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  • Characterization of membrane-associated glycoproteins using lectin affinity chromatography and mass spectrometry.

Characterization of membrane-associated glycoproteins using lectin affinity chromatography and mass spectrometry.

Methods in molecular biology (Clifton, N.J.) (2013-01-09)
Yashu Liu, Jintang He, David M Lubman
ABSTRACT

Membrane-associated glycoproteins play critical roles in many biological processes and are often the therapeutic targets for drug discovery. Lectin affinity chromatography is one of the most widely used approaches for enrichment of glycoproteins at the protein level. Here, we describe a strategy for the characterization of membrane glycoproteins including membrane protein extraction, lectin affinity chromatography, protein digestion, and analysis by LC-MS/MS.

MATERIALS
Product Number
Brand
Product Description

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PNGase F from Elizabethkingia meningoseptica, lyophilized powder, recombinant, expressed in E. coli
Sigma-Aldrich
PNGase F from Elizabethkingia meningoseptica, ready-to-use solution, recombinant, expressed in E. coli
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PNGase F from Elizabethkingia meningoseptica, recombinant, expressed in E. coli, set of 100 units nanomolar unit
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PNGase F from Elizabethkingia meningoseptica, BioReagent, ≥95% (SDS-PAGE), for proteomics
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Glycopeptidase A from almonds, buffered aqueous glycerol solution, ≥0.05 unit/mL
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PNGase F from Elizabethkingia miricola, buffered aqueous solution