exonuclease i Takara Search Results


  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 99
    New England Biolabs exonuclease i
    Exonuclease I, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 5008 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/exonuclease i/product/New England Biolabs
    Average 99 stars, based on 5008 article reviews
    Price from $9.99 to $1999.99
    exonuclease i - by Bioz Stars, 2020-08
    99/100 stars
      Buy from Supplier

    96
    TaKaRa exonuclease i
    Amount of residual DNAs in the presence of 0% (w/v) (open circles), 5% (w/v) (closed circles), 10% (w/v) (closed triangles), 15% (w/v) (closed squares) and 20% (w/v) (closed diamonds) of PEG and ( A ) 0.1 U DNase I, ( B ) 0.15 U S1 nuclease, ( C ) 1 U exonuclease III (inset shows 10 U), ( D ) 0.5 U <t>exonuclease</t> I (inset shows 5 U). A ssDNA was used as a substrate for S1 nuclease and exonuclease I and a dsDNA was used as a substrate for DNase I and exonuclease III. PEG 4000 was used as the crowding agent for DNase I and S1 nuclease reactions, and PEG 8000 was used for exonucleases III and I. Error bars (smaller than ±2%) were omitted for clarity.
    Exonuclease I, supplied by TaKaRa, used in various techniques. Bioz Stars score: 96/100, based on 612 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/exonuclease i/product/TaKaRa
    Average 96 stars, based on 612 article reviews
    Price from $9.99 to $1999.99
    exonuclease i - by Bioz Stars, 2020-08
    96/100 stars
      Buy from Supplier

    99
    TaKaRa alkaline phosphatase exonuclease i shrimp
    Amount of residual DNAs in the presence of 0% (w/v) (open circles), 5% (w/v) (closed circles), 10% (w/v) (closed triangles), 15% (w/v) (closed squares) and 20% (w/v) (closed diamonds) of PEG and ( A ) 0.1 U DNase I, ( B ) 0.15 U S1 nuclease, ( C ) 1 U exonuclease III (inset shows 10 U), ( D ) 0.5 U <t>exonuclease</t> I (inset shows 5 U). A ssDNA was used as a substrate for S1 nuclease and exonuclease I and a dsDNA was used as a substrate for DNase I and exonuclease III. PEG 4000 was used as the crowding agent for DNase I and S1 nuclease reactions, and PEG 8000 was used for exonucleases III and I. Error bars (smaller than ±2%) were omitted for clarity.
    Alkaline Phosphatase Exonuclease I Shrimp, supplied by TaKaRa, used in various techniques. Bioz Stars score: 99/100, based on 16 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/alkaline phosphatase exonuclease i shrimp/product/TaKaRa
    Average 99 stars, based on 16 article reviews
    Price from $9.99 to $1999.99
    alkaline phosphatase exonuclease i shrimp - by Bioz Stars, 2020-08
    99/100 stars
      Buy from Supplier

    Image Search Results


    Amount of residual DNAs in the presence of 0% (w/v) (open circles), 5% (w/v) (closed circles), 10% (w/v) (closed triangles), 15% (w/v) (closed squares) and 20% (w/v) (closed diamonds) of PEG and ( A ) 0.1 U DNase I, ( B ) 0.15 U S1 nuclease, ( C ) 1 U exonuclease III (inset shows 10 U), ( D ) 0.5 U exonuclease I (inset shows 5 U). A ssDNA was used as a substrate for S1 nuclease and exonuclease I and a dsDNA was used as a substrate for DNase I and exonuclease III. PEG 4000 was used as the crowding agent for DNase I and S1 nuclease reactions, and PEG 8000 was used for exonucleases III and I. Error bars (smaller than ±2%) were omitted for clarity.

    Journal: Nucleic Acids Research

    Article Title: Regulation of DNA nucleases by molecular crowding

    doi: 10.1093/nar/gkm445

    Figure Lengend Snippet: Amount of residual DNAs in the presence of 0% (w/v) (open circles), 5% (w/v) (closed circles), 10% (w/v) (closed triangles), 15% (w/v) (closed squares) and 20% (w/v) (closed diamonds) of PEG and ( A ) 0.1 U DNase I, ( B ) 0.15 U S1 nuclease, ( C ) 1 U exonuclease III (inset shows 10 U), ( D ) 0.5 U exonuclease I (inset shows 5 U). A ssDNA was used as a substrate for S1 nuclease and exonuclease I and a dsDNA was used as a substrate for DNase I and exonuclease III. PEG 4000 was used as the crowding agent for DNase I and S1 nuclease reactions, and PEG 8000 was used for exonucleases III and I. Error bars (smaller than ±2%) were omitted for clarity.

    Article Snippet: Exonuclease I from Escherichia coli , S1 nuclease from Asergillus oryzae and exonuclease III from E. coli were purchased from Takara Bio (Tokyo, Japan).

    Techniques:

    Initial velocities ( v ) for the DNase I ( A ) and exonuclease I ( B ) hydrolysis reactions in the presence of 0% (w/v) (open circles), 5% (w/v) (closed circles), 10% (w/v) (closed triangles), 15% (w/v) (closed squares) and 20% (w/v) PEG (closed diamonds). The DNase I reaction was carried out in a buffer containing 100 mM NaCl, 5 mM MgCl 2 and 50 mM HEPES (pH 7.2) at 25°C in the absence or presence of PEG 4000. The exonuclease I reaction was carried out in a buffer containing 100 mM NaCl, 6.7 mM MgCl 2 , 10 mM 2-mercaptoethanol and 67 mM glycine-KOH (pH 9.5) at 37°C in the absence or presence of PEG 8000. The dsDNA and ssDNA concentrations in kinetic assays were 0.1–20 μM for DNase I and 0.1–10 μM for exonuclease I. The value of v was plotted versus the concentration of substrate DNA. Error bars (smaller than ±1%) were omitted for clarity.

    Journal: Nucleic Acids Research

    Article Title: Regulation of DNA nucleases by molecular crowding

    doi: 10.1093/nar/gkm445

    Figure Lengend Snippet: Initial velocities ( v ) for the DNase I ( A ) and exonuclease I ( B ) hydrolysis reactions in the presence of 0% (w/v) (open circles), 5% (w/v) (closed circles), 10% (w/v) (closed triangles), 15% (w/v) (closed squares) and 20% (w/v) PEG (closed diamonds). The DNase I reaction was carried out in a buffer containing 100 mM NaCl, 5 mM MgCl 2 and 50 mM HEPES (pH 7.2) at 25°C in the absence or presence of PEG 4000. The exonuclease I reaction was carried out in a buffer containing 100 mM NaCl, 6.7 mM MgCl 2 , 10 mM 2-mercaptoethanol and 67 mM glycine-KOH (pH 9.5) at 37°C in the absence or presence of PEG 8000. The dsDNA and ssDNA concentrations in kinetic assays were 0.1–20 μM for DNase I and 0.1–10 μM for exonuclease I. The value of v was plotted versus the concentration of substrate DNA. Error bars (smaller than ±1%) were omitted for clarity.

    Article Snippet: Exonuclease I from Escherichia coli , S1 nuclease from Asergillus oryzae and exonuclease III from E. coli were purchased from Takara Bio (Tokyo, Japan).

    Techniques: Concentration Assay

    Residual activities of DNase I and exonuclease I after incubation for 0–30 min at 60°C. Hydrolysis by DNase I in the absence (open circles) or presence (closed circles) of 20% (w/v) PEG 4000 was carried out for 10 min at 25°C. Hydrolysis by exonuclease I in the absence (open triangles) or presence (closed triangles) of 20% (w/v) PEG 8000 was carried out for 10 min at 37°C.

    Journal: Nucleic Acids Research

    Article Title: Regulation of DNA nucleases by molecular crowding

    doi: 10.1093/nar/gkm445

    Figure Lengend Snippet: Residual activities of DNase I and exonuclease I after incubation for 0–30 min at 60°C. Hydrolysis by DNase I in the absence (open circles) or presence (closed circles) of 20% (w/v) PEG 4000 was carried out for 10 min at 25°C. Hydrolysis by exonuclease I in the absence (open triangles) or presence (closed triangles) of 20% (w/v) PEG 8000 was carried out for 10 min at 37°C.

    Article Snippet: Exonuclease I from Escherichia coli , S1 nuclease from Asergillus oryzae and exonuclease III from E. coli were purchased from Takara Bio (Tokyo, Japan).

    Techniques: Incubation

    The genomic structures of the  POLD1  ( a ) and  POLE  ( b ) genes and the functional domains in their protein products. The exons corresponding to the 3′ exonuclease, that is, proofreading, domains are indicated in red and the genomic regions sequenced

    Journal: European Journal of Human Genetics

    Article Title: Concurrent genetic alterations in DNA polymerase proofreading and mismatch repair in human colorectal cancer

    doi: 10.1038/ejhg.2010.216

    Figure Lengend Snippet: The genomic structures of the POLD1 ( a ) and POLE ( b ) genes and the functional domains in their protein products. The exons corresponding to the 3′ exonuclease, that is, proofreading, domains are indicated in red and the genomic regions sequenced

    Article Snippet: The 2.5-kbp genomic sequences in the POLD1 and POLE genes that encompass the regions encoding the proofreading domains of pol delta and epsilon ( ) were amplified by PCR using Taq polymerase with the 3′ exonuclease activity, EX Taq (TaKaRa Bio Inc., Otsu, Japan), and the oligonucleotide primers shown in .

    Techniques: Functional Assay

    The distal region of the IL-6 promoter contains functional C/EBP motifs A. IL-6 promoter Luciferase activity in PC3 cells transfected with the pGL2-IL-6 deletion mutants shown on the left and pRV with and without treatment with rGal-3BP (2.5 µg/ml) for 24 hours. The data represent the mean (±SD) ratio Firefly Luciferase/Renilla Luciferase and are representative of one among three separate experiments each performed in triplicate samples. B. Sequencing analysis of the region of the IL-6 promoter extending from position −1586 to −1255 showing the presence of 3 C/EBP domains. C. EMSA of nuclear extracts from PC3 cells treated with rGAL-3BP (5 µg/ml) using biotinylated oligonucleotides in the presence of 10× fold excess of non-biotinylated oligonucleotides when indicated.

    Journal: Cancer research

    Article Title: A GALECTIN-3-DEPENDENT PATHWAY UPREGULATES INTERLEUKIN-6 IN THE MICROENVIRONMENT OF HUMAN NEUROBLASTOMA

    doi: 10.1158/0008-5472.CAN-11-2165

    Figure Lengend Snippet: The distal region of the IL-6 promoter contains functional C/EBP motifs A. IL-6 promoter Luciferase activity in PC3 cells transfected with the pGL2-IL-6 deletion mutants shown on the left and pRV with and without treatment with rGal-3BP (2.5 µg/ml) for 24 hours. The data represent the mean (±SD) ratio Firefly Luciferase/Renilla Luciferase and are representative of one among three separate experiments each performed in triplicate samples. B. Sequencing analysis of the region of the IL-6 promoter extending from position −1586 to −1255 showing the presence of 3 C/EBP domains. C. EMSA of nuclear extracts from PC3 cells treated with rGAL-3BP (5 µg/ml) using biotinylated oligonucleotides in the presence of 10× fold excess of non-biotinylated oligonucleotides when indicated.

    Article Snippet: IL-6 promoter deletion mutants in the pGL2-IL-6-Luc construct were generated either by Exonuclease III digestion using the Deletion Kit for kilo sequencing (Takara) in accordance with the instructions of the manufacturer (deletion −1041) or by restriction endonuclease digestion with KpnI and NheI (deletion mutant −212) followed by Klenow fragment reaction at 37°C for 15 minutes.

    Techniques: Functional Assay, Luciferase, Activity Assay, Transfection, Sequencing

    Exonuclease III digestion patterns of wt and tailless nucleosomes. Nucleosomes were digested for 0 (lanes 2, 6, 10, 14, and 18), 2 (lanes 3, 7, 11, 15, and 19), 4 (lanes 4, 8, 12, 16, and 20), or 8 (lanes 5, 9, 13, 17, and 21) min at 37 °C by Escherichia coli exonuclease III. The reaction was stopped by the addition of proteinase K, and the DNA was extracted with phenol/chloroform, precipitated with ethanol, and dissolved in Hi–Di Formamide. The purified DNA samples were analyzed by 10% denaturing PAGE.

    Journal: FEBS Open Bio

    Article Title: Contribution of histone N-terminal tails to the structure and stability of nucleosomes

    doi: 10.1016/j.fob.2013.08.007

    Figure Lengend Snippet: Exonuclease III digestion patterns of wt and tailless nucleosomes. Nucleosomes were digested for 0 (lanes 2, 6, 10, 14, and 18), 2 (lanes 3, 7, 11, 15, and 19), 4 (lanes 4, 8, 12, 16, and 20), or 8 (lanes 5, 9, 13, 17, and 21) min at 37 °C by Escherichia coli exonuclease III. The reaction was stopped by the addition of proteinase K, and the DNA was extracted with phenol/chloroform, precipitated with ethanol, and dissolved in Hi–Di Formamide. The purified DNA samples were analyzed by 10% denaturing PAGE.

    Article Snippet: Briefly, each reconstituted nucleosome, containing tlH2A, tlH2B, tlH3, or tlH4, was treated with 5 units of Escherichia coli exonuclease III (Takara), in 10 μl of 50 mM Tris–HCl (pH 8.0), 5 mM MgCl2 , and 1 mM DTT.

    Techniques: Purification, Polyacrylamide Gel Electrophoresis

    The DNA end close to CENP-A is asymmetrically flexible in the CENP-A/H3.3 nucleosome. (a) MNase assay. The H3.3, CENP-A, and CENP-A/H3.3 nucleosomes were treated with MNase (0, 0.3, 0.5 and 0.7 units), and the resulting DNA fragments were analyzed by native PAGE. The gel image shown is a representative of four independent experiments, in which similar results were obtained. (b) ExoIII assay. The H3.3, CENP-A, or CENP-A/H3.3 nucleosomes were incubated with or without 2.0 units of ExoIII for 2.5, 5 and 7.5 minutes at 37°C, and the resultant DNA fragments were extracted and analyzed by 14% denaturing PAGE with 7 M urea. The gel image shown is a representative of three independent experiments, in which similar results were obtained.

    Journal: Scientific Reports

    Article Title: Crystal structure and stable property of the cancer-associated heterotypic nucleosome containing CENP-A and H3.3

    doi: 10.1038/srep07115

    Figure Lengend Snippet: The DNA end close to CENP-A is asymmetrically flexible in the CENP-A/H3.3 nucleosome. (a) MNase assay. The H3.3, CENP-A, and CENP-A/H3.3 nucleosomes were treated with MNase (0, 0.3, 0.5 and 0.7 units), and the resulting DNA fragments were analyzed by native PAGE. The gel image shown is a representative of four independent experiments, in which similar results were obtained. (b) ExoIII assay. The H3.3, CENP-A, or CENP-A/H3.3 nucleosomes were incubated with or without 2.0 units of ExoIII for 2.5, 5 and 7.5 minutes at 37°C, and the resultant DNA fragments were extracted and analyzed by 14% denaturing PAGE with 7 M urea. The gel image shown is a representative of three independent experiments, in which similar results were obtained.

    Article Snippet: MNase and exonuclease III treatment assays The H3.3, CENP-A, or CENP-A/H3.3 nucleosomes (0.4 μM) were treated with MNase (Takara) or ExoIII (Takara).

    Techniques: Clear Native PAGE, Incubation, Polyacrylamide Gel Electrophoresis

    Stability of the CENP-A/H3.3 nucleosome. (a) Schematic representation of the thermal stability assay. (b) Thermal stability curve of the H3.3 nucleosome. The fluorescence intensity was plotted against each temperature (from 55°C to 90°C). The derivative values of the H3.3 stability curve presented in the upper panel are plotted against the temperatures (bottom panel). Means ± s.d. ( n = 3) are shown. (c) A thermal stability curve of the CENP-A nucleosome. The fluorescence intensity was plotted against each temperature (from 55°C to 90°C). The derivative values of the CENP-A stability curve presented in the upper panel are plotted against the temperatures (bottom panel). Means ± s.d. ( n = 3) are shown. (d) Tetrasomes, reconstituted with the H3.3-H4 tetramer or the CENP-A-H4 tetramer and DNA, were analyzed by 6% native PAGE. Lane 1 indicates the H3.3 tetrasome before incubation. Lanes 2, 3, 4, 5, and 6 indicate the H3.3 tetrasomes after 25°C, 35°C, 45°C, 55°C, and 65°C incubations, respectively. Lane 7 indicates the CENP-A tetrasome before incubation. Lanes 8, 9, 10, 11, and 12 indicate the CENP-A tetrasomes after 25°C, 35°C, 45°C, 55°C, and 65°C incubations, respectively. DNA was visualized by ethidium bromide staining. The gel image is a representative of seven independent experiments with similar results. (e) A thermal stability curve of the CENP-A/H3.3 nucleosome. The fluorescence intensity was plotted against each temperature (from 55°C to 90°C). The derivative values of the CENP-A/H3.3 stability curve presented in the upper panel are plotted against the temperatures (bottom panel). Means ± s.d. ( n = 3) are shown. (f) The H3.3, CENP-A, and CENP-A/H3.3 nucleosomes were incubated for 1 min at each temperature from 25°C, and the samples at 65°C, 72°C, 79°C, and 86°C were analyzed by 6% native PAGE. DNA was visualized by ethidium bromide staining. The gel image is a representative of three independent experiments with similar results.

    Journal: Scientific Reports

    Article Title: Crystal structure and stable property of the cancer-associated heterotypic nucleosome containing CENP-A and H3.3

    doi: 10.1038/srep07115

    Figure Lengend Snippet: Stability of the CENP-A/H3.3 nucleosome. (a) Schematic representation of the thermal stability assay. (b) Thermal stability curve of the H3.3 nucleosome. The fluorescence intensity was plotted against each temperature (from 55°C to 90°C). The derivative values of the H3.3 stability curve presented in the upper panel are plotted against the temperatures (bottom panel). Means ± s.d. ( n = 3) are shown. (c) A thermal stability curve of the CENP-A nucleosome. The fluorescence intensity was plotted against each temperature (from 55°C to 90°C). The derivative values of the CENP-A stability curve presented in the upper panel are plotted against the temperatures (bottom panel). Means ± s.d. ( n = 3) are shown. (d) Tetrasomes, reconstituted with the H3.3-H4 tetramer or the CENP-A-H4 tetramer and DNA, were analyzed by 6% native PAGE. Lane 1 indicates the H3.3 tetrasome before incubation. Lanes 2, 3, 4, 5, and 6 indicate the H3.3 tetrasomes after 25°C, 35°C, 45°C, 55°C, and 65°C incubations, respectively. Lane 7 indicates the CENP-A tetrasome before incubation. Lanes 8, 9, 10, 11, and 12 indicate the CENP-A tetrasomes after 25°C, 35°C, 45°C, 55°C, and 65°C incubations, respectively. DNA was visualized by ethidium bromide staining. The gel image is a representative of seven independent experiments with similar results. (e) A thermal stability curve of the CENP-A/H3.3 nucleosome. The fluorescence intensity was plotted against each temperature (from 55°C to 90°C). The derivative values of the CENP-A/H3.3 stability curve presented in the upper panel are plotted against the temperatures (bottom panel). Means ± s.d. ( n = 3) are shown. (f) The H3.3, CENP-A, and CENP-A/H3.3 nucleosomes were incubated for 1 min at each temperature from 25°C, and the samples at 65°C, 72°C, 79°C, and 86°C were analyzed by 6% native PAGE. DNA was visualized by ethidium bromide staining. The gel image is a representative of three independent experiments with similar results.

    Article Snippet: MNase and exonuclease III treatment assays The H3.3, CENP-A, or CENP-A/H3.3 nucleosomes (0.4 μM) were treated with MNase (Takara) or ExoIII (Takara).

    Techniques: Stability Assay, Fluorescence, Clear Native PAGE, Incubation, Staining

    CENP-C binding to the CENP-A/H3.3 nucleosome. (a) Schematic representations of CENP-C binding to the H3.3 nucleosome, the CENP-A nucleosome, and the CENP-A/H3.3 nucleosome. (b) The binding of CENP-C to the CENP-A/H3.3 nucleosome. CENP-C(426–537) peptide binding to the H3.3 nucleosome (0.2 μM), the CENP-A nucleosome (0.2 μM), and the CENP-A/H3.3 nucleosome (0.2 μM) was evaluated by a gel mobility shift assay. The CENP-C(426–537) peptide concentrations are 0 μM (lanes 1, 3, and 10), 0.2 μM (lanes 4 and 11), 0.4 μM (lanes 5 and 12), 0.6 μM (lanes 6 and 13), 0.8 μM (lanes 2, 7, and 14), 1.0 μM (lanes 8 and 15), and 1.2 μM (lanes 9 and 16). The gel image is a representative of three independent experiments with similar results.

    Journal: Scientific Reports

    Article Title: Crystal structure and stable property of the cancer-associated heterotypic nucleosome containing CENP-A and H3.3

    doi: 10.1038/srep07115

    Figure Lengend Snippet: CENP-C binding to the CENP-A/H3.3 nucleosome. (a) Schematic representations of CENP-C binding to the H3.3 nucleosome, the CENP-A nucleosome, and the CENP-A/H3.3 nucleosome. (b) The binding of CENP-C to the CENP-A/H3.3 nucleosome. CENP-C(426–537) peptide binding to the H3.3 nucleosome (0.2 μM), the CENP-A nucleosome (0.2 μM), and the CENP-A/H3.3 nucleosome (0.2 μM) was evaluated by a gel mobility shift assay. The CENP-C(426–537) peptide concentrations are 0 μM (lanes 1, 3, and 10), 0.2 μM (lanes 4 and 11), 0.4 μM (lanes 5 and 12), 0.6 μM (lanes 6 and 13), 0.8 μM (lanes 2, 7, and 14), 1.0 μM (lanes 8 and 15), and 1.2 μM (lanes 9 and 16). The gel image is a representative of three independent experiments with similar results.

    Article Snippet: MNase and exonuclease III treatment assays The H3.3, CENP-A, or CENP-A/H3.3 nucleosomes (0.4 μM) were treated with MNase (Takara) or ExoIII (Takara).

    Techniques: Binding Assay, Mobility Shift