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sds polyacrylamide gel  (Bio-Rad)


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    Structured Review

    Bio-Rad sds polyacrylamide gel
    Purification and biophysical characterization of EEPD1 . A , domain architecture of human EEPD1. B , Coomassie-stained <t>SDS-PAGE</t> gels showing the purified full-length EEPD1 and its nuclease domain, EEPD1 N uc (aa 261–569). C , chromatograms of the final Size-exclusion chromatography (SEC) chromatograms of full-length EEPD1 and EEPD1 N uc . A total of 3 mg of each protein was loaded onto the columns. D , SEC-MALS traces of EEPD1 and EEPD1nuc domain confirming that both proteins form a stable dimers in solution. E , SEC-MALS analysis demonstrating that EEPD1 dimerization is maintained in a reducing environment (2.0 mM DTT).
    Sds Polyacrylamide Gel, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 99/100, based on 12499 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/mini+protean+tgx+polyacrylamide+gel/MINI-PROTEAN+TGX/pmc13153614-335-11-17
    Average 99 stars, based on 12499 article reviews
    sds polyacrylamide gel - by Bioz Stars, 2026-10
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    Images

    1) Product Images from "Structural basis for the mechanism and stability of the EEPD1 5′ endonuclease"

    Article Title: Structural basis for the mechanism and stability of the EEPD1 5′ endonuclease

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2026.111432

    Purification and biophysical characterization of EEPD1 . A , domain architecture of human EEPD1. B , Coomassie-stained SDS-PAGE gels showing the purified full-length EEPD1 and its nuclease domain, EEPD1 N uc (aa 261–569). C , chromatograms of the final Size-exclusion chromatography (SEC) chromatograms of full-length EEPD1 and EEPD1 N uc . A total of 3 mg of each protein was loaded onto the columns. D , SEC-MALS traces of EEPD1 and EEPD1nuc domain confirming that both proteins form a stable dimers in solution. E , SEC-MALS analysis demonstrating that EEPD1 dimerization is maintained in a reducing environment (2.0 mM DTT).
    Figure Legend Snippet: Purification and biophysical characterization of EEPD1 . A , domain architecture of human EEPD1. B , Coomassie-stained SDS-PAGE gels showing the purified full-length EEPD1 and its nuclease domain, EEPD1 N uc (aa 261–569). C , chromatograms of the final Size-exclusion chromatography (SEC) chromatograms of full-length EEPD1 and EEPD1 N uc . A total of 3 mg of each protein was loaded onto the columns. D , SEC-MALS traces of EEPD1 and EEPD1nuc domain confirming that both proteins form a stable dimers in solution. E , SEC-MALS analysis demonstrating that EEPD1 dimerization is maintained in a reducing environment (2.0 mM DTT).

    Techniques Used: Purification, Staining, SDS Page, Size-exclusion Chromatography

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    Article Snippet: .. Samples were then loaded on a 4%–20% Mini-PROTEAN TGX polyacrylamide gel (Bio-Rad) and transferred onto a polyvinylidene fluoride membrane (Bio-Rad). .. The membranes were blocked with 5% BSA (Sigma-Aldrich) in Tris-buffered saline (TBS) (Fisher Scientific) for 1 h and then incubated with primary antibodies overnight at 4°C.

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    Article Snippet: Samples were prepared with 2× Laemmli sample buffer (Bio-Rad) and boiled for 5 min at 95°C. .. Protein was run on a 4-20% Mini-Protean TGX polyacrylamide gel (Bio-Rad), transferred to an Immun-Blot PVDF Membrane (Bio-Rad), and blocked using Tris-buffered saline with Tween-20 plus 5% Blotting Grade Blocker (Bio-Rad). ..

    Article Title: The cAMP responsive element modulator (CREM) transcription factor influences susceptibility to undernutrition and infection.
    Article Snippet: Samples were prepared with 2× Laemmli sample buffer (Bio-Rad) and boiled for 5 min at 95°C. .. Protein was run on a 4-20% Mini-Protean TGX polyacrylamide gel (Bio-Rad), transferred to an Immun-Blot PVDF Membrane (Bio-Rad), and blocked using Tris-buffered saline with Tween-20 plus 5% Blotting Grade Blocker (Bio-Rad). ..

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    Article Snippet: For K562 cells, cells (in media, as K562 cells are suspension cells) were transferred to microfuge tubes, centrifuged at 300 x g , supernatant was removed, and cells were resuspended in D-PBS (MgCl - , CaCl - ) (Gibco, Cat. #14190250) and counted on an EVE automated cell counter.

    Saline:

    Article Title: The cAMP responsive element modulator (CREM) transcription factor influences susceptibility to undernutrition and infection
    Article Snippet: Samples were prepared with 2× Laemmli sample buffer (Bio-Rad) and boiled for 5 min at 95°C. .. Protein was run on a 4-20% Mini-Protean TGX polyacrylamide gel (Bio-Rad), transferred to an Immun-Blot PVDF Membrane (Bio-Rad), and blocked using Tris-buffered saline with Tween-20 plus 5% Blotting Grade Blocker (Bio-Rad). ..

    Article Title: The cAMP responsive element modulator (CREM) transcription factor influences susceptibility to undernutrition and infection.
    Article Snippet: Samples were prepared with 2× Laemmli sample buffer (Bio-Rad) and boiled for 5 min at 95°C. .. Protein was run on a 4-20% Mini-Protean TGX polyacrylamide gel (Bio-Rad), transferred to an Immun-Blot PVDF Membrane (Bio-Rad), and blocked using Tris-buffered saline with Tween-20 plus 5% Blotting Grade Blocker (Bio-Rad). ..



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    Image Search Results


    Purification and biophysical characterization of EEPD1 . A , domain architecture of human EEPD1. B , Coomassie-stained SDS-PAGE gels showing the purified full-length EEPD1 and its nuclease domain, EEPD1 N uc (aa 261–569). C , chromatograms of the final Size-exclusion chromatography (SEC) chromatograms of full-length EEPD1 and EEPD1 N uc . A total of 3 mg of each protein was loaded onto the columns. D , SEC-MALS traces of EEPD1 and EEPD1nuc domain confirming that both proteins form a stable dimers in solution. E , SEC-MALS analysis demonstrating that EEPD1 dimerization is maintained in a reducing environment (2.0 mM DTT).

    Journal: The Journal of Biological Chemistry

    Article Title: Structural basis for the mechanism and stability of the EEPD1 5′ endonuclease

    doi: 10.1016/j.jbc.2026.111432

    Figure Lengend Snippet: Purification and biophysical characterization of EEPD1 . A , domain architecture of human EEPD1. B , Coomassie-stained SDS-PAGE gels showing the purified full-length EEPD1 and its nuclease domain, EEPD1 N uc (aa 261–569). C , chromatograms of the final Size-exclusion chromatography (SEC) chromatograms of full-length EEPD1 and EEPD1 N uc . A total of 3 mg of each protein was loaded onto the columns. D , SEC-MALS traces of EEPD1 and EEPD1nuc domain confirming that both proteins form a stable dimers in solution. E , SEC-MALS analysis demonstrating that EEPD1 dimerization is maintained in a reducing environment (2.0 mM DTT).

    Article Snippet: The isolated Flag-EEPD1 full length WT sample was loaded onto an SDS polyacrylamide gel (12% Mini-PROTEAN TGX, Bio-Rad Laboratories Inc) and electrophoreses to a distance of 1 cm and stained with Coomassie Brilliant Blue R-250.

    Techniques: Purification, Staining, SDS Page, Size-exclusion Chromatography