dna ladders Thermo Fisher Search Results


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  • 96
    Thermo Fisher deoxyribonucleic acid dna ladder
    Deoxyribonucleic Acid Dna Ladder, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher deoxyribonucleic acid dna amplification
    Deoxyribonucleic Acid Dna Amplification, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 12 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher dna ladders
    Dna Ladders, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 382 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher phix174 rf1 dna
    The POLE3-POLE4 Complex Binds to H3-H4 Dimers and Tetramers and Promotes Tetrasome Formation and Supercoiling In Vitro (A) DSS crosslinking experiments performed in 150 mM NaCl. Lane 4 shows control without crosslinking; lanes 1, 2, and 5 show samples incubated with 1 mM DSS for 30 min at 23°C and resolved by SDS-PAGE and Coomassie staining. Lane 3 was left empty. Two black arrows indicate the molecular weight species identified upon crosslinking of POLE3-POLE4/H3-H4 co-complex. T (tetramers) indicates POLE3-POLE4 binding to H3-H4 tetramers, while D (dimers) indicates POLE3-POLE4 binding to dimers. (B) Western blot analysis of DSS crosslinking experiments performed in 150 mM NaCl. Lane 1 shows control without crosslinking; lane 2 shows sample incubated with 1 mM DSS for 30 min at 23°C. Samples were resolved by SDS-PAGE, transferred to nitrocellulose membranes, and incubated with α-H3, α-H4, α-POLE3, and α-POLE4 antibodies, from left to right. (C) Analytical gel filtration of POLE3-POLE4 complex alone or in combination with H3-H4 or H3(EE)-H4. Experiments were performed in 300 mM NaCl to prevent histone aggregation. (D) SDS-PAGE analysis and Coomassie staining of gel filtration fractions from (C). (E) Tetrasome assembly on linear <t>DNA</t> (Widom 601 sequence) monitored by native PAGE. Lane 2 shows tetrasome preassembled by salt dilution method; lanes 3–5 show linear DNA incubated with the indicated proteins. (F and G) Tetrasome assembly on linear DNA, performed as in (E), with the indicated proteins. (H) Plasmid supercoiling assay resolved by native agarose gel electrophoresis. Lane 1 shows supercoiled control <t>phix174</t> <t>RF1</t> DNA; lane 2, phix174 RF1 DNA relaxed by TOPO I; and lanes 3–7, phix174 RF1 DNA incubated, in the presence of TOPO I, with histones and increasing concentrations of POLE3-POLE4. (I) Plasmid supercoiling assay performed as described in (H) using increasing concentrations of POLE3ΔC-POLE4 or POLE3-POLE4.
    Phix174 Rf1 Dna, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher low dna
    The POLE3-POLE4 Complex Binds to H3-H4 Dimers and Tetramers and Promotes Tetrasome Formation and Supercoiling In Vitro (A) DSS crosslinking experiments performed in 150 mM NaCl. Lane 4 shows control without crosslinking; lanes 1, 2, and 5 show samples incubated with 1 mM DSS for 30 min at 23°C and resolved by SDS-PAGE and Coomassie staining. Lane 3 was left empty. Two black arrows indicate the molecular weight species identified upon crosslinking of POLE3-POLE4/H3-H4 co-complex. T (tetramers) indicates POLE3-POLE4 binding to H3-H4 tetramers, while D (dimers) indicates POLE3-POLE4 binding to dimers. (B) Western blot analysis of DSS crosslinking experiments performed in 150 mM NaCl. Lane 1 shows control without crosslinking; lane 2 shows sample incubated with 1 mM DSS for 30 min at 23°C. Samples were resolved by SDS-PAGE, transferred to nitrocellulose membranes, and incubated with α-H3, α-H4, α-POLE3, and α-POLE4 antibodies, from left to right. (C) Analytical gel filtration of POLE3-POLE4 complex alone or in combination with H3-H4 or H3(EE)-H4. Experiments were performed in 300 mM NaCl to prevent histone aggregation. (D) SDS-PAGE analysis and Coomassie staining of gel filtration fractions from (C). (E) Tetrasome assembly on linear <t>DNA</t> (Widom 601 sequence) monitored by native PAGE. Lane 2 shows tetrasome preassembled by salt dilution method; lanes 3–5 show linear DNA incubated with the indicated proteins. (F and G) Tetrasome assembly on linear DNA, performed as in (E), with the indicated proteins. (H) Plasmid supercoiling assay resolved by native agarose gel electrophoresis. Lane 1 shows supercoiled control <t>phix174</t> <t>RF1</t> DNA; lane 2, phix174 RF1 DNA relaxed by TOPO I; and lanes 3–7, phix174 RF1 DNA incubated, in the presence of TOPO I, with histones and increasing concentrations of POLE3-POLE4. (I) Plasmid supercoiling assay performed as described in (H) using increasing concentrations of POLE3ΔC-POLE4 or POLE3-POLE4.
    Low Dna, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher dna ladder
    Purified plasmids. Note: Lane 1 is the <t>DNA</t> ladder (Fermentas 1Kb ‘O Gene ruler, <t>Inqaba</t> Biotechnology, Pretoria, SA); lane 2 is the vector without insert (pGEM-T, Promega, Anatech SA); lanes 3, 5, 6, 7, 9 and 10 represent recombinant colonies (contains the polymerase chain reaction products: K2E03/01, K5R09/01, B8971/01, E2.5/01, E3.6/02, 8B/01, K4E03/05); lanes 4 and 8 represent vectors without or with partial inserts (samples K2E03/02 and 787/B567/10). The number in bracket is the number assigned to the number selected amplification product of interest (sample k5RO9/1, B8971/01, E2.5/01, E3.6/02, 8B/01, K4E03/05).
    Dna Ladder, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1304 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher dna standard
    Purified plasmids. Note: Lane 1 is the <t>DNA</t> ladder (Fermentas 1Kb ‘O Gene ruler, <t>Inqaba</t> Biotechnology, Pretoria, SA); lane 2 is the vector without insert (pGEM-T, Promega, Anatech SA); lanes 3, 5, 6, 7, 9 and 10 represent recombinant colonies (contains the polymerase chain reaction products: K2E03/01, K5R09/01, B8971/01, E2.5/01, E3.6/02, 8B/01, K4E03/05); lanes 4 and 8 represent vectors without or with partial inserts (samples K2E03/02 and 787/B567/10). The number in bracket is the number assigned to the number selected amplification product of interest (sample k5RO9/1, B8971/01, E2.5/01, E3.6/02, 8B/01, K4E03/05).
    Dna Standard, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 217 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher dna ladder control
    The homology region of the MAD1 promoter possesses open chromatin. ( A ) Upper panel: schematic representation of the positions of the primers used for the ChIP experiments relative to the homology region. Lower panel: chromatin immunoprecipitations were performed with antibodies specific for the indicated proteins on lysates of U937 cells treated with or without G-CSF (10 ng/ml) for 30 min. For control serial dilutions of the input were analyzed. ( B ) U937 cells were lyzed in F-buffer, nuclei prepared and digested with micrococcal nuclease (MNase) for the indicated times. <t>DNA</t> was then extracted and analyzed by agarose gel electrophoresis. The arrowheads identify mono-, di-, tri-, and tetra-nucleosomes. L: molecular size markers. ( C ) MNase or untreated DNA from exponentially growing U937 cells was used in <t>PCR</t> analysis with the indicated primer pairs. Untreated DNA was titrated (0,.25,.5, 1, and 4 ng) for the control PCR reactions and compared to 4 ng of Mnase-treated DNA. The agarose gels with the PCR products are shown in the top panel. The middle panel shows a quantification of the signal obtained from the MNase-treated DNA compared to the control signals. The bottom panel shows the position of the homology region relative to the analyzed promoter region. ( D) U937 cells were grown exponentially or treated for the indicated times with TPA or G-CSF as indicated. MNase or untreated DNA was amplified with primer pairs that span the homology region and neighboring genomic DNA.
    Dna Ladder Control, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1164 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher dna mass ladder
    RT-PCR analysis of plsX gene expression in the plsX polar allele duplication strain. The E. coli plsX polar allele duplication strain YZ143 and the wild-type strain UB1005 were grown to mid-log phase in RB, and total RNA was prepared as described in Materials and Methods. RT-PCRs were performed by using the Ambion RETROscript kit as directed. Lanes 2 through 5, RT-PCRs; lanes 7 through 10, PCRs with approximately 0.5 μg of total RNA as the template, but lacking RT. One microliter of RT reaction product, which corresponded to approximately 0.5 μg of total RNA, was used for each RT-PCR. The primer pairs used were 1 and 4 (lanes 2, 3, 7, and 8) or 1 and 3 (lanes 4, 5, 9, and 10). In lanes 2, 4, 7, and 9, RNA from strain UB1005 was analyzed. In lanes 3, 5, 8, and 10, RNA from strain YZ143 was analyzed. Lanes 1 and 11 are the 1-kb <t>DNA</t> ladder from <t>BRL,</t> and lane 6 was left vacant.
    Dna Mass Ladder, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 193 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Thermo Fisher 50bp dna ladder
    RhC genotyping: Lane 1 recessive homozygote (cc), lane 2 heterozygote (Cc), M – <t>50bp</t> <t>DNA</t> ladder, lane 3 dominant homozygote (CC).
    50bp Dna Ladder, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 29 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher dna size markers
    Biosynthesis and activity of synthetic RM.TthHB27I. (A) Isolation of synthetic RM.TthHB27I from E . coli . Lane M1, PageRuler™ Unstained Broad Range Protein Ladder; lane M2, Pierce™ Unstained Protein Molecular Weight Marker; lane 1, native wt RM.TthHB27I; lane 2, crude lysate from E . coli [pET21d(+)-synthetic tthHB27IRM ], grown at 30°C; lane 3, supernatant after PEI treatment; lane 4, supernatant after incubation at 65°C; lane 5, 0–50% AmS fractionation cut; lane 6, DEAE-cellulose chromatography; lane 7, heparin-agarose chromatography; lane 8, Phosphocellulose P11 chromatography. (B) Yields of recombinant wt RM.TthHB27I and synthetic RM.TthHB27I biosynthesis. Recombinant E . coli BL21(DE3) strains were subjected to 3 h induction at OD 600 = 0.6–0.7 and 30°C. Cells were lysed and protein lysates were analysed by 7.5% SDS-PAGE. Lanes M1, M2 as in (A); lane 1, synthetic RM.TthHB27I; lane 2, crude lysate from induced E . coli [pET21d(+)-wt- tthHB27IRM ]; lane 3, crude lysate from induced E . coli [pET21d(+)-synthetic tthHB27IRM ]. (C) Comparison of the activities of RM.TthHB27I MTase variants in vivo . 0.5 μg of total <t>DNA</t> from T . thermophilus or induced, recombinant E . coli BL21(DE3) strains were digested with 2 units of synthetic RM.TthHB27I in REase buffer+SAM for 1 h at 65°C. Lane 1, untreated T . thermophilus DNA; lane 2, T . thermophilus DNA digested with synthetic RM.TthHB27I; lane 3, untreated E . coli BL21(DE3) [pET21d(+)-wt- tthHB27IRM ] DNA; lane 4, as in lane 3, but with synthetic RM.TthHB27I; lane 5, untreated E . coli BL21(DE3) [pET21d(+)-synthetic tthHB27IRM ] DNA; lane 6, as in lane 5, but with synthetic RM.TthHB27I; lane M, <t>GeneRuler</t> 1 kb DNA Ladder.
    Dna Size Markers, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 252 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Thermo Fisher dna size marker
    Restriction pattern of some isolated Malassezia strains digested by BstC1 enzyme; Lane 1: M. pachydermatis (500bp, 70bp) lane 2: M. obtusa (580bp), lane 3: M. furfur (400bp, 180bp), lane 4: M. sympodialis (400bp, 180bp), and lane M: <t>DNA</t> ladder <t>50bp,</t> the
    Dna Size Marker, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 95/100, based on 190 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher template dna
    Promoter methylation in cf <t>DNA</t> from serum. (A) Heatmap of promoter methylation detected in cf DNA extracted from serum samples for single genes and combinations of genes. White: no methylation detected; gray: methylation detected; red box: best minimal combination of markers (highest AUC ). (B) Copies per mL of hypermethylated ST 6 GALNAC 3 , ZNF 660 , CCDC 181 , and HAPLN 3 in serum samples from 10 patients with BPH and 27 patients with PC analyzed by droplet digital <t>PCR</t> . P ‐values for trend of methylation in BPH
    Template Dna, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 10786 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    The POLE3-POLE4 Complex Binds to H3-H4 Dimers and Tetramers and Promotes Tetrasome Formation and Supercoiling In Vitro (A) DSS crosslinking experiments performed in 150 mM NaCl. Lane 4 shows control without crosslinking; lanes 1, 2, and 5 show samples incubated with 1 mM DSS for 30 min at 23°C and resolved by SDS-PAGE and Coomassie staining. Lane 3 was left empty. Two black arrows indicate the molecular weight species identified upon crosslinking of POLE3-POLE4/H3-H4 co-complex. T (tetramers) indicates POLE3-POLE4 binding to H3-H4 tetramers, while D (dimers) indicates POLE3-POLE4 binding to dimers. (B) Western blot analysis of DSS crosslinking experiments performed in 150 mM NaCl. Lane 1 shows control without crosslinking; lane 2 shows sample incubated with 1 mM DSS for 30 min at 23°C. Samples were resolved by SDS-PAGE, transferred to nitrocellulose membranes, and incubated with α-H3, α-H4, α-POLE3, and α-POLE4 antibodies, from left to right. (C) Analytical gel filtration of POLE3-POLE4 complex alone or in combination with H3-H4 or H3(EE)-H4. Experiments were performed in 300 mM NaCl to prevent histone aggregation. (D) SDS-PAGE analysis and Coomassie staining of gel filtration fractions from (C). (E) Tetrasome assembly on linear DNA (Widom 601 sequence) monitored by native PAGE. Lane 2 shows tetrasome preassembled by salt dilution method; lanes 3–5 show linear DNA incubated with the indicated proteins. (F and G) Tetrasome assembly on linear DNA, performed as in (E), with the indicated proteins. (H) Plasmid supercoiling assay resolved by native agarose gel electrophoresis. Lane 1 shows supercoiled control phix174 RF1 DNA; lane 2, phix174 RF1 DNA relaxed by TOPO I; and lanes 3–7, phix174 RF1 DNA incubated, in the presence of TOPO I, with histones and increasing concentrations of POLE3-POLE4. (I) Plasmid supercoiling assay performed as described in (H) using increasing concentrations of POLE3ΔC-POLE4 or POLE3-POLE4.

    Journal: Molecular Cell

    Article Title: POLE3-POLE4 Is a Histone H3-H4 Chaperone that Maintains Chromatin Integrity during DNA Replication

    doi: 10.1016/j.molcel.2018.08.043

    Figure Lengend Snippet: The POLE3-POLE4 Complex Binds to H3-H4 Dimers and Tetramers and Promotes Tetrasome Formation and Supercoiling In Vitro (A) DSS crosslinking experiments performed in 150 mM NaCl. Lane 4 shows control without crosslinking; lanes 1, 2, and 5 show samples incubated with 1 mM DSS for 30 min at 23°C and resolved by SDS-PAGE and Coomassie staining. Lane 3 was left empty. Two black arrows indicate the molecular weight species identified upon crosslinking of POLE3-POLE4/H3-H4 co-complex. T (tetramers) indicates POLE3-POLE4 binding to H3-H4 tetramers, while D (dimers) indicates POLE3-POLE4 binding to dimers. (B) Western blot analysis of DSS crosslinking experiments performed in 150 mM NaCl. Lane 1 shows control without crosslinking; lane 2 shows sample incubated with 1 mM DSS for 30 min at 23°C. Samples were resolved by SDS-PAGE, transferred to nitrocellulose membranes, and incubated with α-H3, α-H4, α-POLE3, and α-POLE4 antibodies, from left to right. (C) Analytical gel filtration of POLE3-POLE4 complex alone or in combination with H3-H4 or H3(EE)-H4. Experiments were performed in 300 mM NaCl to prevent histone aggregation. (D) SDS-PAGE analysis and Coomassie staining of gel filtration fractions from (C). (E) Tetrasome assembly on linear DNA (Widom 601 sequence) monitored by native PAGE. Lane 2 shows tetrasome preassembled by salt dilution method; lanes 3–5 show linear DNA incubated with the indicated proteins. (F and G) Tetrasome assembly on linear DNA, performed as in (E), with the indicated proteins. (H) Plasmid supercoiling assay resolved by native agarose gel electrophoresis. Lane 1 shows supercoiled control phix174 RF1 DNA; lane 2, phix174 RF1 DNA relaxed by TOPO I; and lanes 3–7, phix174 RF1 DNA incubated, in the presence of TOPO I, with histones and increasing concentrations of POLE3-POLE4. (I) Plasmid supercoiling assay performed as described in (H) using increasing concentrations of POLE3ΔC-POLE4 or POLE3-POLE4.

    Article Snippet: The circular plasmid, phix174 RF1 DNA was pre-treated with topoisomerase I (Invitrogen, 10 μ/lg DNA) for 30 min and then added (0.4 u μ g in 1 μL) into each of the chaperone-histone mix and incubated for an additional 60 min.

    Techniques: In Vitro, Incubation, SDS Page, Staining, Molecular Weight, Binding Assay, Western Blot, Filtration, Sequencing, Clear Native PAGE, Plasmid Preparation, Agarose Gel Electrophoresis

    Purified plasmids. Note: Lane 1 is the DNA ladder (Fermentas 1Kb ‘O Gene ruler, Inqaba Biotechnology, Pretoria, SA); lane 2 is the vector without insert (pGEM-T, Promega, Anatech SA); lanes 3, 5, 6, 7, 9 and 10 represent recombinant colonies (contains the polymerase chain reaction products: K2E03/01, K5R09/01, B8971/01, E2.5/01, E3.6/02, 8B/01, K4E03/05); lanes 4 and 8 represent vectors without or with partial inserts (samples K2E03/02 and 787/B567/10). The number in bracket is the number assigned to the number selected amplification product of interest (sample k5RO9/1, B8971/01, E2.5/01, E3.6/02, 8B/01, K4E03/05).

    Journal: Journal of the South African Veterinary Association

    Article Title: Molecular characterisation of Mycoplasma species isolated from the genital tract of Dorper sheep in South Africa

    doi: 10.4102/jsava.v86i1.1199

    Figure Lengend Snippet: Purified plasmids. Note: Lane 1 is the DNA ladder (Fermentas 1Kb ‘O Gene ruler, Inqaba Biotechnology, Pretoria, SA); lane 2 is the vector without insert (pGEM-T, Promega, Anatech SA); lanes 3, 5, 6, 7, 9 and 10 represent recombinant colonies (contains the polymerase chain reaction products: K2E03/01, K5R09/01, B8971/01, E2.5/01, E3.6/02, 8B/01, K4E03/05); lanes 4 and 8 represent vectors without or with partial inserts (samples K2E03/02 and 787/B567/10). The number in bracket is the number assigned to the number selected amplification product of interest (sample k5RO9/1, B8971/01, E2.5/01, E3.6/02, 8B/01, K4E03/05).

    Article Snippet: Amplified products were analysed together with a DNA ladder (O'Gene rulerTM , Fermentas Life Sciences, Inqaba Biotechnical, Industries [Pty] Ltd, Pretoria, SA) on a 1.5% agarose gel (Celtic Molecular Diagnostics, SA).

    Techniques: Purification, Plasmid Preparation, Recombinant, Polymerase Chain Reaction, Amplification

    Electrophoretic analysis of unamplified DNA on a 1% agarose gel. Note: Lane 1 is the DNA ladder (Fermentas 1Kb ‘O Gene ruler, Inqaba Biotechnical, industries [Pty] Ltd, Pretoria, SA); lanes 2–8 represent unamplified DNA from samples D7 (14.27 ng/µL); E3.5/01 (202.88 ng/µL); KIR03/01 (329.08 ng/µL); B3/01 (282.74 ng/µL); B12291/09 (282.74 ng/µL); D1/01 (2.43 ng/µL); D5/01 (7.01 ng/µL); E3.7/01 (266.61 ng/µL); lanes 9–10 are extracted DNA from negative and positive controls, namely Escherichia coli strain S4 (09:K30) (17.08 ng/µL) and Mycoplasma reference strain (Y-goat 11706) (299.61 ng/1 µL).

    Journal: Journal of the South African Veterinary Association

    Article Title: Molecular characterisation of Mycoplasma species isolated from the genital tract of Dorper sheep in South Africa

    doi: 10.4102/jsava.v86i1.1199

    Figure Lengend Snippet: Electrophoretic analysis of unamplified DNA on a 1% agarose gel. Note: Lane 1 is the DNA ladder (Fermentas 1Kb ‘O Gene ruler, Inqaba Biotechnical, industries [Pty] Ltd, Pretoria, SA); lanes 2–8 represent unamplified DNA from samples D7 (14.27 ng/µL); E3.5/01 (202.88 ng/µL); KIR03/01 (329.08 ng/µL); B3/01 (282.74 ng/µL); B12291/09 (282.74 ng/µL); D1/01 (2.43 ng/µL); D5/01 (7.01 ng/µL); E3.7/01 (266.61 ng/µL); lanes 9–10 are extracted DNA from negative and positive controls, namely Escherichia coli strain S4 (09:K30) (17.08 ng/µL) and Mycoplasma reference strain (Y-goat 11706) (299.61 ng/1 µL).

    Article Snippet: Amplified products were analysed together with a DNA ladder (O'Gene rulerTM , Fermentas Life Sciences, Inqaba Biotechnical, Industries [Pty] Ltd, Pretoria, SA) on a 1.5% agarose gel (Celtic Molecular Diagnostics, SA).

    Techniques: Agarose Gel Electrophoresis

    Polymerase chain reaction amplification products (4 reactions per isolate) on a 1% agarose gel for downstream applications. Note: Lane 1 is the DNA ladder (fermentas 1Kb ‘O Gene ruler, Inqaba Biotechnical Industries [Pty] Ltd, Pretoria, SA); lanes 2–13 represent isolates (B8971/06; D1/01, C1/01, K5R09/01, D7/01, KIR03/01, K2E03/01, 8B/01, 787/B567/10, E3.6/02, E2.5/01, K5R01/01). Lane 14 is the negative control (water).

    Journal: Journal of the South African Veterinary Association

    Article Title: Molecular characterisation of Mycoplasma species isolated from the genital tract of Dorper sheep in South Africa

    doi: 10.4102/jsava.v86i1.1199

    Figure Lengend Snippet: Polymerase chain reaction amplification products (4 reactions per isolate) on a 1% agarose gel for downstream applications. Note: Lane 1 is the DNA ladder (fermentas 1Kb ‘O Gene ruler, Inqaba Biotechnical Industries [Pty] Ltd, Pretoria, SA); lanes 2–13 represent isolates (B8971/06; D1/01, C1/01, K5R09/01, D7/01, KIR03/01, K2E03/01, 8B/01, 787/B567/10, E3.6/02, E2.5/01, K5R01/01). Lane 14 is the negative control (water).

    Article Snippet: Amplified products were analysed together with a DNA ladder (O'Gene rulerTM , Fermentas Life Sciences, Inqaba Biotechnical, Industries [Pty] Ltd, Pretoria, SA) on a 1.5% agarose gel (Celtic Molecular Diagnostics, SA).

    Techniques: Polymerase Chain Reaction, Amplification, Agarose Gel Electrophoresis, Negative Control

    Polymerase chain reaction products generated with Croc primers on a 1% agarose gel. Note: Lane 1 is the DNA ladder (Fermentas 1 Kb ‘O Gene ruler, Inqaba Biotechnical, industries [Pty] Ltd, Pretoria, SA); lanes 2–8 represent isolates D7/01; E3.5/01; KIR03/01; B3/01; B12291/09; D1/01; D5/01; E3.7/01; lanes 9–10 represent the negative and positive controls respectively, namely Escherichia coli strain S4 (09:K30) (17.08 ng/µL) and Mycoplasma reference strain (Y-goat 11706).

    Journal: Journal of the South African Veterinary Association

    Article Title: Molecular characterisation of Mycoplasma species isolated from the genital tract of Dorper sheep in South Africa

    doi: 10.4102/jsava.v86i1.1199

    Figure Lengend Snippet: Polymerase chain reaction products generated with Croc primers on a 1% agarose gel. Note: Lane 1 is the DNA ladder (Fermentas 1 Kb ‘O Gene ruler, Inqaba Biotechnical, industries [Pty] Ltd, Pretoria, SA); lanes 2–8 represent isolates D7/01; E3.5/01; KIR03/01; B3/01; B12291/09; D1/01; D5/01; E3.7/01; lanes 9–10 represent the negative and positive controls respectively, namely Escherichia coli strain S4 (09:K30) (17.08 ng/µL) and Mycoplasma reference strain (Y-goat 11706).

    Article Snippet: Amplified products were analysed together with a DNA ladder (O'Gene rulerTM , Fermentas Life Sciences, Inqaba Biotechnical, Industries [Pty] Ltd, Pretoria, SA) on a 1.5% agarose gel (Celtic Molecular Diagnostics, SA).

    Techniques: Polymerase Chain Reaction, Generated, Agarose Gel Electrophoresis

    The homology region of the MAD1 promoter possesses open chromatin. ( A ) Upper panel: schematic representation of the positions of the primers used for the ChIP experiments relative to the homology region. Lower panel: chromatin immunoprecipitations were performed with antibodies specific for the indicated proteins on lysates of U937 cells treated with or without G-CSF (10 ng/ml) for 30 min. For control serial dilutions of the input were analyzed. ( B ) U937 cells were lyzed in F-buffer, nuclei prepared and digested with micrococcal nuclease (MNase) for the indicated times. DNA was then extracted and analyzed by agarose gel electrophoresis. The arrowheads identify mono-, di-, tri-, and tetra-nucleosomes. L: molecular size markers. ( C ) MNase or untreated DNA from exponentially growing U937 cells was used in PCR analysis with the indicated primer pairs. Untreated DNA was titrated (0,.25,.5, 1, and 4 ng) for the control PCR reactions and compared to 4 ng of Mnase-treated DNA. The agarose gels with the PCR products are shown in the top panel. The middle panel shows a quantification of the signal obtained from the MNase-treated DNA compared to the control signals. The bottom panel shows the position of the homology region relative to the analyzed promoter region. ( D) U937 cells were grown exponentially or treated for the indicated times with TPA or G-CSF as indicated. MNase or untreated DNA was amplified with primer pairs that span the homology region and neighboring genomic DNA.

    Journal: Nucleic Acids Research

    Article Title: Regulation of the MAD1 promoter by G-CSF

    doi: 10.1093/nar/gkn002

    Figure Lengend Snippet: The homology region of the MAD1 promoter possesses open chromatin. ( A ) Upper panel: schematic representation of the positions of the primers used for the ChIP experiments relative to the homology region. Lower panel: chromatin immunoprecipitations were performed with antibodies specific for the indicated proteins on lysates of U937 cells treated with or without G-CSF (10 ng/ml) for 30 min. For control serial dilutions of the input were analyzed. ( B ) U937 cells were lyzed in F-buffer, nuclei prepared and digested with micrococcal nuclease (MNase) for the indicated times. DNA was then extracted and analyzed by agarose gel electrophoresis. The arrowheads identify mono-, di-, tri-, and tetra-nucleosomes. L: molecular size markers. ( C ) MNase or untreated DNA from exponentially growing U937 cells was used in PCR analysis with the indicated primer pairs. Untreated DNA was titrated (0,.25,.5, 1, and 4 ng) for the control PCR reactions and compared to 4 ng of Mnase-treated DNA. The agarose gels with the PCR products are shown in the top panel. The middle panel shows a quantification of the signal obtained from the MNase-treated DNA compared to the control signals. The bottom panel shows the position of the homology region relative to the analyzed promoter region. ( D) U937 cells were grown exponentially or treated for the indicated times with TPA or G-CSF as indicated. MNase or untreated DNA was amplified with primer pairs that span the homology region and neighboring genomic DNA.

    Article Snippet: PCR products were separated on a 2% agarose gel using a 100 bp DNA ladder as a size marker (Fermentas).

    Techniques: Chromatin Immunoprecipitation, Agarose Gel Electrophoresis, Polymerase Chain Reaction, Amplification

    C/EBP proteins regulate the MAD1 promoter. ( A ) The –184 to + 248 MAD1 promoter reporter gene construct was cotransfected with plasmids expressing different C/EBP proteins. The mean values and standard deviations of three experiments performed in duplicates are shown. ( B ) U937 cells were stimulated for the indicated times with G-CSF. The cells were then crosslinked, lyzed and the indicated proteins immunoprecipitated. The associated DNA was analyzed by PCR using primers that correspond to the 3′ portion of the homology region or to a downstream fragment within the MAD1 gene body. For control serial dilutions of input DNA was analyzed by PCR. ( C ) Transient transfections were performed as described in (A). Reporter constructs with the indicated mutations were used as shown. ( D ) Transient transfections were performed as described (A) with –184 to –58-mintk promoter constructs and mutants thereof. ( E ) C/EBPβ, HA-STAT3 and G-CSFR were expressed in HEK293 cells. Prior to harvesting, the cells were treated with or without G-CSF as indicated. C/EBPβ was immunoprecipitated and the associated STAT3 detected by western blotting using an antibody specific for the HA-tag. The lysates show the expression controls. ( F ) The experimental approach was as in panel E. The relative STAT3 interaction with C/EBPβ upon stimulation with G-CSF and the indicated receptor mutants is displayed.

    Journal: Nucleic Acids Research

    Article Title: Regulation of the MAD1 promoter by G-CSF

    doi: 10.1093/nar/gkn002

    Figure Lengend Snippet: C/EBP proteins regulate the MAD1 promoter. ( A ) The –184 to + 248 MAD1 promoter reporter gene construct was cotransfected with plasmids expressing different C/EBP proteins. The mean values and standard deviations of three experiments performed in duplicates are shown. ( B ) U937 cells were stimulated for the indicated times with G-CSF. The cells were then crosslinked, lyzed and the indicated proteins immunoprecipitated. The associated DNA was analyzed by PCR using primers that correspond to the 3′ portion of the homology region or to a downstream fragment within the MAD1 gene body. For control serial dilutions of input DNA was analyzed by PCR. ( C ) Transient transfections were performed as described in (A). Reporter constructs with the indicated mutations were used as shown. ( D ) Transient transfections were performed as described (A) with –184 to –58-mintk promoter constructs and mutants thereof. ( E ) C/EBPβ, HA-STAT3 and G-CSFR were expressed in HEK293 cells. Prior to harvesting, the cells were treated with or without G-CSF as indicated. C/EBPβ was immunoprecipitated and the associated STAT3 detected by western blotting using an antibody specific for the HA-tag. The lysates show the expression controls. ( F ) The experimental approach was as in panel E. The relative STAT3 interaction with C/EBPβ upon stimulation with G-CSF and the indicated receptor mutants is displayed.

    Article Snippet: PCR products were separated on a 2% agarose gel using a 100 bp DNA ladder as a size marker (Fermentas).

    Techniques: Construct, Expressing, Immunoprecipitation, Polymerase Chain Reaction, Transfection, Western Blot

    PCR-RFLP pattern of Fasciola after digestion with Tsp509I restriction enzyme. Lane M: 100bp DNA ladder, Lanes 1 and 2: F. hepatica from sheep, Lane 3: F. gigantica from sheep, Lanes 4 and 6: F. hepatica from cattle, Lane 5: F. gigantica from cattle

    Journal: Iranian Journal of Parasitology

    Article Title: Molecular Identification and Differentiation of Fasciola Isolates Using PCR- RFLP Method Based on Internal Transcribed Spacer (ITS1, 5.8S rDNA, ITS2)

    doi:

    Figure Lengend Snippet: PCR-RFLP pattern of Fasciola after digestion with Tsp509I restriction enzyme. Lane M: 100bp DNA ladder, Lanes 1 and 2: F. hepatica from sheep, Lane 3: F. gigantica from sheep, Lanes 4 and 6: F. hepatica from cattle, Lane 5: F. gigantica from cattle

    Article Snippet: To estimate the size of the amplicons, a 100bp DNA ladder (Fermentas) was used in gels.

    Techniques: Polymerase Chain Reaction

    Detection of inoculated P solubilizing bacteria at 35 DAS. Viable count after 35 days to study the survival of Pseudomonas sp. MS16 ( A ) and Enterobacter sp. MS32 ( B ) on the roots of wheat plants. Yellow, circular and shiny colonies indicated by red arrows show the presence of Pseudomonas sp. MS16 while Off-white, circular, and shiny colonies indicated by yellow arrows show presence of Enterobacter sp. MS32 among total indigenous bacterial soil population. Amplification of colony of isolated bacteria by using BOX primer in PCR ( C ). BOX-PCR of re-isolated colonies obtained from rhizosphere of plants grown in pots inoculated with; (A) Pseudomonas sp. MS16; Lane 1: 1 Kb DNA Ladder, Lane 2: Re-isolated colony of Pseudomonas sp. MS16; Lane: 3-6 Colonies of other isolates obtained, Lane:7 Negative control, Lane 8: 100bp DNA Ladder. (B) Enterobacter sp. MS32; Lane 1: 1 Kb DNA Ladder, Lane 2: Re-isolated colony of Enterobacter sp. MS32, Lane: 3-6 Colonies of other isolates obtained, Lane:7 Negative control, Lane 8: 100bp DNA Ladder.

    Journal: PLoS ONE

    Article Title: Phosphate solubilizing bacteria with glucose dehydrogenase gene for phosphorus uptake and beneficial effects on wheat

    doi: 10.1371/journal.pone.0204408

    Figure Lengend Snippet: Detection of inoculated P solubilizing bacteria at 35 DAS. Viable count after 35 days to study the survival of Pseudomonas sp. MS16 ( A ) and Enterobacter sp. MS32 ( B ) on the roots of wheat plants. Yellow, circular and shiny colonies indicated by red arrows show the presence of Pseudomonas sp. MS16 while Off-white, circular, and shiny colonies indicated by yellow arrows show presence of Enterobacter sp. MS32 among total indigenous bacterial soil population. Amplification of colony of isolated bacteria by using BOX primer in PCR ( C ). BOX-PCR of re-isolated colonies obtained from rhizosphere of plants grown in pots inoculated with; (A) Pseudomonas sp. MS16; Lane 1: 1 Kb DNA Ladder, Lane 2: Re-isolated colony of Pseudomonas sp. MS16; Lane: 3-6 Colonies of other isolates obtained, Lane:7 Negative control, Lane 8: 100bp DNA Ladder. (B) Enterobacter sp. MS32; Lane 1: 1 Kb DNA Ladder, Lane 2: Re-isolated colony of Enterobacter sp. MS32, Lane: 3-6 Colonies of other isolates obtained, Lane:7 Negative control, Lane 8: 100bp DNA Ladder.

    Article Snippet: 1kb and 100bp DNA ladders (Fermentas, Germany) was used as a size markers.

    Techniques: Amplification, Isolation, Polymerase Chain Reaction, Negative Control

    RT-PCR analysis of plsX gene expression in the plsX polar allele duplication strain. The E. coli plsX polar allele duplication strain YZ143 and the wild-type strain UB1005 were grown to mid-log phase in RB, and total RNA was prepared as described in Materials and Methods. RT-PCRs were performed by using the Ambion RETROscript kit as directed. Lanes 2 through 5, RT-PCRs; lanes 7 through 10, PCRs with approximately 0.5 μg of total RNA as the template, but lacking RT. One microliter of RT reaction product, which corresponded to approximately 0.5 μg of total RNA, was used for each RT-PCR. The primer pairs used were 1 and 4 (lanes 2, 3, 7, and 8) or 1 and 3 (lanes 4, 5, 9, and 10). In lanes 2, 4, 7, and 9, RNA from strain UB1005 was analyzed. In lanes 3, 5, 8, and 10, RNA from strain YZ143 was analyzed. Lanes 1 and 11 are the 1-kb DNA ladder from BRL, and lane 6 was left vacant.

    Journal: Journal of Bacteriology

    Article Title: Transcriptional Analysis of Essential Genes of the Escherichia coli Fatty Acid Biosynthesis Gene Cluster by Functional Replacement with the Analogous Salmonella typhimurium Gene Cluster

    doi:

    Figure Lengend Snippet: RT-PCR analysis of plsX gene expression in the plsX polar allele duplication strain. The E. coli plsX polar allele duplication strain YZ143 and the wild-type strain UB1005 were grown to mid-log phase in RB, and total RNA was prepared as described in Materials and Methods. RT-PCRs were performed by using the Ambion RETROscript kit as directed. Lanes 2 through 5, RT-PCRs; lanes 7 through 10, PCRs with approximately 0.5 μg of total RNA as the template, but lacking RT. One microliter of RT reaction product, which corresponded to approximately 0.5 μg of total RNA, was used for each RT-PCR. The primer pairs used were 1 and 4 (lanes 2, 3, 7, and 8) or 1 and 3 (lanes 4, 5, 9, and 10). In lanes 2, 4, 7, and 9, RNA from strain UB1005 was analyzed. In lanes 3, 5, 8, and 10, RNA from strain YZ143 was analyzed. Lanes 1 and 11 are the 1-kb DNA ladder from BRL, and lane 6 was left vacant.

    Article Snippet: The concentrations of the competitive DNA fragments were then determined either by absorption at 260 nm or by comparing the fluorescence intensities with those of a DNA mass ladder (purchased from Gibco BRL) by densitometry of ethidium bromide-stained agarose gels.

    Techniques: Reverse Transcription Polymerase Chain Reaction, Expressing

    RhC genotyping: Lane 1 recessive homozygote (cc), lane 2 heterozygote (Cc), M – 50bp DNA ladder, lane 3 dominant homozygote (CC).

    Journal: Bosnian Journal of Basic Medical Sciences

    Article Title: Molecular – genetic variance of RH blood group system within human population of Bosnia and Herzegovina

    doi:

    Figure Lengend Snippet: RhC genotyping: Lane 1 recessive homozygote (cc), lane 2 heterozygote (Cc), M – 50bp DNA ladder, lane 3 dominant homozygote (CC).

    Article Snippet: For fragments sizing we used 50bp DNA Ladder (Fermentas, Maryland, USA).

    Techniques:

    Biosynthesis and activity of synthetic RM.TthHB27I. (A) Isolation of synthetic RM.TthHB27I from E . coli . Lane M1, PageRuler™ Unstained Broad Range Protein Ladder; lane M2, Pierce™ Unstained Protein Molecular Weight Marker; lane 1, native wt RM.TthHB27I; lane 2, crude lysate from E . coli [pET21d(+)-synthetic tthHB27IRM ], grown at 30°C; lane 3, supernatant after PEI treatment; lane 4, supernatant after incubation at 65°C; lane 5, 0–50% AmS fractionation cut; lane 6, DEAE-cellulose chromatography; lane 7, heparin-agarose chromatography; lane 8, Phosphocellulose P11 chromatography. (B) Yields of recombinant wt RM.TthHB27I and synthetic RM.TthHB27I biosynthesis. Recombinant E . coli BL21(DE3) strains were subjected to 3 h induction at OD 600 = 0.6–0.7 and 30°C. Cells were lysed and protein lysates were analysed by 7.5% SDS-PAGE. Lanes M1, M2 as in (A); lane 1, synthetic RM.TthHB27I; lane 2, crude lysate from induced E . coli [pET21d(+)-wt- tthHB27IRM ]; lane 3, crude lysate from induced E . coli [pET21d(+)-synthetic tthHB27IRM ]. (C) Comparison of the activities of RM.TthHB27I MTase variants in vivo . 0.5 μg of total DNA from T . thermophilus or induced, recombinant E . coli BL21(DE3) strains were digested with 2 units of synthetic RM.TthHB27I in REase buffer+SAM for 1 h at 65°C. Lane 1, untreated T . thermophilus DNA; lane 2, T . thermophilus DNA digested with synthetic RM.TthHB27I; lane 3, untreated E . coli BL21(DE3) [pET21d(+)-wt- tthHB27IRM ] DNA; lane 4, as in lane 3, but with synthetic RM.TthHB27I; lane 5, untreated E . coli BL21(DE3) [pET21d(+)-synthetic tthHB27IRM ] DNA; lane 6, as in lane 5, but with synthetic RM.TthHB27I; lane M, GeneRuler 1 kb DNA Ladder.

    Journal: PLoS ONE

    Article Title: Thermostable proteins bioprocesses: The activity of restriction endonuclease-methyltransferase from Thermus thermophilus (RM.TthHB27I) cloned in Escherichia coli is critically affected by the codon composition of the synthetic gene

    doi: 10.1371/journal.pone.0186633

    Figure Lengend Snippet: Biosynthesis and activity of synthetic RM.TthHB27I. (A) Isolation of synthetic RM.TthHB27I from E . coli . Lane M1, PageRuler™ Unstained Broad Range Protein Ladder; lane M2, Pierce™ Unstained Protein Molecular Weight Marker; lane 1, native wt RM.TthHB27I; lane 2, crude lysate from E . coli [pET21d(+)-synthetic tthHB27IRM ], grown at 30°C; lane 3, supernatant after PEI treatment; lane 4, supernatant after incubation at 65°C; lane 5, 0–50% AmS fractionation cut; lane 6, DEAE-cellulose chromatography; lane 7, heparin-agarose chromatography; lane 8, Phosphocellulose P11 chromatography. (B) Yields of recombinant wt RM.TthHB27I and synthetic RM.TthHB27I biosynthesis. Recombinant E . coli BL21(DE3) strains were subjected to 3 h induction at OD 600 = 0.6–0.7 and 30°C. Cells were lysed and protein lysates were analysed by 7.5% SDS-PAGE. Lanes M1, M2 as in (A); lane 1, synthetic RM.TthHB27I; lane 2, crude lysate from induced E . coli [pET21d(+)-wt- tthHB27IRM ]; lane 3, crude lysate from induced E . coli [pET21d(+)-synthetic tthHB27IRM ]. (C) Comparison of the activities of RM.TthHB27I MTase variants in vivo . 0.5 μg of total DNA from T . thermophilus or induced, recombinant E . coli BL21(DE3) strains were digested with 2 units of synthetic RM.TthHB27I in REase buffer+SAM for 1 h at 65°C. Lane 1, untreated T . thermophilus DNA; lane 2, T . thermophilus DNA digested with synthetic RM.TthHB27I; lane 3, untreated E . coli BL21(DE3) [pET21d(+)-wt- tthHB27IRM ] DNA; lane 4, as in lane 3, but with synthetic RM.TthHB27I; lane 5, untreated E . coli BL21(DE3) [pET21d(+)-synthetic tthHB27IRM ] DNA; lane 6, as in lane 5, but with synthetic RM.TthHB27I; lane M, GeneRuler 1 kb DNA Ladder.

    Article Snippet: DNA isolation kits (DNA Cleanup Micro Kit, GeneJet Plasmid Miniprep Kit and GeneJET Gel Extraction), DNA size markers (100 bp Plus DNA Ladder, GeneRuler 1 kb DNA Ladder), protein molecular weight standards (PageRuler™ Unstained Broad Range Protein Ladder and Pierce™ Unstained Protein Molecular Weight Marker) were from Thermo Fisher Scientific/Fermentas (Vilnius, Lithuania).

    Techniques: Activity Assay, Isolation, Molecular Weight, Marker, Incubation, Affinity Magnetic Separation, Fractionation, Chromatography, Recombinant, SDS Page, In Vivo

    Comparison of the enzymatic activities of native wt RM.TthHB27I and recombinant synthetic RM.TthHB27I thermozymes. Lanes M1, GeneRuler 1 kb DNA Ladder; lanes M2, 100 bp Plus DNA Ladder; lanes K, untreated PCR fragment. (A) Titration of native wt RM.TthHB27I MTase activity. 0.5 μg of 1789 bp PCR DNA substrate was incubated for 6 h with decreasing amounts of native wt RM.TthHB27I in the MTase reaction buffer supplemented with 100 μM SAM and 6 mM Ca 2+ at 65°C. Lanes 1–9, PCR fragment methylated with 2-fold serial dilutions of native wt RM.TthHB27I, starting from the thermozyme: recognition site molar ratio of 8: 1. (B) As in (A), but performed with synthetic RM.TthHB27I. (C) Titration of native wt RM.TthHB27I REase activity without cofactors/analogues. 0.5 μg of 1789 bp PCR DNA substrate was incubated for 1 h with decreasing amount of native wt RM.TthHB27I in REase buffer at 65°C. Lanes 1–10, PCR fragment digested with native wt RM.TthHB27I at the thermozyme: recognition site molar ratios shown above the lanes. (D) As in (C), except that performed with synthetic RM.TthHB27I. (E) Titration of native wt RM.TthHB27I REase activity in the presence of SAM. 0.5 μg of 1789 bp PCR DNA substrate was incubated for 1 h with decreasing amount of native wt RM.TthHB27I in REase buffer at 65°C. Lanes 1–10, PCR fragment digested with native wt RM.TthHB27I at the thermozyme: recognition site molar ratio shown above the lanes. (F) As in (E), except that performed with synthetic RM.TthHB27I.

    Journal: PLoS ONE

    Article Title: Thermostable proteins bioprocesses: The activity of restriction endonuclease-methyltransferase from Thermus thermophilus (RM.TthHB27I) cloned in Escherichia coli is critically affected by the codon composition of the synthetic gene

    doi: 10.1371/journal.pone.0186633

    Figure Lengend Snippet: Comparison of the enzymatic activities of native wt RM.TthHB27I and recombinant synthetic RM.TthHB27I thermozymes. Lanes M1, GeneRuler 1 kb DNA Ladder; lanes M2, 100 bp Plus DNA Ladder; lanes K, untreated PCR fragment. (A) Titration of native wt RM.TthHB27I MTase activity. 0.5 μg of 1789 bp PCR DNA substrate was incubated for 6 h with decreasing amounts of native wt RM.TthHB27I in the MTase reaction buffer supplemented with 100 μM SAM and 6 mM Ca 2+ at 65°C. Lanes 1–9, PCR fragment methylated with 2-fold serial dilutions of native wt RM.TthHB27I, starting from the thermozyme: recognition site molar ratio of 8: 1. (B) As in (A), but performed with synthetic RM.TthHB27I. (C) Titration of native wt RM.TthHB27I REase activity without cofactors/analogues. 0.5 μg of 1789 bp PCR DNA substrate was incubated for 1 h with decreasing amount of native wt RM.TthHB27I in REase buffer at 65°C. Lanes 1–10, PCR fragment digested with native wt RM.TthHB27I at the thermozyme: recognition site molar ratios shown above the lanes. (D) As in (C), except that performed with synthetic RM.TthHB27I. (E) Titration of native wt RM.TthHB27I REase activity in the presence of SAM. 0.5 μg of 1789 bp PCR DNA substrate was incubated for 1 h with decreasing amount of native wt RM.TthHB27I in REase buffer at 65°C. Lanes 1–10, PCR fragment digested with native wt RM.TthHB27I at the thermozyme: recognition site molar ratio shown above the lanes. (F) As in (E), except that performed with synthetic RM.TthHB27I.

    Article Snippet: DNA isolation kits (DNA Cleanup Micro Kit, GeneJet Plasmid Miniprep Kit and GeneJET Gel Extraction), DNA size markers (100 bp Plus DNA Ladder, GeneRuler 1 kb DNA Ladder), protein molecular weight standards (PageRuler™ Unstained Broad Range Protein Ladder and Pierce™ Unstained Protein Molecular Weight Marker) were from Thermo Fisher Scientific/Fermentas (Vilnius, Lithuania).

    Techniques: Recombinant, Polymerase Chain Reaction, Titration, Activity Assay, Incubation, Methylation

    Restriction pattern of some isolated Malassezia strains digested by BstC1 enzyme; Lane 1: M. pachydermatis (500bp, 70bp) lane 2: M. obtusa (580bp), lane 3: M. furfur (400bp, 180bp), lane 4: M. sympodialis (400bp, 180bp), and lane M: DNA ladder 50bp, the

    Journal: Journal of Clinical and Diagnostic Research : JCDR

    Article Title: Molecular and Phenotypic Identification and Speciation of Malassezia Yeasts Isolated from Egyptian Patients with Pityriasis Versicolor

    doi: 10.7860/JCDR/2017/27747.10416

    Figure Lengend Snippet: Restriction pattern of some isolated Malassezia strains digested by BstC1 enzyme; Lane 1: M. pachydermatis (500bp, 70bp) lane 2: M. obtusa (580bp), lane 3: M. furfur (400bp, 180bp), lane 4: M. sympodialis (400bp, 180bp), and lane M: DNA ladder 50bp, the

    Article Snippet: The expected size of the amplified PCR products were of 580 bp and visualized by1.5% (w/v) agarose gel electrophoresis in Tris Borate EDTA (TBE) buffer, stained with ethidium bromide (0.5 μg/mL), in comparison with DNA size marker (Thermo Scientific™ GeneRuler™ 50bp DNA Ladder, USA) and examined under UV trans-illumination.

    Techniques: Isolation

    26S rDNA PCR products of some isolated Malassezia strains (Lanes 1-4: M. furfur , M. sympodialis , M. obtusa , M. pachydermatis (580 bp) and lane M: DNA ladder 50bp, the bands were; 1000, 900, 800, 700, 600, 500, 400, 300, 250, 200, 150, 100, 50. It contains

    Journal: Journal of Clinical and Diagnostic Research : JCDR

    Article Title: Molecular and Phenotypic Identification and Speciation of Malassezia Yeasts Isolated from Egyptian Patients with Pityriasis Versicolor

    doi: 10.7860/JCDR/2017/27747.10416

    Figure Lengend Snippet: 26S rDNA PCR products of some isolated Malassezia strains (Lanes 1-4: M. furfur , M. sympodialis , M. obtusa , M. pachydermatis (580 bp) and lane M: DNA ladder 50bp, the bands were; 1000, 900, 800, 700, 600, 500, 400, 300, 250, 200, 150, 100, 50. It contains

    Article Snippet: The expected size of the amplified PCR products were of 580 bp and visualized by1.5% (w/v) agarose gel electrophoresis in Tris Borate EDTA (TBE) buffer, stained with ethidium bromide (0.5 μg/mL), in comparison with DNA size marker (Thermo Scientific™ GeneRuler™ 50bp DNA Ladder, USA) and examined under UV trans-illumination.

    Techniques: Polymerase Chain Reaction, Isolation

    Promoter methylation in cf DNA from serum. (A) Heatmap of promoter methylation detected in cf DNA extracted from serum samples for single genes and combinations of genes. White: no methylation detected; gray: methylation detected; red box: best minimal combination of markers (highest AUC ). (B) Copies per mL of hypermethylated ST 6 GALNAC 3 , ZNF 660 , CCDC 181 , and HAPLN 3 in serum samples from 10 patients with BPH and 27 patients with PC analyzed by droplet digital PCR . P ‐values for trend of methylation in BPH

    Journal: Molecular Oncology

    Article Title: Biomarker potential of ST6GALNAC3 and ZNF660 promoter hypermethylation in prostate cancer tissue and liquid biopsies

    doi: 10.1002/1878-0261.12183

    Figure Lengend Snippet: Promoter methylation in cf DNA from serum. (A) Heatmap of promoter methylation detected in cf DNA extracted from serum samples for single genes and combinations of genes. White: no methylation detected; gray: methylation detected; red box: best minimal combination of markers (highest AUC ). (B) Copies per mL of hypermethylated ST 6 GALNAC 3 , ZNF 660 , CCDC 181 , and HAPLN 3 in serum samples from 10 patients with BPH and 27 patients with PC analyzed by droplet digital PCR . P ‐values for trend of methylation in BPH

    Article Snippet: For all reactions, 3 pmol of each primer, 1 pmol probe, 5 ng bisulfite‐converted template DNA, and TaqMan® Universal PCR Master Mix No UNG (Applied Biosystems, Foster City, CA, USA) were used.

    Techniques: Methylation, Digital PCR