Lectin Enrichment

The method of lectin enrichment is widely used in N-linked glycopeptide enrichment. CD BioGlyco is committed to improving the identification ability of glycosylation sites and the enrichment efficiency of glycopeptides, to achieve the goal of providing efficient services to customers. We are confident to be your indispensable research assistant in the field of glycobiology.

Background

Glycosylation is one of the most important post-translational modifications of proteins and is ubiquitous in organisms. Large-scale N-linked glycosylation site identification is an important part of glycoproteomics research. Therefore the enrichment of N-linked glycopeptide is crucial for the high-throughput identification of N-glycosylation sites. Due to the high heterogeneity of glycosylation sites and modifications, the complexity of glycosylated peptide detection is increased. Glycoproteins or glycopeptides should be enriched to improve the detection sensitivity.

Lectins have the property of recognizing carbohydrates through carbohydrate binding sites. The lectin enrichment method is to selectively identify some monosaccharides or glycans with special structures by lectins to realize the enrichment of glycoproteins. Different types of glycopeptides can be enriched by different lectins or a combination of various lectins. For example, it was reported that the N-linked glycosylation sites of the brain, kidney, liver, and heart of mice were comprehensively interpreted by using three lectins (convalina agglutinin, wheat germ agglutinin, and ricinus communis agglutinin I).

Fig 1. Sample preparation and enrichment of N-glycosylated peptides.Fig.1 Sample preparation and enrichment of N-glycosylated peptides. (Zielinska, 2010)

Enrichment Strategies

CD BioGlyco has established a variety of lectin-based enrichment strategies for improved coverage of glycan analysis. The methods we provide include but are not limited to:

  • Enrichment of N-linked glycopeptides by a combination of lectin enrichment and hydrazide chemistry, the glycosylation sites were then identified by LTQ Orbitrap XL tandem mass spectrometry.
  • Using multiple lectins and optimizing the combination of different lectins, combined with hydrophilic interaction chromatography to enrich glycosylation sites of glycoproteins from various samples.
  • Specific lectins are added to capture the corresponding glycans followed by the release of N-glycans by peptide N-glycosidase F (PNGase F). Bound and non-bound glycans are released and analyzed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS).

Applications

  • Enrichment and identification of potential biomarkers
  • Search for aberrant glycoproteins that can be used as tumor markers
  • Characterization of glycoproteomics
  • Study of glycosylation profiles in cancer

Advantages of Us

  • Advanced equipment
  • Procedure with simplicity and flexibility
  • Cost-effectiveness
  • Detailed after-sale service

At CD BioGlyco, our researchers constantly study cutting-edge knowledge in the field of glycobiology to actively improve our experimental process and help our customers achieve their goals in a timely, efficient, and economical manner. If you are interested in our services, please contact us and we will respond immediately and try our best to offer scientific assistance.

Reference:

  1. Zielinska, D.F.; et al. Precision mapping of an in vivo N-glycoproteome reveals rigid topological and sequence constraints. Cell. 2010, 141(5):897-907.
This service is for Research Use Only, not intended for any clinical use.

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