Structured Review

Midland Certified Reagent dna sequence
Dna Sequence, supplied by Midland Certified Reagent, used in various techniques. Bioz Stars score: 92/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/dna sequence/product/Midland Certified Reagent
Average 92 stars, based on 2 article reviews
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dna sequence - by Bioz Stars, 2020-09
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Sequencing:

Article Title: Identification of regions of the P2X7 receptor that contribute to human and rat species differences in antagonist effects
Article Snippet: .. The DNA sequence of the rat ECD was based on the rat cDNA clone described previously ( ) and was synthesized as a Pml 1-to- Xcm 1 fragment in pUC19 (Midland Certified Reagent Co. Inc., Midland, TX, USA, 79701). .. The rat ECD Pml 1/ Xcm 1 fragment was then subcloned into the unique Pml 1- and Xcm 1-digested pFBM1-humP2X7 plasmid used for generating BacMam reagents ( ).

Article Title: Adaptation of a Luciferase Gene Reporter and lac Expression System to Borrelia burgdorferi ▿ ▿ †
Article Snippet: .. Overlapping (20 bp) 50-mer oligonucleotides then were synthesized from the optimized DNA sequence (Midland Certified Reagent Co., Midland, TX), and the gene was constructed using the assembly PCR technique ( ). .. This oligonucleotide pool served as the template in the primary assembly PCR.

IA:

Article Title: Transition-state destabilization reveals how human DNA polymerase β proceeds across the chemically unstable lesion N7-methylguanine
Article Snippet: .. DNA sequences used for kinetic and X-ray crystallographic studies The oligonucleotides for kinetic assays (upstream primer, 5′-FAM/GGGGGCTCGTAAGGATTC-3′, downstream primer, 5′-phosphate/AGTCGG-3′ and template, 5′-CCGACT(X)GAATCCTTACGAGCCCCC-3′, X = dG, 2FdG or Fm7dG) were synthesized by Midland Certified Reagent Co. (Midland, TX, USA) and Integrated DNA Technologies (Coralville, IA, USA). .. The template DNA was prepared via solid-phase DNA synthesis using ultramild deprotection conditions (50 mM K2 CO3 in MeOH, 25°C, 24 h).

Polymerase Cycling Assembly:

Article Title: Adaptation of a Luciferase Gene Reporter and lac Expression System to Borrelia burgdorferi ▿ ▿ †
Article Snippet: .. Overlapping (20 bp) 50-mer oligonucleotides then were synthesized from the optimized DNA sequence (Midland Certified Reagent Co., Midland, TX), and the gene was constructed using the assembly PCR technique ( ). .. This oligonucleotide pool served as the template in the primary assembly PCR.

Construct:

Article Title: Adaptation of a Luciferase Gene Reporter and lac Expression System to Borrelia burgdorferi ▿ ▿ †
Article Snippet: .. Overlapping (20 bp) 50-mer oligonucleotides then were synthesized from the optimized DNA sequence (Midland Certified Reagent Co., Midland, TX), and the gene was constructed using the assembly PCR technique ( ). .. This oligonucleotide pool served as the template in the primary assembly PCR.

Synthesized:

Article Title: Identification of regions of the P2X7 receptor that contribute to human and rat species differences in antagonist effects
Article Snippet: .. The DNA sequence of the rat ECD was based on the rat cDNA clone described previously ( ) and was synthesized as a Pml 1-to- Xcm 1 fragment in pUC19 (Midland Certified Reagent Co. Inc., Midland, TX, USA, 79701). .. The rat ECD Pml 1/ Xcm 1 fragment was then subcloned into the unique Pml 1- and Xcm 1-digested pFBM1-humP2X7 plasmid used for generating BacMam reagents ( ).

Article Title: Direct observation of the hole protonation state and hole localization site in DNA-oligomers
Article Snippet: .. Starting with this phosphoramidite of G*, the ds DNA sequences d[G*CG*CG*CG*C]2 , d[G*GGCCC]2 , d[GG*GCCC]2 , d[GGG*CCC]2 , were synthesized (Midland Certified, TX) and desalted and dried for this work. .. Moreover, again employing the phosphoramidite of G*, the ds DNA oligomers d[TG*GGCCCA]2 , d[TGG*GCCCA]2 , d[TGGG*CCCA]2 were synthesized, desalted, HPLC-purified, and dried (Midland Certified, TX).

Article Title: Adaptation of a Luciferase Gene Reporter and lac Expression System to Borrelia burgdorferi ▿ ▿ †
Article Snippet: .. Overlapping (20 bp) 50-mer oligonucleotides then were synthesized from the optimized DNA sequence (Midland Certified Reagent Co., Midland, TX), and the gene was constructed using the assembly PCR technique ( ). .. This oligonucleotide pool served as the template in the primary assembly PCR.

Article Title: Transition-state destabilization reveals how human DNA polymerase β proceeds across the chemically unstable lesion N7-methylguanine
Article Snippet: .. DNA sequences used for kinetic and X-ray crystallographic studies The oligonucleotides for kinetic assays (upstream primer, 5′-FAM/GGGGGCTCGTAAGGATTC-3′, downstream primer, 5′-phosphate/AGTCGG-3′ and template, 5′-CCGACT(X)GAATCCTTACGAGCCCCC-3′, X = dG, 2FdG or Fm7dG) were synthesized by Midland Certified Reagent Co. (Midland, TX, USA) and Integrated DNA Technologies (Coralville, IA, USA). .. The template DNA was prepared via solid-phase DNA synthesis using ultramild deprotection conditions (50 mM K2 CO3 in MeOH, 25°C, 24 h).

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    Midland Certified Reagent high affinity histone octamer binding dna sequence
    <t>DNA</t> heteroduplexes and human histone octamers used in this study. A , schematic diagram of DNA substrates. Substrate I is a 147-bp fragment containing tandem repeats of a high affinity histone <t>octamer-binding</t> DNA sequence and a centrally located G-T mismatch. Substrate II is a 200-bp heteroduplex containing the high affinity nucleosome positioning sequence 601 in one terminus and a biotin residue ( black sphere ) in the other terminus. Substrate III is a 428-bp heteroduplex consisting of two pieces of the 601 nucleosome positioning sequence. Open triangles in each case represent the mismatch. B , analysis of purified recombinant human histone octamer by 18% SDS-PAGE.
    High Affinity Histone Octamer Binding Dna Sequence, supplied by Midland Certified Reagent, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/high affinity histone octamer binding dna sequence/product/Midland Certified Reagent
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    high affinity histone octamer binding dna sequence - by Bioz Stars, 2020-09
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    93
    Midland Certified Reagent dna sequences
    <t>DNA</t> hairpin sequences and the structure of the <t>PdC</t> used in the experiment. The PdC incorporated into the hairpins is indicated by “P”.
    Dna Sequences, supplied by Midland Certified Reagent, used in various techniques. Bioz Stars score: 93/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dna sequences/product/Midland Certified Reagent
    Average 93 stars, based on 9 article reviews
    Price from $9.99 to $1999.99
    dna sequences - by Bioz Stars, 2020-09
    93/100 stars
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    85
    Midland Certified Reagent box1 dna sequences
    Structural model of PmrA C <t>–box1</t> <t>DNA</t> complex. ( A ) The best complex model from HADDOCK docking with yellow surface display of DNA and ribbon presentation of PmrA C , showing that the α3 helix and the C-terminal β-hairpin fit into the major and minor groove of the DNA, respectively. The residues showing H-bond and non-bonded interactions with DNA are in blue and red, respectively. The inter-molecular salt bridge identified between the two PmrA C molecules is shown. ( B ) Schematic presentation of the detailed interactions between the two PmrA C molecules and box1 DNA identified in more than five of the best 10 models. The H-bonds and non-bonded contacts are indicated by blue and red dotted lines, respectively.
    Box1 Dna Sequences, supplied by Midland Certified Reagent, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/box1 dna sequences/product/Midland Certified Reagent
    Average 85 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    box1 dna sequences - by Bioz Stars, 2020-09
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    92
    Midland Certified Reagent dna sequencing
    Structural model of PmrA C <t>–box1</t> <t>DNA</t> complex. ( A ) The best complex model from HADDOCK docking with yellow surface display of DNA and ribbon presentation of PmrA C , showing that the α3 helix and the C-terminal β-hairpin fit into the major and minor groove of the DNA, respectively. The residues showing H-bond and non-bonded interactions with DNA are in blue and red, respectively. The inter-molecular salt bridge identified between the two PmrA C molecules is shown. ( B ) Schematic presentation of the detailed interactions between the two PmrA C molecules and box1 DNA identified in more than five of the best 10 models. The H-bonds and non-bonded contacts are indicated by blue and red dotted lines, respectively.
    Dna Sequencing, supplied by Midland Certified Reagent, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dna sequencing/product/Midland Certified Reagent
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    dna sequencing - by Bioz Stars, 2020-09
    92/100 stars
      Buy from Supplier

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    DNA heteroduplexes and human histone octamers used in this study. A , schematic diagram of DNA substrates. Substrate I is a 147-bp fragment containing tandem repeats of a high affinity histone octamer-binding DNA sequence and a centrally located G-T mismatch. Substrate II is a 200-bp heteroduplex containing the high affinity nucleosome positioning sequence 601 in one terminus and a biotin residue ( black sphere ) in the other terminus. Substrate III is a 428-bp heteroduplex consisting of two pieces of the 601 nucleosome positioning sequence. Open triangles in each case represent the mismatch. B , analysis of purified recombinant human histone octamer by 18% SDS-PAGE.

    Journal: The Journal of Biological Chemistry

    Article Title: Evidence That Nucleosomes Inhibit Mismatch Repair in Eukaryotic Cells *

    doi: 10.1074/jbc.M109.049874

    Figure Lengend Snippet: DNA heteroduplexes and human histone octamers used in this study. A , schematic diagram of DNA substrates. Substrate I is a 147-bp fragment containing tandem repeats of a high affinity histone octamer-binding DNA sequence and a centrally located G-T mismatch. Substrate II is a 200-bp heteroduplex containing the high affinity nucleosome positioning sequence 601 in one terminus and a biotin residue ( black sphere ) in the other terminus. Substrate III is a 428-bp heteroduplex consisting of two pieces of the 601 nucleosome positioning sequence. Open triangles in each case represent the mismatch. B , analysis of purified recombinant human histone octamer by 18% SDS-PAGE.

    Article Snippet: Two complementary 147-mer fragment oligonucleotides ( DNA substrate I , A ) containing tandem repeats of a high affinity histone octamer-binding DNA sequence, TATAAACGCC , were synthesized in The Midland Certified Reagent Company (Midland, TX).

    Techniques: Binding Assay, Sequencing, Purification, Recombinant, SDS Page

    DNA hairpin sequences and the structure of the PdC used in the experiment. The PdC incorporated into the hairpins is indicated by “P”.

    Journal: Biophysical Journal

    Article Title: DNA Hairpins Containing the Cytidine Analog Pyrrolo-dC: Structural, Thermodynamic, and Spectroscopic Studies

    doi: 10.1016/j.bpj.2008.12.3890

    Figure Lengend Snippet: DNA hairpin sequences and the structure of the PdC used in the experiment. The PdC incorporated into the hairpins is indicated by “P”.

    Article Snippet: All DNA sequences, including those with PdC substitutions, were obtained from the Midland Certified Reagent Company (Midland, TX).

    Techniques:

    Structural model of PmrA C –box1 DNA complex. ( A ) The best complex model from HADDOCK docking with yellow surface display of DNA and ribbon presentation of PmrA C , showing that the α3 helix and the C-terminal β-hairpin fit into the major and minor groove of the DNA, respectively. The residues showing H-bond and non-bonded interactions with DNA are in blue and red, respectively. The inter-molecular salt bridge identified between the two PmrA C molecules is shown. ( B ) Schematic presentation of the detailed interactions between the two PmrA C molecules and box1 DNA identified in more than five of the best 10 models. The H-bonds and non-bonded contacts are indicated by blue and red dotted lines, respectively.

    Journal: Nucleic Acids Research

    Article Title: Solution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniae

    doi: 10.1093/nar/gkt1345

    Figure Lengend Snippet: Structural model of PmrA C –box1 DNA complex. ( A ) The best complex model from HADDOCK docking with yellow surface display of DNA and ribbon presentation of PmrA C , showing that the α3 helix and the C-terminal β-hairpin fit into the major and minor groove of the DNA, respectively. The residues showing H-bond and non-bonded interactions with DNA are in blue and red, respectively. The inter-molecular salt bridge identified between the two PmrA C molecules is shown. ( B ) Schematic presentation of the detailed interactions between the two PmrA C molecules and box1 DNA identified in more than five of the best 10 models. The H-bonds and non-bonded contacts are indicated by blue and red dotted lines, respectively.

    Article Snippet: The box1 DNA sequences with dT-EDTA at THY4 or THY28 were from Midland Certified Inc. (TX, USA).

    Techniques:

    PmrA C and PmrA F recognize box1 DNA with different modes. ( A ) 1D proton NMR spectra of imino signals of box1 at different ratios of DNA to PmrA C (black 1:0, red 1:0.5, green 1:1 and blue 1:2). The imino signals from THY3 to ADE24 were completely assigned. ( B ) 1D spectra of the titration of PmrA F into box1 DNA. The color representation is the same as in (A). ( C ) The intensity ratio of each imino signal at ratio of protein to DNA of 0.5 to 0. Blue bars are for the PmrA C complex and red are for the PmrA F complex. The overlapped imino signals were not plotted and the sequence for box1 DNA is shown below. ( D ) and ( E ) CD spectra for box1 DNA at different ratios of DNA to PmrA C and PmrA F , respectively.

    Journal: Nucleic Acids Research

    Article Title: Solution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniae

    doi: 10.1093/nar/gkt1345

    Figure Lengend Snippet: PmrA C and PmrA F recognize box1 DNA with different modes. ( A ) 1D proton NMR spectra of imino signals of box1 at different ratios of DNA to PmrA C (black 1:0, red 1:0.5, green 1:1 and blue 1:2). The imino signals from THY3 to ADE24 were completely assigned. ( B ) 1D spectra of the titration of PmrA F into box1 DNA. The color representation is the same as in (A). ( C ) The intensity ratio of each imino signal at ratio of protein to DNA of 0.5 to 0. Blue bars are for the PmrA C complex and red are for the PmrA F complex. The overlapped imino signals were not plotted and the sequence for box1 DNA is shown below. ( D ) and ( E ) CD spectra for box1 DNA at different ratios of DNA to PmrA C and PmrA F , respectively.

    Article Snippet: The box1 DNA sequences with dT-EDTA at THY4 or THY28 were from Midland Certified Inc. (TX, USA).

    Techniques: Proton NMR, Titration, Sequencing

    NMR investigations of PmrA C –DNA complexes. ( A ) The regions of amide resonances and N ε H resonances of Arg side-chains (inset) of overlaid 2D 1 H, 15 N TROSY-HSQC spectra for PmrA C in the absence (black) or presence (red) of box1a DNA. The amide resonances in complex state are indicated. ( B ) Weighted chemical shift perturbations for backbone 15 N and 1 H N resonances as calculated by the equation Δδ = {[(Δδ HN ) 2 +(Δδ N /5) 2 ]/2} 0.5 . The solid black bar represents the Δδ values for the box1a complex, green x for box1 and orange x for box1b. The black line indicates 0.33 ppm (the mean Δδ value of box1a complex plus 1 SD). ( C ) Structural mapping of chemical shift perturbations of the box1a complex. The residues with chemical shift perturbation > 0.33 ppm are in red,

    Journal: Nucleic Acids Research

    Article Title: Solution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniae

    doi: 10.1093/nar/gkt1345

    Figure Lengend Snippet: NMR investigations of PmrA C –DNA complexes. ( A ) The regions of amide resonances and N ε H resonances of Arg side-chains (inset) of overlaid 2D 1 H, 15 N TROSY-HSQC spectra for PmrA C in the absence (black) or presence (red) of box1a DNA. The amide resonances in complex state are indicated. ( B ) Weighted chemical shift perturbations for backbone 15 N and 1 H N resonances as calculated by the equation Δδ = {[(Δδ HN ) 2 +(Δδ N /5) 2 ]/2} 0.5 . The solid black bar represents the Δδ values for the box1a complex, green x for box1 and orange x for box1b. The black line indicates 0.33 ppm (the mean Δδ value of box1a complex plus 1 SD). ( C ) Structural mapping of chemical shift perturbations of the box1a complex. The residues with chemical shift perturbation > 0.33 ppm are in red,

    Article Snippet: The box1 DNA sequences with dT-EDTA at THY4 or THY28 were from Midland Certified Inc. (TX, USA).

    Techniques: Nuclear Magnetic Resonance

    Inter-molecular PRE for the PmrA C –box1 DNA complex. ( A ) A portion of 2D 1 H, 15 N TROSY-HSQC acquiring in the paramagnetic state (in red; EDTA is chelated with Mn 2+ ) overlaid with that in the diamagnetic state (in black; EDTA is chelated with Ca 2+ ) for PmrA C –box1 complex with dT-EDTA at THY4. ( B ) and ( C ) The ratios of peak intensity from the paramagnetic to diamagnetic state with dT-EDTA at THY4 and THY28, respectively. The proline and the severely overlapped residues are shown with gray bars. In (B), the residues with intensity ratio

    Journal: Nucleic Acids Research

    Article Title: Solution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniae

    doi: 10.1093/nar/gkt1345

    Figure Lengend Snippet: Inter-molecular PRE for the PmrA C –box1 DNA complex. ( A ) A portion of 2D 1 H, 15 N TROSY-HSQC acquiring in the paramagnetic state (in red; EDTA is chelated with Mn 2+ ) overlaid with that in the diamagnetic state (in black; EDTA is chelated with Ca 2+ ) for PmrA C –box1 complex with dT-EDTA at THY4. ( B ) and ( C ) The ratios of peak intensity from the paramagnetic to diamagnetic state with dT-EDTA at THY4 and THY28, respectively. The proline and the severely overlapped residues are shown with gray bars. In (B), the residues with intensity ratio

    Article Snippet: The box1 DNA sequences with dT-EDTA at THY4 or THY28 were from Midland Certified Inc. (TX, USA).

    Techniques:

    NMR study of the PmrA F –box1 DNA complex. ( A ) 2D 1 H, 15 N TROSY-HSQC spectra for the PmrA F –box1 complex with ratio of protein to DNA of 2:1 shown in black and that of BeF3 − -activated PmrA N in green. The good superimposition of the two spectra indicates that the N-terminal domain of PmrA F in the complex state shows the free-state-like homodimeric conformation. ( B ) 2D 1 H, 15 N TROSY-HSQC spectra for the PmrA F –box1 complex (black) overlaid with that of PmrA C –box1a complex (red) and PmrA C –box1b complex (blue). Two sets of resonance peaks were observed for a number of residues in the C-terminal domain of PmrA F in complex with box1 and some are labeled.

    Journal: Nucleic Acids Research

    Article Title: Solution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniae

    doi: 10.1093/nar/gkt1345

    Figure Lengend Snippet: NMR study of the PmrA F –box1 DNA complex. ( A ) 2D 1 H, 15 N TROSY-HSQC spectra for the PmrA F –box1 complex with ratio of protein to DNA of 2:1 shown in black and that of BeF3 − -activated PmrA N in green. The good superimposition of the two spectra indicates that the N-terminal domain of PmrA F in the complex state shows the free-state-like homodimeric conformation. ( B ) 2D 1 H, 15 N TROSY-HSQC spectra for the PmrA F –box1 complex (black) overlaid with that of PmrA C –box1a complex (red) and PmrA C –box1b complex (blue). Two sets of resonance peaks were observed for a number of residues in the C-terminal domain of PmrA F in complex with box1 and some are labeled.

    Article Snippet: The box1 DNA sequences with dT-EDTA at THY4 or THY28 were from Midland Certified Inc. (TX, USA).

    Techniques: Nuclear Magnetic Resonance, Labeling

    DNA recognition by PmrA C or PmrA F . ( A ) The DNA sequences of box1 and box2 on the promoter region of K. pneumoniae pbgP gene. Their positions relative to the pbgP start codon are labeled. The first and second hexanucleotides are shown in bold and the synthesized DNA fragments are indicated. ( B ) Fluorescence polarization experiments of binding of PmrA C and box1a or box1b sequence and ( C ) binding of PmrA C or PmrA F and box1 sequence. ( D ) and ( E ) Isothermal titration calorimetry of binding of PmrA C and box2b and box2, respectively.

    Journal: Nucleic Acids Research

    Article Title: Solution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniae

    doi: 10.1093/nar/gkt1345

    Figure Lengend Snippet: DNA recognition by PmrA C or PmrA F . ( A ) The DNA sequences of box1 and box2 on the promoter region of K. pneumoniae pbgP gene. Their positions relative to the pbgP start codon are labeled. The first and second hexanucleotides are shown in bold and the synthesized DNA fragments are indicated. ( B ) Fluorescence polarization experiments of binding of PmrA C and box1a or box1b sequence and ( C ) binding of PmrA C or PmrA F and box1 sequence. ( D ) and ( E ) Isothermal titration calorimetry of binding of PmrA C and box2b and box2, respectively.

    Article Snippet: The box1 DNA sequences with dT-EDTA at THY4 or THY28 were from Midland Certified Inc. (TX, USA).

    Techniques: Labeling, Synthesized, Fluorescence, Binding Assay, Sequencing, Isothermal Titration Calorimetry