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  • 99
    Thermo Fisher oligonucleotides oligos
    The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled <t>50-mer</t> DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.
    Oligonucleotides Oligos, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Millipore primer oligonucleotides
    The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled <t>50-mer</t> DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.
    Primer Oligonucleotides, supplied by Millipore, used in various techniques. Bioz Stars score: 96/100, based on 68 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Thermo Fisher primer oligonucleotides
    The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled <t>50-mer</t> DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.
    Primer Oligonucleotides, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 90/100, based on 138 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    GE Healthcare primer oligonucleotides
    The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled <t>50-mer</t> DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.
    Primer Oligonucleotides, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 90/100, based on 28 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/primer oligonucleotides/product/GE Healthcare
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    91
    Bioneer Corporation primer oligonucleotides
    The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled <t>50-mer</t> DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.
    Primer Oligonucleotides, supplied by Bioneer Corporation, used in various techniques. Bioz Stars score: 91/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    MWG-Biotech oligonucleotides primers
    The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled <t>50-mer</t> DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.
    Oligonucleotides Primers, supplied by MWG-Biotech, used in various techniques. Bioz Stars score: 88/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Genewiz primer oligos
    The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled <t>50-mer</t> DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.
    Primer Oligos, supplied by Genewiz, used in various techniques. Bioz Stars score: 93/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Bio-Synthesis Inc oligonucleotide substrates primer oligonucleotides
    The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled <t>50-mer</t> DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.
    Oligonucleotide Substrates Primer Oligonucleotides, supplied by Bio-Synthesis Inc, used in various techniques. Bioz Stars score: 85/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Promega primer oligonucleotides
    The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled <t>50-mer</t> DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.
    Primer Oligonucleotides, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher random primer oligonucleotides
    The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled <t>50-mer</t> DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.
    Random Primer Oligonucleotides, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 139 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Millipore oligonucleotide primers
    The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled <t>50-mer</t> DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.
    Oligonucleotide Primers, supplied by Millipore, used in various techniques. Bioz Stars score: 92/100, based on 1670 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Stratagene t7 primer oligonucleotides
    The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled <t>50-mer</t> DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.
    T7 Primer Oligonucleotides, supplied by Stratagene, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Millipore oligonucleotides oligos
    Schematic image illustrating the Golden gate cloning of multiple gRNAs into the concatemer vector containing 3 <t>gRNA</t> expression cassettes . Annealed <t>oligos</t> (gRNA targets), DNA ligase and the Bbs I restriction enzyme are mixed with the gRNA concatemer vector in a single reaction. Repeated temperature cycles facilitate repeated digestion (21 °C) and ligation (37 °C). Bbs I digestion generates the custom-designed overhangs unique for each cassette. During the ligation, gRNAs are integrated into the vector by cassette-specific integration, determined by the matching overhangs of the gRNA and the vector. If the original fragment containing the two Bbs I restriction sites is ligated back into the vector it will again be removed in the following round of digestion. In contrast, upon ligation of a gRNA the Bbs I restriction site is disrupted and hence the gRNA cannot be removed during the following rounds of digestion. Blue – Bbs I enzyme, pink – T7 DNA ligase, U6 – U6 promoter, gRNA1.1–1.3 represent different gRNAs for the same gene (e.g. gRNA1.1 – gRNA1 for gene 1).
    Oligonucleotides Oligos, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled 50-mer DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.

    Journal: The Journal of Experimental Medicine

    Article Title: MSH2-MSH6 stimulates DNA polymerase ?, suggesting a role for A:T mutations in antibody genes

    doi: 10.1084/jem.20042066

    Figure Lengend Snippet: The MSH2–MSH6 heterodimer binds to a U:G mismatch. Increasing amounts of the MSH2–MSH6 complex (0–60 nM) were incubated with 1 fmol of the various labeled 50-mer DNA substrates, which are depicted at the top of the figure. Bound complexes were detected by a shift in the substrate after electrophoresis.

    Article Snippet: For generation of DNA substrates containing a T:G or U:G mismatch, 50-mer oligonucleotides of the following sequences were obtained from Invitrogen: top strand (5′-CATTATCCTAAACATAACTTAACTAGXTTAACTTAATTCTTCAATATACC-3′) and bottom strand (5′-GGTATATTGAAGAATTAAGTTAAGCTAGTTAAGTTATGTTTAGGATAATG-3′).

    Techniques: Incubation, Labeling, Electrophoresis

    Effects of zinc and hypoxia on nuclear localization and DNA binding of MTF-1. (A) C 2 C 12 cells were untreated (control) with 100 μmol/L ZnCl 2 , or exposed to hypoxia (pO 2 = 1%) for 16 h, as indicated. Extracts were analyzed by electrophoretic mobility shift assays (EMSA) using labeled MRE-s oligos. Only the region of the gel containing the specific MTF-1 complexes is shown. (B) Immunoblotting detection of MTF-1 in whole-cell (WCE), nuclear, and cytosolic extracts. Extracts were prepared from L cells that were untreated (0), treated with 100 μmol/L ZnCl 2 (Zn), or exposed to hypoxia (Hx) (pO 2 = 1%), as indicated, and analyzed by immunoblotting with antibodies against MTF-1 and tubulin. Because tubulin is not an appropriate loading control for nuclear extracts, a particular band detected on the blot by staining with amido black is shown. The results shown in panels A and B are representative of 3 independent experiments. (C) ChIP assays were performed using chromatin isolated from L cells that were untreated or treatedwith 100 μmol/L ZnCl 2 for 3 h or exposed to hypoxia for 16 h, prior to formaldehyde crosslinking. Immunoprecipitation of crosslinked chromatin was done with MTF-1 (anti-MTF-1) or HIF-1α (anti-HIF1α) antibodies or a pre-immune normal rabbit serum (PI), as indicated. DNA from both the IP input (prior to immunoprecipitation) and the IP-bound fractions was amplified by PCR with primer pairs for the mouse Mt-1 or Glut-1 promoter. Input, amplification of DNA prior to immunoprecipitation. The input sample contained 0.4% of the supernatant used for immunoprecipitation of crosslinked MTF-1. The PCR products were analyzed by agarose gel electrophoresis. These ChIP assays were performed 3 times using 3 different chromatin preparations with similar results.

    Journal: Biochemistry and cell biology = Biochimie et biologie cellulaire

    Article Title: Hypoxia acts through multiple signaling pathways to induce metallothionein transactivation by the metal-responsive transcription factor-1 (MTF-1)

    doi: 10.1139/o11-063

    Figure Lengend Snippet: Effects of zinc and hypoxia on nuclear localization and DNA binding of MTF-1. (A) C 2 C 12 cells were untreated (control) with 100 μmol/L ZnCl 2 , or exposed to hypoxia (pO 2 = 1%) for 16 h, as indicated. Extracts were analyzed by electrophoretic mobility shift assays (EMSA) using labeled MRE-s oligos. Only the region of the gel containing the specific MTF-1 complexes is shown. (B) Immunoblotting detection of MTF-1 in whole-cell (WCE), nuclear, and cytosolic extracts. Extracts were prepared from L cells that were untreated (0), treated with 100 μmol/L ZnCl 2 (Zn), or exposed to hypoxia (Hx) (pO 2 = 1%), as indicated, and analyzed by immunoblotting with antibodies against MTF-1 and tubulin. Because tubulin is not an appropriate loading control for nuclear extracts, a particular band detected on the blot by staining with amido black is shown. The results shown in panels A and B are representative of 3 independent experiments. (C) ChIP assays were performed using chromatin isolated from L cells that were untreated or treatedwith 100 μmol/L ZnCl 2 for 3 h or exposed to hypoxia for 16 h, prior to formaldehyde crosslinking. Immunoprecipitation of crosslinked chromatin was done with MTF-1 (anti-MTF-1) or HIF-1α (anti-HIF1α) antibodies or a pre-immune normal rabbit serum (PI), as indicated. DNA from both the IP input (prior to immunoprecipitation) and the IP-bound fractions was amplified by PCR with primer pairs for the mouse Mt-1 or Glut-1 promoter. Input, amplification of DNA prior to immunoprecipitation. The input sample contained 0.4% of the supernatant used for immunoprecipitation of crosslinked MTF-1. The PCR products were analyzed by agarose gel electrophoresis. These ChIP assays were performed 3 times using 3 different chromatin preparations with similar results.

    Article Snippet: The transfection reagent ExGen500 was purchased from MBI Fermentas (Burlington, Ont.), DNA modifying enzymes were obtained from New England Biolabs (Pickering, Ont.), and synthetic oligonucleotides (oligos) were from Invitrogen (Carlsbad, Calif.) or Sigma–Aldrich (St-Louis, Mo.).

    Techniques: Binding Assay, Electrophoretic Mobility Shift Assay, Labeling, Staining, Chromatin Immunoprecipitation, Isolation, Cross-linking Immunoprecipitation, Immunoprecipitation, Amplification, Polymerase Chain Reaction, Agarose Gel Electrophoresis

    Effect of antisense oligos for the TRPC1 gene on TRPC1 protein expression, SOCE and astrocyte proliferation

    Journal:

    Article Title: Visualization of localized store-operated calcium entry in mouse astrocytes. Close proximity to the endoplasmic reticulum

    doi: 10.1113/jphysiol.2005.085035

    Figure Lengend Snippet: Effect of antisense oligos for the TRPC1 gene on TRPC1 protein expression, SOCE and astrocyte proliferation

    Article Snippet: Next Generation™ antisense oligonucleotides (AS-oligos) were synthesized by Sequitur, Inc. (Natick, MA, USA).

    Techniques: Expressing

    Schematic image illustrating the Golden gate cloning of multiple gRNAs into the concatemer vector containing 3 gRNA expression cassettes . Annealed oligos (gRNA targets), DNA ligase and the Bbs I restriction enzyme are mixed with the gRNA concatemer vector in a single reaction. Repeated temperature cycles facilitate repeated digestion (21 °C) and ligation (37 °C). Bbs I digestion generates the custom-designed overhangs unique for each cassette. During the ligation, gRNAs are integrated into the vector by cassette-specific integration, determined by the matching overhangs of the gRNA and the vector. If the original fragment containing the two Bbs I restriction sites is ligated back into the vector it will again be removed in the following round of digestion. In contrast, upon ligation of a gRNA the Bbs I restriction site is disrupted and hence the gRNA cannot be removed during the following rounds of digestion. Blue – Bbs I enzyme, pink – T7 DNA ligase, U6 – U6 promoter, gRNA1.1–1.3 represent different gRNAs for the same gene (e.g. gRNA1.1 – gRNA1 for gene 1).

    Journal: Developmental Biology

    Article Title: Simultaneous paralogue knockout using a CRISPR-concatemer in mouse small intestinal organoids

    doi: 10.1016/j.ydbio.2016.10.016

    Figure Lengend Snippet: Schematic image illustrating the Golden gate cloning of multiple gRNAs into the concatemer vector containing 3 gRNA expression cassettes . Annealed oligos (gRNA targets), DNA ligase and the Bbs I restriction enzyme are mixed with the gRNA concatemer vector in a single reaction. Repeated temperature cycles facilitate repeated digestion (21 °C) and ligation (37 °C). Bbs I digestion generates the custom-designed overhangs unique for each cassette. During the ligation, gRNAs are integrated into the vector by cassette-specific integration, determined by the matching overhangs of the gRNA and the vector. If the original fragment containing the two Bbs I restriction sites is ligated back into the vector it will again be removed in the following round of digestion. In contrast, upon ligation of a gRNA the Bbs I restriction site is disrupted and hence the gRNA cannot be removed during the following rounds of digestion. Blue – Bbs I enzyme, pink – T7 DNA ligase, U6 – U6 promoter, gRNA1.1–1.3 represent different gRNAs for the same gene (e.g. gRNA1.1 – gRNA1 for gene 1).

    Article Snippet: 2.1.2 Multiple gRNA cloning gRNAs were ordered as oligonucleotides (oligos) from Sigma Aldrich.

    Techniques: Clone Assay, Plasmid Preparation, Expressing, Ligation