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TaKaRa dntps
Dntps, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 1537 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/dntps/product/TaKaRa
Average 99 stars, based on 1537 article reviews
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dntps - by Bioz Stars, 2020-04
99/100 stars

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    TaKaRa telomeric repeat amplification protocol trap lig assay dntp mix
    The Pt-tripod binds the intramolecular hybrid-1 human <t>telomeric</t> G-quadruplex and inhibits telomerase activity. a The chemical structure of the Pt-tripod with proton numbering. b The folding topology of the hybrid-1 human telomeric G-quadruplex adopted by Tel26 in K + solution 44 . Deep gray box = ( syn ) guanine, light gray box = ( anti ) guanine. c Imino proton regions of the 1D 1 H NMR titration spectra of Tel26 interacting with Pt-tripod in 100 mM K + , pH 7.0 solution, at 25 °C. Ratios of Pt-tripod/Tel26 are shown in the spectra. The imino assignments are labeled. Peaks arising from the new complexes are marked with asterisks. d CD spectra of the Tel26 titrated by the Pt-tripod in 100 mM K + solution. Ratios of Pt-tripod/Tel26 are shown in the spectra. e The Pt-tripod showed excellent telomerase inhibition property by the <t>TRAP-LIG</t> assay. The band labeled as ITAS is an internal control primer. The IC 50 value is determined to be 1.22 ± 0.10 μM. Error value represents the standard deviation, n = 3
    Telomeric Repeat Amplification Protocol Trap Lig Assay Dntp Mix, supplied by TaKaRa, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/telomeric repeat amplification protocol trap lig assay dntp mix/product/TaKaRa
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    telomeric repeat amplification protocol trap lig assay dntp mix - by Bioz Stars, 2020-04
    93/100 stars
      Buy from Supplier

    99
    TaKaRa dntps
    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 <t>dNTPs.</t> ( 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 <t>NaCl,</t> 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.
    Dntps, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 1675 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntps/product/TaKaRa
    Average 99 stars, based on 1675 article reviews
    Price from $9.99 to $1999.99
    dntps - by Bioz Stars, 2020-04
    99/100 stars
      Buy from Supplier

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    The Pt-tripod binds the intramolecular hybrid-1 human telomeric G-quadruplex and inhibits telomerase activity. a The chemical structure of the Pt-tripod with proton numbering. b The folding topology of the hybrid-1 human telomeric G-quadruplex adopted by Tel26 in K + solution 44 . Deep gray box = ( syn ) guanine, light gray box = ( anti ) guanine. c Imino proton regions of the 1D 1 H NMR titration spectra of Tel26 interacting with Pt-tripod in 100 mM K + , pH 7.0 solution, at 25 °C. Ratios of Pt-tripod/Tel26 are shown in the spectra. The imino assignments are labeled. Peaks arising from the new complexes are marked with asterisks. d CD spectra of the Tel26 titrated by the Pt-tripod in 100 mM K + solution. Ratios of Pt-tripod/Tel26 are shown in the spectra. e The Pt-tripod showed excellent telomerase inhibition property by the TRAP-LIG assay. The band labeled as ITAS is an internal control primer. The IC 50 value is determined to be 1.22 ± 0.10 μM. Error value represents the standard deviation, n = 3

    Journal: Nature Communications

    Article Title: Solution structures of multiple G-quadruplex complexes induced by a platinum(II)-based tripod reveal dynamic binding

    doi: 10.1038/s41467-018-05810-4

    Figure Lengend Snippet: The Pt-tripod binds the intramolecular hybrid-1 human telomeric G-quadruplex and inhibits telomerase activity. a The chemical structure of the Pt-tripod with proton numbering. b The folding topology of the hybrid-1 human telomeric G-quadruplex adopted by Tel26 in K + solution 44 . Deep gray box = ( syn ) guanine, light gray box = ( anti ) guanine. c Imino proton regions of the 1D 1 H NMR titration spectra of Tel26 interacting with Pt-tripod in 100 mM K + , pH 7.0 solution, at 25 °C. Ratios of Pt-tripod/Tel26 are shown in the spectra. The imino assignments are labeled. Peaks arising from the new complexes are marked with asterisks. d CD spectra of the Tel26 titrated by the Pt-tripod in 100 mM K + solution. Ratios of Pt-tripod/Tel26 are shown in the spectra. e The Pt-tripod showed excellent telomerase inhibition property by the TRAP-LIG assay. The band labeled as ITAS is an internal control primer. The IC 50 value is determined to be 1.22 ± 0.10 μM. Error value represents the standard deviation, n = 3

    Article Snippet: Telomeric repeat amplification protocol (TRAP-LIG) assay dNTP mix, RNase inhibitor, and Taq polymerase were purchased from TaKaRa Biotechnology.

    Techniques: Activity Assay, Nuclear Magnetic Resonance, Titration, Labeling, Inhibition, Standard Deviation

    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

    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

    Optimization of iTaq (DNA polymerase), dNTPs, and Mg 2+ for the duplex real-time PCR. (A) Amplification data of the duplex real-time PCR system directly combined by two single-plex systems without any extra reagents. RFU means relative fluorescence units. (B) Amplification data of V 2 – 5 phage at different concentrations of additional MgCl 2 and dNTPs and (C) DNA polymerase (iTaq).

    Journal: Frontiers in Microbiology

    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

    doi: 10.3389/fmicb.2019.03023

    Figure Lengend Snippet: Optimization of iTaq (DNA polymerase), dNTPs, and Mg 2+ for the duplex real-time PCR. (A) Amplification data of the duplex real-time PCR system directly combined by two single-plex systems without any extra reagents. RFU means relative fluorescence units. (B) Amplification data of V 2 – 5 phage at different concentrations of additional MgCl 2 and dNTPs and (C) DNA polymerase (iTaq).

    Article Snippet: DNA polymerase (iTaq), Mg2+ , dNTPs, 6× loading buffer, and DNA marker were bought from Takara Bio (Beijing, China).

    Techniques: Real-time Polymerase Chain Reaction, Amplification, Fluorescence