pyrophosphatase  (New England Biolabs)


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    Structured Review

    New England Biolabs pyrophosphatase
    Pyrophosphatase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pyrophosphatase/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pyrophosphatase - by Bioz Stars, 2022-05
    95/100 stars

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    New England Biolabs inorganic pyrophosphatase
    CtaI loads PHBA onto holo -CtaH. ( A ) MALDI-TOF spectral overlay of holo -CtaH loading reactions performed with PHBA and either CtaI or CtaD. The expected average masses of holo -CtaH and PHBA-S-CtaH are indicated. ( B ) HPLC absorbance profiles (250 nm) of reactions performed with NAC, PHBA, and CtaI. ( C ) Quantification of ATP hydrolysis products using a malachite green assay. Error bars represent the SD from the mean ( n = 3). PPase, inorganic <t>pyrophosphatase.</t> ( D ) HPLC profiles of CtaI reactions with NAC. Red strikethrough indicates heat-inactivated enzyme; red asterisk, NAC-specific peak.
    Inorganic Pyrophosphatase, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/inorganic pyrophosphatase/product/New England Biolabs
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    inorganic pyrophosphatase - by Bioz Stars, 2022-05
    95/100 stars
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    CtaI loads PHBA onto holo -CtaH. ( A ) MALDI-TOF spectral overlay of holo -CtaH loading reactions performed with PHBA and either CtaI or CtaD. The expected average masses of holo -CtaH and PHBA-S-CtaH are indicated. ( B ) HPLC absorbance profiles (250 nm) of reactions performed with NAC, PHBA, and CtaI. ( C ) Quantification of ATP hydrolysis products using a malachite green assay. Error bars represent the SD from the mean ( n = 3). PPase, inorganic pyrophosphatase. ( D ) HPLC profiles of CtaI reactions with NAC. Red strikethrough indicates heat-inactivated enzyme; red asterisk, NAC-specific peak.

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

    Article Title: Reconstitution of polythioamide antibiotic backbone formation reveals unusual thiotemplated assembly strategy

    doi: 10.1073/pnas.1918759117

    Figure Lengend Snippet: CtaI loads PHBA onto holo -CtaH. ( A ) MALDI-TOF spectral overlay of holo -CtaH loading reactions performed with PHBA and either CtaI or CtaD. The expected average masses of holo -CtaH and PHBA-S-CtaH are indicated. ( B ) HPLC absorbance profiles (250 nm) of reactions performed with NAC, PHBA, and CtaI. ( C ) Quantification of ATP hydrolysis products using a malachite green assay. Error bars represent the SD from the mean ( n = 3). PPase, inorganic pyrophosphatase. ( D ) HPLC profiles of CtaI reactions with NAC. Red strikethrough indicates heat-inactivated enzyme; red asterisk, NAC-specific peak.

    Article Snippet: Where indicated, 0.01 U of inorganic pyrophosphatase (New England BioLabs) was added to the reaction mixture.

    Techniques: High Performance Liquid Chromatography, Malachite Green Assay

    Overexpression of the Arabidopsis soluble pyrophosphatase PPa5 is sufficient to complement fugu5–1 (A) Comparison of 6-week old rosettes phenotypes of Col-0, fugu5–1 and overexpression lines of Arabidopsis vacuolar pyrophosphatase AVP1 and yeast soluble pyrophosphatase IPP1. (B) Representative images showing the localization of UBQ:PPa5-GFP to cytosol and nuclues in shoot (upper panel) and root cells (lower panel). Scale bars: 10μm. (C) Cotyledon phenotypes of 5 days old seedlings of Col-0, fugu5–1 and UBQ:PPa5-GFP in Col-0 and fugu5–1 backgrounds. (D) Comparison of 6-week old short day grown rosette phenotypes of Col-0, fugu5–1 and UBQ:PPa5-GFP in Col-0 and fugu5–1 backgrounds. (E) Measurements of fresh weight and whole rosette area of Col-0, fugu5–1 and UBQ:PPa5-GFP in Col-0 and fugu5–1 backgrounds. Plants were grown for 6 weeks under short-day conditions. To determine rosette area Rosette Tracker plug-in of ImageJ is used. Error bars represent SD of the mean of n=20 of 3 biological replicates. (F) Analysis of UBQ:PPa5-GFP protein amount in Col-0 and fugu5–1 background with anti-GFP. Soluble proteins from 6-week old rosettes grown under short-day conditions were extracted. An internal control provided by SPL detection kit (DyeAGNOSTICS) was used for normalization. One representative image from three biological replicates is depicted. (G) Soluble proteins of Col-0, fugu5–1 and UBQ:PPa5-GFP in Col-0 and fugu5–1 backgrounds were used to determine K + -stimulated PP i hydrolysis. Plants were grown for 6 weeks under short-day conditions. Error bars represent SD of n=3 biological replicates. Significant differences are indicated by different letters (Two-way ANOVA followed by Tukey’s test, p

    Journal: bioRxiv

    Article Title: Pyrophosphate modulates stress responses via SUMOylation

    doi: 10.1101/504373

    Figure Lengend Snippet: Overexpression of the Arabidopsis soluble pyrophosphatase PPa5 is sufficient to complement fugu5–1 (A) Comparison of 6-week old rosettes phenotypes of Col-0, fugu5–1 and overexpression lines of Arabidopsis vacuolar pyrophosphatase AVP1 and yeast soluble pyrophosphatase IPP1. (B) Representative images showing the localization of UBQ:PPa5-GFP to cytosol and nuclues in shoot (upper panel) and root cells (lower panel). Scale bars: 10μm. (C) Cotyledon phenotypes of 5 days old seedlings of Col-0, fugu5–1 and UBQ:PPa5-GFP in Col-0 and fugu5–1 backgrounds. (D) Comparison of 6-week old short day grown rosette phenotypes of Col-0, fugu5–1 and UBQ:PPa5-GFP in Col-0 and fugu5–1 backgrounds. (E) Measurements of fresh weight and whole rosette area of Col-0, fugu5–1 and UBQ:PPa5-GFP in Col-0 and fugu5–1 backgrounds. Plants were grown for 6 weeks under short-day conditions. To determine rosette area Rosette Tracker plug-in of ImageJ is used. Error bars represent SD of the mean of n=20 of 3 biological replicates. (F) Analysis of UBQ:PPa5-GFP protein amount in Col-0 and fugu5–1 background with anti-GFP. Soluble proteins from 6-week old rosettes grown under short-day conditions were extracted. An internal control provided by SPL detection kit (DyeAGNOSTICS) was used for normalization. One representative image from three biological replicates is depicted. (G) Soluble proteins of Col-0, fugu5–1 and UBQ:PPa5-GFP in Col-0 and fugu5–1 backgrounds were used to determine K + -stimulated PP i hydrolysis. Plants were grown for 6 weeks under short-day conditions. Error bars represent SD of n=3 biological replicates. Significant differences are indicated by different letters (Two-way ANOVA followed by Tukey’s test, p

    Article Snippet: To determine the effects of PPi hydrolysis on the FRET assay, 0.8U E. coli inorganic pyrophosphatase (NEB) was used and the buffer solution that the pyrophophatase includes was added to the control wells (20 mM Tris-HCl, 100 mM NaCl, 1 mM Dithiothreitol, 0.1 mM EDTA, 50% Glycerol, pH 8.0).

    Techniques: Over Expression

    Increased PPi levels interfere with SUMOylation in yeast (A) Amount of the soluble pyrophosphatase protein in a conditional Ipp1 mutant of S. cerevisiae (GAL:HA-IPP1). Wt strain (W303) is used as a control. (B) Amount of total sumoylation in W303 determined before and after heat stress. (C) Measurement of total SUMO protein in conditional IPP1 mutant of S. cerevisiae (GAL:HA-IPP1). (A-C) Yeast is grown in synthetic complete medium supplemented with galactose at 28°C. After growing until OD 600 0.5, part of the Ipp1 conditional mutant is switched to glucose supplemented medium to suppress the promoter and samples are collected at the indicated time points. For the heat treatment, cultures are switched to 40°C incubator for 1 hour. Error bars represent SD of n≥2 biological replicates.

    Journal: bioRxiv

    Article Title: Pyrophosphate modulates stress responses via SUMOylation

    doi: 10.1101/504373

    Figure Lengend Snippet: Increased PPi levels interfere with SUMOylation in yeast (A) Amount of the soluble pyrophosphatase protein in a conditional Ipp1 mutant of S. cerevisiae (GAL:HA-IPP1). Wt strain (W303) is used as a control. (B) Amount of total sumoylation in W303 determined before and after heat stress. (C) Measurement of total SUMO protein in conditional IPP1 mutant of S. cerevisiae (GAL:HA-IPP1). (A-C) Yeast is grown in synthetic complete medium supplemented with galactose at 28°C. After growing until OD 600 0.5, part of the Ipp1 conditional mutant is switched to glucose supplemented medium to suppress the promoter and samples are collected at the indicated time points. For the heat treatment, cultures are switched to 40°C incubator for 1 hour. Error bars represent SD of n≥2 biological replicates.

    Article Snippet: To determine the effects of PPi hydrolysis on the FRET assay, 0.8U E. coli inorganic pyrophosphatase (NEB) was used and the buffer solution that the pyrophophatase includes was added to the control wells (20 mM Tris-HCl, 100 mM NaCl, 1 mM Dithiothreitol, 0.1 mM EDTA, 50% Glycerol, pH 8.0).

    Techniques: Mutagenesis

    Overexpression of the Arabidopsis soluble pyrophosphatase PPa5 is sufficient to complement fugu5-1 . ( A ) Comparison of 6-week-old rosettes phenotypes of Col-0, fugu5-1 and overexpression lines of Arabidopsis vacuolar pyrophosphatase AVP1 and yeast soluble pyrophosphatase IPP1. ( B ) Representative images showing the localization of UBQ:PPa5-GFP to cytosol and nucleus in shoot (upper panel) and root cells (lower panel). Scale bars: 10 µm. ( C ) Cotyledon phenotypes of 5 days old seedlings of Col-0, fugu5-1 and UBQ:PPa5-GFP in Col-0 and fugu5-1 backgrounds. ( D ) Comparison of 6-week-old short day grown rosette phenotypes of Col-0, fugu5-1 and UBQ:PPa5-GFP in Col-0 and fugu5-1 backgrounds. ( E ) Measurements of fresh weight and whole rosette area of Col-0, fugu5-1 and UBQ:PPa5-GFP in Col-0 and fugu5-1 backgrounds. Plants were grown for 6 weeks under short-day conditions. To determine rosette area Rosette Tracker plug-in of ImageJ is used. Error bars represent SD of the mean of n = 20 of 3 biological replicates. ( F ) Analysis of UBQ:PPa5-GFP protein amount in Col-0 and fugu5-1 background with anti-GFP. Soluble proteins from 6-week-old rosettes grown under short-day conditions were extracted. An internal control provided by SPL detection kit (DyeAGNOSTICS) was used for normalization. One representative image from three biological replicates is depicted. ( G ) Soluble proteins of Col-0, fugu5-1 and UBQ:PPa5-GFP in Col-0 and fugu5-1 backgrounds were used to determine K + -stimulated PP i hydrolysis. Plants were grown for 6 weeks under short-day conditions. Error bars represent SD of n = 3 biological replicates. Significant differences are indicated by different letters (Two-way ANOVA followed by Tukey’s test, p

    Journal: eLife

    Article Title: Pyrophosphate modulates plant stress responses via SUMOylation

    doi: 10.7554/eLife.44213

    Figure Lengend Snippet: Overexpression of the Arabidopsis soluble pyrophosphatase PPa5 is sufficient to complement fugu5-1 . ( A ) Comparison of 6-week-old rosettes phenotypes of Col-0, fugu5-1 and overexpression lines of Arabidopsis vacuolar pyrophosphatase AVP1 and yeast soluble pyrophosphatase IPP1. ( B ) Representative images showing the localization of UBQ:PPa5-GFP to cytosol and nucleus in shoot (upper panel) and root cells (lower panel). Scale bars: 10 µm. ( C ) Cotyledon phenotypes of 5 days old seedlings of Col-0, fugu5-1 and UBQ:PPa5-GFP in Col-0 and fugu5-1 backgrounds. ( D ) Comparison of 6-week-old short day grown rosette phenotypes of Col-0, fugu5-1 and UBQ:PPa5-GFP in Col-0 and fugu5-1 backgrounds. ( E ) Measurements of fresh weight and whole rosette area of Col-0, fugu5-1 and UBQ:PPa5-GFP in Col-0 and fugu5-1 backgrounds. Plants were grown for 6 weeks under short-day conditions. To determine rosette area Rosette Tracker plug-in of ImageJ is used. Error bars represent SD of the mean of n = 20 of 3 biological replicates. ( F ) Analysis of UBQ:PPa5-GFP protein amount in Col-0 and fugu5-1 background with anti-GFP. Soluble proteins from 6-week-old rosettes grown under short-day conditions were extracted. An internal control provided by SPL detection kit (DyeAGNOSTICS) was used for normalization. One representative image from three biological replicates is depicted. ( G ) Soluble proteins of Col-0, fugu5-1 and UBQ:PPa5-GFP in Col-0 and fugu5-1 backgrounds were used to determine K + -stimulated PP i hydrolysis. Plants were grown for 6 weeks under short-day conditions. Error bars represent SD of n = 3 biological replicates. Significant differences are indicated by different letters (Two-way ANOVA followed by Tukey’s test, p

    Article Snippet: To determine the effects of PPi hydrolysis on the FRET assay, 0.8U E. coli inorganic pyrophosphatase (NEB) was used and the buffer solution that the pyrophophatase includes was added to the control wells (20 mM Tris-HCl, 100 mM NaCl, 1 mM Dithiothreitol, 0.1 mM EDTA, 50% Glycerol, pH 8.0).

    Techniques: Over Expression

    Increased PPi levels interfere with SUMOylation in yeast. ( A ) Amount of the soluble pyrophosphatase protein in a conditional Ipp1 mutant of S. cerevisiae (GAL:HA-IPP1). Asterisk indicates significant difference compared to GAL:HA-IPP1 in galactose time point 0 hr (Student’s t test; ***p

    Journal: eLife

    Article Title: Pyrophosphate modulates plant stress responses via SUMOylation

    doi: 10.7554/eLife.44213

    Figure Lengend Snippet: Increased PPi levels interfere with SUMOylation in yeast. ( A ) Amount of the soluble pyrophosphatase protein in a conditional Ipp1 mutant of S. cerevisiae (GAL:HA-IPP1). Asterisk indicates significant difference compared to GAL:HA-IPP1 in galactose time point 0 hr (Student’s t test; ***p

    Article Snippet: To determine the effects of PPi hydrolysis on the FRET assay, 0.8U E. coli inorganic pyrophosphatase (NEB) was used and the buffer solution that the pyrophophatase includes was added to the control wells (20 mM Tris-HCl, 100 mM NaCl, 1 mM Dithiothreitol, 0.1 mM EDTA, 50% Glycerol, pH 8.0).

    Techniques: Mutagenesis

    MicroRNA synthesized by rolling circle transcription (RCT) site-specific disconnection (SSD) with various concentrations of circular cDNA template . ( a ) Time course of RCT in the absence of inorganic pyrophosphatase (IPP). ( b ) Effect of IPP on the amount of RNA products. Lane L, 25 nt RNA marker; Lane S, standard sample of chemically synthesized mir-16 (1 μl, 100 μmol/l). In ( b ), RCT was processed for 4 hours, with 0.1 μmol/l Aid-DNA-16-1 and 1.0 U/ml IPP.

    Journal: Molecular Therapy. Nucleic Acids

    Article Title: Preparation of Small RNAs Using Rolling Circle Transcription and Site-Specific RNA Disconnection

    doi: 10.1038/mtna.2014.66

    Figure Lengend Snippet: MicroRNA synthesized by rolling circle transcription (RCT) site-specific disconnection (SSD) with various concentrations of circular cDNA template . ( a ) Time course of RCT in the absence of inorganic pyrophosphatase (IPP). ( b ) Effect of IPP on the amount of RNA products. Lane L, 25 nt RNA marker; Lane S, standard sample of chemically synthesized mir-16 (1 μl, 100 μmol/l). In ( b ), RCT was processed for 4 hours, with 0.1 μmol/l Aid-DNA-16-1 and 1.0 U/ml IPP.

    Article Snippet: Inorganic pyrophosphatase (0.02 U) purchased from New England Biolabs, was applied to selected RCT reactions.

    Techniques: Synthesized, Marker