dntp  (TaKaRa)


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    Name:
    dNTP Mixture
    Description:

    Catalog Number:
    4030
    Price:
    None
    Category:
    PCR
    Size:
    3 2 µmol Each 1 25 mL
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    Structured Review

    TaKaRa dntp

    https://www.bioz.com/result/dntp/product/TaKaRa
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    Related Articles

    Plasmid Preparation:

    Article Title: A transcription and translation-coupled DNA replication system using rolling-circle replication
    Article Snippet: The phi29 phage was kindly provided by Osamu Makino of Sophia University, Japan. .. Assay of the TTcDR reaction The optimized composition of the TTcDR system was as follows: template plasmid DNA (1 ng/μl), dNTPs (0.3 mM each, Takara), [32 -P] dCTP (3.3 μM, PerkinElmer), magnesium acetate (7.9 mM, Wako), potassium glutamate (70 mM, Wako), spermidine (0.375 mM, Nakarai), dithiothreitol (6 mM, Nakarai), ATP (0.375 mM, GE Healthcare), GTP (0.25 mM, GE Healthcare), CTP (0.125 mM, GE Healthcare), UTP (0.125 mM, GE Healthcare), creatine phosphate (25 mM, Nakarai), E. coli tRNA mixture (0.518 μg/μl, Roche), 10-formyl-5,6,7,8-tetrahydrofolic acid (10 ng/μl), Cys (0.3 mM, Wako), Tyr (0.3 mM, Wako), the other 18 amino acids except for Cys and Tyr (0.36 mM, Wako), 2-[4-(2-hydroxyethyl)-1-piperazinyl]ethanesulfonic acid (100 mM, pH 7.6, Sigma), ribosomes (1 μM), IF1 (25 μM), IF2 (1 μM), IF3 (4.9 μM), EF-G (1.1 μM), EF-Tu (80 μM), EF-Ts (3.3 μM), RF1 (0.05 μM), RF2 (0.05 μM), RF3 (0.17 μM), RRF (3.9 μM), AlaRS (730 nM), ArgRS (30 nM), AsnRS (420 nM), AspRS (120 nM), CysRS (20 nM), GlnRS (60 nM), GluRS (230 nM), GlyRS (90 nM), HisRS (90 nM), IleRS (370 nM), LeuRS (40 nM), LysRS (120 nM), MetRS (110 nM), PheRS (130 nM), ProRS (170 nM), SerRS (80 nM), ThrRS (80 nM), TrpRS (30 nM), TyrRS (150 nM), ValRS (20 nM), MTF (590 nM), creatine kinase (0.25 μM), myokinase (1.4 μM), nucleoside-diphosphate kinase (20 nM), pyrophosphatase (40 nM), yeast inorganic pyrophosphatase (0.2 mU/μl, New England BioLabs (NEB)), ribonuclease inhibitor (0.1 U/μl; Promega), and T7 RNA polymerase (0.42 U/μl; Takara). .. Most of the proteins described above were purified according to a previously described method except for yeast inorganic pyrophosphatase, ribonuclease inhibitor, and T7 RNA polymerase.

    Amplification:

    Article Title: Essential Domains for Ribonucleoprotein Complex Formation Required for Retrotransposition of Telomere-Specific Non-Long Terminal Repeat Retrotransposon SART1 †
    Article Snippet: In the in vitro rescue experiment (shown in Fig. ) 50 ng of WT SART1 ORF1p, which was purified in parallel, was simultaneously added to the buffer. .. After heat inactivation at 80°C for 20 min, 1 μl of the reaction mixture was amplified by PCR for 35 cycles of 98°C for 20 s, 60°C for 30 s, and 72°C for 30 s, with an initial denaturation at 96°C for 2 min and a final extension at 72°C for 5 min. PCR mixtures contained 200 μM concentrations of each dNTP, 2 mM MgCl2 , 50 mM KCl, 0.5 U of Ex- Taq (TaKaRa), and 0.5 μM concentrations of each primer (see Table S1 in the supplemental material). .. Purified SART1 complex was overlaid onto 3.3 ml of 10 to 40% glycerol gradient in the HG500 buffer.

    Polymerase Chain Reaction:

    Article Title: Essential Domains for Ribonucleoprotein Complex Formation Required for Retrotransposition of Telomere-Specific Non-Long Terminal Repeat Retrotransposon SART1 †
    Article Snippet: In the in vitro rescue experiment (shown in Fig. ) 50 ng of WT SART1 ORF1p, which was purified in parallel, was simultaneously added to the buffer. .. After heat inactivation at 80°C for 20 min, 1 μl of the reaction mixture was amplified by PCR for 35 cycles of 98°C for 20 s, 60°C for 30 s, and 72°C for 30 s, with an initial denaturation at 96°C for 2 min and a final extension at 72°C for 5 min. PCR mixtures contained 200 μM concentrations of each dNTP, 2 mM MgCl2 , 50 mM KCl, 0.5 U of Ex- Taq (TaKaRa), and 0.5 μM concentrations of each primer (see Table S1 in the supplemental material). .. Purified SART1 complex was overlaid onto 3.3 ml of 10 to 40% glycerol gradient in the HG500 buffer.

    Article Title: Molecular characterization and phylogenetic analysis of a dengue virus serotype 3 isolated from a Chinese traveler returned from Laos
    Article Snippet: First, viral RNA was reverse transcribed using the GoScript Reverse Transcription System (Promega, WI, USA) following the manufacturer’s instructions. .. The RT reaction was conducted under the following conditions: 25 °C for 5 min, followed by 1 h at 42 °C, then 72 °C for 15 min. Next, the PCR was carried out in a reaction mixture of 50 μL containing 5 μL of 10 × La Taq Buffer (Mg2+ Plus), 8 μL of dNTP mixture (2.5 mM), 2 μM of forward and backward primers, and one unit of high fidelity La Taq DNA polymerase (TaKaRa, Dalian, China). .. PCR amplification was performed under the following parameters [ ]: 94 °C for 5 min, followed by 35 cycles of denaturation at 94 °C for 30 s, annealing at 55 °C for 30 s, extension at 72 °C for 2 min and final extension at 72 °C for 5 min.

    Article Title: Ammonia oxidizers in the sea-surface microlayer of a coastal marine inlet
    Article Snippet: An approximately 256-bp fragment of archaeal amoA was amplified by using the Arch- amoA -for/Arch- amoA -rev primer set. .. PCR was performed in triplicate using a 20-μL reaction mixture consisting of 3 μL of 10-fold-diluted template DNA (5 to 8 ng μL–1 ), 0.2 μM of each primer, 0.2 mM of each dNTP, 2 μL of 10× Ex Taq Buffer, and 0.5 U of Ex Taq HS (Takara). .. The PCR thermal cycling conditions consisted of initial denaturation at 95°C for 3 min; 40 cycles of amplification at 98°C for 10 s, annealing at 58°C for 30 s, and elongation at 72°C for 1 min; and final elongation at 72°C for 10 min. Amplified PCR products were pooled and purified by using a Qiaquick PCR Purification Kit (Qiagen KK, Tokyo, Japan).

    DNA Synthesis:

    Article Title: Chemical Incorporation of Chain-Terminating Nucleoside Analogs as 3′-Blocking DNA Damage and Their Removal by Human ERCC1-XPF Endonuclease
    Article Snippet: Time course experiments were performed in the same reaction mixture, except for the enzyme amount (92 fmol), by varying the incubation time (0, 30, 60, 90 min). .. Resumption of DNA Synthesis by DNA Polymerase after the Removal of CTNAs The hybridized oligonucleotides (400 fmol) were first treated with ERCC1-XPF (230 fmol) in 10 µL of 50 mM Tris-HCl buffer (pH 8.0), containing 2 mM MgCl2 , 0.5 mM DTT and 0.1 mg·mL−1 BSA, at 25 °C for 16 h. To the reaction mixture was added 5 µL of 30 mM Tris-HCl buffer (pH 7.9), containing 150 mM NaCl, 30 mM MgCl2 , 30 mM DTT, 300 µM dNTPs and the Klenow fragment of Escherichia coli DNA polymerase I, lacking the 3′–5′ exonuclease activity (KF− , 0.1 unit, Takara Bio). ..

    Activity Assay:

    Article Title: Chemical Incorporation of Chain-Terminating Nucleoside Analogs as 3′-Blocking DNA Damage and Their Removal by Human ERCC1-XPF Endonuclease
    Article Snippet: Time course experiments were performed in the same reaction mixture, except for the enzyme amount (92 fmol), by varying the incubation time (0, 30, 60, 90 min). .. Resumption of DNA Synthesis by DNA Polymerase after the Removal of CTNAs The hybridized oligonucleotides (400 fmol) were first treated with ERCC1-XPF (230 fmol) in 10 µL of 50 mM Tris-HCl buffer (pH 8.0), containing 2 mM MgCl2 , 0.5 mM DTT and 0.1 mg·mL−1 BSA, at 25 °C for 16 h. To the reaction mixture was added 5 µL of 30 mM Tris-HCl buffer (pH 7.9), containing 150 mM NaCl, 30 mM MgCl2 , 30 mM DTT, 300 µM dNTPs and the Klenow fragment of Escherichia coli DNA polymerase I, lacking the 3′–5′ exonuclease activity (KF− , 0.1 unit, Takara Bio). ..

    Marker:

    Article Title: Small Molecular Contaminant and Microorganism Can Be Simultaneously Detected Based on Nanobody-Phage: Using Carcinogen Aflatoxin and Its Main Fungal Aspergillus Section Flavi spp. in Stored Maize for Demonstration
    Article Snippet: The Universal Probes Supermix was supplied by Bio-Rad (Hercules, CA, United States). .. DNA polymerase (iTaq), Mg2+ , dNTPs, 6× loading buffer, and DNA marker were bought from Takara Bio (Beijing, China). .. The anti-aflatoxins monoclonal antibody 1C11 (mAb 1C11) and V2–5 phage displaying nanobody specific for 1C11 were produced by our team ( ; ).

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    TaKaRa dntps
    ( A ) Sequences of the 25 nt template ( III ) and 20 nt primer ( IV ). ( B ) PAGE of extension reactions beyond the 1-deaza-dG residue in the template. ( C ) PAGE of extension reactions subsequent to 1-deaza-dG in the primer with Therminator™ DNA polymerase and ( D ) with <t>AMV</t> reverse transcriptase. Conditions used are described in Materials and Methods. Added <t>dNTPs</t> are indicated at the top of each gel. Z indicates 1-deaza-dGTP; P indicates reaction without dNTP.
    Dntps, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntps/product/TaKaRa
    Average 99 stars, based on 1 article reviews
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    99
    TaKaRa t4 dna ligase
    Schematic illustration of noncanonical self-assembly and biomedical applications of multifunctional DNA NFs. ( a ) RCR-based assembly of NFs. The linear DNA template was first hybridized with a primer and then ligated to form a circular template by <t>T4</t> DNA
    T4 Dna Ligase, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/t4 dna ligase/product/TaKaRa
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    Image Search Results


    ( A ) Sequences of the 25 nt template ( III ) and 20 nt primer ( IV ). ( B ) PAGE of extension reactions beyond the 1-deaza-dG residue in the template. ( C ) PAGE of extension reactions subsequent to 1-deaza-dG in the primer with Therminator™ DNA polymerase and ( D ) with AMV reverse transcriptase. Conditions used are described in Materials and Methods. Added dNTPs are indicated at the top of each gel. Z indicates 1-deaza-dGTP; P indicates reaction without dNTP.

    Journal: Nucleic Acids Research

    Article Title: A new, but old, nucleoside analog: the first synthesis of 1-deaza-2?-deoxyguanosine and its properties as a nucleoside and as oligodeoxynucleotides

    doi: 10.1093/nar/gkh154

    Figure Lengend Snippet: ( A ) Sequences of the 25 nt template ( III ) and 20 nt primer ( IV ). ( B ) PAGE of extension reactions beyond the 1-deaza-dG residue in the template. ( C ) PAGE of extension reactions subsequent to 1-deaza-dG in the primer with Therminator™ DNA polymerase and ( D ) with AMV reverse transcriptase. Conditions used are described in Materials and Methods. Added dNTPs are indicated at the top of each gel. Z indicates 1-deaza-dGTP; P indicates reaction without dNTP.

    Article Snippet: AMV reverse transcriptase, M-MLV reverse transcriptase and dNTPs were purchased from Takara Biomedicals (Japan).

    Techniques: Polyacrylamide Gel Electrophoresis

    Gli1, cyclin D1, Bcl-2 and Bax mRNA levels in blank, Lipofectamine, siRNA-Gli1, BCNU and combination groups. Semi-quantitative real-time polymerase chain reaction was performed using SuperScript III One-Step RT-PCR kit (12574-018, Invitrogen, Thermo Scientific, Waltham, MA, USA) on PCR thermo cycler (C1000, Bio-Rad, Hercules, CA, USA). The 20 μl reaction system was formed by cDNA (5 μl), 10× buffer (2 μl), 25 mmol/L MgCl 2 (0.8 μl), 2.5 mmol/L dNTP (2 μl), DNA polymerase (0.2 μl; Takara, Tokyo, Japan), and upstream and downstream primers (1 μl each). M, markers; 1, blank group; 2, Lipofectamine group; 3, BCNU group; 4, siRNA-Gli1 group; 5, combination group.

    Journal: International Journal of Clinical and Experimental Pathology

    Article Title: Knockdown of Gli1 by small-interfering RNA enhances the effects of BCNU on the proliferation and apoptosis of glioma U251 cells

    doi:

    Figure Lengend Snippet: Gli1, cyclin D1, Bcl-2 and Bax mRNA levels in blank, Lipofectamine, siRNA-Gli1, BCNU and combination groups. Semi-quantitative real-time polymerase chain reaction was performed using SuperScript III One-Step RT-PCR kit (12574-018, Invitrogen, Thermo Scientific, Waltham, MA, USA) on PCR thermo cycler (C1000, Bio-Rad, Hercules, CA, USA). The 20 μl reaction system was formed by cDNA (5 μl), 10× buffer (2 μl), 25 mmol/L MgCl 2 (0.8 μl), 2.5 mmol/L dNTP (2 μl), DNA polymerase (0.2 μl; Takara, Tokyo, Japan), and upstream and downstream primers (1 μl each). M, markers; 1, blank group; 2, Lipofectamine group; 3, BCNU group; 4, siRNA-Gli1 group; 5, combination group.

    Article Snippet: The 20 μl reaction system was formed by cDNA (5 μl), 10× buffer (2 μl), 25 mmol/L MgCl2 (0.8 μl), 2.5 mmol/L dNTP (2 μl), DNA polymerase (0.2 μl; Takara, Tokyo, Japan), and upstream and downstream primers (1 μl each).

    Techniques: Real-time Polymerase Chain Reaction, Reverse Transcription Polymerase Chain Reaction, Polymerase Chain Reaction

    Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of dNTPs. ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM NaCl, 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.

    Journal: Molecules

    Article Title: Chemical Incorporation of Chain-Terminating Nucleoside Analogs as 3′-Blocking DNA Damage and Their Removal by Human ERCC1-XPF Endonuclease

    doi: 10.3390/molecules21060766

    Figure Lengend Snippet: Primer extension from the CTNA-blocked termini by the Klenow fragment of Escherichia coli DNA polymerase I, with or without its proofreading 3′–5′ exonuclease activity (KF + or KF − , respectively, from Takara Bio, Inc., Shiga, Japan), in the ( A ) presence or ( B ) absence of dNTPs. ( A ) The 32 P-labeled oligonucleotides, 32 P-d(TCCGTTGAAGCCTGCTTT)X, where X represents no added nucleoside (OH, lanes 1–3), 2’-deoxyadenosine (lanes 4–6), acyclovir (ACV, lanes 7–9), abacavir (ABC, lanes 10–12), carbovir (CBV, lanes 13–15) or lamivudine ((−)3TC, lanes 16–18), were hybridized with their complementary strands, d(CTCGTCAGCTANAAAGCAGGCTTCAACGGA), where N represents A (for ABC and an oligonucleotide without CTNAs), G (for A and (−)3TC) or C (for ACV and CBV). Each substrate was incubated at 37 °C for 10 min, in the absence (lanes 1, 4, 7, 10, 13 and 16) or presence of KF − (0.1 unit, lanes 2, 5, 8, 11, 14 and 17) or KF + (0.1 unit, lanes 3, 6, 9, 12, 15 and 18), in 10 mM Tris-HCl buffer (pH 7.9) containing 50 mM NaCl, 10 mM MgCl 2 , 10 mM DTT and 100 µM dNTPs; ( B ) The 32 P-labeled substrates were incubated with KF + at 37 °C for the indicated incubation time, in the same reaction buffer without dNTPs.

    Article Snippet: Resumption of DNA Synthesis by DNA Polymerase after the Removal of CTNAs The hybridized oligonucleotides (400 fmol) were first treated with ERCC1-XPF (230 fmol) in 10 µL of 50 mM Tris-HCl buffer (pH 8.0), containing 2 mM MgCl2 , 0.5 mM DTT and 0.1 mg·mL−1 BSA, at 25 °C for 16 h. To the reaction mixture was added 5 µL of 30 mM Tris-HCl buffer (pH 7.9), containing 150 mM NaCl, 30 mM MgCl2 , 30 mM DTT, 300 µM dNTPs and the Klenow fragment of Escherichia coli DNA polymerase I, lacking the 3′–5′ exonuclease activity (KF− , 0.1 unit, Takara Bio).

    Techniques: Activity Assay, Labeling, Incubation

    Repair of the CTNA-containing oligonucleotides by human ERCC1-XPF endonuclease and DNA polymerase. Panels A and B represent the reaction scheme and the results, respectively. First, the 32 P-labeled substrates (400 fmol) were incubated at 25 °C for 16 h, in the absence (lanes 1, 2, 5, 6, 9, 10, 13, 14, 17, 18, 21 and 22) or presence (the other lanes) of ERCC1-XPF (230 fmol), in 10 µL of 50 mM Tris-HCl buffer (pH 8.0) containing 2 mM MgCl 2 , 0.5 mM DTT and 0.1 mg·mL −1 BSA. Then, a polymerase reaction mixture (5 µL, containing 30 mM Tris-HCl, (pH 7.9), 150 mM NaCl, 30 mM MgCl 2 , 30 mM DTT, 300 µM dNTPs and 0.1 unit of KF − for even lanes) or 5 mM EDTA (5 µL for odd lanes) was added to the reaction mixture, and the total reaction mixtures (15 µL) were incubated at 37 °C for 10 min. The cleavage sites observed with ERCC1-XPF are indicated by black triangles. The fully extended products were quantified, and the values are shown.

    Journal: Molecules

    Article Title: Chemical Incorporation of Chain-Terminating Nucleoside Analogs as 3′-Blocking DNA Damage and Their Removal by Human ERCC1-XPF Endonuclease

    doi: 10.3390/molecules21060766

    Figure Lengend Snippet: Repair of the CTNA-containing oligonucleotides by human ERCC1-XPF endonuclease and DNA polymerase. Panels A and B represent the reaction scheme and the results, respectively. First, the 32 P-labeled substrates (400 fmol) were incubated at 25 °C for 16 h, in the absence (lanes 1, 2, 5, 6, 9, 10, 13, 14, 17, 18, 21 and 22) or presence (the other lanes) of ERCC1-XPF (230 fmol), in 10 µL of 50 mM Tris-HCl buffer (pH 8.0) containing 2 mM MgCl 2 , 0.5 mM DTT and 0.1 mg·mL −1 BSA. Then, a polymerase reaction mixture (5 µL, containing 30 mM Tris-HCl, (pH 7.9), 150 mM NaCl, 30 mM MgCl 2 , 30 mM DTT, 300 µM dNTPs and 0.1 unit of KF − for even lanes) or 5 mM EDTA (5 µL for odd lanes) was added to the reaction mixture, and the total reaction mixtures (15 µL) were incubated at 37 °C for 10 min. The cleavage sites observed with ERCC1-XPF are indicated by black triangles. The fully extended products were quantified, and the values are shown.

    Article Snippet: Resumption of DNA Synthesis by DNA Polymerase after the Removal of CTNAs The hybridized oligonucleotides (400 fmol) were first treated with ERCC1-XPF (230 fmol) in 10 µL of 50 mM Tris-HCl buffer (pH 8.0), containing 2 mM MgCl2 , 0.5 mM DTT and 0.1 mg·mL−1 BSA, at 25 °C for 16 h. To the reaction mixture was added 5 µL of 30 mM Tris-HCl buffer (pH 7.9), containing 150 mM NaCl, 30 mM MgCl2 , 30 mM DTT, 300 µM dNTPs and the Klenow fragment of Escherichia coli DNA polymerase I, lacking the 3′–5′ exonuclease activity (KF− , 0.1 unit, Takara Bio).

    Techniques: Labeling, Incubation

    Schematic illustration of noncanonical self-assembly and biomedical applications of multifunctional DNA NFs. ( a ) RCR-based assembly of NFs. The linear DNA template was first hybridized with a primer and then ligated to form a circular template by T4 DNA

    Journal: Nature protocols

    Article Title: Preparation and biomedical applications of programmable and multifunctional DNA nanoflowers

    doi: 10.1038/nprot.2015.078

    Figure Lengend Snippet: Schematic illustration of noncanonical self-assembly and biomedical applications of multifunctional DNA NFs. ( a ) RCR-based assembly of NFs. The linear DNA template was first hybridized with a primer and then ligated to form a circular template by T4 DNA

    Article Snippet: Acetonitrile (CH3 CN; Sigma-Aldrich, cat. no. L810045-06) Oxidizer (0.02 M, tetrahydrofuran:H2 O:pyridine:iodine = 90.54:9.05:0.41:0.43 (vol/vol/vol/wt); Sigma-Aldrich, cat. no. L860045-06) dA-CE phosphoramidite (Glen Research, cat. no. 10-1000-10e, 1.0g) dmf-dG-CE phosphoramidite (Glen Research, cat. no. 10-1020-10e, 1.0g) dT-CE phosphoramidite (Glen Research, cat. no. 10-1030-10e, 1.0g) ac-dC-CE phosphoramidite (Glen Research, cat. no. 10-1015-10e, 1.0g) Chemical phosphorylation reagent II (CPR II; Glen Research, cat. no. 10-1901-90, 100μmoles) Thymidine lcaa CPG (1,000 Å, ChemGenes, cat. no. N-5104, 5g) Deoxyadenosine ( n -bz) 3′-lcaa CPG (1,000 Å, ChemGenes, cat. no. N-5101, 5g) Ammonium hydroxide (Sinopharm Chemical Reagent, cat. no. 10002118) Methylamine water solution (Sinopharm Chemical Reagent, cat. no. 80081228) Absolute ethanol (General-Reagent, cat. no. P1090446) Glacial acetic acid (Sinopharm Chemical Reagent, cat. no. 10000218) Triethylamine ((C2 H5 )3 N; Sigma-Aldrich, cat. no. T0886-500ML) Sodium chloride (NaCl; Adamas, cat. no. 81793B) Magnesium chloride hexahydrate (MgCl2 ·6H2 O; Sinopharm Chemical Reagent, cat. no. 10012818) Acetonitrile (CH3 CN; Adamas, cat. no. 80988C) T4 DNA ligase (400,000 units/ml; New England Biolabs, cat. no. M0202S) DNA ligation buffer, 10× (10×(50 mM Tris-HCl, 1 mM MgCl2 , 1 mM ATP and 1 mM DTT); New England Biolabs, cat. no. M0202S) dNTP (10 mM; Takara, cat. no. 4019) Cyanine 3-dUTP (1 mM; Enzo Life Sciences, cat. no. ENZ-42501) Cyanine 5-dUTP (1 mM; Enzo Life Sciences, cat. no. ENZ-42502) Fluorescein-12-ddUTP (1 mM; Enzo Life Sciences, cat. no. ENZ-42833) (6) ROX-12-ddUTP (0.1 mM; Enzo Life Sciences, cat. no. ENZ-42857) BSA, 10× (New England Biolabs, cat. no. M0269S) Phi29 DNA polymerase (10,000 units/ml; New England Biolabs, cat. no. M0269S) phi29 DNA polymerase buffer, 10× (10×(50 mM Tris-HCl, 10 mM (NH4 )2 SO4 , 10 mM MgCl2 and 4 mM DTT); New England Biolabs, cat. no. M0269S) Dulbecco’s PBS (1× DPBS basic; Gibco, cat. no. C14190500BT-500ml) Agarose (HydraGene, cat. no. R9012LE-100g) Ethidium bromide (Dingguo, cat. no. NEP028) !

    Techniques: