Sialic Acid Linkage-Specific Glycosylation Profiling

Protein glycosylation mediates cell-to-cell interactions and is involved in the occurrence and development of various diseases. CD BioGlyco has been committed to sialic acid research for many years, and we provide protein N-glycosylation analysis services using matrix-assisted laser desorption/ionization-time of flight mass spectrometry (MALDI-TOF-MS) of sialic acid linkage-specific permethylation.

Glycosylation

Glycosylation is an important and common protein post-translational modification, which is involved in almost all biological regulatory pathways, such as cell-cell interactions, immune regulation, cancer development, etc. Protein glycosylation is mainly divided into N-glycosylation and O-glycosylation. N-glycosylation is the attachment of glycans to the side chain nitrogen atoms of asparagine (Asn) residues, whereas O-glycosylation is the attachment of glycans to the side-chain oxygen atoms of serine (Ser) and threonine (Thr) residues. N-glycans on mammalian proteins often contain terminal sialic acids, which bind to lectins. Sialic acid and sialylated glycans have been found to have important biological functions that affect the progression of the disease.

Sialic Acid Linkage-Specific Glycosylation Profiling

Sialic acid is usually attached to the end of many glycan structures by α2,3- or α2,6-glycosidic bonds and sialylated glycans play important roles in physiological and pathological processes. MALDI-TOF-MS is a commonly used technique for glycan analysis that rapidly provides detailed information on glycan composition, which is used to study glycosylation. However, direct analysis of sialylated glycans by MALDI-TOF-MS is difficult due to the structural diversity of sialylated glycans and the influence of ionization bias. Attempts have been made to stabilize and neutralize sialic acids by permethylation or derivatization with specific carboxyl groups, which have the potential to differentiate between α2,3- and α2,6-linked sialic acids.

MALDI-TOF-MS/MS analysis of sialylated glycan. Fig.1 MALDI-TOF-MS/MS analysis of sialylated glycans. (Jiang, 2017)

Our Services

Due to the structural diversity and ionization properties of sialylated glycans, permethylation of glycans before glycosylation characterization has become the most widely used method to facilitate glycan analysis. At CD BioGlyco, we have developed a complete sialic acid linkage-specific glycosylation profiling analysis process. We provide fast, sensitive, and robust protein N-glycosylation analysis services using MALDI-TOF-MS of sialic acid linkage-specific permethylation. Our analysis process is as follows:

  • Sample collection
  • Release and purification of N-glycans
  • Linkage-specific permethylation of sialylated glycans
  • MALDI-TOF-MS analysis

Advantages of Us

  • Fast, sensitive, and robust
  • Rich experience in sialic acid analysis
  • Complete and clear project reports
  • Worry-free after-sales service

CD BioGlyco provides a one-stop Sialic Acid Analysis Service through different efficient Strategies for our clients worldwide. If you are interested in our sialic acid linkage-specific glycosylation profiling strategy, please feel free to contact us for more information.

Reference:

  1. Jiang, K.; et al. Sialic acid linkage-specific permethylation for improved profiling of protein glycosylation by MALDI-TOF MS. Analytica chimica acta. 2017, 981: 53-61.
This service is for Research Use Only, not intended for any clinical use.

About Us

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