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Avantor polyethyleneimine plate
Polyethyleneimine Plate, supplied by Avantor, used in various techniques. Bioz Stars score: 85/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Incubation:

Article Title: Synergistic Action of the Saccharomyces cerevisiae Homologous Recombination Factors Rad54 and Rad51 in Chromatin Remodeling
Article Snippet: Briefly, Rad54 or rad54 Δ129 (30 nM in and 20 nM in ) and Rad51 or mutants (300 nM or as indicated) were incubated on ice for 20 min in 24.5 μl of buffer A (30 mM Tris-HCl, pH 7.4, 5 mM MgCl2 , 1 mM DTT, and 100 μg/ml BSA) with 1.5 mM [γ-32 P] ATP. .. At the indicated times, a 1.8 μl of the reaction was mixed with 2 μl of 0.5 M EDTA before being analyzed by thin layer chromatography in a polyethyleneimine plate (J. T. Baker), as described previously [ ].

Thin Layer Chromatography:

Article Title: Synergistic Action of the Saccharomyces cerevisiae Homologous Recombination Factors Rad54 and Rad51 in Chromatin Remodeling
Article Snippet: .. At the indicated times, a 1.8 μl of the reaction was mixed with 2 μl of 0.5 M EDTA before being analyzed by thin layer chromatography in a polyethyleneimine plate (J. T. Baker), as described previously [ ]. .. The level of ATP hydrolysis was determined by phosphorimaging analysis of the chromatography plate.

ATPase Assay:

Article Title: Synergistic Action of the Saccharomyces cerevisiae Homologous Recombination Factors Rad54 and Rad51 in Chromatin Remodeling
Article Snippet: Paragraph title: 2.7. ATPase assay ... At the indicated times, a 1.8 μl of the reaction was mixed with 2 μl of 0.5 M EDTA before being analyzed by thin layer chromatography in a polyethyleneimine plate (J. T. Baker), as described previously [ ].

Chromatography:

Article Title: Synergistic Action of the Saccharomyces cerevisiae Homologous Recombination Factors Rad54 and Rad51 in Chromatin Remodeling
Article Snippet: At the indicated times, a 1.8 μl of the reaction was mixed with 2 μl of 0.5 M EDTA before being analyzed by thin layer chromatography in a polyethyleneimine plate (J. T. Baker), as described previously [ ]. .. The level of ATP hydrolysis was determined by phosphorimaging analysis of the chromatography plate.

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  • 86
    Avantor polyethyleneimine cellulose tlc plate
    Mutagenesis of m1A in E . coli . The base composition at the lesion site for m1A processed in the designated cell strains was obtained by the REAP assay. This <t>polyethyleneimine</t> <t>TLC</t> plate reveals that m1A is weakly mutagenic. The assay reproducibly detected subtle differences in mutagenicity, such as the suppression of A to T mutations by AlkB (center lanes), and the enhancement of such mutations by SOS polymerases (right lanes).
    Polyethyleneimine Cellulose Tlc Plate, supplied by Avantor, 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/polyethyleneimine cellulose tlc plate/product/Avantor
    Average 86 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    polyethyleneimine cellulose tlc plate - by Bioz Stars, 2020-04
    86/100 stars
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    87
    Avantor pei cellulose plates
    Ras activation. ( a ) Activation of endogenous Ras in MGSA/GRO-expressing clones: <t>GTP-bound</t> Ras was affinity-precipitated from 400 μ g of whole cell extract of V 1 , γ 3 -14 or Mel-a-6 using a GST-c-Raf-1/Ras binding domain (RBD) fusion protein. Ras proteins were detected with a pan-Ras antibody. Lane 1 is a negative control of GST alone to precipitate Ras proteins from extract of Mel-a-6 cells. The amount of Bcl 2 protein is shown in the lower panel for control of total proteins in extracts from different clones. The bar graph represents the mean of fold-induction (±s.e.m.) of the band density of activated Ras quantitated by a densitometer from three independent experiments. ( b ) Activation of endogenous Ras in parental melan-a cells treated with MGSA/GRO α : GTP-bound Ras was affinity-precipitated from 400 μ g of whole cell extract of parental melan-a cells treated with MGSA/GRO α for the indicated times using the GST-c-Raf-1 RBD fusion protein. Ras protein bands were detected with a pan-Ras antibody. The expression of Bcl2 protein is shown in the lower panel to control for protein content in extracts. ( c ) Ras-GTP/GDP-binding and GTPase activity in MGSA/GRO-expressing clones: Left-panel: Ras proteins were immunoprecipitated from 400 μ g of whole cell extract of V 1 , γ 3 -14 or Mel-a-6 with 2 μ g of anti-pan-ras antibody (AB-3). Ras immune complexes were incubated with 1 μ l of [ α - 32 P]GTP (3000 Ci/mmol, Amersham) in 100 μ l GTP/GDP-binding buffer and processed as described in Materials and methods. The results are reported as a mean of fold-induction (±s.e.m.) from three independent experiments. The fold induction was calculated as the radioactivity (c.p.m.) of 32 P-labeled nucleotides from γ 3 -14 or Mel-a-6 divided by the radioactivity of 32 P-labeled nucleotides from V 1 . Right-panel: The released 32 P-labeled GTP and GDP were loaded on <t>PEI-cellulose</t> plates, resolved by 0.75 M KH 2 PO 4 and then visualized by autoradiography. ( d ) Ras-GTP/GDP-binding and GTPase activity in ELR-mutant clones: GTP/GDP-binding and GTPase activity assays were performed using 400 μ g of whole cell extract of V 1 , Mel-a-6, E6A/ELR, L7A/ELR and R8A/ELR as described above
    Pei Cellulose Plates, supplied by Avantor, used in various techniques. Bioz Stars score: 87/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pei cellulose plates/product/Avantor
    Average 87 stars, based on 5 article reviews
    Price from $9.99 to $1999.99
    pei cellulose plates - by Bioz Stars, 2020-04
    87/100 stars
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    85
    Avantor polyethyleneimine cellulose plate
    ATPase and helicase assays of recombinant TbPIF5. (A) Coomassie-stained SDS-PAGE gel and Western blot of purified recombinant TbPIF5. (B) Assay of TbPIF5 ATPase activity. The substrates and products were separated by <t>polyethyleneimine</t> thin layer chromatography; arrow shows origin. The [ 32 P]Pi standard in the left-hand lane was prepared from [γ- 32 P] ATP by boiling 5 min in 1 M HCl. (C) Assay of TbPIF5 helicase activity. Substrates and products were separated by 12% polyacrylamide gel electrophoresis. (D) Helicase activity was measured at various concentrations of Mg ++ -ATP. (E) Assay of polarity of TbPIF5 helicase activity. Helicase substrates are diagrammed in Panels C (strand lengths are not to scale) and E (strand lengths for oligonucleotides a, b and c are 21, 21 and 90 nucleotides). * indicates 5′ 32 P end label.
    Polyethyleneimine Cellulose Plate, supplied by Avantor, used in various techniques. Bioz Stars score: 85/100, based on 7 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/polyethyleneimine cellulose plate/product/Avantor
    Average 85 stars, based on 7 article reviews
    Price from $9.99 to $1999.99
    polyethyleneimine cellulose plate - by Bioz Stars, 2020-04
    85/100 stars
      Buy from Supplier

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    Mutagenesis of m1A in E . coli . The base composition at the lesion site for m1A processed in the designated cell strains was obtained by the REAP assay. This polyethyleneimine TLC plate reveals that m1A is weakly mutagenic. The assay reproducibly detected subtle differences in mutagenicity, such as the suppression of A to T mutations by AlkB (center lanes), and the enhancement of such mutations by SOS polymerases (right lanes).

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Mutagenesis, genotoxicity, and repair of 1-methyladenine, 3-alkylcytosines, 1-methylguanine, and 3-methylthymine in alkB Escherichia coli

    doi: 10.1073/pnas.0403489101

    Figure Lengend Snippet: Mutagenesis of m1A in E . coli . The base composition at the lesion site for m1A processed in the designated cell strains was obtained by the REAP assay. This polyethyleneimine TLC plate reveals that m1A is weakly mutagenic. The assay reproducibly detected subtle differences in mutagenicity, such as the suppression of A to T mutations by AlkB (center lanes), and the enhancement of such mutations by SOS polymerases (right lanes).

    Article Snippet: After the DNA was resuspended in 5 μl of 30 mM NaOAc (pH 5.3), 10 mM ZnCl2 , and 1 μg of nuclease P1 (Roche), and incubated at 50°C for 1 h, 0.5-μl samples were spotted 1 cm apart onto a 20 × 20 cm polyethyleneimine cellulose TLC plate (PEI-TLC, J. T. Baker) that had been prewashed in water for 2 min the previous night and air dried.

    Techniques: Mutagenesis, Thin Layer Chromatography

    Ras activation. ( a ) Activation of endogenous Ras in MGSA/GRO-expressing clones: GTP-bound Ras was affinity-precipitated from 400 μ g of whole cell extract of V 1 , γ 3 -14 or Mel-a-6 using a GST-c-Raf-1/Ras binding domain (RBD) fusion protein. Ras proteins were detected with a pan-Ras antibody. Lane 1 is a negative control of GST alone to precipitate Ras proteins from extract of Mel-a-6 cells. The amount of Bcl 2 protein is shown in the lower panel for control of total proteins in extracts from different clones. The bar graph represents the mean of fold-induction (±s.e.m.) of the band density of activated Ras quantitated by a densitometer from three independent experiments. ( b ) Activation of endogenous Ras in parental melan-a cells treated with MGSA/GRO α : GTP-bound Ras was affinity-precipitated from 400 μ g of whole cell extract of parental melan-a cells treated with MGSA/GRO α for the indicated times using the GST-c-Raf-1 RBD fusion protein. Ras protein bands were detected with a pan-Ras antibody. The expression of Bcl2 protein is shown in the lower panel to control for protein content in extracts. ( c ) Ras-GTP/GDP-binding and GTPase activity in MGSA/GRO-expressing clones: Left-panel: Ras proteins were immunoprecipitated from 400 μ g of whole cell extract of V 1 , γ 3 -14 or Mel-a-6 with 2 μ g of anti-pan-ras antibody (AB-3). Ras immune complexes were incubated with 1 μ l of [ α - 32 P]GTP (3000 Ci/mmol, Amersham) in 100 μ l GTP/GDP-binding buffer and processed as described in Materials and methods. The results are reported as a mean of fold-induction (±s.e.m.) from three independent experiments. The fold induction was calculated as the radioactivity (c.p.m.) of 32 P-labeled nucleotides from γ 3 -14 or Mel-a-6 divided by the radioactivity of 32 P-labeled nucleotides from V 1 . Right-panel: The released 32 P-labeled GTP and GDP were loaded on PEI-cellulose plates, resolved by 0.75 M KH 2 PO 4 and then visualized by autoradiography. ( d ) Ras-GTP/GDP-binding and GTPase activity in ELR-mutant clones: GTP/GDP-binding and GTPase activity assays were performed using 400 μ g of whole cell extract of V 1 , Mel-a-6, E6A/ELR, L7A/ELR and R8A/ELR as described above

    Journal: Oncogene

    Article Title: MGSA/GRO-mediated melanocyte transformation involves induction of Ras expression

    doi: 10.1038/sj.onc.1203820

    Figure Lengend Snippet: Ras activation. ( a ) Activation of endogenous Ras in MGSA/GRO-expressing clones: GTP-bound Ras was affinity-precipitated from 400 μ g of whole cell extract of V 1 , γ 3 -14 or Mel-a-6 using a GST-c-Raf-1/Ras binding domain (RBD) fusion protein. Ras proteins were detected with a pan-Ras antibody. Lane 1 is a negative control of GST alone to precipitate Ras proteins from extract of Mel-a-6 cells. The amount of Bcl 2 protein is shown in the lower panel for control of total proteins in extracts from different clones. The bar graph represents the mean of fold-induction (±s.e.m.) of the band density of activated Ras quantitated by a densitometer from three independent experiments. ( b ) Activation of endogenous Ras in parental melan-a cells treated with MGSA/GRO α : GTP-bound Ras was affinity-precipitated from 400 μ g of whole cell extract of parental melan-a cells treated with MGSA/GRO α for the indicated times using the GST-c-Raf-1 RBD fusion protein. Ras protein bands were detected with a pan-Ras antibody. The expression of Bcl2 protein is shown in the lower panel to control for protein content in extracts. ( c ) Ras-GTP/GDP-binding and GTPase activity in MGSA/GRO-expressing clones: Left-panel: Ras proteins were immunoprecipitated from 400 μ g of whole cell extract of V 1 , γ 3 -14 or Mel-a-6 with 2 μ g of anti-pan-ras antibody (AB-3). Ras immune complexes were incubated with 1 μ l of [ α - 32 P]GTP (3000 Ci/mmol, Amersham) in 100 μ l GTP/GDP-binding buffer and processed as described in Materials and methods. The results are reported as a mean of fold-induction (±s.e.m.) from three independent experiments. The fold induction was calculated as the radioactivity (c.p.m.) of 32 P-labeled nucleotides from γ 3 -14 or Mel-a-6 divided by the radioactivity of 32 P-labeled nucleotides from V 1 . Right-panel: The released 32 P-labeled GTP and GDP were loaded on PEI-cellulose plates, resolved by 0.75 M KH 2 PO 4 and then visualized by autoradiography. ( d ) Ras-GTP/GDP-binding and GTPase activity in ELR-mutant clones: GTP/GDP-binding and GTPase activity assays were performed using 400 μ g of whole cell extract of V 1 , Mel-a-6, E6A/ELR, L7A/ELR and R8A/ELR as described above

    Article Snippet: The released 32 P-labeled nucleotides were counted directly by Cerenkov scintillation counting (Beckman LS 3801), and then GTP and GDP were loaded on PEI-cellulose plates (JT Baker Inc., Phillipsburg, NJ, USA), resolved by 0.75 M KH2 PO4 and then visualized by autoradiography.

    Techniques: Activation Assay, Expressing, Clone Assay, Binding Assay, Negative Control, Activity Assay, Immunoprecipitation, Incubation, Radioactivity, Labeling, Autoradiography, Mutagenesis

    Fig. 5. hNURF exhibits intrinsic nucleosome-dependent ATPase activity. ( A ) hNURF exhibits DNA- and nucleosome-stimulated ATPase activity. ATPase activity assays performed on [γ- 32 P]ATP followed by separation of free phosphate (Pi) from ATP by PEI-cellulose TLC and autoradiography of TLC plates. hNURF activity is stimulated by supplementing the reaction with DNA (50 ng) and is potentiated further by nucleosomes (50 ng); compare lanes 4, 5 and 6. ( B ) hNURF activity responds to increasing amounts of nucleosomes. A 25 fmol concentration of hNURF or buffer was incubated with increasing amounts (0, 50, 100 or 250 ng) of either free DNA or free nucleosomes. Points represent the average of three reactions, with standard error as indicated. ( C ) hNURF exhibits a dose-dependent ATPase activity in the presence of nucleosomes. ATPase activity of three different hNURF concentrations (20, 50 and 100 fmol) with buffer, free DNA or nucleosomal DNA. Points represent the average of three reactions, with standard error as indicated. ( D ) Time course of hNURF ATPase activity. hNURF (100 fmol) was incubated with buffer, free DNA or nucleosomal DNA, and reactions were assayed for ATPase activity at the indicted times. Points represent the average of three reactions, with standard error as indicated.

    Journal: The EMBO Journal

    Article Title: Isolation of human NURF: a regulator of Engrailed gene expression

    doi: 10.1093/emboj/cdg582

    Figure Lengend Snippet: Fig. 5. hNURF exhibits intrinsic nucleosome-dependent ATPase activity. ( A ) hNURF exhibits DNA- and nucleosome-stimulated ATPase activity. ATPase activity assays performed on [γ- 32 P]ATP followed by separation of free phosphate (Pi) from ATP by PEI-cellulose TLC and autoradiography of TLC plates. hNURF activity is stimulated by supplementing the reaction with DNA (50 ng) and is potentiated further by nucleosomes (50 ng); compare lanes 4, 5 and 6. ( B ) hNURF activity responds to increasing amounts of nucleosomes. A 25 fmol concentration of hNURF or buffer was incubated with increasing amounts (0, 50, 100 or 250 ng) of either free DNA or free nucleosomes. Points represent the average of three reactions, with standard error as indicated. ( C ) hNURF exhibits a dose-dependent ATPase activity in the presence of nucleosomes. ATPase activity of three different hNURF concentrations (20, 50 and 100 fmol) with buffer, free DNA or nucleosomal DNA. Points represent the average of three reactions, with standard error as indicated. ( D ) Time course of hNURF ATPase activity. hNURF (100 fmol) was incubated with buffer, free DNA or nucleosomal DNA, and reactions were assayed for ATPase activity at the indicted times. Points represent the average of three reactions, with standard error as indicated.

    Article Snippet: Reactions were performed at 30°C for 1 h. Free phosphate and ATP were separated by TLC on PEI-cellulose plates (J.T.Baker, USA).

    Techniques: Activity Assay, Thin Layer Chromatography, Autoradiography, Concentration Assay, Incubation

    ATPase and helicase assays of recombinant TbPIF5. (A) Coomassie-stained SDS-PAGE gel and Western blot of purified recombinant TbPIF5. (B) Assay of TbPIF5 ATPase activity. The substrates and products were separated by polyethyleneimine thin layer chromatography; arrow shows origin. The [ 32 P]Pi standard in the left-hand lane was prepared from [γ- 32 P] ATP by boiling 5 min in 1 M HCl. (C) Assay of TbPIF5 helicase activity. Substrates and products were separated by 12% polyacrylamide gel electrophoresis. (D) Helicase activity was measured at various concentrations of Mg ++ -ATP. (E) Assay of polarity of TbPIF5 helicase activity. Helicase substrates are diagrammed in Panels C (strand lengths are not to scale) and E (strand lengths for oligonucleotides a, b and c are 21, 21 and 90 nucleotides). * indicates 5′ 32 P end label.

    Journal: PLoS Pathogens

    Article Title: TbPIF5 Is a Trypanosoma brucei Mitochondrial DNA Helicase Involved in Processing of Minicircle Okazaki Fragments

    doi: 10.1371/journal.ppat.1000589

    Figure Lengend Snippet: ATPase and helicase assays of recombinant TbPIF5. (A) Coomassie-stained SDS-PAGE gel and Western blot of purified recombinant TbPIF5. (B) Assay of TbPIF5 ATPase activity. The substrates and products were separated by polyethyleneimine thin layer chromatography; arrow shows origin. The [ 32 P]Pi standard in the left-hand lane was prepared from [γ- 32 P] ATP by boiling 5 min in 1 M HCl. (C) Assay of TbPIF5 helicase activity. Substrates and products were separated by 12% polyacrylamide gel electrophoresis. (D) Helicase activity was measured at various concentrations of Mg ++ -ATP. (E) Assay of polarity of TbPIF5 helicase activity. Helicase substrates are diagrammed in Panels C (strand lengths are not to scale) and E (strand lengths for oligonucleotides a, b and c are 21, 21 and 90 nucleotides). * indicates 5′ 32 P end label.

    Article Snippet: Samples (1 µl) were spotted onto a polyethyleneimine-cellulose plate (J. T. Baker, USA) and developed in 1.0 M formic acid/0.5 M LiCl followed by autoradiography.

    Techniques: Recombinant, Staining, SDS Page, Western Blot, Purification, Activity Assay, Thin Layer Chromatography, Polyacrylamide Gel Electrophoresis