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nvs compounds cycloheximide chx focus biomolecules  (Focus Biomolecules)

 
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    Focus Biomolecules nvs compounds cycloheximide chx focus biomolecules
    (A) Immunoblot showing the protein levels of GCN1 and eRF1 in HEKR4 PTC reporter cells treated with negative control (Ctrl) or GCN1-targeting siRNA (GCN1 KD) in combination with a 6-hour incubation of 2.5 μM NVS1.1 or DMSO as control treatment. Vinculin served as a loading control. (B) Representative immunoblot showing protein levels of eRF1 and GAPDH (loading control) of HEKR4 PTC reporter cells treated with 2.5 μM NVS1.1 for 6 hours in the absence or presence of the translation elongation inhibitor <t>cycloheximide</t> (CHX). (C) (Top) Polysome profile showing A 260 readout of lysate deriving from HEKR4 PTC reporter cells treated with 25 μM NVS1.1 for 30 min that was separated over a 15%-50% sucrose gradient and fractionated. (Bottom) The proteins in every odd-numbered fraction of the gradient were precipitated and analyzed by immunoblotting for the indicated proteins. The fractions 3 and 5 were diluted 1/15 and 1/3, respectively. (D). Heavy polysome fractions from (C) were pooled and the proteins were analyzed by label-free mass spectrometry. Detected diGly events on lysine residues indicative of ubiquitination were normalized to the corresponding protein abundance. The fold change of the diGly frequency (log 2 diGly (NVS1.1/DMSO)) is shown for the protein eRF1 and for ribosomal proteins that showed a statistically significant difference (pVal < 0.05) upon NVS1.1 treatment
    Nvs Compounds Cycloheximide Chx Focus Biomolecules, supplied by Focus Biomolecules, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nvs compounds cycloheximide chx focus biomolecules/product/Focus Biomolecules
    Average 90 stars, based on 1 article reviews
    nvs compounds cycloheximide chx focus biomolecules - by Bioz Stars, 2026-02
    90/100 stars

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    1) Product Images from "Drug-induced eRF1 degradation promotes readthrough and reveals a new branch of ribosome quality control"

    Article Title: Drug-induced eRF1 degradation promotes readthrough and reveals a new branch of ribosome quality control

    Journal: bioRxiv

    doi: 10.1101/2023.01.31.526456

    (A) Immunoblot showing the protein levels of GCN1 and eRF1 in HEKR4 PTC reporter cells treated with negative control (Ctrl) or GCN1-targeting siRNA (GCN1 KD) in combination with a 6-hour incubation of 2.5 μM NVS1.1 or DMSO as control treatment. Vinculin served as a loading control. (B) Representative immunoblot showing protein levels of eRF1 and GAPDH (loading control) of HEKR4 PTC reporter cells treated with 2.5 μM NVS1.1 for 6 hours in the absence or presence of the translation elongation inhibitor cycloheximide (CHX). (C) (Top) Polysome profile showing A 260 readout of lysate deriving from HEKR4 PTC reporter cells treated with 25 μM NVS1.1 for 30 min that was separated over a 15%-50% sucrose gradient and fractionated. (Bottom) The proteins in every odd-numbered fraction of the gradient were precipitated and analyzed by immunoblotting for the indicated proteins. The fractions 3 and 5 were diluted 1/15 and 1/3, respectively. (D). Heavy polysome fractions from (C) were pooled and the proteins were analyzed by label-free mass spectrometry. Detected diGly events on lysine residues indicative of ubiquitination were normalized to the corresponding protein abundance. The fold change of the diGly frequency (log 2 diGly (NVS1.1/DMSO)) is shown for the protein eRF1 and for ribosomal proteins that showed a statistically significant difference (pVal < 0.05) upon NVS1.1 treatment
    Figure Legend Snippet: (A) Immunoblot showing the protein levels of GCN1 and eRF1 in HEKR4 PTC reporter cells treated with negative control (Ctrl) or GCN1-targeting siRNA (GCN1 KD) in combination with a 6-hour incubation of 2.5 μM NVS1.1 or DMSO as control treatment. Vinculin served as a loading control. (B) Representative immunoblot showing protein levels of eRF1 and GAPDH (loading control) of HEKR4 PTC reporter cells treated with 2.5 μM NVS1.1 for 6 hours in the absence or presence of the translation elongation inhibitor cycloheximide (CHX). (C) (Top) Polysome profile showing A 260 readout of lysate deriving from HEKR4 PTC reporter cells treated with 25 μM NVS1.1 for 30 min that was separated over a 15%-50% sucrose gradient and fractionated. (Bottom) The proteins in every odd-numbered fraction of the gradient were precipitated and analyzed by immunoblotting for the indicated proteins. The fractions 3 and 5 were diluted 1/15 and 1/3, respectively. (D). Heavy polysome fractions from (C) were pooled and the proteins were analyzed by label-free mass spectrometry. Detected diGly events on lysine residues indicative of ubiquitination were normalized to the corresponding protein abundance. The fold change of the diGly frequency (log 2 diGly (NVS1.1/DMSO)) is shown for the protein eRF1 and for ribosomal proteins that showed a statistically significant difference (pVal < 0.05) upon NVS1.1 treatment

    Techniques Used: Western Blot, Negative Control, Incubation, Control, Mass Spectrometry, Ubiquitin Proteomics, Quantitative Proteomics



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    nvs compounds cycloheximide chx focus biomolecules  (Focus Biomolecules)
    90
    Focus Biomolecules nvs compounds cycloheximide chx focus biomolecules
    (A) Immunoblot showing the protein levels of GCN1 and eRF1 in HEKR4 PTC reporter cells treated with negative control (Ctrl) or GCN1-targeting siRNA (GCN1 KD) in combination with a 6-hour incubation of 2.5 μM NVS1.1 or DMSO as control treatment. Vinculin served as a loading control. (B) Representative immunoblot showing protein levels of eRF1 and GAPDH (loading control) of HEKR4 PTC reporter cells treated with 2.5 μM NVS1.1 for 6 hours in the absence or presence of the translation elongation inhibitor <t>cycloheximide</t> (CHX). (C) (Top) Polysome profile showing A 260 readout of lysate deriving from HEKR4 PTC reporter cells treated with 25 μM NVS1.1 for 30 min that was separated over a 15%-50% sucrose gradient and fractionated. (Bottom) The proteins in every odd-numbered fraction of the gradient were precipitated and analyzed by immunoblotting for the indicated proteins. The fractions 3 and 5 were diluted 1/15 and 1/3, respectively. (D). Heavy polysome fractions from (C) were pooled and the proteins were analyzed by label-free mass spectrometry. Detected diGly events on lysine residues indicative of ubiquitination were normalized to the corresponding protein abundance. The fold change of the diGly frequency (log 2 diGly (NVS1.1/DMSO)) is shown for the protein eRF1 and for ribosomal proteins that showed a statistically significant difference (pVal < 0.05) upon NVS1.1 treatment
    Nvs Compounds Cycloheximide Chx Focus Biomolecules, supplied by Focus Biomolecules, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/nvs compounds cycloheximide chx focus biomolecules/product/Focus Biomolecules
    Average 90 stars, based on 1 article reviews
    nvs compounds cycloheximide chx focus biomolecules - by Bioz Stars, 2026-02
    90/100 stars
    		  Buy from Supplier

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    (A) Immunoblot showing the protein levels of GCN1 and eRF1 in HEKR4 PTC reporter cells treated with negative control (Ctrl) or GCN1-targeting siRNA (GCN1 KD) in combination with a 6-hour incubation of 2.5 μM NVS1.1 or DMSO as control treatment. Vinculin served as a loading control. (B) Representative immunoblot showing protein levels of eRF1 and GAPDH (loading control) of HEKR4 PTC reporter cells treated with 2.5 μM NVS1.1 for 6 hours in the absence or presence of the translation elongation inhibitor cycloheximide (CHX). (C) (Top) Polysome profile showing A 260 readout of lysate deriving from HEKR4 PTC reporter cells treated with 25 μM NVS1.1 for 30 min that was separated over a 15%-50% sucrose gradient and fractionated. (Bottom) The proteins in every odd-numbered fraction of the gradient were precipitated and analyzed by immunoblotting for the indicated proteins. The fractions 3 and 5 were diluted 1/15 and 1/3, respectively. (D). Heavy polysome fractions from (C) were pooled and the proteins were analyzed by label-free mass spectrometry. Detected diGly events on lysine residues indicative of ubiquitination were normalized to the corresponding protein abundance. The fold change of the diGly frequency (log 2 diGly (NVS1.1/DMSO)) is shown for the protein eRF1 and for ribosomal proteins that showed a statistically significant difference (pVal < 0.05) upon NVS1.1 treatment

    Journal: bioRxiv

    Article Title: Drug-induced eRF1 degradation promotes readthrough and reveals a new branch of ribosome quality control

    doi: 10.1101/2023.01.31.526456

    Figure Lengend Snippet: (A) Immunoblot showing the protein levels of GCN1 and eRF1 in HEKR4 PTC reporter cells treated with negative control (Ctrl) or GCN1-targeting siRNA (GCN1 KD) in combination with a 6-hour incubation of 2.5 μM NVS1.1 or DMSO as control treatment. Vinculin served as a loading control. (B) Representative immunoblot showing protein levels of eRF1 and GAPDH (loading control) of HEKR4 PTC reporter cells treated with 2.5 μM NVS1.1 for 6 hours in the absence or presence of the translation elongation inhibitor cycloheximide (CHX). (C) (Top) Polysome profile showing A 260 readout of lysate deriving from HEKR4 PTC reporter cells treated with 25 μM NVS1.1 for 30 min that was separated over a 15%-50% sucrose gradient and fractionated. (Bottom) The proteins in every odd-numbered fraction of the gradient were precipitated and analyzed by immunoblotting for the indicated proteins. The fractions 3 and 5 were diluted 1/15 and 1/3, respectively. (D). Heavy polysome fractions from (C) were pooled and the proteins were analyzed by label-free mass spectrometry. Detected diGly events on lysine residues indicative of ubiquitination were normalized to the corresponding protein abundance. The fold change of the diGly frequency (log 2 diGly (NVS1.1/DMSO)) is shown for the protein eRF1 and for ribosomal proteins that showed a statistically significant difference (pVal < 0.05) upon NVS1.1 treatment

    Article Snippet: The NVS compounds, Bortezomib (BTZ, Merck, Cat# 504314), MLN4924 (Selleckchem, Cat# S7109) and Cycloheximide (CHX, Focus Biomolecules, Cat# 10-117) were all dissolved in DMSO, which also served as vehicle control.

    Techniques: Western Blot, Negative Control, Incubation, Control, Mass Spectrometry, Ubiquitin Proteomics, Quantitative Proteomics