In-gel digestion for mass spectrometric characterization of proteins and proteomes

HAVLIŠ, Jan and Mathias MANN. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nature Protocols. U.S.A.: Nature Publishing Group, 2008, vol. 1, No 6, p. 2856-2860. ISSN 1745-2473.

Basic information

Original name

In-gel digestion for mass spectrometric characterization of proteins and proteomes

Authors

HAVLIŠ, Jan and Mathias MANN

Edition

Nature Protocols, U.S.A. Nature Publishing Group, 2008, 1745-2473

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Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

Genetics and molecular biology

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 16.821

Organization unit

Faculty of Science

UT WoS

000251155700042

Keywords in English

ASSISTED-LASER-DESORPTION/IONIZATION; POLYACRYLAMIDE-GELS; NANOELECTROSPRAY; MODEL; SILAC; MS

Tags

ASSISTED-LASER-DESORPTION/IONIZATION, model, MS, NANOELECTROSPRAY, POLYACRYLAMIDE-GELS, SILAC

Tags

International impact, Reviewed

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Abstract

V originále

In-gel digestion of proteins isolated by gel electrophoresis is a cornerstone of mass spectrometry (MS)-driven proteomics. The 10-year-old recipe by Shevchenko et al. has been optimized to increase the speed and sensitivity of analysis. The protocol is for the in-gel digestion of both silver and Coomassie-stained protein spots or bands and can be followed by MALDI-MS or LC-MS/MS analysis to identify proteins at sensitivities better than a few femtomoles of protein starting material.