag + ; (b) 40 nmol/L oligo-2 + 1500 pmol/L Ag + ; (c) 10 nmol/L oligo-1 + 40 nmol/L oligo-2; (d) 10 nmol/L oligo-1 + 40 nmol/L oligo-2 + 10 U Exo III; (e) 10 nmol/L oligo-1 + 40 nmol/L oligo-2 + 10 U Exo III + 1500 pmol/L Ag + . Experimental conditions: 50 mmol/L K + and 160 nmol/L NMM.

    Article Snippet: Exo III was purchased from the Thermo Fisher Scientific Inc. (USA).

    Techniques: Fluorescence