Sechi | Quantitative Proteomics by Mass Spectrometry | Buch | 978-1-4939-8066-6 | www.sack.de

Buch, Englisch, Band 1410, 306 Seiten, Previously published in hardcover, Format (B × H): 178 mm x 254 mm, Gewicht: 605 g

Reihe: Methods in Molecular Biology

Sechi

Quantitative Proteomics by Mass Spectrometry


Softcover Nachdruck of the original 2. Auflage 2016
ISBN: 978-1-4939-8066-6
Verlag: Springer

Buch, Englisch, Band 1410, 306 Seiten, Previously published in hardcover, Format (B × H): 178 mm x 254 mm, Gewicht: 605 g

Reihe: Methods in Molecular Biology

ISBN: 978-1-4939-8066-6
Verlag: Springer


This volume describes prominent methodologies developed by laboratories that have been leading the field of quantitative proteomics by mass spectrometry. The procedures for performing the experiments are described in an easy-to-understand manner with many technical details that usually are not reported in typical research articles. This second edition of Quantitative Proteomics by Mass Spectrometry provides a broad perspective of the methodologies used for quantifying proteins and post-translational modifications in different types of biomedical specimens. Written in the highly successful Methods in Molecular Biology series format, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls.

Authoritative and thorough, Quantitative Proteomics by Mass Spectrometry, Second Edition is a valuable resource to help researchers understand and learn about the latest tools used in the study of quantitative proteomics by mass spectrometry.

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Increased
Depth and Breadth of Plasma Protein Quantitation via Two Dimensional Liquid
Chromatography/Multiple Reaction Monitoring-Mass Spectrometry with Labeled
Peptide Standards.- Quantitative
Analysis of the Wirt5-Regulated Lysine Succinylation Proteome in Mammalian
Cells.- Determining
the Composition and Stability of Protein Complexes Using an Integrated Label-Free
and Stable Isotope Labeling Strategy.- Label-Free
Quantitation for Clinical Proteomics.- Proteogenomic
Methods to Improve Genome Annotation.- Mass
Spectrometry-Based Quantitative O-GlcNAcomic Analysis.- Isolating and
Quantifying Plasma HDL Proteins by Sequential Density Gradient
Ultracentrifugation and Targeted Proteomics.- A Method for
Label-Free Differential Top-Down Proteomics.- Multiplexed Immunoaffinity Enrichment of
Peptides with Anti-Peptide Antibodies and Quantification by Stable Isotope
Dilution Multiple Reaction Monitoring Mass Spectrometry.- High
Throughput Quantitative Proteomics Enabled by Mass Defect-Based 12-Plex DiLeu
Isobaric Tags.- Isotopic
N, N-Dimethyl Leucine (iDiLeu) for Absolute Quantification of Peptides Using a
Standard Curve Approach.- Selecting
Optimal Peptides for Targeted Proteomic Experiments in Human Plasma Using In Vitro Synthesized Proteins as
Analytical Standards.- Using
the CPTAC Assay Portal to Identify and Implement Highly Characterized Targeted
Proteomics Assays.- Large-Scale
and Deep Quantitative Proteome Profiling Using Isobaric Lableing Coupled with
Two-Dimensional LC-MS/MS.- Multiple
and Selective Reaction Monitoring Using Triple Quadrupole Mass Spectrometer:

Pre-Clinical Large Cohort Analysis.- Methods
for SWATH™: Data Independent Acquisition on TripleTOF Mass Spectrometers.- Measurement
of Phosphorylated Peptides with Absolute Quantification.- Proteomic Analysis of Protein Turnover by Metabolic Whole Rodent Pulse-Chase Isotopic Labeling and Shotgun Mass Spectrometry Analysis.



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