dttp  (Millipore)


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    Name:
    dTTP
    Description:
    dTTP is a 100 mM clear colorless solution of lithium salt pH 7 dTTP solution in water pH 7 100 mM lithium salt
    Catalog Number:
    11051482001
    Price:
    None
    Applications:
    Use dTTP, lithium salt, for DNA sequencing, labeling, and all types of amplification reactions or primer-extension reactions.It has been used in PCR fingrprinting and PCR techniques.
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    Structured Review

    Millipore dttp
    (A) Structures of 2' deoxynucleoside triphosphates used or referred to in this study are <t>dATP,</t> dCTP, dGTP, <t>dTTP,</t> Ind-TP, 5-FITP, 5-AITP, 5-NITP, 5-PhITP, 5-CE-ITP, 5-CH-ITP, and 5-NapITP. For convenience, dR is used to represent the 2'-deoxyribose 5'-triphosphate portion of the nucleotides. (B) Defined DNA substrates used for kinetic analysis. “X” in the template strand denotes T or the presence of a tetrahydrofuran moiety that mimics an abasic site.
    dTTP is a 100 mM clear colorless solution of lithium salt pH 7 dTTP solution in water pH 7 100 mM lithium salt
    https://www.bioz.com/result/dttp/product/Millipore
    Average 93 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    dttp - by Bioz Stars, 2020-05
    93/100 stars

    Images

    1) Product Images from "The Mechanism and Dynamics of Translesion DNA Synthesis Catalyzed by the Escherichia coli Klenow fragment"

    Article Title: The Mechanism and Dynamics of Translesion DNA Synthesis Catalyzed by the Escherichia coli Klenow fragment

    Journal: Biochemistry

    doi: 10.1021/bi800324r

    (A) Structures of 2' deoxynucleoside triphosphates used or referred to in this study are dATP, dCTP, dGTP, dTTP, Ind-TP, 5-FITP, 5-AITP, 5-NITP, 5-PhITP, 5-CE-ITP, 5-CH-ITP, and 5-NapITP. For convenience, dR is used to represent the 2'-deoxyribose 5'-triphosphate portion of the nucleotides. (B) Defined DNA substrates used for kinetic analysis. “X” in the template strand denotes T or the presence of a tetrahydrofuran moiety that mimics an abasic site.
    Figure Legend Snippet: (A) Structures of 2' deoxynucleoside triphosphates used or referred to in this study are dATP, dCTP, dGTP, dTTP, Ind-TP, 5-FITP, 5-AITP, 5-NITP, 5-PhITP, 5-CE-ITP, 5-CH-ITP, and 5-NapITP. For convenience, dR is used to represent the 2'-deoxyribose 5'-triphosphate portion of the nucleotides. (B) Defined DNA substrates used for kinetic analysis. “X” in the template strand denotes T or the presence of a tetrahydrofuran moiety that mimics an abasic site.

    Techniques Used:

    2) Product Images from "Human DNA polymerase ? polymorphism, Arg137Gln, impairs its polymerase activity and interaction with PCNA and the cellular base excision repair capacity"

    Article Title: Human DNA polymerase ? polymorphism, Arg137Gln, impairs its polymerase activity and interaction with PCNA and the cellular base excision repair capacity

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gkp201

    The Pol β polymorphism R137Q is defective in polymerase activity. ( A ) Top panel, schematic of the biotin-labeled 1-nt gapped DNA substrate (Pol-GAP); bottom panel, polymerase activity assay in which Pol-GAP was incubated with 50 μM each of dATP, dGTP, dTTP and 8 μM dCTP- 32 P and varying amounts of purified Pol β protein (WT and R137Q). WT and R137Q DNA polymerization products were separated by denaturing gel electrophoresis and visualized with a phosphorimager. ( B ) DNA polymerization products were pulled down by Sepharose–avidin beads. After washing, the amount of radio-nucleotide incorporated into the products was determined by liquid scintillation counting. ( C ) Gel shift assay of DNA-binding affinity of R137Q and WT Pol β. In this assay, Pol-GAP was labeled by 32 P as shown in figure. ( D ) ELISA-based isotherm adsorption assay of DNA-binding affinity of R137Q and WT Pol β. The DNA substrate was the same as that used in (A). WT, filled squares; R137, filled circles.
    Figure Legend Snippet: The Pol β polymorphism R137Q is defective in polymerase activity. ( A ) Top panel, schematic of the biotin-labeled 1-nt gapped DNA substrate (Pol-GAP); bottom panel, polymerase activity assay in which Pol-GAP was incubated with 50 μM each of dATP, dGTP, dTTP and 8 μM dCTP- 32 P and varying amounts of purified Pol β protein (WT and R137Q). WT and R137Q DNA polymerization products were separated by denaturing gel electrophoresis and visualized with a phosphorimager. ( B ) DNA polymerization products were pulled down by Sepharose–avidin beads. After washing, the amount of radio-nucleotide incorporated into the products was determined by liquid scintillation counting. ( C ) Gel shift assay of DNA-binding affinity of R137Q and WT Pol β. In this assay, Pol-GAP was labeled by 32 P as shown in figure. ( D ) ELISA-based isotherm adsorption assay of DNA-binding affinity of R137Q and WT Pol β. The DNA substrate was the same as that used in (A). WT, filled squares; R137, filled circles.

    Techniques Used: Activity Assay, Labeling, Incubation, Purification, Nucleic Acid Electrophoresis, Avidin-Biotin Assay, Electrophoretic Mobility Shift Assay, Binding Assay, Enzyme-linked Immunosorbent Assay, Adsorption

    3) Product Images from "DCTPP1 attenuates the sensitivity of human gastric cancer cells to 5-fluorouracil by up-regulating MDR1 expression epigenetically"

    Article Title: DCTPP1 attenuates the sensitivity of human gastric cancer cells to 5-fluorouracil by up-regulating MDR1 expression epigenetically

    Journal: Oncotarget

    doi: 10.18632/oncotarget.11864

    Intracellular 5-methyl-dCTP, dCTP and dTTP concentrations in DCTPP1 -knockdown and control BGC-823 cells. The concentrations of A. 5-methyl-dCTP, B. dCTP, and C. dTTP in DCTPP1 -knockdown and control BGC-823 cells were measured by LC-MS/MS assay. All the values shown were represented as means ± SD. (ns: not significant; **: P
    Figure Legend Snippet: Intracellular 5-methyl-dCTP, dCTP and dTTP concentrations in DCTPP1 -knockdown and control BGC-823 cells. The concentrations of A. 5-methyl-dCTP, B. dCTP, and C. dTTP in DCTPP1 -knockdown and control BGC-823 cells were measured by LC-MS/MS assay. All the values shown were represented as means ± SD. (ns: not significant; **: P

    Techniques Used: Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry

    4) Product Images from "The dTTPase mechanism of T7 DNA helicase resembles the binding change mechanism of the F1-ATPase"

    Article Title: The dTTPase mechanism of T7 DNA helicase resembles the binding change mechanism of the F1-ATPase

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    doi:

    Identification of 4A′-bound nucleotides and their dissociation kinetics. ( A ) 4A′ (2 μM hexamer) and [α- 32 P]dTTP (200 μM) were mixed at 18°C for 30 s and nonradiolabeled dTTP (10 mM) was added at time zero. After varying chase times (30 s to 20 min), aliquots were filtered through NC membranes. A total of 3.7 ± 0.87 nt (error calculated from seven independent measurements) were bound to 4A′ at zero chase time (•). After addition of dTTP chase, the 2–3 4A′-bound nucleotides exchanged at 0.008 ± 0.002 s −1 (○). ( B ) To identity the tightly bound nucleotides, NC membranes were extracted and the eluted nucleotides were analyzed by polyethyleneimine-cellulose TLC. Here the PhosphorImager scan of the TLC plate is shown. Lane 1, dTDP (20%) and dTTP (80%) bound to 4A′ before chase was added. Lanes 2–9, nucleotides bound after 0.5, 3, 6, 9, 12, 15, 20, 25 min of chase. In all lanes, dTDP is 6–17% and dTTP is 94–83%. Lane 10, dTDP bound to 4A′ after 90 min of incubation. Lane 11, almost no dTDP remained bound after 30-s chase with unlabeled dTTP. ( C ) The exchange of 4A′-bound dTMP-PCP was measured by preincubating 4A′ (0.83 μM hexamer) with [α- 32 P]dTMP-PCP (98 μM) and adding 5 mM dTTP as chase. Three to four dTMP-PCP are bound before chase was added (•). Two dTMP-PCPs exchanged with unlabeled dTTP in the medium (○) with a rate constant of 0.002 ± 0.0004 s −1 ; one dTMP-PCP did not exchange even after 50-min chase time. ( Inset ) dTTP hydrolysis in the presence of dTMP-PCP. Reaction conditions were same as in C , except 4A′ was preincubated with dTMP-PCP and hydrolysis of 5 mM [α- 32 P]dTTP was measured. dTTP was hydrolyzed without lag at 0.1 ± 0.001 s −1 in the presence of dTMP-PCP (▴) and at 0.14 ± 0.003 s −1 in the absence of dTMP-PCP (♦).
    Figure Legend Snippet: Identification of 4A′-bound nucleotides and their dissociation kinetics. ( A ) 4A′ (2 μM hexamer) and [α- 32 P]dTTP (200 μM) were mixed at 18°C for 30 s and nonradiolabeled dTTP (10 mM) was added at time zero. After varying chase times (30 s to 20 min), aliquots were filtered through NC membranes. A total of 3.7 ± 0.87 nt (error calculated from seven independent measurements) were bound to 4A′ at zero chase time (•). After addition of dTTP chase, the 2–3 4A′-bound nucleotides exchanged at 0.008 ± 0.002 s −1 (○). ( B ) To identity the tightly bound nucleotides, NC membranes were extracted and the eluted nucleotides were analyzed by polyethyleneimine-cellulose TLC. Here the PhosphorImager scan of the TLC plate is shown. Lane 1, dTDP (20%) and dTTP (80%) bound to 4A′ before chase was added. Lanes 2–9, nucleotides bound after 0.5, 3, 6, 9, 12, 15, 20, 25 min of chase. In all lanes, dTDP is 6–17% and dTTP is 94–83%. Lane 10, dTDP bound to 4A′ after 90 min of incubation. Lane 11, almost no dTDP remained bound after 30-s chase with unlabeled dTTP. ( C ) The exchange of 4A′-bound dTMP-PCP was measured by preincubating 4A′ (0.83 μM hexamer) with [α- 32 P]dTMP-PCP (98 μM) and adding 5 mM dTTP as chase. Three to four dTMP-PCP are bound before chase was added (•). Two dTMP-PCPs exchanged with unlabeled dTTP in the medium (○) with a rate constant of 0.002 ± 0.0004 s −1 ; one dTMP-PCP did not exchange even after 50-min chase time. ( Inset ) dTTP hydrolysis in the presence of dTMP-PCP. Reaction conditions were same as in C , except 4A′ was preincubated with dTMP-PCP and hydrolysis of 5 mM [α- 32 P]dTTP was measured. dTTP was hydrolyzed without lag at 0.1 ± 0.001 s −1 in the presence of dTMP-PCP (▴) and at 0.14 ± 0.003 s −1 in the absence of dTMP-PCP (♦).

    Techniques Used: Thin Layer Chromatography, Incubation

    Pre-steady-state pulse–chase kinetics of dTTP hydrolysis. 4A′ (3.3 μM hexamer) was mixed with [α- 32 P]dTTP (100–600 μM) in a rapid quench-flow instrument at 18°C, and the reactions were chased with dTTP or EDTA (see Materials and Methods ). ( A ) Representative time course of the pulse–chase kinetics at 100 μM dTTP is shown. ( Inset ) The entire pulse–chase time course to 60 s. The pulse–chase kinetics fit best to two exponentials (solid line) followed by a linear phase. The first phase amplitude is 1.09 ± 0.05 dTTP per hexamer, fast exponential rate constant is 10.0 ± 1.1 s −1 , second phase amplitude is 0.61 ± 0.07 dTTP per hexamer, second exponential rate constant is 0.23 ± 0.07 s −1 , and steady-state dTTPase turnover is 0.06 ± 0.002 s −1 . The dotted line shows the poor fit to one exponential followed by a linear equation. ( B ) The [dTTP] dependence of the first phase amplitude (▴) and rate constant [EDTA chase data (•) and dTTP chase data (♦)] are shown. The linear [dTTP] dependence of the fast exponential rate constant provided a k on of 0.07 ± 0.01 mM −1 ⋅s −1 (slope) and a k off of 0.4 ± 1.1 s −1 ( y intercept).
    Figure Legend Snippet: Pre-steady-state pulse–chase kinetics of dTTP hydrolysis. 4A′ (3.3 μM hexamer) was mixed with [α- 32 P]dTTP (100–600 μM) in a rapid quench-flow instrument at 18°C, and the reactions were chased with dTTP or EDTA (see Materials and Methods ). ( A ) Representative time course of the pulse–chase kinetics at 100 μM dTTP is shown. ( Inset ) The entire pulse–chase time course to 60 s. The pulse–chase kinetics fit best to two exponentials (solid line) followed by a linear phase. The first phase amplitude is 1.09 ± 0.05 dTTP per hexamer, fast exponential rate constant is 10.0 ± 1.1 s −1 , second phase amplitude is 0.61 ± 0.07 dTTP per hexamer, second exponential rate constant is 0.23 ± 0.07 s −1 , and steady-state dTTPase turnover is 0.06 ± 0.002 s −1 . The dotted line shows the poor fit to one exponential followed by a linear equation. ( B ) The [dTTP] dependence of the first phase amplitude (▴) and rate constant [EDTA chase data (•) and dTTP chase data (♦)] are shown. The linear [dTTP] dependence of the fast exponential rate constant provided a k on of 0.07 ± 0.01 mM −1 ⋅s −1 (slope) and a k off of 0.4 ± 1.1 s −1 ( y intercept).

    Techniques Used: Pulse Chase, Flow Cytometry

    Number of catalytically competent dTTPs bound to 4A′ during steady-state dTTPase turnover. In a three-syringe experimental set-up ( Materials and Methods ), 4A′ (2 μM hexamer) was mixed with [α- 32 P]dTTP (150 μM) for 60 s. Nonradiolabeled dTTP (7 mM) was added at 60 s, and the reactions were chased for 10–60 s prior to acid-quenching. As shown (▴), only one additional dTTP per hexamer was hydrolyzed to dTDP during the chase period. When reactions were not chased, the steady state hydrolysis of [α- 32 P]dTTP (150 μM) continues at 0.14 ± 0.006 s −1 (•).
    Figure Legend Snippet: Number of catalytically competent dTTPs bound to 4A′ during steady-state dTTPase turnover. In a three-syringe experimental set-up ( Materials and Methods ), 4A′ (2 μM hexamer) was mixed with [α- 32 P]dTTP (150 μM) for 60 s. Nonradiolabeled dTTP (7 mM) was added at 60 s, and the reactions were chased for 10–60 s prior to acid-quenching. As shown (▴), only one additional dTTP per hexamer was hydrolyzed to dTDP during the chase period. When reactions were not chased, the steady state hydrolysis of [α- 32 P]dTTP (150 μM) continues at 0.14 ± 0.006 s −1 (•).

    Techniques Used:

    Pre-steady-state acid-quenched kinetics of dTTP hydrolysis. 4A′ (3.3 μM hexamer) was mixed with [α- 32 P]dTTP (50–600 μM) in a rapid quench-flow instrument at 18°C, and reactions were quenched with 1 M HCl. ( A ) Representative dTTPase time course at 100 μM dTTP (•) is shown. The data were fit to a single exponential followed by a linear phase with a burst amplitude of 0.80 ± 0.04 dTTP per hexamer, a burst rate constant of 0.34 ± 0.04 s −1 , and a dTTPase turnover rate of 0.043 ± 0.0007 s −1 . ( B ) The [dTTP] dependence of the burst amplitude (▴) and the burst rate constant (•) is shown. The [dTTP] dependence of the burst rate constant fit to a hyberbola with a maximum dTTP hydrolysis rate constant of 0.66 ± 0.083 s −1 and K ½ of 167 ± 57 μM.
    Figure Legend Snippet: Pre-steady-state acid-quenched kinetics of dTTP hydrolysis. 4A′ (3.3 μM hexamer) was mixed with [α- 32 P]dTTP (50–600 μM) in a rapid quench-flow instrument at 18°C, and reactions were quenched with 1 M HCl. ( A ) Representative dTTPase time course at 100 μM dTTP (•) is shown. The data were fit to a single exponential followed by a linear phase with a burst amplitude of 0.80 ± 0.04 dTTP per hexamer, a burst rate constant of 0.34 ± 0.04 s −1 , and a dTTPase turnover rate of 0.043 ± 0.0007 s −1 . ( B ) The [dTTP] dependence of the burst amplitude (▴) and the burst rate constant (•) is shown. The [dTTP] dependence of the burst rate constant fit to a hyberbola with a maximum dTTP hydrolysis rate constant of 0.66 ± 0.083 s −1 and K ½ of 167 ± 57 μM.

    Techniques Used: Flow Cytometry

    Related Articles

    Flow Cytometry:

    Article Title: High Spatiotemporal-Resolution Magnetic Tweezers: Calibration and Applications for DNA Dynamics
    Article Snippet: .. For the experiments in which we observe the effect of dTTP (Sigma Aldrich, Zwijndrecht, The Netherlands) on the hopping transition of the hairpin (see and ), we exchange buffer A from the flow cell with buffer B, which contains 20 mM Tris-HCl, pH 7.5, 50 mM NaCl, 7 mM MgCl2 , 3 mM EDTA, 0.01% Tween-20, and varying concentrations of dTTP. ..

    In Vitro:

    Article Title: Human DNA polymerase ? polymorphism, Arg137Gln, impairs its polymerase activity and interaction with PCNA and the cellular base excision repair capacity
    Article Snippet: .. In vitro polymerase activity assay The polymerase activity assay utilized 50 mM Tris–HCl (pH 8.0), 10 mM MgCl2 , 2 mM DTT, 20 mM NaCl, 10% glycerol, 0.1 µM biotin-labeled DNA substrate Pol-GAP (see and A for detail), 50 µM each dATP, dGTP and dTTP (Sigma), 8 µM 2 µCi [α-32 P]-dCTP and 0–10 ng WT or R137Q Pol β. .. Reactions were carried out at 37°C for 30 min. A portion of reaction product was taken out and incubated with avidin–Sepharose 4B beads, washed and quantified on liquid scintillation analyzer.

    Synthesized:

    Article Title: The Mechanism and Dynamics of Translesion DNA Synthesis Catalyzed by the Escherichia coli Klenow fragment
    Article Snippet: .. Oligonucleotides, including those containing a tetrahydrofuran moiety mimicking an abasic site, were synthesized by Operon Technologies (Alameda, CA). dATP, dCTP, dGTP, and dTTP were obtained from Sigma in greater than 99% purity. .. All non-natural indolyl-deoxyribose triphosphates were synthesized, purified, and characterized as previously described ( - ).

    Concentration Assay:

    Article Title: The dTTPase mechanism of T7 DNA helicase resembles the binding change mechanism of the F1-ATPase
    Article Snippet: .. A total of 15 μl of 4A′ at a desired concentration in 50 mM Tris-acetate (pH 7.5), 40 mM sodium acetate, 1 mM DTT, 10% glycerol, and 1 mM magnesium acetate was mixed with 15 μl mixture of dTTP (Sigma) and [α-32 P] dTTP (20 μCi per 10 reaction points; 1 Ci = 37 GBq; Amersham or ICN) prepared in the same buffer except with 19 mM magnesium acetate. .. The quenched reactions were analyzed by polyethyleneimine-cellulose TLC and the products were quantitated using a PhosphorImager (Molecular Dynamics).

    other:

    Article Title: Identification of a Region of the Herpes Simplex Virus Single-Stranded DNA-Binding Protein Involved in Cooperative Binding
    Article Snippet: [α-32 P]dATP and [3 H]dTTP were purchased from New England Nuclear Laboratories. dCTP, dGTP, dATP, and dTTP were purchased from Sigma.

    Activity Assay:

    Article Title: Human DNA polymerase ? polymorphism, Arg137Gln, impairs its polymerase activity and interaction with PCNA and the cellular base excision repair capacity
    Article Snippet: .. In vitro polymerase activity assay The polymerase activity assay utilized 50 mM Tris–HCl (pH 8.0), 10 mM MgCl2 , 2 mM DTT, 20 mM NaCl, 10% glycerol, 0.1 µM biotin-labeled DNA substrate Pol-GAP (see and A for detail), 50 µM each dATP, dGTP and dTTP (Sigma), 8 µM 2 µCi [α-32 P]-dCTP and 0–10 ng WT or R137Q Pol β. .. Reactions were carried out at 37°C for 30 min. A portion of reaction product was taken out and incubated with avidin–Sepharose 4B beads, washed and quantified on liquid scintillation analyzer.

    Polymerase Chain Reaction:

    Article Title: Soybean Resistance to White Mold: Evaluation of Soybean Germplasm Under Different Conditions and Validation of QTL
    Article Snippet: .. Total reaction volume of 15.0 μL contained 50 ng of genomic DNA, 0.3 μM each of forward and reverse primers, 0.2 mM of dATP, dCTP, dGTP, and dTTP (Sigma-Aldrich, St. Louis, MO), 3.0 mM MgCl2 , 2.5 units of Taq polymerase, and 1.0 × PCR buffer. .. The PCR was performed using a regular program as follows; an initial denaturation at 95°C for 2 min, followed by 38 cycles of denaturation at 94°C for 25 s, 25 s of annealing at primer specific annealing temperature, 45 s of extension at 70°C, a final extension at 72°C for 10 min, followed by a final hold at 4°C.

    Chloramphenicol Acetyltransferase Assay:

    Article Title: DCTPP1 attenuates the sensitivity of human gastric cancer cells to 5-fluorouracil by up-regulating MDR1 expression epigenetically
    Article Snippet: .. Rabbit anti-Phospho-BRCA1 Ab (Cat# 9009), rabbit anti-Phospho-H2A.X Ab (Cat# 2197), rabbit anti-caspase-3 (8G10) mAb (Cat# 9665), rabbit anti-cleaved caspase-3 (Asp 175) mAb (Cat# 9664), rabbit anti-Bax pAb (Cat2772), rabbit anti-Bcl-2 (50E3) mAb (Cat# 2870), HRP-linked anti-rabbit IgG Ab (Cat# 7074) and HRP-linked anti-mouse IgG Ab (Cat# 7076) were purchased from Cell Signaling Technology (Beverly, MA, USA). dCTP, dTTP and 5-FU were purchased from Sigma and 5-methyl-dCTP was purchased from New England BioLabs (Ipswich, MA, USA). .. Construction of DCTPP1 -knockdown BGC-823 cells Stable DCTPP1 -knockdown BGC-823 cells were constructed by transfecting RNAi-Ready pSIREN-RetroQ retroviral vector (Clontech, CA, USA) containing shRNA oligonucleotides targeting DCTPP1 as described in our previous report [ ].

    Plasmid Preparation:

    Article Title: Functional Mapping of the DNA Binding Domain of Bovine Papillomavirus E1 Protein
    Article Snippet: .. Reactions contained 10 mM Tris-HCl (pH 9.0) at 25°C, 50 mM KCl, 0.1% Triton X-100, 3 mM MgCl2 , 200 μM dATP, 200 μM dCTP, 200 μM dGTP, 200 μM dTTP (Sigma), 1.25 μl of template plasmid DNA extracted from yeast, 1.5 pmol of each primer from the SSCP1/SSCP2 primer pair or SSCP3/SSCP4 primer pair (Sigma-Genosys), and 0.25 U of Taq polymerase (Promega) in a 12.25-μl reaction volume. ..

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    Millipore dttp millipore filters
    Dttp Millipore Filters, supplied by Millipore, used in various techniques. Bioz Stars score: 93/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dttp millipore filters/product/Millipore
    Average 93 stars, based on 2 article reviews
    Price from $9.99 to $1999.99
    dttp millipore filters - by Bioz Stars, 2020-05
    93/100 stars
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