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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
要旨

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 Elizabethkingia meningoseptica由来, BioReagent, ≥95% (SDS-PAGE)
Sigma-Aldrich
PNGase F from Elizabethkingia miricola, buffered aqueous solution
Sigma-Aldrich
PNGase F Elizabethkingia meningoseptica由来, ready-to-use solution, recombinant, expressed in E. coli
Sigma-Aldrich
PNGase F Elizabethkingia meningoseptica由来, lyophilized powder, recombinant, expressed in E. coli
Sigma-Aldrich
グリコペプチダーゼA from almonds, buffered aqueous glycerol solution, ≥0.05 unit/mL
Sigma-Aldrich
PNGase F Elizabethkingia meningoseptica由来, recombinant, expressed in E. coli, set of 100 units nanomolar unit