Native detection of protein O-GlcNAcylation by gel electrophoresis

Chuan Fu; Daan M. F.  van Aalten

doi:10.1039/C9AN02506E

Native detection of protein O-GlcNAcylation by gel electrophoresis

Chuan Fu
, Daan M. F. van Aalten (Lead / Corresponding author)

Research output: Contribution to journal › Article › peer-review

5 Citations (Scopus)

128 Downloads (Pure)

Abstract

O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans. Studies of this modification are hampered by the lack of convenient methods for detecting native O-GlcNAcylation. Here, we describe a novel gel-based approach, Separation of OGlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.

Original language	English
Pages (from-to)	6826-6830
Number of pages	5
Journal	Analyst
Volume	145
Issue number	21
Early online date	2 Sept 2020
DOIs	https://doi.org/10.1039/C9AN02506E
Publication status	Published - 7 Nov 2020

ASJC Scopus subject areas

Analytical Chemistry
Biochemistry
Environmental Chemistry
Spectroscopy
Electrochemistry

Access to Document

10.1039/C9AN02506ELicence: CC BY

Final Published VersionFinal published version, 1.02 MBLicence: CC BY

Cite this

@article{c8760924b6a44024bc84003a535a5d83,

title = "Native detection of protein O-GlcNAcylation by gel electrophoresis",

abstract = "O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans. Studies of this modification are hampered by the lack of convenient methods for detecting native O-GlcNAcylation. Here, we describe a novel gel-based approach, Separation of OGlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.",

author = "Chuan Fu and \{van Aalten\}, \{Daan M. F.\}",

note = "This work was funded by a Wellcome Trust Senior Research Fellowship (110061)",

year = "2020",

month = nov,

day = "7",

doi = "10.1039/C9AN02506E",

language = "English",

volume = "145",

pages = "6826--6830",

journal = "Analyst",

issn = "0003-2654",

publisher = "Royal Society of Chemistry",

number = "21",

}

TY - JOUR

T1 - Native detection of protein O-GlcNAcylation by gel electrophoresis

AU - Fu, Chuan

AU - van Aalten, Daan M. F.

N1 - This work was funded by a Wellcome Trust Senior Research Fellowship (110061)

PY - 2020/11/7

Y1 - 2020/11/7

N2 - O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans. Studies of this modification are hampered by the lack of convenient methods for detecting native O-GlcNAcylation. Here, we describe a novel gel-based approach, Separation of OGlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.

AB - O-GlcNAcylation is an abundant and dynamic protein posttranslational modification (PTM), with crucial roles in metazoans. Studies of this modification are hampered by the lack of convenient methods for detecting native O-GlcNAcylation. Here, we describe a novel gel-based approach, Separation of OGlcNAcylated Proteins by Polyacrylamide Gel Electrophoresis (SOPAGE), which enables detection of O-GlcNAc levels and dynamics.

UR - https://www.scopus.com/pages/publications/85094653966

U2 - 10.1039/C9AN02506E

DO - 10.1039/C9AN02506E

M3 - Article

SN - 0003-2654

VL - 145

SP - 6826

EP - 6830

JO - Analyst

JF - Analyst

IS - 21

ER -

Native detection of protein O-GlcNAcylation by gel electrophoresis

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Molecular Mechanisms of O-GICNAC Signalling (Investigator award)

Cite this

Native detection of protein O-GlcNAcylation by gel electrophoresis

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Projects

Molecular Mechanisms of O-GICNAC Signalling (Investigator award)

Cite this