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lpp  (New England Biolabs)


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    Structured Review

    New England Biolabs lpp
    a) xAM images of UReKA1 and UReKA2 incubated with PKA at various timepoints at 634kPa (for maximal signal). b) Normalized nonlinear US signal of UReKA1 (blue) and UReKA2 (orange) over time (n=3). c) Normalized phosphorylated fraction of UReKA1 (blue) and UReKA2 (orange) over time (n=1). d) Nonlinear ultrasound images (left) and signal (right) of UReKA1 incubated with PKA and phosphorylated UReKA1 incubated with <t>LPP</t> with or without buoyancy purification. (n=2). e-f) Schematics of the proposed molecular mechanism of UReKA with reversible phosphorylation reaction for the phosphorylation as forward reaction (e) <t>and</t> <t>dephosphorylation</t> of GvpC as reverse reaction (f).
    Lpp, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 97/100, based on 2834 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lpp/product/New England Biolabs
    Average 97 stars, based on 2834 article reviews
    lpp - by Bioz Stars, 2026-05
    97/100 stars

    Images

    1) Product Images from "Ultrasonic Reporter of Kinase Activity"

    Article Title: Ultrasonic Reporter of Kinase Activity

    Journal: bioRxiv

    doi: 10.64898/2025.11.30.691048

    a) xAM images of UReKA1 and UReKA2 incubated with PKA at various timepoints at 634kPa (for maximal signal). b) Normalized nonlinear US signal of UReKA1 (blue) and UReKA2 (orange) over time (n=3). c) Normalized phosphorylated fraction of UReKA1 (blue) and UReKA2 (orange) over time (n=1). d) Nonlinear ultrasound images (left) and signal (right) of UReKA1 incubated with PKA and phosphorylated UReKA1 incubated with LPP with or without buoyancy purification. (n=2). e-f) Schematics of the proposed molecular mechanism of UReKA with reversible phosphorylation reaction for the phosphorylation as forward reaction (e) and dephosphorylation of GvpC as reverse reaction (f).
    Figure Legend Snippet: a) xAM images of UReKA1 and UReKA2 incubated with PKA at various timepoints at 634kPa (for maximal signal). b) Normalized nonlinear US signal of UReKA1 (blue) and UReKA2 (orange) over time (n=3). c) Normalized phosphorylated fraction of UReKA1 (blue) and UReKA2 (orange) over time (n=1). d) Nonlinear ultrasound images (left) and signal (right) of UReKA1 incubated with PKA and phosphorylated UReKA1 incubated with LPP with or without buoyancy purification. (n=2). e-f) Schematics of the proposed molecular mechanism of UReKA with reversible phosphorylation reaction for the phosphorylation as forward reaction (e) and dephosphorylation of GvpC as reverse reaction (f).

    Techniques Used: Incubation, Purification, Phospho-proteomics, De-Phosphorylation Assay



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    a) xAM images of UReKA1 and UReKA2 incubated with PKA at various timepoints at 634kPa (for maximal signal). b) Normalized nonlinear US signal of UReKA1 (blue) and UReKA2 (orange) over time (n=3). c) Normalized phosphorylated fraction of UReKA1 (blue) and UReKA2 (orange) over time (n=1). d) Nonlinear ultrasound images (left) and signal (right) of UReKA1 incubated with PKA and phosphorylated UReKA1 incubated with <t>LPP</t> with or without buoyancy purification. (n=2). e-f) Schematics of the proposed molecular mechanism of UReKA with reversible phosphorylation reaction for the phosphorylation as forward reaction (e) <t>and</t> <t>dephosphorylation</t> of GvpC as reverse reaction (f).
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    Image Search Results


    a) xAM images of UReKA1 and UReKA2 incubated with PKA at various timepoints at 634kPa (for maximal signal). b) Normalized nonlinear US signal of UReKA1 (blue) and UReKA2 (orange) over time (n=3). c) Normalized phosphorylated fraction of UReKA1 (blue) and UReKA2 (orange) over time (n=1). d) Nonlinear ultrasound images (left) and signal (right) of UReKA1 incubated with PKA and phosphorylated UReKA1 incubated with LPP with or without buoyancy purification. (n=2). e-f) Schematics of the proposed molecular mechanism of UReKA with reversible phosphorylation reaction for the phosphorylation as forward reaction (e) and dephosphorylation of GvpC as reverse reaction (f).

    Journal: bioRxiv

    Article Title: Ultrasonic Reporter of Kinase Activity

    doi: 10.64898/2025.11.30.691048

    Figure Lengend Snippet: a) xAM images of UReKA1 and UReKA2 incubated with PKA at various timepoints at 634kPa (for maximal signal). b) Normalized nonlinear US signal of UReKA1 (blue) and UReKA2 (orange) over time (n=3). c) Normalized phosphorylated fraction of UReKA1 (blue) and UReKA2 (orange) over time (n=1). d) Nonlinear ultrasound images (left) and signal (right) of UReKA1 incubated with PKA and phosphorylated UReKA1 incubated with LPP with or without buoyancy purification. (n=2). e-f) Schematics of the proposed molecular mechanism of UReKA with reversible phosphorylation reaction for the phosphorylation as forward reaction (e) and dephosphorylation of GvpC as reverse reaction (f).

    Article Snippet: For dephosphorylation assays, 10 units of LPP (P0753L; NEB) per μL of engineered GVs at OD500 = 10 were mixed with PMP Buffer (50 mM HEPES, 100 mM NaCl, 2 mM DTT, 0.01% Brij 35, pH 7.5) and 1 mM MnCl 2 , followed by incubation with slow rotation at 37°C for 10–12 hours.

    Techniques: Incubation, Purification, Phospho-proteomics, De-Phosphorylation Assay

    A) Schematic representation of HMW tau dephosphorylation by the Lambda Protein Phosphatase (LPP). B) Seeding activity assay using FRET reporter HEK cell; the integrated FRET intensity was quantified by flow cytometry. Data represents mean ± S.D. of three individual experiments performed in triplicate with HMW Tau isolated from the AD case 1971. Results were analyzed using the unpaired student t-test, ** for p < 0.005. C), D) Dot blot quantification of HMW tau, originating from the same case as panel B, treated or not with Lambda PP and probed with the anti-phospho tau AT8 or the total tau antibody D5D8N.

    Journal: bioRxiv

    Article Title: Rare bioactive tau oligomers from Alzheimer brain support both templated misfolding and fibril formation

    doi: 10.1101/2025.09.24.678227

    Figure Lengend Snippet: A) Schematic representation of HMW tau dephosphorylation by the Lambda Protein Phosphatase (LPP). B) Seeding activity assay using FRET reporter HEK cell; the integrated FRET intensity was quantified by flow cytometry. Data represents mean ± S.D. of three individual experiments performed in triplicate with HMW Tau isolated from the AD case 1971. Results were analyzed using the unpaired student t-test, ** for p < 0.005. C), D) Dot blot quantification of HMW tau, originating from the same case as panel B, treated or not with Lambda PP and probed with the anti-phospho tau AT8 or the total tau antibody D5D8N.

    Article Snippet: HMW tau was subjected to dephosphorylation using Lambda Protein Phosphatase (LPP) kit (New England Biolabs (NEB), #P0753S).

    Techniques: De-Phosphorylation Assay, Activity Assay, Flow Cytometry, Isolation, Dot Blot