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PerkinElmer 800 ci mmol α
800 Ci Mmol α, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/800 ci mmol α/product/PerkinElmer
Average 86 stars, based on 1 article reviews
Price from $9.99 to $1999.99
800 ci mmol α - by Bioz Stars, 2020-04
86/100 stars

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Radioactivity:

Article Title: The RNA-binding protein Staufen1 is increased in DM1 skeletal muscle and promotes alternative pre-mRNA splicing
Article Snippet: .. 800 Ci/mmol α-[32 P]ATP (PerkinElmer) was used for radiolabeling RNA probes. .. Unincorporated nu cleotides were removed, and probes were purified by electrophoresis on 6% Tris-glycine-polyacrylamide gels.

In Vitro:

Article Title: The RNA-binding protein Staufen1 is increased in DM1 skeletal muscle and promotes alternative pre-mRNA splicing
Article Snippet: Gel shift RNA probes were transcribed from a linearized pcDNA3 vector containing the DMPK 3′UTR templates using an in vitro transcription kit (MAXIScript; Invitrogen) according to the manufacturer’s instructions. .. 800 Ci/mmol α-[32 P]ATP (PerkinElmer) was used for radiolabeling RNA probes.

Electrophoretic Mobility Shift Assay:

Article Title: The RNA-binding protein Staufen1 is increased in DM1 skeletal muscle and promotes alternative pre-mRNA splicing
Article Snippet: Paragraph title: Gel shift ... 800 Ci/mmol α-[32 P]ATP (PerkinElmer) was used for radiolabeling RNA probes.

Purification:

Article Title: The RNA-binding protein Staufen1 is increased in DM1 skeletal muscle and promotes alternative pre-mRNA splicing
Article Snippet: 800 Ci/mmol α-[32 P]ATP (PerkinElmer) was used for radiolabeling RNA probes. .. Unincorporated nu cleotides were removed, and probes were purified by electrophoresis on 6% Tris-glycine-polyacrylamide gels.

Electrophoresis:

Article Title: The RNA-binding protein Staufen1 is increased in DM1 skeletal muscle and promotes alternative pre-mRNA splicing
Article Snippet: 800 Ci/mmol α-[32 P]ATP (PerkinElmer) was used for radiolabeling RNA probes. .. Unincorporated nu cleotides were removed, and probes were purified by electrophoresis on 6% Tris-glycine-polyacrylamide gels.

Affinity Purification:

Article Title: The RNA-binding protein Staufen1 is increased in DM1 skeletal muscle and promotes alternative pre-mRNA splicing
Article Snippet: 800 Ci/mmol α-[32 P]ATP (PerkinElmer) was used for radiolabeling RNA probes. .. Bacterially expressed recombinant GST-hStaufen1 was affinity purified on a glutathione–Sepharose matrix (GE Healthcare) and quantified using a bicinchoninic acid kit.

Recombinant:

Article Title: The RNA-binding protein Staufen1 is increased in DM1 skeletal muscle and promotes alternative pre-mRNA splicing
Article Snippet: 800 Ci/mmol α-[32 P]ATP (PerkinElmer) was used for radiolabeling RNA probes. .. Bacterially expressed recombinant GST-hStaufen1 was affinity purified on a glutathione–Sepharose matrix (GE Healthcare) and quantified using a bicinchoninic acid kit.

Plasmid Preparation:

Article Title: The RNA-binding protein Staufen1 is increased in DM1 skeletal muscle and promotes alternative pre-mRNA splicing
Article Snippet: Gel shift RNA probes were transcribed from a linearized pcDNA3 vector containing the DMPK 3′UTR templates using an in vitro transcription kit (MAXIScript; Invitrogen) according to the manufacturer’s instructions. .. 800 Ci/mmol α-[32 P]ATP (PerkinElmer) was used for radiolabeling RNA probes.

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  • 96
    PerkinElmer α 32 p gtp
    Characterization of LdRab1 and its mutants. A , <t>GTP</t> binding of purified LdRab1:WT and its mutants was detected using an [α- 32 P]GTP overlay assay. LdRab5:WT and GST proteins were used as control. B , GTPase activity of LdRab1 and its mutants was determined as described under “Experimental Procedures.” C , to determine the levels of overexpression of LdRab1:WT and its mutants as GFP fusion proteins in Leishmania , cell lysates were analyzed by Western blotting using anti-GFP antibody. Untransfected Leishmania was used as control. D , to determine the levels of overexpression of LdRab1:WT and its mutants as GFP fusion proteins in Leishmania , cell lysates were analyzed by Western blotting using anti-LdRab1 antibody. Untransfected Leishmania was used as control. E , the same membrane was exposed for a longer duration to detect endogenous Rab1. F , to determine the localization of Rab1:WT and its mutants in Leishmania , cells were transfected with indicated constructs to overexpress the respective protein in Leishmania as GFP fusion protein. Cells were visualized in a LSM 510 Meta confocal microscope. Green , localization of the indicated LdRab1; blue , nucleus ( Nu ). Results are representative of three independent preparations.
    α 32 P Gtp, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 96/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/α 32 p gtp/product/PerkinElmer
    Average 96 stars, based on 37 article reviews
    Price from $9.99 to $1999.99
    α 32 p gtp - by Bioz Stars, 2020-04
    96/100 stars
      Buy from Supplier

    93
    PerkinElmer α 32 p ctp
    Small molecule inhibitors that contain fragments obtained by STD spectroscopy. (a) Chemical structures of five small molecules obtained by virtual filtration using the ZINC database 15 and high-throughput docking using AutoDock 16 (list of 16 compounds presented in Fig. S1 ). The two subsets are based on the scaffolds obtained by STD spectroscopy: 2H-chromene-3-carbothioamide and indole (emphasized in thick grey). ( b ) Inhibitory effect of small molecules on bacteriophage T7 primase. Primase-dependent DNA synthesis. The reaction contained 0.3 mM dATP, dGTP, dCTP and [α– 32 P] dTTP (0.1 μCi), 100 μM ATP and <t>CTP,</t> 10 nM gp5/trx, 200 nM monomeric concentration of gp4A, 10 nM M13 ssDNA and 350 μM of each of the compounds. The reaction mixture was incubated for 30 min at 37 °C and spotted on DE81 filter paper. The amount of radioactivity remaining on the filter paper was measured (inset presents experimental setup). The amounts of RNA–primed DNA syntheses were determined by measuring the incorporation of dTMP (see Methods). The error bars were derived from three independent experiments. ( c ) Template-directed pppAC ribonucleotide synthesis catalyzed by T7 DNA primase. Reaction conditions involve incubating the primase domain with an oligonucleotide containing a primase recognition sequence. In this assay (bottom left), the DNA template containing the primase recognition site 5′-GTCA 10 -3′ enables the synthesis of only diribonucleotides pppAC. The reaction also contained [α- 32 P] CTP, ATP, and increasing amounts of the tested compounds (1.1, 3.3 and 10 μM). After incubation, the radioactive products were analyzed by electrophoresis through a 25% polyacrylamide gel containing 3 M urea and visualized using autoradiography ( Fig. S2b presents results for all compounds). Bottom right: Quantification of gel bands representing the reaction products (5′-pppAC-3′).
    α 32 P Ctp, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 93/100, based on 23 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/α 32 p ctp/product/PerkinElmer
    Average 93 stars, based on 23 article reviews
    Price from $9.99 to $1999.99
    α 32 p ctp - by Bioz Stars, 2020-04
    93/100 stars
      Buy from Supplier

    95
    PerkinElmer α 32 p atp
    Nocturnin alters iNOS mRNA half-life. ( A ) Nocturnin-mediated deadenylation releases 5′AMP. Recombinant GST-NOC protein was incubated with an RNA substrate containing a 100 nt poly(A) tail labeled with [α- 32 P] <t>-ATP</t> at 37°C for 30 min. The radiolableled product of the reaction was determined by two-dimensional thin layer chromatography analysis as described in the Materials and Methods . The dotted line denotes the position of the cold 5′AMP marker. ( B–D ) The stability of the iNOS mRNA ( B ), but not TNFα ( C ) or β-catenin ( D ) is significantly reduced in the MEFs lacking Nocturnin. MEFs were treated with LPS for 3 hours before the experiment. At time 0, LPS was removed and replaced with media containing actinomycin D and cells were collected for RNA isolation at the times indicated. mRNA levels were determined by quantitative RT-PCR and normalized against Gapdh mRNA. In each case, the mRNA level at time 0 was set as 100% and data were plotted as mean (±SEM) of 4–6 independent MEF cell lines for each genotype.
    α 32 P Atp, supplied by PerkinElmer, used in various techniques. Bioz Stars score: 95/100, based on 31 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/α 32 p atp/product/PerkinElmer
    Average 95 stars, based on 31 article reviews
    Price from $9.99 to $1999.99
    α 32 p atp - by Bioz Stars, 2020-04
    95/100 stars
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    Image Search Results


    Characterization of LdRab1 and its mutants. A , GTP binding of purified LdRab1:WT and its mutants was detected using an [α- 32 P]GTP overlay assay. LdRab5:WT and GST proteins were used as control. B , GTPase activity of LdRab1 and its mutants was determined as described under “Experimental Procedures.” C , to determine the levels of overexpression of LdRab1:WT and its mutants as GFP fusion proteins in Leishmania , cell lysates were analyzed by Western blotting using anti-GFP antibody. Untransfected Leishmania was used as control. D , to determine the levels of overexpression of LdRab1:WT and its mutants as GFP fusion proteins in Leishmania , cell lysates were analyzed by Western blotting using anti-LdRab1 antibody. Untransfected Leishmania was used as control. E , the same membrane was exposed for a longer duration to detect endogenous Rab1. F , to determine the localization of Rab1:WT and its mutants in Leishmania , cells were transfected with indicated constructs to overexpress the respective protein in Leishmania as GFP fusion protein. Cells were visualized in a LSM 510 Meta confocal microscope. Green , localization of the indicated LdRab1; blue , nucleus ( Nu ). Results are representative of three independent preparations.

    Journal: The Journal of Biological Chemistry

    Article Title: Functional Characterization of Monomeric GTPase Rab1 in the Secretory Pathway of Leishmania

    doi: 10.1074/jbc.M115.670018

    Figure Lengend Snippet: Characterization of LdRab1 and its mutants. A , GTP binding of purified LdRab1:WT and its mutants was detected using an [α- 32 P]GTP overlay assay. LdRab5:WT and GST proteins were used as control. B , GTPase activity of LdRab1 and its mutants was determined as described under “Experimental Procedures.” C , to determine the levels of overexpression of LdRab1:WT and its mutants as GFP fusion proteins in Leishmania , cell lysates were analyzed by Western blotting using anti-GFP antibody. Untransfected Leishmania was used as control. D , to determine the levels of overexpression of LdRab1:WT and its mutants as GFP fusion proteins in Leishmania , cell lysates were analyzed by Western blotting using anti-LdRab1 antibody. Untransfected Leishmania was used as control. E , the same membrane was exposed for a longer duration to detect endogenous Rab1. F , to determine the localization of Rab1:WT and its mutants in Leishmania , cells were transfected with indicated constructs to overexpress the respective protein in Leishmania as GFP fusion protein. Cells were visualized in a LSM 510 Meta confocal microscope. Green , localization of the indicated LdRab1; blue , nucleus ( Nu ). Results are representative of three independent preparations.

    Article Snippet: [α-32 P]GTP (800 Ci/mmol) was procured from PerkinElmer Life Sciences.

    Techniques: Binding Assay, Purification, GTP Overlay Assay, Activity Assay, Over Expression, Western Blot, Transfection, Construct, Microscopy

    Characterization of LdSar1 and its mutants. A , GTP binding of purified LdSar1:WT and its mutants was detected using an [α- 32 P]GTP overlay assay. LdRab5:WT and GST proteins were used as control. B , GTPase activity of LdSar1 and its mutants was determined as described under “Experimental procedures.” C , to determine the localization of LdSar1 mutants in Leishmania , cells were transfected with the indicated construct to overexpress the respective protein in Leishmania as GFP fusion protein. Finally, cells were visualized under confocal microscope. Results are representative of three independent observations.

    Journal: The Journal of Biological Chemistry

    Article Title: GTPase Sar1 regulates the trafficking and secretion of the virulence factor gp63 in Leishmania

    doi: 10.1074/jbc.M117.784033

    Figure Lengend Snippet: Characterization of LdSar1 and its mutants. A , GTP binding of purified LdSar1:WT and its mutants was detected using an [α- 32 P]GTP overlay assay. LdRab5:WT and GST proteins were used as control. B , GTPase activity of LdSar1 and its mutants was determined as described under “Experimental procedures.” C , to determine the localization of LdSar1 mutants in Leishmania , cells were transfected with the indicated construct to overexpress the respective protein in Leishmania as GFP fusion protein. Finally, cells were visualized under confocal microscope. Results are representative of three independent observations.

    Article Snippet: [α-32 P]GTP (800 Ci/mmol) was procured from PerkinElmer Life Sciences.

    Techniques: Binding Assay, Purification, GTP Overlay Assay, Activity Assay, Transfection, Construct, Microscopy

    Small molecule inhibitors that contain fragments obtained by STD spectroscopy. (a) Chemical structures of five small molecules obtained by virtual filtration using the ZINC database 15 and high-throughput docking using AutoDock 16 (list of 16 compounds presented in Fig. S1 ). The two subsets are based on the scaffolds obtained by STD spectroscopy: 2H-chromene-3-carbothioamide and indole (emphasized in thick grey). ( b ) Inhibitory effect of small molecules on bacteriophage T7 primase. Primase-dependent DNA synthesis. The reaction contained 0.3 mM dATP, dGTP, dCTP and [α– 32 P] dTTP (0.1 μCi), 100 μM ATP and CTP, 10 nM gp5/trx, 200 nM monomeric concentration of gp4A, 10 nM M13 ssDNA and 350 μM of each of the compounds. The reaction mixture was incubated for 30 min at 37 °C and spotted on DE81 filter paper. The amount of radioactivity remaining on the filter paper was measured (inset presents experimental setup). The amounts of RNA–primed DNA syntheses were determined by measuring the incorporation of dTMP (see Methods). The error bars were derived from three independent experiments. ( c ) Template-directed pppAC ribonucleotide synthesis catalyzed by T7 DNA primase. Reaction conditions involve incubating the primase domain with an oligonucleotide containing a primase recognition sequence. In this assay (bottom left), the DNA template containing the primase recognition site 5′-GTCA 10 -3′ enables the synthesis of only diribonucleotides pppAC. The reaction also contained [α- 32 P] CTP, ATP, and increasing amounts of the tested compounds (1.1, 3.3 and 10 μM). After incubation, the radioactive products were analyzed by electrophoresis through a 25% polyacrylamide gel containing 3 M urea and visualized using autoradiography ( Fig. S2b presents results for all compounds). Bottom right: Quantification of gel bands representing the reaction products (5′-pppAC-3′).

    Journal: Scientific Reports

    Article Title: Identification of DNA primase inhibitors via a combined fragment-based and virtual screening

    doi: 10.1038/srep36322

    Figure Lengend Snippet: Small molecule inhibitors that contain fragments obtained by STD spectroscopy. (a) Chemical structures of five small molecules obtained by virtual filtration using the ZINC database 15 and high-throughput docking using AutoDock 16 (list of 16 compounds presented in Fig. S1 ). The two subsets are based on the scaffolds obtained by STD spectroscopy: 2H-chromene-3-carbothioamide and indole (emphasized in thick grey). ( b ) Inhibitory effect of small molecules on bacteriophage T7 primase. Primase-dependent DNA synthesis. The reaction contained 0.3 mM dATP, dGTP, dCTP and [α– 32 P] dTTP (0.1 μCi), 100 μM ATP and CTP, 10 nM gp5/trx, 200 nM monomeric concentration of gp4A, 10 nM M13 ssDNA and 350 μM of each of the compounds. The reaction mixture was incubated for 30 min at 37 °C and spotted on DE81 filter paper. The amount of radioactivity remaining on the filter paper was measured (inset presents experimental setup). The amounts of RNA–primed DNA syntheses were determined by measuring the incorporation of dTMP (see Methods). The error bars were derived from three independent experiments. ( c ) Template-directed pppAC ribonucleotide synthesis catalyzed by T7 DNA primase. Reaction conditions involve incubating the primase domain with an oligonucleotide containing a primase recognition sequence. In this assay (bottom left), the DNA template containing the primase recognition site 5′-GTCA 10 -3′ enables the synthesis of only diribonucleotides pppAC. The reaction also contained [α- 32 P] CTP, ATP, and increasing amounts of the tested compounds (1.1, 3.3 and 10 μM). After incubation, the radioactive products were analyzed by electrophoresis through a 25% polyacrylamide gel containing 3 M urea and visualized using autoradiography ( Fig. S2b presents results for all compounds). Bottom right: Quantification of gel bands representing the reaction products (5′-pppAC-3′).

    Article Snippet: [α–32 P]–CTP (800 Ci/mmol) was purchased from Perkin Elmer.

    Techniques: Spectroscopy, Filtration, High Throughput Screening Assay, DNA Synthesis, Concentration Assay, Incubation, Radioactivity, Derivative Assay, Sequencing, Electrophoresis, Autoradiography

    Nocturnin alters iNOS mRNA half-life. ( A ) Nocturnin-mediated deadenylation releases 5′AMP. Recombinant GST-NOC protein was incubated with an RNA substrate containing a 100 nt poly(A) tail labeled with [α- 32 P] -ATP at 37°C for 30 min. The radiolableled product of the reaction was determined by two-dimensional thin layer chromatography analysis as described in the Materials and Methods . The dotted line denotes the position of the cold 5′AMP marker. ( B–D ) The stability of the iNOS mRNA ( B ), but not TNFα ( C ) or β-catenin ( D ) is significantly reduced in the MEFs lacking Nocturnin. MEFs were treated with LPS for 3 hours before the experiment. At time 0, LPS was removed and replaced with media containing actinomycin D and cells were collected for RNA isolation at the times indicated. mRNA levels were determined by quantitative RT-PCR and normalized against Gapdh mRNA. In each case, the mRNA level at time 0 was set as 100% and data were plotted as mean (±SEM) of 4–6 independent MEF cell lines for each genotype.

    Journal: PLoS ONE

    Article Title: The Circadian Deadenylase Nocturnin Is Necessary for Stabilization of the iNOS mRNA in Mice

    doi: 10.1371/journal.pone.0026954

    Figure Lengend Snippet: Nocturnin alters iNOS mRNA half-life. ( A ) Nocturnin-mediated deadenylation releases 5′AMP. Recombinant GST-NOC protein was incubated with an RNA substrate containing a 100 nt poly(A) tail labeled with [α- 32 P] -ATP at 37°C for 30 min. The radiolableled product of the reaction was determined by two-dimensional thin layer chromatography analysis as described in the Materials and Methods . The dotted line denotes the position of the cold 5′AMP marker. ( B–D ) The stability of the iNOS mRNA ( B ), but not TNFα ( C ) or β-catenin ( D ) is significantly reduced in the MEFs lacking Nocturnin. MEFs were treated with LPS for 3 hours before the experiment. At time 0, LPS was removed and replaced with media containing actinomycin D and cells were collected for RNA isolation at the times indicated. mRNA levels were determined by quantitative RT-PCR and normalized against Gapdh mRNA. In each case, the mRNA level at time 0 was set as 100% and data were plotted as mean (±SEM) of 4–6 independent MEF cell lines for each genotype.

    Article Snippet: Radiolabeled RNA substrate was synthesized by transcribing BamHI linearized DNA constructs with SP6 polymerase (GIBCO-BRL) in the presence of [α-32 P]-ATP (800 Ci/mmol, Perkin Elmer) and 625 µM of a 5′ GpppG cap analog (Amersham Pharmacia Biotech).

    Techniques: Recombinant, Incubation, Labeling, Thin Layer Chromatography, Marker, Isolation, Quantitative RT-PCR