8 oxodgtp  (Jena Bioscience)


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    Name:
    8 Oxo dGTP
    Description:

    Catalog Number:
    NU-1117L
    Price:
    352.16
    Category:
    Nucleotides Nucleosides
    Size:
    5 x 30 µl
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    Structured Review

    Jena Bioscience 8 oxodgtp
    Pol µ dGMP and 8-oxodGMP insertion coupled with ligation. a Lane 1 is the minus enzyme control for the single-nucleotide gapped DNA substrate with template base T. Lanes 2–4 and 5–7 are the reaction products in the presence of dGTP and <t>8-oxodGTP,</t> respectively, and correspond to time points of 10, 30, and 60 s. The position of 5′-adenylate product is indicated as magenta arrow. b Graph shows time-dependent changes in the products of insertion (pink and purple for 8-oxodGTP and dGTP insertions, respectively) and ligation (cyan and blue for ligation following insertion of 8-oxodGTP and dGTP, respectively). The data represent the average of four independent experiments ± SD. Corresponding uncropped gel image and presentation of the data in line graph format are shown in Supplementary Fig. 2

    https://www.bioz.com/result/8 oxodgtp/product/Jena Bioscience
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    8 oxodgtp - by Bioz Stars, 2021-07
    93/100 stars

    Images

    1) Product Images from "Pol μ dGTP mismatch insertion opposite T coupled with ligation reveals promutagenic DNA repair intermediate"

    Article Title: Pol μ dGTP mismatch insertion opposite T coupled with ligation reveals promutagenic DNA repair intermediate

    Journal: Nature Communications

    doi: 10.1038/s41467-018-06700-5

    Pol µ dGMP and 8-oxodGMP insertion coupled with ligation. a Lane 1 is the minus enzyme control for the single-nucleotide gapped DNA substrate with template base T. Lanes 2–4 and 5–7 are the reaction products in the presence of dGTP and 8-oxodGTP, respectively, and correspond to time points of 10, 30, and 60 s. The position of 5′-adenylate product is indicated as magenta arrow. b Graph shows time-dependent changes in the products of insertion (pink and purple for 8-oxodGTP and dGTP insertions, respectively) and ligation (cyan and blue for ligation following insertion of 8-oxodGTP and dGTP, respectively). The data represent the average of four independent experiments ± SD. Corresponding uncropped gel image and presentation of the data in line graph format are shown in Supplementary Fig. 2
    Figure Legend Snippet: Pol µ dGMP and 8-oxodGMP insertion coupled with ligation. a Lane 1 is the minus enzyme control for the single-nucleotide gapped DNA substrate with template base T. Lanes 2–4 and 5–7 are the reaction products in the presence of dGTP and 8-oxodGTP, respectively, and correspond to time points of 10, 30, and 60 s. The position of 5′-adenylate product is indicated as magenta arrow. b Graph shows time-dependent changes in the products of insertion (pink and purple for 8-oxodGTP and dGTP insertions, respectively) and ligation (cyan and blue for ligation following insertion of 8-oxodGTP and dGTP, respectively). The data represent the average of four independent experiments ± SD. Corresponding uncropped gel image and presentation of the data in line graph format are shown in Supplementary Fig. 2

    Techniques Used: Ligation

    2) Product Images from "Pol μ dGTP mismatch insertion opposite T coupled with ligation reveals promutagenic DNA repair intermediate"

    Article Title: Pol μ dGTP mismatch insertion opposite T coupled with ligation reveals promutagenic DNA repair intermediate

    Journal: Nature Communications

    doi: 10.1038/s41467-018-06700-5

    Pol µ dGMP and 8-oxodGMP insertion coupled with ligation. a Lane 1 is the minus enzyme control for the single-nucleotide gapped DNA substrate with template base T. Lanes 2–4 and 5–7 are the reaction products in the presence of dGTP and 8-oxodGTP, respectively, and correspond to time points of 10, 30, and 60 s. The position of 5′-adenylate product is indicated as magenta arrow. b
    Figure Legend Snippet: Pol µ dGMP and 8-oxodGMP insertion coupled with ligation. a Lane 1 is the minus enzyme control for the single-nucleotide gapped DNA substrate with template base T. Lanes 2–4 and 5–7 are the reaction products in the presence of dGTP and 8-oxodGTP, respectively, and correspond to time points of 10, 30, and 60 s. The position of 5′-adenylate product is indicated as magenta arrow. b

    Techniques Used: Ligation

    Related Articles

    Incubation:

    Article Title: MutT from the fish pathogen Aliivibrio salmonicida is a cold-active nucleotide-pool sanitization enzyme with unexpectedly high thermostability
    Article Snippet: Thermodynamic activation parameters were calculated using the following equations : (1) Δ G # = RT × ( ln k B T / h - ln k cat ) (2) Δ H # = E a - RT (3) Δ S # = ( Δ H # - Δ G # ) / T where ΔG # is the free energy of activation, ΔH # is the activation enthalpy, ΔS # is the activation entropy, R is the gas constant (8.314 J mol−1 K−1 ), k B is the Boltzmann constant (1.3805 × 10−23 J K−1 ), h the Planck constant (6.6256 × 10−34 J s) and T the temperature in kelvin. .. To determine the E a of As MutT and Vc MutT, the enzymes (As MutT at 64 nM and Vc MutT at 30 nM) were incubated with nine different substrate concentrations of 8-oxo-dGTP (Jena Bioscience) ranging from 10 to 50 μM at 4, 11, 18, 25, 32, and 37 °C in a total reaction volume of 100 μL (as described above). ..

    Activity Assay:

    Article Title: MutT from the fish pathogen Aliivibrio salmonicida is a cold-active nucleotide-pool sanitization enzyme with unexpectedly high thermostability
    Article Snippet: .. The results ( ) show that both As MutT and Vc MutT possess activity for 8-oxo-dGTP and can thus be considered as MutT enzymes. ..

    other:

    Article Title: MutT from the fish pathogen Aliivibrio salmonicida is a cold-active nucleotide-pool sanitization enzyme with unexpectedly high thermostability
    Article Snippet: A central question in the field is how MutT enzymes favour the recognition of 8-oxo-dGTP over dGTP?

    Article Title: MutT from the fish pathogen Aliivibrio salmonicida is a cold-active nucleotide-pool sanitization enzyme with unexpectedly high thermostability
    Article Snippet: A close inspection of the substrate-binding pocket also shows that both As MutT and Vc MutT possess a tyrosine residue (Tyr76), which is in a position to hydrogen bond with the oxygen atom (O8) at C8 of 8-oxo-dGTP ( D).

    Functional Assay:

    Article Title: MutT from the fish pathogen Aliivibrio salmonicida is a cold-active nucleotide-pool sanitization enzyme with unexpectedly high thermostability
    Article Snippet: 4 Concluding remarks Here we have studied MutT enzymes from the psychrophilic fish pathogen A . salmonicida and the mesophilic human pathogen V . cholerae . .. Our results show that both enzymes are functional MutT enzymes, catalysing the degradation of 8-oxo-dGTP to 8-oxo-dGMP and PPi , thus both organisms have these important nucleotide sanitizing enzymes to fight ROS attacks from their host during infection. .. We have also shown that As MutT is a cold-active enzyme with higher catalytic efficiency and lower energy of activation compared to Vc MutT.

    Infection:

    Article Title: MutT from the fish pathogen Aliivibrio salmonicida is a cold-active nucleotide-pool sanitization enzyme with unexpectedly high thermostability
    Article Snippet: 4 Concluding remarks Here we have studied MutT enzymes from the psychrophilic fish pathogen A . salmonicida and the mesophilic human pathogen V . cholerae . .. Our results show that both enzymes are functional MutT enzymes, catalysing the degradation of 8-oxo-dGTP to 8-oxo-dGMP and PPi , thus both organisms have these important nucleotide sanitizing enzymes to fight ROS attacks from their host during infection. .. We have also shown that As MutT is a cold-active enzyme with higher catalytic efficiency and lower energy of activation compared to Vc MutT.

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    Jena Bioscience 8 oxo dgtp
    (A) Ribbon diagram of the Vc MutT X-ray structure with β-strands in firebrick red, α-helices in brown and loops in grey. (B) Homology model of Vc MutT-closed (grey) made from Ec <t>MutT-8-oxo-dGTP-Mn</t> superimposed on Vc MutT (firebrick red). 8-oxo-dGMP and Mn 2+ are modelled from the Ec MutT-8-oxo-dGTP-Mn structure. (C) Hydrogen bonding interactions between 8-oxo-dGMP and Vc MutT (crystal structure in firebrick red and closed homology model in grey). The super imposed As MutT models (closed in dark-grey and open in sky-blue) are also shown. Residues involved in Mn 2+ coordination and residues promoting conformational stabilization to the enzymes structure are indicated. (D) Hydrogen bonds between the Vc MutT-closed model and 8-oxo-dGMP. Electrostatic surface of the homology model of (E) Vc MutT-closed and (F) As MutT-closed with important residue differences highlighted. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
    8 Oxo Dgtp, supplied by Jena Bioscience, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/8 oxo dgtp/product/Jena Bioscience
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    8 oxo dgtp - by Bioz Stars, 2021-07
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    Image Search Results


    (A) Ribbon diagram of the Vc MutT X-ray structure with β-strands in firebrick red, α-helices in brown and loops in grey. (B) Homology model of Vc MutT-closed (grey) made from Ec MutT-8-oxo-dGTP-Mn superimposed on Vc MutT (firebrick red). 8-oxo-dGMP and Mn 2+ are modelled from the Ec MutT-8-oxo-dGTP-Mn structure. (C) Hydrogen bonding interactions between 8-oxo-dGMP and Vc MutT (crystal structure in firebrick red and closed homology model in grey). The super imposed As MutT models (closed in dark-grey and open in sky-blue) are also shown. Residues involved in Mn 2+ coordination and residues promoting conformational stabilization to the enzymes structure are indicated. (D) Hydrogen bonds between the Vc MutT-closed model and 8-oxo-dGMP. Electrostatic surface of the homology model of (E) Vc MutT-closed and (F) As MutT-closed with important residue differences highlighted. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Journal: FEBS Open Bio

    Article Title: MutT from the fish pathogen Aliivibrio salmonicida is a cold-active nucleotide-pool sanitization enzyme with unexpectedly high thermostability

    doi: 10.1016/j.fob.2015.01.006

    Figure Lengend Snippet: (A) Ribbon diagram of the Vc MutT X-ray structure with β-strands in firebrick red, α-helices in brown and loops in grey. (B) Homology model of Vc MutT-closed (grey) made from Ec MutT-8-oxo-dGTP-Mn superimposed on Vc MutT (firebrick red). 8-oxo-dGMP and Mn 2+ are modelled from the Ec MutT-8-oxo-dGTP-Mn structure. (C) Hydrogen bonding interactions between 8-oxo-dGMP and Vc MutT (crystal structure in firebrick red and closed homology model in grey). The super imposed As MutT models (closed in dark-grey and open in sky-blue) are also shown. Residues involved in Mn 2+ coordination and residues promoting conformational stabilization to the enzymes structure are indicated. (D) Hydrogen bonds between the Vc MutT-closed model and 8-oxo-dGMP. Electrostatic surface of the homology model of (E) Vc MutT-closed and (F) As MutT-closed with important residue differences highlighted. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: A central question in the field is how MutT enzymes favour the recognition of 8-oxo-dGTP over dGTP?

    Techniques:

    Pol µ dGMP and 8-oxodGMP insertion coupled with ligation. a Lane 1 is the minus enzyme control for the single-nucleotide gapped DNA substrate with template base T. Lanes 2–4 and 5–7 are the reaction products in the presence of dGTP and 8-oxodGTP, respectively, and correspond to time points of 10, 30, and 60 s. The position of 5′-adenylate product is indicated as magenta arrow. b Graph shows time-dependent changes in the products of insertion (pink and purple for 8-oxodGTP and dGTP insertions, respectively) and ligation (cyan and blue for ligation following insertion of 8-oxodGTP and dGTP, respectively). The data represent the average of four independent experiments ± SD. Corresponding uncropped gel image and presentation of the data in line graph format are shown in Supplementary Fig. 2

    Journal: Nature Communications

    Article Title: Pol μ dGTP mismatch insertion opposite T coupled with ligation reveals promutagenic DNA repair intermediate

    doi: 10.1038/s41467-018-06700-5

    Figure Lengend Snippet: Pol µ dGMP and 8-oxodGMP insertion coupled with ligation. a Lane 1 is the minus enzyme control for the single-nucleotide gapped DNA substrate with template base T. Lanes 2–4 and 5–7 are the reaction products in the presence of dGTP and 8-oxodGTP, respectively, and correspond to time points of 10, 30, and 60 s. The position of 5′-adenylate product is indicated as magenta arrow. b Graph shows time-dependent changes in the products of insertion (pink and purple for 8-oxodGTP and dGTP insertions, respectively) and ligation (cyan and blue for ligation following insertion of 8-oxodGTP and dGTP, respectively). The data represent the average of four independent experiments ± SD. Corresponding uncropped gel image and presentation of the data in line graph format are shown in Supplementary Fig. 2

    Article Snippet: Briefly, the reaction mixture (10 μl in final volume) included 50 mM Tris(HCl), pH 7.5, 100 mM KCl, 10 mM MgCl2 , 1 mM ATP, 100 μg ml−1 BSA, 10% glycerol, 1 mM DTT, and 200 μM of 8-oxodGTP (Jena Bioscience), dGTP or dATP (NEB), 300 nM DNA substrate, and 100 nM enzyme mixture.

    Techniques: Ligation

    Pol µ dGMP and 8-oxodGMP insertion coupled with ligation. a Lane 1 is the minus enzyme control for the single-nucleotide gapped DNA substrate with template base T. Lanes 2–4 and 5–7 are the reaction products in the presence of dGTP and 8-oxodGTP, respectively, and correspond to time points of 10, 30, and 60 s. The position of 5′-adenylate product is indicated as magenta arrow. b

    Journal: Nature Communications

    Article Title: Pol μ dGTP mismatch insertion opposite T coupled with ligation reveals promutagenic DNA repair intermediate

    doi: 10.1038/s41467-018-06700-5

    Figure Lengend Snippet: Pol µ dGMP and 8-oxodGMP insertion coupled with ligation. a Lane 1 is the minus enzyme control for the single-nucleotide gapped DNA substrate with template base T. Lanes 2–4 and 5–7 are the reaction products in the presence of dGTP and 8-oxodGTP, respectively, and correspond to time points of 10, 30, and 60 s. The position of 5′-adenylate product is indicated as magenta arrow. b

    Article Snippet: Briefly, the reaction mixture (10 μl in final volume) included 50 mM Tris(HCl), pH 7.5, 100 mM KCl, 10 mM MgCl2 , 1 mM ATP, 100 μg ml−1 BSA, 10% glycerol, 1 mM DTT, and 200 μM of 8-oxodGTP (Jena Bioscience), dGTP or dATP (NEB), 300 nM DNA substrate, and 100 nM enzyme mixture.

    Techniques: Ligation