dntp mixture  (TaKaRa)

 
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    Name:
    dNTP Mixture
    Description:
    Our dNTPs for PCR are 98 pure and are tested for quality control in a variety of applications Individual dNTPs are supplied at a concentration of 100 mM and can be diluted with water or buffer as needed The dNTP Set Cat 4025 provides one of each of the four deoxynucleotide triphosphates
    Catalog Number:
    4030
    Price:
    None
    Size:
    3 2 µmol Each 1 25 mL
    Category:
    dNTPs dNTPs Other PCR related products PCR
    Buy from Supplier


    Structured Review

    TaKaRa dntp mixture
    Our dNTPs for PCR are 98 pure and are tested for quality control in a variety of applications Individual dNTPs are supplied at a concentration of 100 mM and can be diluted with water or buffer as needed The dNTP Set Cat 4025 provides one of each of the four deoxynucleotide triphosphates
    https://www.bioz.com/result/dntp mixture/product/TaKaRa
    Average 99 stars, based on 731 article reviews
    Price from $9.99 to $1999.99
    dntp mixture - by Bioz Stars, 2020-07
    99/100 stars

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    Related Articles

    Amplification:

    Article Title: Essential Domains for Ribonucleoprotein Complex Formation Required for Retrotransposition of Telomere-Specific Non-Long Terminal Repeat Retrotransposon SART1 †
    Article Snippet: .. 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: Development and characterization of 16 novel microsatellite markers by Transcriptome sequencing for Angelica dahurica and test for cross-species amplification
    Article Snippet: .. The amplification reactions were carried out with 2720 thermal cycler (Applied Biosystems, Foster City, CA) in 20 μl volume containing 20 ng of genomic DNA, 0.2 mM of each dNTP, 0.4 μM of each primer, 10 × PCR buffer (Mg2+ free), 2.5 mM Mg2+ , 1 unit of Taq DNA polymerase (Takara, Dalian, China) with the following conditions: initial denaturation at 95 °C for 5 min, followed by 35 cycles of 94 °C, 30 s; 50 to 55 °C, 60 s; 72 °C, 45 s and a final extension of 72 °C for 8 min. ..

    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: .. 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: .. 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 ( ; ).

    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: .. 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). ..

    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: .. 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: Source identification of airborne Escherichia coli of swine house surroundings using ERIC-PCR and REP-PCR
    Article Snippet: .. 2.5 ERIC-PCR and REP-PCR The PCR reaction mixture (25 μL) contained 1.5 U Taq DNA polymerase (TaKaRa), 300 ng μL−1 of each primer, 0.875 mM of each dNTP, 1× reaction buffer and 1.5 mM MgCl2 (TaKaRa). .. Amplification was performed in a thermocycler (Eppendorf, Germany) as follows: an initial denaturation (94 °C, 5 min) followed by 35 cycles of denaturation (94 °C, 1 min), annealing (1 min at 42 °C), and extension (65 °C, 8 min) with a single final extension (65 °C, 16 min).

    Article Title: Development and characterization of 16 novel microsatellite markers by Transcriptome sequencing for Angelica dahurica and test for cross-species amplification
    Article Snippet: .. The amplification reactions were carried out with 2720 thermal cycler (Applied Biosystems, Foster City, CA) in 20 μl volume containing 20 ng of genomic DNA, 0.2 mM of each dNTP, 0.4 μM of each primer, 10 × PCR buffer (Mg2+ free), 2.5 mM Mg2+ , 1 unit of Taq DNA polymerase (Takara, Dalian, China) with the following conditions: initial denaturation at 95 °C for 5 min, followed by 35 cycles of 94 °C, 30 s; 50 to 55 °C, 60 s; 72 °C, 45 s and a final extension of 72 °C for 8 min. ..

    Plasmid Preparation:

    Article Title: A transcription and translation-coupled DNA replication system using rolling-circle replication
    Article Snippet: .. 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.

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  • 92
    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: 92/100, 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 92 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, 2020-07
    92/100 stars
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    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 2026 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dntps/product/TaKaRa
    Average 99 stars, based on 2026 article reviews
    Price from $9.99 to $1999.99
    dntps - by Bioz Stars, 2020-07
    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