ctp Search Results


  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars

  • N/A
    This Ambion solution is a component of the MAXIscript Kits SKU s AM1312 AM1316 AM1314 AM1326 AM1324 AM1318 AM1322 AM1320 AM1310 and AM1308 and is supplied in one tube containing
      Buy from Supplier

    86
    GE Healthcare α 32 p ctp
    Detection of eIF4B in ribosomal initiation complexes with poliovirus IRES RNA. (A) Radioactivity profile of the gradients. [α- 32 <t>P]CTP-labeled</t> poliovirus IRES 1-745 RNA was incubated with RRL for 10 min at 30°C either in the absence of translation inhibitors (solid line), in the presence of 4 mM GMP-PNP (broken line), or in the presence of 0.17 mM anisomycin (dotted line). Samples were irradiated with UV, and initiation complexes were separated on a 10 to 35% sucrose gradient. Fractions were collected from the bottom (fraction 1), and aliquots were used for scintillation counting. The amount of radioactivity in each fraction relative to the total amount of radioactivity in the entire gradient (% cpm) is plotted versus the fraction number. The ribosomal 80S and 48S peaks are indicated. (B and C) Identification of ribosomal subunits in gradients run in parallel with the gradients in panel A. (B) Nucleic acids isolated from gradient fractions were heated, separated on an 1% agarose gel, and stained with ethidium bromide. The positions of 18S and 28S rRNAs from a preparation of ribosomal RNAs (R) are labeled on the left. (C) Immunoblot of gradient fractions with an antibody directed against ribosomal protein S6. (D) UV cross-linked proteins from the gradients shown in panel A. Fractions were treated with RNase A, and proteins were precipitated with TCA, resolved on SDS-polyacrylamide gels, and visualized by autoradiography. Molecular masses of marker proteins (M) are given in kilodaltons. The position of eIF4B is indicated by arrows on the right.
    α 32 P Ctp, supplied by GE Healthcare, 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/α 32 p ctp/product/GE Healthcare
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α 32 p ctp - by Bioz Stars, 2021-03
    86/100 stars
      Buy from Supplier

    86
    Agilent technologies cyanine 3 ctp
    Detection of eIF4B in ribosomal initiation complexes with poliovirus IRES RNA. (A) Radioactivity profile of the gradients. [α- 32 <t>P]CTP-labeled</t> poliovirus IRES 1-745 RNA was incubated with RRL for 10 min at 30°C either in the absence of translation inhibitors (solid line), in the presence of 4 mM GMP-PNP (broken line), or in the presence of 0.17 mM anisomycin (dotted line). Samples were irradiated with UV, and initiation complexes were separated on a 10 to 35% sucrose gradient. Fractions were collected from the bottom (fraction 1), and aliquots were used for scintillation counting. The amount of radioactivity in each fraction relative to the total amount of radioactivity in the entire gradient (% cpm) is plotted versus the fraction number. The ribosomal 80S and 48S peaks are indicated. (B and C) Identification of ribosomal subunits in gradients run in parallel with the gradients in panel A. (B) Nucleic acids isolated from gradient fractions were heated, separated on an 1% agarose gel, and stained with ethidium bromide. The positions of 18S and 28S rRNAs from a preparation of ribosomal RNAs (R) are labeled on the left. (C) Immunoblot of gradient fractions with an antibody directed against ribosomal protein S6. (D) UV cross-linked proteins from the gradients shown in panel A. Fractions were treated with RNase A, and proteins were precipitated with TCA, resolved on SDS-polyacrylamide gels, and visualized by autoradiography. Molecular masses of marker proteins (M) are given in kilodaltons. The position of eIF4B is indicated by arrows on the right.
    Cyanine 3 Ctp, supplied by Agilent technologies, 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/cyanine 3 ctp/product/Agilent technologies
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    cyanine 3 ctp - by Bioz Stars, 2021-03
    86/100 stars
      Buy from Supplier

    86
    PerkinElmer α 32 p ctp
    Effects of the flap-tip deletion on duplex-stabilized pausing and exit-channel duplex formation ( a ) Structural model of an E.coli RNAP EC showing the β flap region (light blue) and the location of two β flap-tip deletions highlighted in green (ΔFT1) or red (ΔFT2). The β flap-tip sequences of wild-type and the two flap-tip deletions are shown (red, acidic amino acids; blue, basic amino acids). ( b ) Schematic of pause duration experiment. ECs were reconstituted on an ePEC scaffold 2-nt before the pause site (G17 EC) and incubated with 2 µM [α- 32 <t>P]CTP</t> to extend to C18. UTP and GTP were then added to elongate through the his pause site (U19); pause half-lives of ePECs were measured (Online Methods). The plot shown depicts the effect of asRNA and NusA 23 for wild-type RNAP. ( c ) Effect of flap-tip deletions on asRNA-stabilized pausing with or without asRNA or full-length NusA (2.5 µM). Error bars, s.d. ( n = 3). ( d ) The observed rate of the duplex formation ( k obs ) for the scaffold alone ( Fig. 1a ) or for ePECs containing wild-type and ΔFT RNAPs. k obs values were determined with 5 µM or 15 µM asRNA in the absence or presence of full-length NusA (2.5 µM) or 4 µM NusA-NTD at 37 °C. Error bars, s.d. ( n = 3).
    α 32 P Ctp, 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/α 32 p ctp/product/PerkinElmer
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    α 32 p ctp - by Bioz Stars, 2021-03
    86/100 stars
      Buy from Supplier

    86
    Agilent technologies cy3 ctp
    Effects of the flap-tip deletion on duplex-stabilized pausing and exit-channel duplex formation ( a ) Structural model of an E.coli RNAP EC showing the β flap region (light blue) and the location of two β flap-tip deletions highlighted in green (ΔFT1) or red (ΔFT2). The β flap-tip sequences of wild-type and the two flap-tip deletions are shown (red, acidic amino acids; blue, basic amino acids). ( b ) Schematic of pause duration experiment. ECs were reconstituted on an ePEC scaffold 2-nt before the pause site (G17 EC) and incubated with 2 µM [α- 32 <t>P]CTP</t> to extend to C18. UTP and GTP were then added to elongate through the his pause site (U19); pause half-lives of ePECs were measured (Online Methods). The plot shown depicts the effect of asRNA and NusA 23 for wild-type RNAP. ( c ) Effect of flap-tip deletions on asRNA-stabilized pausing with or without asRNA or full-length NusA (2.5 µM). Error bars, s.d. ( n = 3). ( d ) The observed rate of the duplex formation ( k obs ) for the scaffold alone ( Fig. 1a ) or for ePECs containing wild-type and ΔFT RNAPs. k obs values were determined with 5 µM or 15 µM asRNA in the absence or presence of full-length NusA (2.5 µM) or 4 µM NusA-NTD at 37 °C. Error bars, s.d. ( n = 3).
    Cy3 Ctp, supplied by Agilent technologies, 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/cy3 ctp/product/Agilent technologies
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    cy3 ctp - by Bioz Stars, 2021-03
    86/100 stars
      Buy from Supplier



    Image Search Results


    Detection of eIF4B in ribosomal initiation complexes with poliovirus IRES RNA. (A) Radioactivity profile of the gradients. [α- 32 P]CTP-labeled poliovirus IRES 1-745 RNA was incubated with RRL for 10 min at 30°C either in the absence of translation inhibitors (solid line), in the presence of 4 mM GMP-PNP (broken line), or in the presence of 0.17 mM anisomycin (dotted line). Samples were irradiated with UV, and initiation complexes were separated on a 10 to 35% sucrose gradient. Fractions were collected from the bottom (fraction 1), and aliquots were used for scintillation counting. The amount of radioactivity in each fraction relative to the total amount of radioactivity in the entire gradient (% cpm) is plotted versus the fraction number. The ribosomal 80S and 48S peaks are indicated. (B and C) Identification of ribosomal subunits in gradients run in parallel with the gradients in panel A. (B) Nucleic acids isolated from gradient fractions were heated, separated on an 1% agarose gel, and stained with ethidium bromide. The positions of 18S and 28S rRNAs from a preparation of ribosomal RNAs (R) are labeled on the left. (C) Immunoblot of gradient fractions with an antibody directed against ribosomal protein S6. (D) UV cross-linked proteins from the gradients shown in panel A. Fractions were treated with RNase A, and proteins were precipitated with TCA, resolved on SDS-polyacrylamide gels, and visualized by autoradiography. Molecular masses of marker proteins (M) are given in kilodaltons. The position of eIF4B is indicated by arrows on the right.

    Journal: Journal of Virology

    Article Title: Interaction of Translation Initiation Factor eIF4B with the Poliovirus Internal Ribosome Entry Site

    doi:

    Figure Lengend Snippet: Detection of eIF4B in ribosomal initiation complexes with poliovirus IRES RNA. (A) Radioactivity profile of the gradients. [α- 32 P]CTP-labeled poliovirus IRES 1-745 RNA was incubated with RRL for 10 min at 30°C either in the absence of translation inhibitors (solid line), in the presence of 4 mM GMP-PNP (broken line), or in the presence of 0.17 mM anisomycin (dotted line). Samples were irradiated with UV, and initiation complexes were separated on a 10 to 35% sucrose gradient. Fractions were collected from the bottom (fraction 1), and aliquots were used for scintillation counting. The amount of radioactivity in each fraction relative to the total amount of radioactivity in the entire gradient (% cpm) is plotted versus the fraction number. The ribosomal 80S and 48S peaks are indicated. (B and C) Identification of ribosomal subunits in gradients run in parallel with the gradients in panel A. (B) Nucleic acids isolated from gradient fractions were heated, separated on an 1% agarose gel, and stained with ethidium bromide. The positions of 18S and 28S rRNAs from a preparation of ribosomal RNAs (R) are labeled on the left. (C) Immunoblot of gradient fractions with an antibody directed against ribosomal protein S6. (D) UV cross-linked proteins from the gradients shown in panel A. Fractions were treated with RNase A, and proteins were precipitated with TCA, resolved on SDS-polyacrylamide gels, and visualized by autoradiography. Molecular masses of marker proteins (M) are given in kilodaltons. The position of eIF4B is indicated by arrows on the right.

    Article Snippet: Labeled RNAs were synthesized as described previously ( ) by using SP6 RNA polymerase in the presence of 2.5 μM [α-32 P]CTP, -ATP, -GTP, or -UTP (400 Ci/mmol; Amersham) as indicated with 15 μM nonradioactive labeling nucleotide added.

    Techniques: Radioactivity, Labeling, Incubation, Irradiation, Isolation, Agarose Gel Electrophoresis, Staining, Autoradiography, Marker

    ). Enzymes used for linearization of the templates for in vitro transcription are indicated together with the positions of the last nucleotide of the poliovirus sequence present in the respective RNAs. (B) UV cross-linking assay using RRL and [α- 32 P]CTP-labeled poliovirus IRES RNAs. The nucleotide numbers of the poliovirus sequences are indicated on the top. RNA 1-745 contains the authentic poliovirus initiator AUG at nucleotides 743 to 745 plus 156 additional nucleotides of luciferase sequence at the 3

    Journal: Journal of Virology

    Article Title: Interaction of Translation Initiation Factor eIF4B with the Poliovirus Internal Ribosome Entry Site

    doi:

    Figure Lengend Snippet: ). Enzymes used for linearization of the templates for in vitro transcription are indicated together with the positions of the last nucleotide of the poliovirus sequence present in the respective RNAs. (B) UV cross-linking assay using RRL and [α- 32 P]CTP-labeled poliovirus IRES RNAs. The nucleotide numbers of the poliovirus sequences are indicated on the top. RNA 1-745 contains the authentic poliovirus initiator AUG at nucleotides 743 to 745 plus 156 additional nucleotides of luciferase sequence at the 3" end (up to the Bsi WI site). Molecular masses of marker proteins are indicated. (C) Competitions. [α- 32 P]CTP-labeled poliovirus IRES RNA 1-745 was used in all lanes. Unlabeled competitor RNAs are indicated on the top together with the molar concentrations used for competition. Molecular masses of marker proteins are indicated. 4B, eIF4B.

    Article Snippet: Labeled RNAs were synthesized as described previously ( ) by using SP6 RNA polymerase in the presence of 2.5 μM [α-32 P]CTP, -ATP, -GTP, or -UTP (400 Ci/mmol; Amersham) as indicated with 15 μM nonradioactive labeling nucleotide added.

    Techniques: In Vitro, Sequencing, Labeling, Luciferase, Marker

    eIF4B binds to the poliovirus IRES RNA. (A) Detection of eIF4B in RRL. UV cross-linking assays were performed with poliovirus IRES RNA labeled with either [α- 32 P]ATP, -CTP, -GTP or -UTP as indicated. Proteins were resolved on SDS-10% polyacrylamide gels and visualized by autoradiography. Molecular masses of marker proteins are indicated. (B) Immunoprecipitation of eIF4B. The binding reaction was performed with RRL and [α- 32 P]CTP-labeled IRES RNA. After the UV cross-linking reaction, eIF4B was immunoprecipitated (IP) with anti-eIF4B antiserum (α-4B) (lane 1). Preimmune serum was used as negative control (pre.) (lane 2). Ten percent of the proteins from the supernatants (sup.) (right panel) was concentrated by TCA-precipitation (lanes 3 and 4), resolved on SDS-10% polyacrylamide gels, and visualized by autoradiography. 4B, eIF4B. (C) No effect of La protein on eIF4B binding. Poliovirus IRES RNA was used in the UV cross-linking assay by using RRL either without (lane 1) or after adding increasing amounts of recombinant La protein (rec. La) as indicated (lanes 2 to 7). (D and E) Immunoblots with anti-La antibodies 4B6 (D) and 3B9 (E). The bands representing endogenous La (end. La) and added recombinant La (rec. La) are indicated.

    Journal: Journal of Virology

    Article Title: Interaction of Translation Initiation Factor eIF4B with the Poliovirus Internal Ribosome Entry Site

    doi:

    Figure Lengend Snippet: eIF4B binds to the poliovirus IRES RNA. (A) Detection of eIF4B in RRL. UV cross-linking assays were performed with poliovirus IRES RNA labeled with either [α- 32 P]ATP, -CTP, -GTP or -UTP as indicated. Proteins were resolved on SDS-10% polyacrylamide gels and visualized by autoradiography. Molecular masses of marker proteins are indicated. (B) Immunoprecipitation of eIF4B. The binding reaction was performed with RRL and [α- 32 P]CTP-labeled IRES RNA. After the UV cross-linking reaction, eIF4B was immunoprecipitated (IP) with anti-eIF4B antiserum (α-4B) (lane 1). Preimmune serum was used as negative control (pre.) (lane 2). Ten percent of the proteins from the supernatants (sup.) (right panel) was concentrated by TCA-precipitation (lanes 3 and 4), resolved on SDS-10% polyacrylamide gels, and visualized by autoradiography. 4B, eIF4B. (C) No effect of La protein on eIF4B binding. Poliovirus IRES RNA was used in the UV cross-linking assay by using RRL either without (lane 1) or after adding increasing amounts of recombinant La protein (rec. La) as indicated (lanes 2 to 7). (D and E) Immunoblots with anti-La antibodies 4B6 (D) and 3B9 (E). The bands representing endogenous La (end. La) and added recombinant La (rec. La) are indicated.

    Article Snippet: Labeled RNAs were synthesized as described previously ( ) by using SP6 RNA polymerase in the presence of 2.5 μM [α-32 P]CTP, -ATP, -GTP, or -UTP (400 Ci/mmol; Amersham) as indicated with 15 μM nonradioactive labeling nucleotide added.

    Techniques: Labeling, Autoradiography, Marker, Immunoprecipitation, Binding Assay, Negative Control, TCA Precipitation, Recombinant, Western Blot

    Effects of the flap-tip deletion on duplex-stabilized pausing and exit-channel duplex formation ( a ) Structural model of an E.coli RNAP EC showing the β flap region (light blue) and the location of two β flap-tip deletions highlighted in green (ΔFT1) or red (ΔFT2). The β flap-tip sequences of wild-type and the two flap-tip deletions are shown (red, acidic amino acids; blue, basic amino acids). ( b ) Schematic of pause duration experiment. ECs were reconstituted on an ePEC scaffold 2-nt before the pause site (G17 EC) and incubated with 2 µM [α- 32 P]CTP to extend to C18. UTP and GTP were then added to elongate through the his pause site (U19); pause half-lives of ePECs were measured (Online Methods). The plot shown depicts the effect of asRNA and NusA 23 for wild-type RNAP. ( c ) Effect of flap-tip deletions on asRNA-stabilized pausing with or without asRNA or full-length NusA (2.5 µM). Error bars, s.d. ( n = 3). ( d ) The observed rate of the duplex formation ( k obs ) for the scaffold alone ( Fig. 1a ) or for ePECs containing wild-type and ΔFT RNAPs. k obs values were determined with 5 µM or 15 µM asRNA in the absence or presence of full-length NusA (2.5 µM) or 4 µM NusA-NTD at 37 °C. Error bars, s.d. ( n = 3).

    Journal: Nature structural & molecular biology

    Article Title: RNA polymerase pausing and nascent RNA structure formation are linked through clamp domain movement

    doi: 10.1038/nsmb.2867

    Figure Lengend Snippet: Effects of the flap-tip deletion on duplex-stabilized pausing and exit-channel duplex formation ( a ) Structural model of an E.coli RNAP EC showing the β flap region (light blue) and the location of two β flap-tip deletions highlighted in green (ΔFT1) or red (ΔFT2). The β flap-tip sequences of wild-type and the two flap-tip deletions are shown (red, acidic amino acids; blue, basic amino acids). ( b ) Schematic of pause duration experiment. ECs were reconstituted on an ePEC scaffold 2-nt before the pause site (G17 EC) and incubated with 2 µM [α- 32 P]CTP to extend to C18. UTP and GTP were then added to elongate through the his pause site (U19); pause half-lives of ePECs were measured (Online Methods). The plot shown depicts the effect of asRNA and NusA 23 for wild-type RNAP. ( c ) Effect of flap-tip deletions on asRNA-stabilized pausing with or without asRNA or full-length NusA (2.5 µM). Error bars, s.d. ( n = 3). ( d ) The observed rate of the duplex formation ( k obs ) for the scaffold alone ( Fig. 1a ) or for ePECs containing wild-type and ΔFT RNAPs. k obs values were determined with 5 µM or 15 µM asRNA in the absence or presence of full-length NusA (2.5 µM) or 4 µM NusA-NTD at 37 °C. Error bars, s.d. ( n = 3).

    Article Snippet: [α-32 P]CTP was obtained from PerkinElmer Life Sciences; NTPs, from GE Healthcare (Piscataway, NJ); cystamine dihydrochloride (CSSC), from MP Biomedicals; DNA-modifying enzymes, from NEB or Agilent; and DNA purification reagents, from Promega.

    Techniques: Incubation