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licl extraction buffer  (Thermo Fisher)


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    Structured Review

    Thermo Fisher licl extraction buffer
    ( A ) Schematic representation of the workflow for MS-based proteomic analysis of protein extracts from human ICM and donor patient myocardial tissue. Soluble proteins are depleted in the first <t>LiCl</t> <t>extraction</t> (LiCl) followed by solubilization of “insoluble” ECM proteins by extraction with buffer containing the photocleavable surfactant, Azo. ( B ) CVs of protein intensities across extracts from failing ICM and nonfailing donor tissues. The median CV of protein intensities was below 5% for extracts from both groups, indicating high quantitative reproducibility. CVs were calculated by (SD/mean intensity) × 100% for each quantified value in each replicate. ( C ) Upset plot and bar graph (inset) showing more than 6,000 unique protein identifications overall, as well as the degree of overlap between groups. ( D and E ) Simplified depiction of major categories of ECM proteins (per MatrisomeDB, ref. ) ( D ) and breakdown of the number of proteins in each category identified in this study ( E ). The inner circle shows the total number of proteins in each category while the outer circle indicates those that were identified herein. Black segments correspond to proteins present in MatrisomeDB that were not identified in human ICM and donor myocardial tissue.
    Licl Extraction Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 26601 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/licl extraction buffer/product/Thermo Fisher
    Average 99 stars, based on 26601 article reviews
    licl extraction buffer - by Bioz Stars, 2026-02
    99/100 stars

    Images

    1) Product Images from "Extracellular matrix alterations in chronic ischemic cardiomyopathy revealed by quantitative proteomics"

    Article Title: Extracellular matrix alterations in chronic ischemic cardiomyopathy revealed by quantitative proteomics

    Journal: JCI Insight

    doi: 10.1172/jci.insight.196933

    ( A ) Schematic representation of the workflow for MS-based proteomic analysis of protein extracts from human ICM and donor patient myocardial tissue. Soluble proteins are depleted in the first LiCl extraction (LiCl) followed by solubilization of “insoluble” ECM proteins by extraction with buffer containing the photocleavable surfactant, Azo. ( B ) CVs of protein intensities across extracts from failing ICM and nonfailing donor tissues. The median CV of protein intensities was below 5% for extracts from both groups, indicating high quantitative reproducibility. CVs were calculated by (SD/mean intensity) × 100% for each quantified value in each replicate. ( C ) Upset plot and bar graph (inset) showing more than 6,000 unique protein identifications overall, as well as the degree of overlap between groups. ( D and E ) Simplified depiction of major categories of ECM proteins (per MatrisomeDB, ref. ) ( D ) and breakdown of the number of proteins in each category identified in this study ( E ). The inner circle shows the total number of proteins in each category while the outer circle indicates those that were identified herein. Black segments correspond to proteins present in MatrisomeDB that were not identified in human ICM and donor myocardial tissue.
    Figure Legend Snippet: ( A ) Schematic representation of the workflow for MS-based proteomic analysis of protein extracts from human ICM and donor patient myocardial tissue. Soluble proteins are depleted in the first LiCl extraction (LiCl) followed by solubilization of “insoluble” ECM proteins by extraction with buffer containing the photocleavable surfactant, Azo. ( B ) CVs of protein intensities across extracts from failing ICM and nonfailing donor tissues. The median CV of protein intensities was below 5% for extracts from both groups, indicating high quantitative reproducibility. CVs were calculated by (SD/mean intensity) × 100% for each quantified value in each replicate. ( C ) Upset plot and bar graph (inset) showing more than 6,000 unique protein identifications overall, as well as the degree of overlap between groups. ( D and E ) Simplified depiction of major categories of ECM proteins (per MatrisomeDB, ref. ) ( D ) and breakdown of the number of proteins in each category identified in this study ( E ). The inner circle shows the total number of proteins in each category while the outer circle indicates those that were identified herein. Black segments correspond to proteins present in MatrisomeDB that were not identified in human ICM and donor myocardial tissue.

    Techniques Used: Extraction



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    99
    Thermo Fisher licl extraction buffer
    ( A ) Schematic representation of the workflow for MS-based proteomic analysis of protein extracts from human ICM and donor patient myocardial tissue. Soluble proteins are depleted in the first <t>LiCl</t> <t>extraction</t> (LiCl) followed by solubilization of “insoluble” ECM proteins by extraction with buffer containing the photocleavable surfactant, Azo. ( B ) CVs of protein intensities across extracts from failing ICM and nonfailing donor tissues. The median CV of protein intensities was below 5% for extracts from both groups, indicating high quantitative reproducibility. CVs were calculated by (SD/mean intensity) × 100% for each quantified value in each replicate. ( C ) Upset plot and bar graph (inset) showing more than 6,000 unique protein identifications overall, as well as the degree of overlap between groups. ( D and E ) Simplified depiction of major categories of ECM proteins (per MatrisomeDB, ref. ) ( D ) and breakdown of the number of proteins in each category identified in this study ( E ). The inner circle shows the total number of proteins in each category while the outer circle indicates those that were identified herein. Black segments correspond to proteins present in MatrisomeDB that were not identified in human ICM and donor myocardial tissue.
    Licl Extraction Buffer, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/licl extraction buffer/product/Thermo Fisher
    Average 99 stars, based on 1 article reviews
    licl extraction buffer - by Bioz Stars, 2026-02
    99/100 stars
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    Image Search Results


    ( A ) Schematic representation of the workflow for MS-based proteomic analysis of protein extracts from human ICM and donor patient myocardial tissue. Soluble proteins are depleted in the first LiCl extraction (LiCl) followed by solubilization of “insoluble” ECM proteins by extraction with buffer containing the photocleavable surfactant, Azo. ( B ) CVs of protein intensities across extracts from failing ICM and nonfailing donor tissues. The median CV of protein intensities was below 5% for extracts from both groups, indicating high quantitative reproducibility. CVs were calculated by (SD/mean intensity) × 100% for each quantified value in each replicate. ( C ) Upset plot and bar graph (inset) showing more than 6,000 unique protein identifications overall, as well as the degree of overlap between groups. ( D and E ) Simplified depiction of major categories of ECM proteins (per MatrisomeDB, ref. ) ( D ) and breakdown of the number of proteins in each category identified in this study ( E ). The inner circle shows the total number of proteins in each category while the outer circle indicates those that were identified herein. Black segments correspond to proteins present in MatrisomeDB that were not identified in human ICM and donor myocardial tissue.

    Journal: JCI Insight

    Article Title: Extracellular matrix alterations in chronic ischemic cardiomyopathy revealed by quantitative proteomics

    doi: 10.1172/jci.insight.196933

    Figure Lengend Snippet: ( A ) Schematic representation of the workflow for MS-based proteomic analysis of protein extracts from human ICM and donor patient myocardial tissue. Soluble proteins are depleted in the first LiCl extraction (LiCl) followed by solubilization of “insoluble” ECM proteins by extraction with buffer containing the photocleavable surfactant, Azo. ( B ) CVs of protein intensities across extracts from failing ICM and nonfailing donor tissues. The median CV of protein intensities was below 5% for extracts from both groups, indicating high quantitative reproducibility. CVs were calculated by (SD/mean intensity) × 100% for each quantified value in each replicate. ( C ) Upset plot and bar graph (inset) showing more than 6,000 unique protein identifications overall, as well as the degree of overlap between groups. ( D and E ) Simplified depiction of major categories of ECM proteins (per MatrisomeDB, ref. ) ( D ) and breakdown of the number of proteins in each category identified in this study ( E ). The inner circle shows the total number of proteins in each category while the outer circle indicates those that were identified herein. Black segments correspond to proteins present in MatrisomeDB that were not identified in human ICM and donor myocardial tissue.

    Article Snippet: Pellets were homogenized in 20 volumes (~300 μL) of LiCl extraction buffer (3 M LiCl, 1 mM TCEP, 10 mM EDTA, and 1× Halt Protease Inhibitor Cocktail from Thermo Fisher Scientific) using a handheld Teflon homogenizer (Bel-Art).

    Techniques: Extraction