dinucleotide apu Search Results


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  • 85
    RiboMed dinucleotide apu
    Dinucleotide Apu, supplied by RiboMed, used in various techniques. Bioz Stars score: 85/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dinucleotide apu/product/RiboMed
    Average 85 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    dinucleotide apu - by Bioz Stars, 2020-05
    85/100 stars
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    85
    Millipore dinucleotide apu
    Dinucleotide Apu, supplied by Millipore, used in various techniques. Bioz Stars score: 85/100, based on 18 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dinucleotide apu/product/Millipore
    Average 85 stars, based on 18 article reviews
    Price from $9.99 to $1999.99
    dinucleotide apu - by Bioz Stars, 2020-05
    85/100 stars
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    91
    TriLink apu dinucleotide primer
    Apu Dinucleotide Primer, supplied by TriLink, used in various techniques. Bioz Stars score: 91/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/apu dinucleotide primer/product/TriLink
    Average 91 stars, based on 23 article reviews
    Price from $9.99 to $1999.99
    apu dinucleotide primer - by Bioz Stars, 2020-05
    91/100 stars
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    85
    TriLink dinucleotide apu
    Displacement of <t>RNAP</t> βR529C by Mfd in vitro . (A) EMSA showing the displacement of RNAP βR529C by Mfd. Initiation complexes (IC) were formed by incubation of RNAP βR529C holoenzyme with a radio-labelled fragment of pSRT7A1 (F). Elongation complexes stalled at + 21 (EC) were formed by addition of 100 µM <t>ApU,</t> 2 mM ATP, 10 µM GTP, 10 µM CTP and 10 µM 3'dUTP. 250 nM Mfd was added and samples were loaded on a gel at the time points indicated. (B) Time course of the displacement of stalled elongation complexes by Mfd at 37 °C. Elongation complexes were formed with wild-type RNAP (open triangles) and with RNAP βR529C (filled diamonds). The stability of RNAP βR529C elongation complexes was also monitored in the absence of Mfd (filled squares). Data points represent the percentage of elongation complex present at each time point, relative to the amount at t=0 and are expressed as the average of three independent experiments (with standard deviation).
    Dinucleotide Apu, supplied by TriLink, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dinucleotide apu/product/TriLink
    Average 85 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    dinucleotide apu - by Bioz Stars, 2020-05
    85/100 stars
      Buy from Supplier

    Image Search Results


    Displacement of RNAP βR529C by Mfd in vitro . (A) EMSA showing the displacement of RNAP βR529C by Mfd. Initiation complexes (IC) were formed by incubation of RNAP βR529C holoenzyme with a radio-labelled fragment of pSRT7A1 (F). Elongation complexes stalled at + 21 (EC) were formed by addition of 100 µM ApU, 2 mM ATP, 10 µM GTP, 10 µM CTP and 10 µM 3'dUTP. 250 nM Mfd was added and samples were loaded on a gel at the time points indicated. (B) Time course of the displacement of stalled elongation complexes by Mfd at 37 °C. Elongation complexes were formed with wild-type RNAP (open triangles) and with RNAP βR529C (filled diamonds). The stability of RNAP βR529C elongation complexes was also monitored in the absence of Mfd (filled squares). Data points represent the percentage of elongation complex present at each time point, relative to the amount at t=0 and are expressed as the average of three independent experiments (with standard deviation).

    Journal: DNA repair

    Article Title: Transcription coupled nucleotide excision repair in Escherichia coli can be affected by changing the arginine at position 529 of the β subunit of RNA polymerase

    doi: 10.1016/j.dnarep.2007.04.002

    Figure Lengend Snippet: Displacement of RNAP βR529C by Mfd in vitro . (A) EMSA showing the displacement of RNAP βR529C by Mfd. Initiation complexes (IC) were formed by incubation of RNAP βR529C holoenzyme with a radio-labelled fragment of pSRT7A1 (F). Elongation complexes stalled at + 21 (EC) were formed by addition of 100 µM ApU, 2 mM ATP, 10 µM GTP, 10 µM CTP and 10 µM 3'dUTP. 250 nM Mfd was added and samples were loaded on a gel at the time points indicated. (B) Time course of the displacement of stalled elongation complexes by Mfd at 37 °C. Elongation complexes were formed with wild-type RNAP (open triangles) and with RNAP βR529C (filled diamonds). The stability of RNAP βR529C elongation complexes was also monitored in the absence of Mfd (filled squares). Data points represent the percentage of elongation complex present at each time point, relative to the amount at t=0 and are expressed as the average of three independent experiments (with standard deviation).

    Article Snippet: Transcription was therefore initiated using the dinucleotide ApU and RNAP was stalled at +21 by the addition of 3'dUTP (TriLink Biotechnologies).

    Techniques: In Vitro, Incubation, Standard Deviation