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  • 99
    New England Biolabs escherichia coli uracil dna glycosylase
    Pol β dRP lyase activity assay. ( A ) <t>DNA</t> oligo (15-mer) was 5′-end labeled with γ- 32 P-ATP. Experiments were conducted as described in Materials and Methods. The reaction with Pol β was initiated ∼30 s after <t>UDG</t> incubation. A negative control was included to subtract the spontaneous loss of the 5′-dRP. A heat control (H), as described in Materials and Methods, was included to determine the actual dRP substrate generated after the 5.5-min UDG incubation. Full length Pol β (FL) or the N-terminal domain of Pol β (8 kDa) were used to determine dRP lyase activity. A representative phosphor image of a 20% polyacrylamide denaturing gel of the replicates plotted in panel (B) is shown. ( B ) NCP crystal structure pdb file 3LZ0 ( 37 ) was modified to show the structural location of the 5′-dRP group (black spheres). This is the back view of that shown in Figure 1 . Data represent the mean of three independent experiments ± SD. Kinetic parameters are provided in Table 2 (full length Pol β) and Table 3 (8 kDa domain of Pol β). As shown in Table 2 , the ratio (DNA/NCP) of the enzymatic rates for this 5′-end labeled substrate is comparable to the ratio found by the 3′-end labeling assay ( Supplementary Figure S3 ). The rate of spontaneous loss, estimated from the –Pol β control, for the NCP is ∼3.2 nM/min, which is 8-fold faster than the rate in DNA of 0.4 nM/min.
    Escherichia Coli Uracil Dna Glycosylase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Millipore escherichia coli uracil dna glycosylase
    Pol β dRP lyase activity assay. ( A ) <t>DNA</t> oligo (15-mer) was 5′-end labeled with γ- 32 P-ATP. Experiments were conducted as described in Materials and Methods. The reaction with Pol β was initiated ∼30 s after <t>UDG</t> incubation. A negative control was included to subtract the spontaneous loss of the 5′-dRP. A heat control (H), as described in Materials and Methods, was included to determine the actual dRP substrate generated after the 5.5-min UDG incubation. Full length Pol β (FL) or the N-terminal domain of Pol β (8 kDa) were used to determine dRP lyase activity. A representative phosphor image of a 20% polyacrylamide denaturing gel of the replicates plotted in panel (B) is shown. ( B ) NCP crystal structure pdb file 3LZ0 ( 37 ) was modified to show the structural location of the 5′-dRP group (black spheres). This is the back view of that shown in Figure 1 . Data represent the mean of three independent experiments ± SD. Kinetic parameters are provided in Table 2 (full length Pol β) and Table 3 (8 kDa domain of Pol β). As shown in Table 2 , the ratio (DNA/NCP) of the enzymatic rates for this 5′-end labeled substrate is comparable to the ratio found by the 3′-end labeling assay ( Supplementary Figure S3 ). The rate of spontaneous loss, estimated from the –Pol β control, for the NCP is ∼3.2 nM/min, which is 8-fold faster than the rate in DNA of 0.4 nM/min.
    Escherichia Coli Uracil Dna Glycosylase, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Price from $9.99 to $1999.99
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    94
    Bio-Rad e coli cj236
    Pol β dRP lyase activity assay. ( A ) <t>DNA</t> oligo (15-mer) was 5′-end labeled with γ- 32 P-ATP. Experiments were conducted as described in Materials and Methods. The reaction with Pol β was initiated ∼30 s after <t>UDG</t> incubation. A negative control was included to subtract the spontaneous loss of the 5′-dRP. A heat control (H), as described in Materials and Methods, was included to determine the actual dRP substrate generated after the 5.5-min UDG incubation. Full length Pol β (FL) or the N-terminal domain of Pol β (8 kDa) were used to determine dRP lyase activity. A representative phosphor image of a 20% polyacrylamide denaturing gel of the replicates plotted in panel (B) is shown. ( B ) NCP crystal structure pdb file 3LZ0 ( 37 ) was modified to show the structural location of the 5′-dRP group (black spheres). This is the back view of that shown in Figure 1 . Data represent the mean of three independent experiments ± SD. Kinetic parameters are provided in Table 2 (full length Pol β) and Table 3 (8 kDa domain of Pol β). As shown in Table 2 , the ratio (DNA/NCP) of the enzymatic rates for this 5′-end labeled substrate is comparable to the ratio found by the 3′-end labeling assay ( Supplementary Figure S3 ). The rate of spontaneous loss, estimated from the –Pol β control, for the NCP is ∼3.2 nM/min, which is 8-fold faster than the rate in DNA of 0.4 nM/min.
    E Coli Cj236, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    e coli cj236 - by Bioz Stars, 2021-04
    94/100 stars
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    Image Search Results


    Pol β dRP lyase activity assay. ( A ) DNA oligo (15-mer) was 5′-end labeled with γ- 32 P-ATP. Experiments were conducted as described in Materials and Methods. The reaction with Pol β was initiated ∼30 s after UDG incubation. A negative control was included to subtract the spontaneous loss of the 5′-dRP. A heat control (H), as described in Materials and Methods, was included to determine the actual dRP substrate generated after the 5.5-min UDG incubation. Full length Pol β (FL) or the N-terminal domain of Pol β (8 kDa) were used to determine dRP lyase activity. A representative phosphor image of a 20% polyacrylamide denaturing gel of the replicates plotted in panel (B) is shown. ( B ) NCP crystal structure pdb file 3LZ0 ( 37 ) was modified to show the structural location of the 5′-dRP group (black spheres). This is the back view of that shown in Figure 1 . Data represent the mean of three independent experiments ± SD. Kinetic parameters are provided in Table 2 (full length Pol β) and Table 3 (8 kDa domain of Pol β). As shown in Table 2 , the ratio (DNA/NCP) of the enzymatic rates for this 5′-end labeled substrate is comparable to the ratio found by the 3′-end labeling assay ( Supplementary Figure S3 ). The rate of spontaneous loss, estimated from the –Pol β control, for the NCP is ∼3.2 nM/min, which is 8-fold faster than the rate in DNA of 0.4 nM/min.

    Journal: Nucleic Acids Research

    Article Title: Unencumbered Pol β lyase activity in nucleosome core particles

    doi: 10.1093/nar/gkx593

    Figure Lengend Snippet: Pol β dRP lyase activity assay. ( A ) DNA oligo (15-mer) was 5′-end labeled with γ- 32 P-ATP. Experiments were conducted as described in Materials and Methods. The reaction with Pol β was initiated ∼30 s after UDG incubation. A negative control was included to subtract the spontaneous loss of the 5′-dRP. A heat control (H), as described in Materials and Methods, was included to determine the actual dRP substrate generated after the 5.5-min UDG incubation. Full length Pol β (FL) or the N-terminal domain of Pol β (8 kDa) were used to determine dRP lyase activity. A representative phosphor image of a 20% polyacrylamide denaturing gel of the replicates plotted in panel (B) is shown. ( B ) NCP crystal structure pdb file 3LZ0 ( 37 ) was modified to show the structural location of the 5′-dRP group (black spheres). This is the back view of that shown in Figure 1 . Data represent the mean of three independent experiments ± SD. Kinetic parameters are provided in Table 2 (full length Pol β) and Table 3 (8 kDa domain of Pol β). As shown in Table 2 , the ratio (DNA/NCP) of the enzymatic rates for this 5′-end labeled substrate is comparable to the ratio found by the 3′-end labeling assay ( Supplementary Figure S3 ). The rate of spontaneous loss, estimated from the –Pol β control, for the NCP is ∼3.2 nM/min, which is 8-fold faster than the rate in DNA of 0.4 nM/min.

    Article Snippet: E. coli uracil DNA glycosylase (UDG) was from New England Biolabs.

    Techniques: Activity Assay, Labeling, Incubation, Negative Control, Generated, Modification, End Labeling