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Difference Gel Electrophoresis

Overview of attention for book
Cover of 'Difference Gel Electrophoresis'

Table of Contents

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    Book Overview
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    Chapter 1 Two-Dimensional Gel Electrophoresis and 2D-DIGE
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    Chapter 2 Comparative DIGE Proteomics
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    Chapter 3 2D-DIGE and Fluorescence Image Analysis
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    Chapter 4 DIGE Analysis Software and Protein Identification Approaches
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    Chapter 5 Native DIGE: Efficient Tool to Elucidate Protein Interactomes
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    Chapter 6 Comparative Two-Dimensional Fluorescence Gel Electrophoresis
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    Chapter 7 DIGE-Based Phosphoproteomic Analysis
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    Chapter 8 DIGE Saturation Labeling for Scarce Amounts of Protein from Formalin-Fixed Paraffin-Embedded (FFPE) Tissue
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    Chapter 9 Comparative 3-Sample DIGE Analysis of Skeletal Muscles
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    Chapter 10 DIGE Analysis of ProteoMinerTM Fractionated Serum/Plasma Samples
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    Chapter 11 DIGE Analysis of Human Tissues
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    Chapter 12 DIGE Analysis of Animal Tissues
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    Chapter 13 Rapid 2D DIGE Proteomic Analysis of Mouse Liver
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    Chapter 14 Proteomic Analysis of Lung Tissue by DIGE
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    Chapter 15 Comparative Testis Tissue Proteomics Using 2-Dye Versus 3-Dye DIGE Analysis
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    Chapter 16 DIGE Analysis of Fish Tissues
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    Chapter 17 Protein Digestion for DIGE Analysis
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    Chapter 18 Subcellular Fractionation for DIGE-Based Proteomics
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    Chapter 19 DIGE Analysis of Immunodepleted Plasma
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    Chapter 20 Elucidating Cellular Metabolism and Protein Difference Data from DIGE Proteomics Experiments Using Enzyme Assays
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    Chapter 21 Enzyme Assay Methods to Validate DIGE Proteomics Data
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    Chapter 22 Immunoblot Analysis of DIGE-Based Proteomics
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    Chapter 23 Immunofluorescence Microscopy for DIGE-Based Proteomics
Attention for Chapter 10: DIGE Analysis of ProteoMinerTM Fractionated Serum/Plasma Samples
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Chapter title
DIGE Analysis of ProteoMinerTM Fractionated Serum/Plasma Samples
Chapter number 10
Book title
Difference Gel Electrophoresis
Published in
Methods in molecular biology, January 2018
DOI 10.1007/978-1-4939-7268-5_10
Pubmed ID
Book ISBNs
978-1-4939-7267-8, 978-1-4939-7268-5
Authors

Sandra Murphy, Paul Dowling

Abstract

The discovery of clinically relevant biomarkers using gel-based proteomics has proven extremely challenging, principally because of the large dynamic range of protein abundances in biofluids such as blood and the fact that only a small number of proteins constitute the vast majority of total blood protein mass. Various separation, depletion, enrichment, and quantitative developments coupled with improvements in gel-based protein quantification technologies, specifically difference gel electrophoresis (DIGE), have contributed to significant improvements in the detection and identification of lower abundance proteins. One of these enrichment technologies, Proteominer, will be the focus of this chapter. The Proteominer technology a utilizes hexapeptide bead library with huge diversity to bind and enrich low-abundance proteins but at the same time suppressing the concentration of high-abundance proteins in subsequent analysis.

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Mendeley readers

The data shown below were compiled from readership statistics for 5 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 5 100%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 2 40%
Student > Ph. D. Student 1 20%
Unspecified 1 20%
Unknown 1 20%
Readers by discipline Count As %
Agricultural and Biological Sciences 2 40%
Biochemistry, Genetics and Molecular Biology 1 20%
Unspecified 1 20%
Unknown 1 20%