- 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
PMID23296525
RESUMEN
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.
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Sigma-Aldrich
PNGase F from Elizabethkingia meningoseptica, BioReagent, ≥95% (SDS-PAGE), for proteomics
Sigma-Aldrich
PNGase F from Elizabethkingia meningoseptica, ready-to-use solution, recombinant, expressed in E. coli
Sigma-Aldrich
PNGase F from Elizabethkingia meningoseptica, lyophilized powder, recombinant, expressed in E. coli
Sigma-Aldrich
PNGase F from Elizabethkingia meningoseptica, recombinant, expressed in E. coli, set of 100 units nanomolar unit