phix174 ssdna  (Millipore)


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    Structured Review

    Millipore phix174 ssdna
    DdrC binds to <t>ssDNA</t> and dsDNA with a preference for ssDNA. A Binding of recombinant DdrC to plasmid or viral DNA analyzed by EMSA. 200 ng of supercoiled or linear pBR322 DNA as well as 200 ng of RFI or single-stranded DNA of <t>phiX174</t> virion (31 μM nucleotides of each DNA) were incubated with increasing concentrations of DdrC as indicated in the figure. DNA-protein complexes were separated in 1.2% agarose gels. Products loaded in the right lane of the left panel were treated with SDS and proteinase K. sc: supercoiled dsDNA, oc: open circle dsDNA, Li: linear dsDNA. B Binding of DdrC to oligonucleotides. Increasing concentrations of DdrC were incubated with 3.3 nM of a single-stranded (ss) 67-mer fluorescent oligonucleotide (left panel) or 3.3 nM of the corresponding ds oligonucleotide (right panel). The products of the reactions were separated in 6% native polyacrylamide gels. Lanes C: DNA control without DdrC.
    Phix174 Ssdna, supplied by Millipore, used in various techniques. Bioz Stars score: 91/100, based on 4581 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/phix174 ssdna/product/Millipore
    Average 91 stars, based on 4581 article reviews
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    phix174 ssdna - by Bioz Stars, 2020-09
    91/100 stars

    Images

    1) Product Images from "In vivo and in vitro characterization of DdrC, a DNA damage response protein in Deinococcus radiodurans bacterium"

    Article Title: In vivo and in vitro characterization of DdrC, a DNA damage response protein in Deinococcus radiodurans bacterium

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0177751

    DdrC binds to ssDNA and dsDNA with a preference for ssDNA. A Binding of recombinant DdrC to plasmid or viral DNA analyzed by EMSA. 200 ng of supercoiled or linear pBR322 DNA as well as 200 ng of RFI or single-stranded DNA of phiX174 virion (31 μM nucleotides of each DNA) were incubated with increasing concentrations of DdrC as indicated in the figure. DNA-protein complexes were separated in 1.2% agarose gels. Products loaded in the right lane of the left panel were treated with SDS and proteinase K. sc: supercoiled dsDNA, oc: open circle dsDNA, Li: linear dsDNA. B Binding of DdrC to oligonucleotides. Increasing concentrations of DdrC were incubated with 3.3 nM of a single-stranded (ss) 67-mer fluorescent oligonucleotide (left panel) or 3.3 nM of the corresponding ds oligonucleotide (right panel). The products of the reactions were separated in 6% native polyacrylamide gels. Lanes C: DNA control without DdrC.
    Figure Legend Snippet: DdrC binds to ssDNA and dsDNA with a preference for ssDNA. A Binding of recombinant DdrC to plasmid or viral DNA analyzed by EMSA. 200 ng of supercoiled or linear pBR322 DNA as well as 200 ng of RFI or single-stranded DNA of phiX174 virion (31 μM nucleotides of each DNA) were incubated with increasing concentrations of DdrC as indicated in the figure. DNA-protein complexes were separated in 1.2% agarose gels. Products loaded in the right lane of the left panel were treated with SDS and proteinase K. sc: supercoiled dsDNA, oc: open circle dsDNA, Li: linear dsDNA. B Binding of DdrC to oligonucleotides. Increasing concentrations of DdrC were incubated with 3.3 nM of a single-stranded (ss) 67-mer fluorescent oligonucleotide (left panel) or 3.3 nM of the corresponding ds oligonucleotide (right panel). The products of the reactions were separated in 6% native polyacrylamide gels. Lanes C: DNA control without DdrC.

    Techniques Used: Binding Assay, Recombinant, Plasmid Preparation, Incubation

    Visualization of DdrC-DNA complexes by transmission electron microscopy. A PhiX174 ssDNA (1.4 nM, 7.5 μM nucleotides) was incubated with 1 μM (panels b-d) or 2 μM (panels f-h) of DdrC. Panel a: phiX174 ssDNA control without DdrC. Panel e: Interaction of E . coli SSB protein (1 μM) with ssDNA. Magnification = 85,000. B Supercoiled pBR322 DNA (1.7 nM, 7.5 μM base pairs) incubated with 1 μM (panel b and c) or 2 μM (panel d) of DdrC. Panel a: pBR322 DNA control without protein. Magnification = 85,000. Some“bridge” structures, forming loops or kinks, are indicated by arrows.
    Figure Legend Snippet: Visualization of DdrC-DNA complexes by transmission electron microscopy. A PhiX174 ssDNA (1.4 nM, 7.5 μM nucleotides) was incubated with 1 μM (panels b-d) or 2 μM (panels f-h) of DdrC. Panel a: phiX174 ssDNA control without DdrC. Panel e: Interaction of E . coli SSB protein (1 μM) with ssDNA. Magnification = 85,000. B Supercoiled pBR322 DNA (1.7 nM, 7.5 μM base pairs) incubated with 1 μM (panel b and c) or 2 μM (panel d) of DdrC. Panel a: pBR322 DNA control without protein. Magnification = 85,000. Some“bridge” structures, forming loops or kinks, are indicated by arrows.

    Techniques Used: Transmission Assay, Electron Microscopy, Incubation

    DdrC protects DNA against degradation by nucleases. Protection of supercoiled pBR322 plasmid (3.5 nM) from DNase I activity (0.1 U) (panel a), linear pBR322 (3.5 nM) from Exonuclease III activity (200 U) (panel b) and phiX174 ssDNA (5.9 nM) from Mung Bean Nuclease activity (1 U) (panel c) by 7 μM, 7 μM, and 2 μM DdrC, respectively. Lanes C: DNA controls without protein. Lanes 1: DNA incubation with nuclease alone. Lanes 2: DNA incubation with DdrC alone. Lanes 3: DNA pre-incubated with DdrC 15 min at 4°C before addition of nuclease. Lanes 4: Reaction products corresponding to lane 3 were further treated with Proteinase K/SDS. Panel a, lane 5: DdrC and DNase I were simultaneously incubated with supercoiled DNA before treatment with Proteinase K/SDS.
    Figure Legend Snippet: DdrC protects DNA against degradation by nucleases. Protection of supercoiled pBR322 plasmid (3.5 nM) from DNase I activity (0.1 U) (panel a), linear pBR322 (3.5 nM) from Exonuclease III activity (200 U) (panel b) and phiX174 ssDNA (5.9 nM) from Mung Bean Nuclease activity (1 U) (panel c) by 7 μM, 7 μM, and 2 μM DdrC, respectively. Lanes C: DNA controls without protein. Lanes 1: DNA incubation with nuclease alone. Lanes 2: DNA incubation with DdrC alone. Lanes 3: DNA pre-incubated with DdrC 15 min at 4°C before addition of nuclease. Lanes 4: Reaction products corresponding to lane 3 were further treated with Proteinase K/SDS. Panel a, lane 5: DdrC and DNase I were simultaneously incubated with supercoiled DNA before treatment with Proteinase K/SDS.

    Techniques Used: Plasmid Preparation, Activity Assay, Incubation

    2) Product Images from "Inhibition of double-strand break non-homologous end-joining by cisplatin adducts in human cell extracts"

    Article Title: Inhibition of double-strand break non-homologous end-joining by cisplatin adducts in human cell extracts

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gki528

    NHEJ of short and long AT-rich substrates. Sequence of the ends of the ( A ) short and ( C ) long AT-rich control and cisplatinated DNA substrates. Double-stranded oligonucleotides were ligated into pGEM plasmid DNA (underlined) with the MfeI restriction site shown in boldface. The inserted triangles show the position of the GTG sequence for cisplatination. Graphs ( B ) and ( D ) show the percentage of ligation products formed by MO59K extract and DNA substrates shown in (A) and (C), respectively. Substrates were either buffer treated or cisplatinated (2.65 nmol cisplatin). Experiments were performed in triplicate (±SD) and are representative of three independent experiments.
    Figure Legend Snippet: NHEJ of short and long AT-rich substrates. Sequence of the ends of the ( A ) short and ( C ) long AT-rich control and cisplatinated DNA substrates. Double-stranded oligonucleotides were ligated into pGEM plasmid DNA (underlined) with the MfeI restriction site shown in boldface. The inserted triangles show the position of the GTG sequence for cisplatination. Graphs ( B ) and ( D ) show the percentage of ligation products formed by MO59K extract and DNA substrates shown in (A) and (C), respectively. Substrates were either buffer treated or cisplatinated (2.65 nmol cisplatin). Experiments were performed in triplicate (±SD) and are representative of three independent experiments.

    Techniques Used: Non-Homologous End Joining, Sequencing, Plasmid Preparation, Ligation

    Manufacture of substrate with a single 1,3-d(GpTpG) cisplatin adduct. ( A ) Diagrammatic representation of substrate manufacture. (i) Oligonucleotides were annealed to form double-stranded molecules with A plus 24mer (as shown here) or B plus 24mer. In each case the 24mer was cisplatinated ( cis ). The GTG cisplatination site is indicated by a triangle and EcoRI compatible overhang shown in boldface. Oligonucleotides A and B were phosphorylated at the 5′ end. (ii) These double-stranded molecules were then ligated onto EcoRI linearized pGEM3zf+ plasmid DNA (indicated by horizontal lines and containing no other cisplatin adducts). Acis and Bcis are shown here, Acon and Bcon were constructed identically but lacked the 1,3-d(GpTpG) cisplatin adduct at the GTG cisplatination site. The DNA substrates Acis and Bcis had self-incompatible ends but were compatible with each other. (iii) Position of HindIII site and polarity of exonuclease III digestion. The 12 base fragment resistant to digestion is indicated. ( B ) Exonuclease III analysis of substrates to confirm cisplatin adduct presence. 32 P-end-labelled DNA substrate was subject to restriction enzyme digestion with HindIII, subsequent exonuclease III digestion and denaturing acrylamide (15%) gel electrophoresis. Control Bcon substrate (lanes 1 and 2), cisplatinated Bcis substrate (lanes 3 and 4), oligonucleotide B annealed to control 24mer (lane 5), cisplatinated oligonucleotide B annealed to 24mer (lane 6), 10 bp molecular weight marker (lane 7). Exonuclease III digestion was for 0 h (lanes 1 and 3) and for 2 h (lanes 2 and 4–6). The arrow shows the position of the 12 base fragments (which migrated at ∼13 bases owing to the presence of the cisplatin adduct) remaining owing to the blockage of nuclease action by the cisplatin adduct.
    Figure Legend Snippet: Manufacture of substrate with a single 1,3-d(GpTpG) cisplatin adduct. ( A ) Diagrammatic representation of substrate manufacture. (i) Oligonucleotides were annealed to form double-stranded molecules with A plus 24mer (as shown here) or B plus 24mer. In each case the 24mer was cisplatinated ( cis ). The GTG cisplatination site is indicated by a triangle and EcoRI compatible overhang shown in boldface. Oligonucleotides A and B were phosphorylated at the 5′ end. (ii) These double-stranded molecules were then ligated onto EcoRI linearized pGEM3zf+ plasmid DNA (indicated by horizontal lines and containing no other cisplatin adducts). Acis and Bcis are shown here, Acon and Bcon were constructed identically but lacked the 1,3-d(GpTpG) cisplatin adduct at the GTG cisplatination site. The DNA substrates Acis and Bcis had self-incompatible ends but were compatible with each other. (iii) Position of HindIII site and polarity of exonuclease III digestion. The 12 base fragment resistant to digestion is indicated. ( B ) Exonuclease III analysis of substrates to confirm cisplatin adduct presence. 32 P-end-labelled DNA substrate was subject to restriction enzyme digestion with HindIII, subsequent exonuclease III digestion and denaturing acrylamide (15%) gel electrophoresis. Control Bcon substrate (lanes 1 and 2), cisplatinated Bcis substrate (lanes 3 and 4), oligonucleotide B annealed to control 24mer (lane 5), cisplatinated oligonucleotide B annealed to 24mer (lane 6), 10 bp molecular weight marker (lane 7). Exonuclease III digestion was for 0 h (lanes 1 and 3) and for 2 h (lanes 2 and 4–6). The arrow shows the position of the 12 base fragments (which migrated at ∼13 bases owing to the presence of the cisplatin adduct) remaining owing to the blockage of nuclease action by the cisplatin adduct.

    Techniques Used: Plasmid Preparation, Construct, Nucleic Acid Electrophoresis, Molecular Weight, Marker

    NHEJ of control and cisplatinated DNA substrate. End-joining performed with MO59K extract and DNA substrate treated with cisplatin at the following concentration (nmol) ( A ) 5.3, ( B ) 4.4, ( C ) 3.5, ( D ) 2.65, ( E ) 1.1 and ( F ) buffer only. NHEJ was measured over a time course where DNA was incubated with extract for 0, 0.5, 1, 2, 3 and 4 h (lanes 1–6). The 3.2 kb linear monomer (1×) was joined to form ligated linear dimers (2×), trimers (3×) and higher multimers (m) as indicated. ( G ) Proportion of DNA substrate ligated against time at the indicated cisplatin concentrations.
    Figure Legend Snippet: NHEJ of control and cisplatinated DNA substrate. End-joining performed with MO59K extract and DNA substrate treated with cisplatin at the following concentration (nmol) ( A ) 5.3, ( B ) 4.4, ( C ) 3.5, ( D ) 2.65, ( E ) 1.1 and ( F ) buffer only. NHEJ was measured over a time course where DNA was incubated with extract for 0, 0.5, 1, 2, 3 and 4 h (lanes 1–6). The 3.2 kb linear monomer (1×) was joined to form ligated linear dimers (2×), trimers (3×) and higher multimers (m) as indicated. ( G ) Proportion of DNA substrate ligated against time at the indicated cisplatin concentrations.

    Techniques Used: Non-Homologous End Joining, Concentration Assay, Incubation

    3) Product Images from "Sequence, "subtle" alternative splicing and expression of the CYYR1 (cysteine/tyrosine-rich 1) mRNA in human neuroendocrine tumors"

    Article Title: Sequence, "subtle" alternative splicing and expression of the CYYR1 (cysteine/tyrosine-rich 1) mRNA in human neuroendocrine tumors

    Journal: BMC Cancer

    doi: 10.1186/1471-2407-7-66

    Enzymatic digestion of CYYR1 CDS RT-PCR products from normal brain and an NE tumor . Gel electrophoresis analysis of CYYR1 CDS RT-PCR products, from normal brain and NE 16, after PstI digestion. Expected size bands (CAG - form: 605 bp, CAG + form: 427 bp and 181 bp) were obtained in both samples. M1: GeneRuler marker, 500 ng; M2: DNA M5 marker, 250 ng.
    Figure Legend Snippet: Enzymatic digestion of CYYR1 CDS RT-PCR products from normal brain and an NE tumor . Gel electrophoresis analysis of CYYR1 CDS RT-PCR products, from normal brain and NE 16, after PstI digestion. Expected size bands (CAG - form: 605 bp, CAG + form: 427 bp and 181 bp) were obtained in both samples. M1: GeneRuler marker, 500 ng; M2: DNA M5 marker, 250 ng.

    Techniques Used: Reverse Transcription Polymerase Chain Reaction, Nucleic Acid Electrophoresis, Marker

    RT-PCR of CYYR1 mRNA isoforms . An example of agarose gel loaded with duplicated RT-PCR products: B2M (lanes 1–6, 586 bp), CYYR1 CAG - (lanes 7–12, 321 bp), and CYYR1 CAG + (lanes 13–18, 324 bp) mRNAs for samples NE 16, NE 17 and NE 18, respectively from left to right. DNA M5 marker (M1 and M2, 250 ng and 500 ng, respectively) were used for quantification by Gel Doc 2000 software.
    Figure Legend Snippet: RT-PCR of CYYR1 mRNA isoforms . An example of agarose gel loaded with duplicated RT-PCR products: B2M (lanes 1–6, 586 bp), CYYR1 CAG - (lanes 7–12, 321 bp), and CYYR1 CAG + (lanes 13–18, 324 bp) mRNAs for samples NE 16, NE 17 and NE 18, respectively from left to right. DNA M5 marker (M1 and M2, 250 ng and 500 ng, respectively) were used for quantification by Gel Doc 2000 software.

    Techniques Used: Reverse Transcription Polymerase Chain Reaction, Agarose Gel Electrophoresis, Marker, Software

    CYYR1 mutation in an NE tumor sample . Representative electrophoretograms of a sample with normal sequence NE 15 (A) and the mutated sample NE 16 (B), where a variation (apparently in heterozygotic form) in position 333 of CDS (T replaces C) leads to a P111S amino acid change.
    Figure Legend Snippet: CYYR1 mutation in an NE tumor sample . Representative electrophoretograms of a sample with normal sequence NE 15 (A) and the mutated sample NE 16 (B), where a variation (apparently in heterozygotic form) in position 333 of CDS (T replaces C) leads to a P111S amino acid change.

    Techniques Used: Mutagenesis, Sequencing

    4) Product Images from "In vivo and in vitro characterization of DdrC, a DNA damage response protein in Deinococcus radiodurans bacterium"

    Article Title: In vivo and in vitro characterization of DdrC, a DNA damage response protein in Deinococcus radiodurans bacterium

    Journal: PLoS ONE

    doi: 10.1371/journal.pone.0177751

    DdrC stimulates DNA annealing. Kinetics of two complementary 67-mer oligonucleotides annealing in the absence (w/o protein) or the presence of DdrC, T4 gp32 or SSB using a DAPI fluorescence-based method. The 67-mer oligonucleotide (200 nM) was mixed in 1 ml of reaction buffer with 0.2 μM DdrC protein, or 0.1 μM T4 gp32, or 0.1 μM SSB from E . coli prior to addition of the reverse oligonucleotide. The extent of DNA annealing is defined as follows: (observed fluorescence—67-mer ssDNA fluorescence) x 100 / 67-mer ds DNA fluorescence.
    Figure Legend Snippet: DdrC stimulates DNA annealing. Kinetics of two complementary 67-mer oligonucleotides annealing in the absence (w/o protein) or the presence of DdrC, T4 gp32 or SSB using a DAPI fluorescence-based method. The 67-mer oligonucleotide (200 nM) was mixed in 1 ml of reaction buffer with 0.2 μM DdrC protein, or 0.1 μM T4 gp32, or 0.1 μM SSB from E . coli prior to addition of the reverse oligonucleotide. The extent of DNA annealing is defined as follows: (observed fluorescence—67-mer ssDNA fluorescence) x 100 / 67-mer ds DNA fluorescence.

    Techniques Used: Fluorescence

    DdrC binds to ssDNA and dsDNA with a preference for ssDNA. A Binding of recombinant DdrC to plasmid or viral DNA analyzed by EMSA. 200 ng of supercoiled or linear pBR322 DNA as well as 200 ng of RFI or single-stranded DNA of phiX174 virion (31 μM nucleotides of each DNA) were incubated with increasing concentrations of DdrC as indicated in the figure. DNA-protein complexes were separated in 1.2% agarose gels. Products loaded in the right lane of the left panel were treated with SDS and proteinase K. sc: supercoiled dsDNA, oc: open circle dsDNA, Li: linear dsDNA. B Binding of DdrC to oligonucleotides. Increasing concentrations of DdrC were incubated with 3.3 nM of a single-stranded (ss) 67-mer fluorescent oligonucleotide (left panel) or 3.3 nM of the corresponding ds oligonucleotide (right panel). The products of the reactions were separated in 6% native polyacrylamide gels. Lanes C: DNA control without DdrC.
    Figure Legend Snippet: DdrC binds to ssDNA and dsDNA with a preference for ssDNA. A Binding of recombinant DdrC to plasmid or viral DNA analyzed by EMSA. 200 ng of supercoiled or linear pBR322 DNA as well as 200 ng of RFI or single-stranded DNA of phiX174 virion (31 μM nucleotides of each DNA) were incubated with increasing concentrations of DdrC as indicated in the figure. DNA-protein complexes were separated in 1.2% agarose gels. Products loaded in the right lane of the left panel were treated with SDS and proteinase K. sc: supercoiled dsDNA, oc: open circle dsDNA, Li: linear dsDNA. B Binding of DdrC to oligonucleotides. Increasing concentrations of DdrC were incubated with 3.3 nM of a single-stranded (ss) 67-mer fluorescent oligonucleotide (left panel) or 3.3 nM of the corresponding ds oligonucleotide (right panel). The products of the reactions were separated in 6% native polyacrylamide gels. Lanes C: DNA control without DdrC.

    Techniques Used: Binding Assay, Recombinant, Plasmid Preparation, Incubation

    Visualization of DdrC-DNA complexes by transmission electron microscopy. A PhiX174 ssDNA (1.4 nM, 7.5 μM nucleotides) was incubated with 1 μM (panels b-d) or 2 μM (panels f-h) of DdrC. Panel a: phiX174 ssDNA control without DdrC. Panel e: Interaction of E . coli SSB protein (1 μM) with ssDNA. Magnification = 85,000. B Supercoiled pBR322 DNA (1.7 nM, 7.5 μM base pairs) incubated with 1 μM (panel b and c) or 2 μM (panel d) of DdrC. Panel a: pBR322 DNA control without protein. Magnification = 85,000. Some“bridge” structures, forming loops or kinks, are indicated by arrows.
    Figure Legend Snippet: Visualization of DdrC-DNA complexes by transmission electron microscopy. A PhiX174 ssDNA (1.4 nM, 7.5 μM nucleotides) was incubated with 1 μM (panels b-d) or 2 μM (panels f-h) of DdrC. Panel a: phiX174 ssDNA control without DdrC. Panel e: Interaction of E . coli SSB protein (1 μM) with ssDNA. Magnification = 85,000. B Supercoiled pBR322 DNA (1.7 nM, 7.5 μM base pairs) incubated with 1 μM (panel b and c) or 2 μM (panel d) of DdrC. Panel a: pBR322 DNA control without protein. Magnification = 85,000. Some“bridge” structures, forming loops or kinks, are indicated by arrows.

    Techniques Used: Transmission Assay, Electron Microscopy, Incubation

    DdrC protects DNA against degradation by nucleases. Protection of supercoiled pBR322 plasmid (3.5 nM) from DNase I activity (0.1 U) (panel a), linear pBR322 (3.5 nM) from Exonuclease III activity (200 U) (panel b) and phiX174 ssDNA (5.9 nM) from Mung Bean Nuclease activity (1 U) (panel c) by 7 μM, 7 μM, and 2 μM DdrC, respectively. Lanes C: DNA controls without protein. Lanes 1: DNA incubation with nuclease alone. Lanes 2: DNA incubation with DdrC alone. Lanes 3: DNA pre-incubated with DdrC 15 min at 4°C before addition of nuclease. Lanes 4: Reaction products corresponding to lane 3 were further treated with Proteinase K/SDS. Panel a, lane 5: DdrC and DNase I were simultaneously incubated with supercoiled DNA before treatment with Proteinase K/SDS.
    Figure Legend Snippet: DdrC protects DNA against degradation by nucleases. Protection of supercoiled pBR322 plasmid (3.5 nM) from DNase I activity (0.1 U) (panel a), linear pBR322 (3.5 nM) from Exonuclease III activity (200 U) (panel b) and phiX174 ssDNA (5.9 nM) from Mung Bean Nuclease activity (1 U) (panel c) by 7 μM, 7 μM, and 2 μM DdrC, respectively. Lanes C: DNA controls without protein. Lanes 1: DNA incubation with nuclease alone. Lanes 2: DNA incubation with DdrC alone. Lanes 3: DNA pre-incubated with DdrC 15 min at 4°C before addition of nuclease. Lanes 4: Reaction products corresponding to lane 3 were further treated with Proteinase K/SDS. Panel a, lane 5: DdrC and DNase I were simultaneously incubated with supercoiled DNA before treatment with Proteinase K/SDS.

    Techniques Used: Plasmid Preparation, Activity Assay, Incubation

    5) Product Images from "Inhibition of double-strand break non-homologous end-joining by cisplatin adducts in human cell extracts"

    Article Title: Inhibition of double-strand break non-homologous end-joining by cisplatin adducts in human cell extracts

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gki528

    NHEJ of short and long AT-rich substrates. Sequence of the ends of the ( A ) short and ( C ) long AT-rich control and cisplatinated DNA substrates. Double-stranded oligonucleotides were ligated into pGEM plasmid DNA (underlined) with the MfeI restriction site shown in boldface. The inserted triangles show the position of the GTG sequence for cisplatination. Graphs ( B ) and ( D ) show the percentage of ligation products formed by MO59K extract and DNA substrates shown in (A) and (C), respectively. Substrates were either buffer treated or cisplatinated (2.65 nmol cisplatin). Experiments were performed in triplicate (±SD) and are representative of three independent experiments.
    Figure Legend Snippet: NHEJ of short and long AT-rich substrates. Sequence of the ends of the ( A ) short and ( C ) long AT-rich control and cisplatinated DNA substrates. Double-stranded oligonucleotides were ligated into pGEM plasmid DNA (underlined) with the MfeI restriction site shown in boldface. The inserted triangles show the position of the GTG sequence for cisplatination. Graphs ( B ) and ( D ) show the percentage of ligation products formed by MO59K extract and DNA substrates shown in (A) and (C), respectively. Substrates were either buffer treated or cisplatinated (2.65 nmol cisplatin). Experiments were performed in triplicate (±SD) and are representative of three independent experiments.

    Techniques Used: Non-Homologous End Joining, Sequencing, Plasmid Preparation, Ligation

    6) Product Images from "A real-time DNase assay (ReDA) based on PicoGreen(R) fluorescence"

    Article Title: A real-time DNase assay (ReDA) based on PicoGreen(R) fluorescence

    Journal: Nucleic Acids Research

    doi: 10.1093/nar/gng111

    Survey of dyes. Top lanes: lane 1, size markers; lanes 2–9 SYBR Gold®, dilutions of 1/500, 1/1000, 1/2000, 1/5000, 1/10 000, 1/20 000, no dye, 1/20 000 (without enzyme) respectively (note, SYBR Gold® was observed to decrease DNA mobility when used in concentrations higher than 1/5000); lanes 10–12, ethidium bromide 4.5, 2 and 1 µM respectively. Bottom lanes: lane 13, size markers; lanes 14–18, ethidium bromide (continued) 0.2, 0.1, 0.01, no dye, 0.01 µM (without enzyme) respectively. Lanes 19–24, PicoGreen®, dilutions of 1/200, 1/500, 1/1000, 1/2000, 1/5000, no dye respectively. (–) indicates the negative control in which no enzyme was used.
    Figure Legend Snippet: Survey of dyes. Top lanes: lane 1, size markers; lanes 2–9 SYBR Gold®, dilutions of 1/500, 1/1000, 1/2000, 1/5000, 1/10 000, 1/20 000, no dye, 1/20 000 (without enzyme) respectively (note, SYBR Gold® was observed to decrease DNA mobility when used in concentrations higher than 1/5000); lanes 10–12, ethidium bromide 4.5, 2 and 1 µM respectively. Bottom lanes: lane 13, size markers; lanes 14–18, ethidium bromide (continued) 0.2, 0.1, 0.01, no dye, 0.01 µM (without enzyme) respectively. Lanes 19–24, PicoGreen®, dilutions of 1/200, 1/500, 1/1000, 1/2000, 1/5000, no dye respectively. (–) indicates the negative control in which no enzyme was used.

    Techniques Used: Negative Control

    7) Product Images from "Molecular characterization of a Trichinella spiralis enolase and its interaction with the host’s plasminogen"

    Article Title: Molecular characterization of a Trichinella spiralis enolase and its interaction with the host’s plasminogen

    Journal: Veterinary Research

    doi: 10.1186/s13567-019-0727-y

    Expression and purification of rTsENO and M-rTsENO. A SDS-PAGE of rTsENO and M-TsENO expressed by recombinant plasmids. M: protein marker; 1: uninduced recombinant bacterial lysate; 2: induced recombinant pQE-80L/TsENO; 3: induced recombinant pQE-80L/M-TsENO. B SDS-PAGE of purified rTsENO. M: protein marker; 1: uninduced recombinant bacterial lysate; 2: induced recombinant pQE-80L/TsENO; 3: purified rTsENO (6 µg). C SDS-PAGE of purified M-rTsENO. M: protein marker; 1: uninduced recombinant bacterial lysate; 2: induced recombinant pQE-80L/M-TsENO; 3: purified M-rTsENO (2 µg).
    Figure Legend Snippet: Expression and purification of rTsENO and M-rTsENO. A SDS-PAGE of rTsENO and M-TsENO expressed by recombinant plasmids. M: protein marker; 1: uninduced recombinant bacterial lysate; 2: induced recombinant pQE-80L/TsENO; 3: induced recombinant pQE-80L/M-TsENO. B SDS-PAGE of purified rTsENO. M: protein marker; 1: uninduced recombinant bacterial lysate; 2: induced recombinant pQE-80L/TsENO; 3: purified rTsENO (6 µg). C SDS-PAGE of purified M-rTsENO. M: protein marker; 1: uninduced recombinant bacterial lysate; 2: induced recombinant pQE-80L/M-TsENO; 3: purified M-rTsENO (2 µg).

    Techniques Used: Expressing, Purification, SDS Page, Recombinant, Marker

    8) Product Images from "Mucosally Delivered Salmonella Live Vector Vaccines Elicit Potent Immune Responses against a Foreign Antigen in Neonatal Mice Born to Naive and Immune Mothers "

    Article Title: Mucosally Delivered Salmonella Live Vector Vaccines Elicit Potent Immune Responses against a Foreign Antigen in Neonatal Mice Born to Naive and Immune Mothers

    Journal: Infection and Immunity

    doi: 10.1128/IAI.72.8.4637-4646.2004

    In vivo distribution and persistence of mucosally delivered Salmonella live vector vaccines in neonatal mice. Groups of three to eight neonates were immunized i.n. with 10 9 CFU of CVD 908- htrA or SL3261 carrying pTET lpp . NALT, CLN, PP, lungs, and livers were harvested at different time points from day 1 to 12 postimmunization. The presence of vaccine organisms was determined by culturing tissues from individual mice with or without antibiotic as described in Materials and Methods. Curves indicate the percentages of cultures positive for Salmonella (•) and for Salmonella harboring plasmid pTET lpp (○) for up to 10 days after vaccination.
    Figure Legend Snippet: In vivo distribution and persistence of mucosally delivered Salmonella live vector vaccines in neonatal mice. Groups of three to eight neonates were immunized i.n. with 10 9 CFU of CVD 908- htrA or SL3261 carrying pTET lpp . NALT, CLN, PP, lungs, and livers were harvested at different time points from day 1 to 12 postimmunization. The presence of vaccine organisms was determined by culturing tissues from individual mice with or without antibiotic as described in Materials and Methods. Curves indicate the percentages of cultures positive for Salmonella (•) and for Salmonella harboring plasmid pTET lpp (○) for up to 10 days after vaccination.

    Techniques Used: In Vivo, Plasmid Preparation, Mouse Assay

    Serum IgG responses to LPS and Frag C in mice immunized as neonates with Salmonella live vector vaccines. Mice were immunized i.n. on days 7 and 22 after birth with 10 9 CFU of CVD 908- htrA or SL3261 alone or carrying plasmid pTET lpp . Data represent individual titers in 5 to 10 pups per group. Lines are plotted upon the geometric mean titers for each time point. Arrows indicate each immunization. Significant differences between preimmunization titers and titers achieved after two doses are indicated (*, P
    Figure Legend Snippet: Serum IgG responses to LPS and Frag C in mice immunized as neonates with Salmonella live vector vaccines. Mice were immunized i.n. on days 7 and 22 after birth with 10 9 CFU of CVD 908- htrA or SL3261 alone or carrying plasmid pTET lpp . Data represent individual titers in 5 to 10 pups per group. Lines are plotted upon the geometric mean titers for each time point. Arrows indicate each immunization. Significant differences between preimmunization titers and titers achieved after two doses are indicated (*, P

    Techniques Used: Mouse Assay, Plasmid Preparation

    Serum IgG responses to S. enterica serovar Typhi LPS (A) and Frag C (B) induced by newborn mice immunized with increasing doses of CVD 908- htrA carrying pTET lpp . Neonatal BALB/c mice (5 to 10 pups/group) were immunized i.n. on days 7 and 22 after birth with 10 6 to 10 9 CFU of CVD 908- htrA (pTET lpp ). Arrows indicate each immunization. IgG antibodies to LPS and Frag C were measured by ELISA. LPS titers are expressed in ELISA units (EU) per milliliter (end point titers) as described in Materials and Methods. Frag C titers are expressed in international units of TT neutralizing antibodies per milliliter by extrapolation in the curve of a mouse Frag C control serum calibrated in international units per milliliter against the World Health Organization standard by the in vivo neutralization test in mice. The data represent mean titers in each group. Significant differences between pre- and postimmunization titers are indicated (*, P
    Figure Legend Snippet: Serum IgG responses to S. enterica serovar Typhi LPS (A) and Frag C (B) induced by newborn mice immunized with increasing doses of CVD 908- htrA carrying pTET lpp . Neonatal BALB/c mice (5 to 10 pups/group) were immunized i.n. on days 7 and 22 after birth with 10 6 to 10 9 CFU of CVD 908- htrA (pTET lpp ). Arrows indicate each immunization. IgG antibodies to LPS and Frag C were measured by ELISA. LPS titers are expressed in ELISA units (EU) per milliliter (end point titers) as described in Materials and Methods. Frag C titers are expressed in international units of TT neutralizing antibodies per milliliter by extrapolation in the curve of a mouse Frag C control serum calibrated in international units per milliliter against the World Health Organization standard by the in vivo neutralization test in mice. The data represent mean titers in each group. Significant differences between pre- and postimmunization titers are indicated (*, P

    Techniques Used: Mouse Assay, Enzyme-linked Immunosorbent Assay, In Vivo, Neutralization

    9) Product Images from "A Double-Bromodomain Protein, FSH-S, Activates the Homeotic Gene Ultrabithorax through a Critical Promoter-Proximal Region ▿"

    Article Title: A Double-Bromodomain Protein, FSH-S, Activates the Homeotic Gene Ultrabithorax through a Critical Promoter-Proximal Region ▿

    Journal:

    doi: 10.1128/MCB.00692-07

    FSH-S shares similar binding sites with ZESTE. (A) Identification of FSH-S binding sites. Binding assays were performed with labeled Ubx-6a in the absence (lane 2) or presence of a DNA fragment containing multiple NTF-1 sites (lane 3, N) or oligonucleotides
    Figure Legend Snippet: FSH-S shares similar binding sites with ZESTE. (A) Identification of FSH-S binding sites. Binding assays were performed with labeled Ubx-6a in the absence (lane 2) or presence of a DNA fragment containing multiple NTF-1 sites (lane 3, N) or oligonucleotides

    Techniques Used: Binding Assay, Labeling

    FSH-S binds specific Ubx proximal sequences. (A) Diagram of the Ubx proximal promoter. The region from −226 to +36 is shown. The transcription start site is indicated by a bent arrow. The end points of DNA fragments used in binding assays
    Figure Legend Snippet: FSH-S binds specific Ubx proximal sequences. (A) Diagram of the Ubx proximal promoter. The region from −226 to +36 is shown. The transcription start site is indicated by a bent arrow. The end points of DNA fragments used in binding assays

    Techniques Used: Binding Assay

    10) Product Images from "New Mutations in the Mycobacterial ATP Synthase: New Insights into the Binding of the Diarylquinoline TMC207 to the ATP Synthase C-Ring Structure"

    Article Title: New Mutations in the Mycobacterial ATP Synthase: New Insights into the Binding of the Diarylquinoline TMC207 to the ATP Synthase C-Ring Structure

    Journal: Antimicrobial Agents and Chemotherapy

    doi: 10.1128/AAC.06154-11

    Multiple-sequence alignment of the subunits c from M. abscessus (Mabs), M. tuberculosis (Mtub), M. fortuitum (Mfor), M. smegmatis (Msme), E. coli (Ecol), Spirulina platensis (Spla), and I. tartaricus (Itar). Identical residues are marked with an asterisk.
    Figure Legend Snippet: Multiple-sequence alignment of the subunits c from M. abscessus (Mabs), M. tuberculosis (Mtub), M. fortuitum (Mfor), M. smegmatis (Msme), E. coli (Ecol), Spirulina platensis (Spla), and I. tartaricus (Itar). Identical residues are marked with an asterisk.

    Techniques Used: Sequencing

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    Fluorescence:

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    Cytometry:

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    Expressing:

    Article Title: Phospho-?Np63?/SREBF1 protein interactions
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    Staining:

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