hogg1  (New England Biolabs)


Bioz Verified Symbol New England Biolabs is a verified supplier
Bioz Manufacturer Symbol New England Biolabs manufactures this product  
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 95
    Name:
    NEBuffer 1 1
    Description:
    NEBuffer 1 1 5 0 ml
    Catalog Number:
    b7201s
    Price:
    24
    Size:
    5 0 ml
    Category:
    Buffers
    Buy from Supplier


    Structured Review

    New England Biolabs hogg1
    NEBuffer 1 1
    NEBuffer 1 1 5 0 ml
    https://www.bioz.com/result/hogg1/product/New England Biolabs
    Average 95 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    hogg1 - by Bioz Stars, 2020-07
    95/100 stars

    Images

    1) Product Images from "Simultaneous sensitive detection of multiple DNA glycosylases from lung cancer cells at the single-molecule level sensitive detection of multiple DNA glycosylases from lung cancer cells at the single-molecule level †Electronic supplementary information (ESI) available: Molecular mechanism of the DNA glycosylase-mediated cleavage of molecular beacons and optimization of the experimental conditions. See DOI: 10.1039/c7sc04296e"

    Article Title: Simultaneous sensitive detection of multiple DNA glycosylases from lung cancer cells at the single-molecule level sensitive detection of multiple DNA glycosylases from lung cancer cells at the single-molecule level †Electronic supplementary information (ESI) available: Molecular mechanism of the DNA glycosylase-mediated cleavage of molecular beacons and optimization of the experimental conditions. See DOI: 10.1039/c7sc04296e

    Journal: Chemical Science

    doi: 10.1039/c7sc04296e

    (A) Variance of the initial velocity in response to various concentrations of the Cy3-labeled molecular beacon substrate. The concentration of hOGG1 is 0.1 U μL –1 and the concentration of APE1 is 0.1 U μL –1 . (B) Variance of the initial velocity in response to various concentrations of the Cy5-labeled molecular beacon substrate. The concentration of hAAG is 0.1 U μL –1 and the concentration of APE1 is 0.1 U μL –1 . The error bars represent the standard deviations of the three experiments.
    Figure Legend Snippet: (A) Variance of the initial velocity in response to various concentrations of the Cy3-labeled molecular beacon substrate. The concentration of hOGG1 is 0.1 U μL –1 and the concentration of APE1 is 0.1 U μL –1 . (B) Variance of the initial velocity in response to various concentrations of the Cy5-labeled molecular beacon substrate. The concentration of hAAG is 0.1 U μL –1 and the concentration of APE1 is 0.1 U μL –1 . The error bars represent the standard deviations of the three experiments.

    Techniques Used: Labeling, Concentration Assay

    Variance of the relative catalytic activity with different concentrations of Cd 2+ for hOGG1 alone (black line), hOGG1 + APE1 (red line) and hAAG + APE1 (blue line). The Cy3-labeled molecular beacon (0.3 μM), the Cy5-labeled molecular beacon (0.3 μM), hOGG1 (0.1 U μL –1 ), hAAG (0.1 U μL –1 ) and APE1 (0.1 U μL –1 ) were used in this research. The error bars represent the standard deviations of the three experiments.
    Figure Legend Snippet: Variance of the relative catalytic activity with different concentrations of Cd 2+ for hOGG1 alone (black line), hOGG1 + APE1 (red line) and hAAG + APE1 (blue line). The Cy3-labeled molecular beacon (0.3 μM), the Cy5-labeled molecular beacon (0.3 μM), hOGG1 (0.1 U μL –1 ), hAAG (0.1 U μL –1 ) and APE1 (0.1 U μL –1 ) were used in this research. The error bars represent the standard deviations of the three experiments.

    Techniques Used: Activity Assay, Labeling

    (A) PAGE analysis of the hOGG1-mediated cleavage of the Cy3-labeled molecular beacon (lanes 1–4) and the hAAG-mediated cleavage of the Cy5-labeled molecular beacon (lanes 5–8) with SYBR Gold as the indicator. (B) PAGE analysis of the hOGG1-mediated cleavage of the Cy3-labeled molecular beacon and the hAAG-mediated cleavage of the Cy5-labeled molecular beacon by excitation of Cy3 and Cy5. The green color indicates the Cy3-labeled DNA fragment in the presence of hOGG1 (lane 2) and the red color indicates the Cy5-labeled DNA fragment in the presence of hAAG (lane 4). (C) Fluorescence measurements of the hOGG1-mediated cleavage of the Cy3-labeled molecular beacon in the absence (black line) and presence (green line) of hOGG1. (D) Fluorescence measurements of the hAAG-mediated cleavage of the Cy5-labeled molecular beacon in the absence (blue line) and presence (red line) of hAAG. The hOGG1 concentration is 0.1 U μL –1 and the hAAG concentration is 0.1 U μL –1 , and the APE1 concentration is 0.1 U μL –1 .
    Figure Legend Snippet: (A) PAGE analysis of the hOGG1-mediated cleavage of the Cy3-labeled molecular beacon (lanes 1–4) and the hAAG-mediated cleavage of the Cy5-labeled molecular beacon (lanes 5–8) with SYBR Gold as the indicator. (B) PAGE analysis of the hOGG1-mediated cleavage of the Cy3-labeled molecular beacon and the hAAG-mediated cleavage of the Cy5-labeled molecular beacon by excitation of Cy3 and Cy5. The green color indicates the Cy3-labeled DNA fragment in the presence of hOGG1 (lane 2) and the red color indicates the Cy5-labeled DNA fragment in the presence of hAAG (lane 4). (C) Fluorescence measurements of the hOGG1-mediated cleavage of the Cy3-labeled molecular beacon in the absence (black line) and presence (green line) of hOGG1. (D) Fluorescence measurements of the hAAG-mediated cleavage of the Cy5-labeled molecular beacon in the absence (blue line) and presence (red line) of hAAG. The hOGG1 concentration is 0.1 U μL –1 and the hAAG concentration is 0.1 U μL –1 , and the APE1 concentration is 0.1 U μL –1 .

    Techniques Used: Polyacrylamide Gel Electrophoresis, Labeling, Fluorescence, Concentration Assay

    Simultaneous detection of multiple DNA glycosylases by TIRF-based single-molecule imaging in the absence (A and E) and presence of hOGG1 (B and F), hAAG (C and G) and both hOGG1 and hAAG (D and H). The Cy3 fluorescence signals are shown in green, and the Cy5 fluorescence signals are shown in red. The Cy3-labeled molecular beacon (0.3 μM), the Cy5-labeled molecular beacon (0.3 μM), hOGG1 (0.1 U μL –1 ), hAAG (0.1 U μL –1 ) and APE1 (0.1 U μL –1 ) were used in this research. The scale bar is 5 μm.
    Figure Legend Snippet: Simultaneous detection of multiple DNA glycosylases by TIRF-based single-molecule imaging in the absence (A and E) and presence of hOGG1 (B and F), hAAG (C and G) and both hOGG1 and hAAG (D and H). The Cy3 fluorescence signals are shown in green, and the Cy5 fluorescence signals are shown in red. The Cy3-labeled molecular beacon (0.3 μM), the Cy5-labeled molecular beacon (0.3 μM), hOGG1 (0.1 U μL –1 ), hAAG (0.1 U μL –1 ) and APE1 (0.1 U μL –1 ) were used in this research. The scale bar is 5 μm.

    Techniques Used: Imaging, Fluorescence, Labeling

    Measurement of the Cy3 counts and Cy5 counts in response to the reaction buffer (control), 0.1 g L –1 BSA, 0.1 U μL –1 UDG, 0.1 U μL –1 TDG, 0.1 U μL –1 hOGG1, 0.1 U μL –1 hAAG and 0.1 U μL –1 hOGG1 + 0.1 U μL –1 hAAG. The Cy3-labeled molecular beacon (0.3 μM), Cy5-labeled molecular beacon (0.3 μM) and APE1 (0.1 U μL –1 ) were used in this research. The error bars represent the standard deviations of the three experiments.
    Figure Legend Snippet: Measurement of the Cy3 counts and Cy5 counts in response to the reaction buffer (control), 0.1 g L –1 BSA, 0.1 U μL –1 UDG, 0.1 U μL –1 TDG, 0.1 U μL –1 hOGG1, 0.1 U μL –1 hAAG and 0.1 U μL –1 hOGG1 + 0.1 U μL –1 hAAG. The Cy3-labeled molecular beacon (0.3 μM), Cy5-labeled molecular beacon (0.3 μM) and APE1 (0.1 U μL –1 ) were used in this research. The error bars represent the standard deviations of the three experiments.

    Techniques Used: Labeling

    (A) Measurement of the Cy3 counts generated by different concentrations of hOGG1. The inset shows the linear relationship between the Cy3 counts and the logarithm of the hOGG1 concentration. The Cy3-labeled molecular beacon (0.3 μM) and APE1 (0.1 U μL –1 ) were used in this research. (B) Measurement of the Cy5 counts generated by different concentrations of hAAG. The inset shows the linear relationship between the Cy5 counts and the logarithm of the hAAG concentration. The Cy5-labeled molecular beacon (0.3 μM) and APE1 (0.1 U μL –1 ) were used in this research. The error bars represent the standard deviations of the three experiments.
    Figure Legend Snippet: (A) Measurement of the Cy3 counts generated by different concentrations of hOGG1. The inset shows the linear relationship between the Cy3 counts and the logarithm of the hOGG1 concentration. The Cy3-labeled molecular beacon (0.3 μM) and APE1 (0.1 U μL –1 ) were used in this research. (B) Measurement of the Cy5 counts generated by different concentrations of hAAG. The inset shows the linear relationship between the Cy5 counts and the logarithm of the hAAG concentration. The Cy5-labeled molecular beacon (0.3 μM) and APE1 (0.1 U μL –1 ) were used in this research. The error bars represent the standard deviations of the three experiments.

    Techniques Used: Generated, Concentration Assay, Labeling

    Related Articles

    Centrifugation:

    Article Title: Analysis of the Interaction between Globular Head Modules of Human C1q and Its Candidate Receptor gC1qR
    Article Snippet: .. After centrifugation (13,000 rpm for 15 min), the supernatant was collected and diluted fivefold in buffer I (20 mM Tris–HCl, pH 8.0, 100 mM NaCl, 0.2% Tween 20, 1 mM EDTA, and 5% v/v glycerol) and passed through an amylose resin 15 ml bed column (New England Biolabs). ..

    Article Title: Complement Protein C1q Interacts with DC-SIGN via Its Globular Domain and Thus May Interfere with HIV-1 Transmission
    Article Snippet: .. After centrifugation (13,000 × g for 15 min), the supernatant was diluted fivefold in buffer I (20 mM Tris–HCl, pH 8.0, 100 mM NaCl, 0.2% Tween 20, 1 mM EDTA, and 5% glycerol), passed through an amylose resin column (15 mL; New England Biolabs), and then washed with three bed volumes of buffer I followed by buffer II (50 mL of buffer I without Tween 20). .. The protein was then eluted in 1 mL fractions with 10 mM maltose in 100 mL of buffer II and frozen at −20°C after determining protein concentration and purity via Nanodrop and 10% w/v SDS-PAGE, respectively.

    Agarose Gel Electrophoresis:

    Article Title: A Simple Procedure for Creating Scalable Phenotypic Screening Assays in Human Neurons
    Article Snippet: .. Individual plasmid DNA were incubated with appropriate restriction enzymes (New England Biolabs, Ipswich, MA) and NE Buffer (cat. no. B7201, NEB) for 1 h. Purple loading dye (cat. no. B7024S, NEB) was added to each sample which were loaded carefully on MiniReady Agarose Gel prepared in 1XTBE (cat. no. 101-3004, Biorad) alongside with Quick load purple 1 kb DNA ladder as a reference standard (cat. no. N0552G, NEB). .. The results demonstrated appropriate digest products for each plasmid as well as the maxi-prep RFLP and can be found in the supplemental data (Figure ).

    Isolation:

    Article Title: The Helicobacter pylori HpyAXII restriction-modification system limits exogenous DNA uptake by targeting GTAC sites but shows asymmetric conservation of the DNA methyltransferase and restriction endonuclease components
    Article Snippet: .. Biochemical R.HpyAXII endonuclease activity assay One microliter of freshly prepared soluble fraction obtained from E. coli BL21(DE3) expressing R.HpyAXII was incubated for 3 h at 37°C with 500 ng E. coli ER2925 genomic DNA or pET15b plasmid DNA isolated from E. coli DH10B in presence of NEB buffer 1 (New England Biolabs). ..

    Purification:

    Article Title: ‘Shotgun DNA synthesis’ for the high-throughput construction of large DNA molecules
    Article Snippet: .. For each pool, restriction enzyme digestion was carried out by incubating 2 µl EarI (or EcoP15I), 5 µl NEB buffer 1, 0.5 µl 100× BSA and 10 µl water with 30 µl of purified (and pooled) shotgun synthesis fragments at 37°C for 3 h. For EcoP15I (NEB, Ipswich, MA, USA) restriction enzyme digestion, we used NEB buffer 3 and added 10× ATP. ..

    Concentration Assay:

    Article Title: Characterization of 4-Nitrophenylpropyl-N-alkylamine Interactions with Sigma Receptors
    Article Snippet: .. The extracted material was centrifuged at 100,000 g for 1 h and the supernatant was diluted with a volume of buffer I that reduces the Triton X-100 concentration to 0.5% – 1% before loading onto an amylose column (New England Biolabs, Ipswich, MA). ..

    Incubation:

    Article Title: A Simple Procedure for Creating Scalable Phenotypic Screening Assays in Human Neurons
    Article Snippet: .. Individual plasmid DNA were incubated with appropriate restriction enzymes (New England Biolabs, Ipswich, MA) and NE Buffer (cat. no. B7201, NEB) for 1 h. Purple loading dye (cat. no. B7024S, NEB) was added to each sample which were loaded carefully on MiniReady Agarose Gel prepared in 1XTBE (cat. no. 101-3004, Biorad) alongside with Quick load purple 1 kb DNA ladder as a reference standard (cat. no. N0552G, NEB). .. The results demonstrated appropriate digest products for each plasmid as well as the maxi-prep RFLP and can be found in the supplemental data (Figure ).

    Article Title: The Helicobacter pylori HpyAXII restriction-modification system limits exogenous DNA uptake by targeting GTAC sites but shows asymmetric conservation of the DNA methyltransferase and restriction endonuclease components
    Article Snippet: .. Biochemical R.HpyAXII endonuclease activity assay One microliter of freshly prepared soluble fraction obtained from E. coli BL21(DE3) expressing R.HpyAXII was incubated for 3 h at 37°C with 500 ng E. coli ER2925 genomic DNA or pET15b plasmid DNA isolated from E. coli DH10B in presence of NEB buffer 1 (New England Biolabs). ..

    Activity Assay:

    Article Title: The Helicobacter pylori HpyAXII restriction-modification system limits exogenous DNA uptake by targeting GTAC sites but shows asymmetric conservation of the DNA methyltransferase and restriction endonuclease components
    Article Snippet: .. Biochemical R.HpyAXII endonuclease activity assay One microliter of freshly prepared soluble fraction obtained from E. coli BL21(DE3) expressing R.HpyAXII was incubated for 3 h at 37°C with 500 ng E. coli ER2925 genomic DNA or pET15b plasmid DNA isolated from E. coli DH10B in presence of NEB buffer 1 (New England Biolabs). ..

    Expressing:

    Article Title: The Helicobacter pylori HpyAXII restriction-modification system limits exogenous DNA uptake by targeting GTAC sites but shows asymmetric conservation of the DNA methyltransferase and restriction endonuclease components
    Article Snippet: .. Biochemical R.HpyAXII endonuclease activity assay One microliter of freshly prepared soluble fraction obtained from E. coli BL21(DE3) expressing R.HpyAXII was incubated for 3 h at 37°C with 500 ng E. coli ER2925 genomic DNA or pET15b plasmid DNA isolated from E. coli DH10B in presence of NEB buffer 1 (New England Biolabs). ..

    Plasmid Preparation:

    Article Title: A Simple Procedure for Creating Scalable Phenotypic Screening Assays in Human Neurons
    Article Snippet: .. Individual plasmid DNA were incubated with appropriate restriction enzymes (New England Biolabs, Ipswich, MA) and NE Buffer (cat. no. B7201, NEB) for 1 h. Purple loading dye (cat. no. B7024S, NEB) was added to each sample which were loaded carefully on MiniReady Agarose Gel prepared in 1XTBE (cat. no. 101-3004, Biorad) alongside with Quick load purple 1 kb DNA ladder as a reference standard (cat. no. N0552G, NEB). .. The results demonstrated appropriate digest products for each plasmid as well as the maxi-prep RFLP and can be found in the supplemental data (Figure ).

    Article Title: The Helicobacter pylori HpyAXII restriction-modification system limits exogenous DNA uptake by targeting GTAC sites but shows asymmetric conservation of the DNA methyltransferase and restriction endonuclease components
    Article Snippet: .. Biochemical R.HpyAXII endonuclease activity assay One microliter of freshly prepared soluble fraction obtained from E. coli BL21(DE3) expressing R.HpyAXII was incubated for 3 h at 37°C with 500 ng E. coli ER2925 genomic DNA or pET15b plasmid DNA isolated from E. coli DH10B in presence of NEB buffer 1 (New England Biolabs). ..

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 89
    New England Biolabs hogg1 enzyme
    Level of (A) SB/ALS and 8-oxoGua, or (B) SB, ALS and CPDs in whole blood samples collected 0 h or 5 h following no exposure, (C) PDT exposure, (D) violet irradiation or (D) violet exposure using <t>hOGG1-modified</t> or T4 endoV-modified alkaline comet assay. DNA damage was expressed as % tail DNA. Each data point represents the mean of 600 (A, B, C, D) determinations from three different blood samples or 400 (E) determinations from two different blood samples, all from two individual experiments, ± SEM (ns= non-significant, *** P
    Hogg1 Enzyme, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 89/100, based on 11 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hogg1 enzyme/product/New England Biolabs
    Average 89 stars, based on 11 article reviews
    Price from $9.99 to $1999.99
    hogg1 enzyme - by Bioz Stars, 2020-07
    89/100 stars
      Buy from Supplier

    91
    New England Biolabs hogg1
    AhR expression and DNA strand break formation in AhR siRNA-transfected and nontransfected H358 cells treated with B[ a ]P-7,8-dione. H358 cells were transfected with AhR-siRNA and then treated with B[ a ]P-7,8-dione for 3, 6, or 12 h. The cells were then harvested and were divided into two aliquots. One was used for Western blot analysis, and other was used for the <t>hOGG1-coupled</t> comet assay. A , AhR expression in both AhR siRNA-transfected and nontransfected H358 cells treated with B[ a ]P-7,8-dione. Lane 1 , non-AhR siRNA-transfected cells; lane 2 , nontransfected cells treated with B[ a ]P-7,8-dione; lane 3 , AhR-siRNA transfected cells; lane 4 , AhR siRNA-transfected cells-treated with B[ a ]P-7,8-dione. B , AhR-dependent DNA strand break formation in AhR siRNA-transfected H358 cells treated with DMSO. C , AhR-dependent DNA strand break formation in AhR siRNA-transfected H358 cells treated with B[ a ]P-7,8-dione. Significant effects were observed after hOGG1 treatment. *, p
    Hogg1, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 91/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/hogg1/product/New England Biolabs
    Average 91 stars, based on 12 article reviews
    Price from $9.99 to $1999.99
    hogg1 - by Bioz Stars, 2020-07
    91/100 stars
      Buy from Supplier

    Image Search Results


    Level of (A) SB/ALS and 8-oxoGua, or (B) SB, ALS and CPDs in whole blood samples collected 0 h or 5 h following no exposure, (C) PDT exposure, (D) violet irradiation or (D) violet exposure using hOGG1-modified or T4 endoV-modified alkaline comet assay. DNA damage was expressed as % tail DNA. Each data point represents the mean of 600 (A, B, C, D) determinations from three different blood samples or 400 (E) determinations from two different blood samples, all from two individual experiments, ± SEM (ns= non-significant, *** P

    Journal: Photochemistry and photobiology

    Article Title: Light-based Methods for Whole Blood Bacterial Inactivation Enabled by a Recirculating Flow System

    doi: 10.1111/php.12899

    Figure Lengend Snippet: Level of (A) SB/ALS and 8-oxoGua, or (B) SB, ALS and CPDs in whole blood samples collected 0 h or 5 h following no exposure, (C) PDT exposure, (D) violet irradiation or (D) violet exposure using hOGG1-modified or T4 endoV-modified alkaline comet assay. DNA damage was expressed as % tail DNA. Each data point represents the mean of 600 (A, B, C, D) determinations from three different blood samples or 400 (E) determinations from two different blood samples, all from two individual experiments, ± SEM (ns= non-significant, *** P

    Article Snippet: To evaluate the effects of PDT exposure on induced levels of oxidatively generated damage to DNA nucleobases, the hOGG1 enzyme was used as a lesion-specific enzyme in the Comet assay.

    Techniques: Irradiation, Modification, Alkaline Single Cell Gel Electrophoresis

    AhR expression and DNA strand break formation in AhR siRNA-transfected and nontransfected H358 cells treated with B[ a ]P-7,8-dione. H358 cells were transfected with AhR-siRNA and then treated with B[ a ]P-7,8-dione for 3, 6, or 12 h. The cells were then harvested and were divided into two aliquots. One was used for Western blot analysis, and other was used for the hOGG1-coupled comet assay. A , AhR expression in both AhR siRNA-transfected and nontransfected H358 cells treated with B[ a ]P-7,8-dione. Lane 1 , non-AhR siRNA-transfected cells; lane 2 , nontransfected cells treated with B[ a ]P-7,8-dione; lane 3 , AhR-siRNA transfected cells; lane 4 , AhR siRNA-transfected cells-treated with B[ a ]P-7,8-dione. B , AhR-dependent DNA strand break formation in AhR siRNA-transfected H358 cells treated with DMSO. C , AhR-dependent DNA strand break formation in AhR siRNA-transfected H358 cells treated with B[ a ]P-7,8-dione. Significant effects were observed after hOGG1 treatment. *, p

    Journal: The Journal of Biological Chemistry

    Article Title: Aryl Hydrocarbon Receptor Facilitates DNA Strand Breaks and 8-Oxo-2?-deoxyguanosine Formation by the Aldo-Keto Reductase Product Benzo[a]pyrene-7,8-dione *

    doi: 10.1074/jbc.M109.042143

    Figure Lengend Snippet: AhR expression and DNA strand break formation in AhR siRNA-transfected and nontransfected H358 cells treated with B[ a ]P-7,8-dione. H358 cells were transfected with AhR-siRNA and then treated with B[ a ]P-7,8-dione for 3, 6, or 12 h. The cells were then harvested and were divided into two aliquots. One was used for Western blot analysis, and other was used for the hOGG1-coupled comet assay. A , AhR expression in both AhR siRNA-transfected and nontransfected H358 cells treated with B[ a ]P-7,8-dione. Lane 1 , non-AhR siRNA-transfected cells; lane 2 , nontransfected cells treated with B[ a ]P-7,8-dione; lane 3 , AhR-siRNA transfected cells; lane 4 , AhR siRNA-transfected cells-treated with B[ a ]P-7,8-dione. B , AhR-dependent DNA strand break formation in AhR siRNA-transfected H358 cells treated with DMSO. C , AhR-dependent DNA strand break formation in AhR siRNA-transfected H358 cells treated with B[ a ]P-7,8-dione. Significant effects were observed after hOGG1 treatment. *, p

    Article Snippet: HiPerFect transfection reagent was acquired from Qiagen. hOGG1 was obtained from New England BioLabs Inc. (Beverly, MA).

    Techniques: Expressing, Transfection, Western Blot, Single Cell Gel Electrophoresis

    Cleavage mechanism of 18-mer oligonucleotide containing 8-oxoguanine (oxoG): A) Uncut oligonucleotide containing oxoG, B) Oligonucleotide containing oxoG cut with hOGG1, resulting in β-elimination product, and C) Oligonucleotide containing oxoG cut with Fpg, resulting in β-δ-elimination product. The observed monoisotopic mass values are reported to one decimal place for low molecular mass oligonucleotides, but for higher molecular masses, are reported as integer values due to the inherent lower resolution at high mass.

    Journal: Analytical biochemistry

    Article Title: Characterization of DNA glycosylase activity by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

    doi: 10.1016/j.ab.2009.07.015

    Figure Lengend Snippet: Cleavage mechanism of 18-mer oligonucleotide containing 8-oxoguanine (oxoG): A) Uncut oligonucleotide containing oxoG, B) Oligonucleotide containing oxoG cut with hOGG1, resulting in β-elimination product, and C) Oligonucleotide containing oxoG cut with Fpg, resulting in β-δ-elimination product. The observed monoisotopic mass values are reported to one decimal place for low molecular mass oligonucleotides, but for higher molecular masses, are reported as integer values due to the inherent lower resolution at high mass.

    Article Snippet: UNG (uracil-DNA glycosylase, E. coli ), Fpg (formamidopyrimidine DNA glycosylase, E. coli ), Nth (Endonuclease III, E. coli ) and hOGG1 (human oxoguanine glycosylase 1) were purchased from New England Biolabs (Beverly, MA).

    Techniques:

    Gel electrophoretic profiles of substrate specificity of glycosylases. The oligonucleotide containing U was incubated with UNG followed by NaOH (lane 3) or APE1 (lane 4). The oligonucleotide containing FoU was incubated with hSMUG1 followed by APE1 (lane 6), Fpg (lane 8) and endoIII (lane 10). The oligonucleotide containing oxoG was incubated with Fpg (lane 12) and hOGG1 (lane 14).

    Journal: Analytical biochemistry

    Article Title: Characterization of DNA glycosylase activity by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

    doi: 10.1016/j.ab.2009.07.015

    Figure Lengend Snippet: Gel electrophoretic profiles of substrate specificity of glycosylases. The oligonucleotide containing U was incubated with UNG followed by NaOH (lane 3) or APE1 (lane 4). The oligonucleotide containing FoU was incubated with hSMUG1 followed by APE1 (lane 6), Fpg (lane 8) and endoIII (lane 10). The oligonucleotide containing oxoG was incubated with Fpg (lane 12) and hOGG1 (lane 14).

    Article Snippet: UNG (uracil-DNA glycosylase, E. coli ), Fpg (formamidopyrimidine DNA glycosylase, E. coli ), Nth (Endonuclease III, E. coli ) and hOGG1 (human oxoguanine glycosylase 1) were purchased from New England Biolabs (Beverly, MA).

    Techniques: Incubation