O-Glycosylation Site Occupation

The occurrence and development of many diseases such as cancer are often accompanied by abnormal changes in the glycosylation sites and carbohydrate chains of proteins, so characterizing glycosylation becomes extremely necessary in protein research. CD BioGlyco has advanced technology platforms and a complete database to provide customers comprehensive and time-saving services in glycosylation analysis. We have confidence to be your essential research assistant in the field of glycobiology.

Background

In recent years, the role of O-glycosylation in different proteins or other biological macromolecules has been intensively studied. In order to further understand how O-glycosylation modification confers receptors function, the research on macroheterogeneity (glycosylation site occupancy) becomes an essential step. It is critical to first determine whether the predicted O-glycosylation sites are modified and the relative amounts of the various glycoforms of O-glycosylation at each of those sites. Glycosylation sites analysis can not only obtain information intuitively about the glycosylation changes of numerous disease markers, but also make the further carbohydrate chain structural analysis more direct and convenient.

Unlike N-glycosylation, analyzing O-linked glycans is traditionally considered a difficult task for many reasons, including i) Lack of consensus sequence for the glycosylation sites on the polypeptide. ii) High heterogeneity both in the number of glycans and the extent of their occupancy. iii) Lack of universal enzyme to release O-glycans from the protein. High resolution and sensitivity of mass spectrometry are required for the discovery and confirmation of glycosylation sites.

Graphical summary of MS technologies for the analysis of glycoproteinsFig 1. Graphical summary of MS technologies for the analysis of glycoproteins (Mulagapati, S.; et al. 2017)

Services

In general, O-linked glycoproteins are analyzed in three different ways, and these strategies are mainly carried out using a variety of analytical platforms either stand alone or in combination with other techniques.

  • Glycan profiling: release of O-glycans by enzymatic or chemical treatment, followed by subsequent characterization.
  • Bottom-up approach: digestion of glycoproteins into peptides followed by analysis of the glycan attached peptides.
  • Top-down approach: analysis and characterization of glycans on intact glycoproteins. 

O-glycosylation site occupation analysis in CD BioGlyco including but is not limited to the following MS based glycomics technologies.

Experimental sample

  • Tandem mass spectrometry (MS2)
  • Higher-energy collisional dissociation (HCD)
  • Electrospray ionization (ESI)
  • MALDI in-source decay (ISD)
  • Ion mobility-mass spectrometry (IM-MS)
  • Collision-induced dissociation (CID)
  • Traveling wave ion mobility-mass spectrometry (TWIMS)
  • Matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF)
  • Electron capture dissociation (ECD) and electron transfer dissociation (ETD)

Applications

  • Proteins and other biomacromolecules structure & function research
  • Efficacy, stability, and immunogenicity of protein drugs research
  • Disease pathology and progression
  • Development of new biological drugs

Advantages of Us

  • High sensitivity and high throughput
  • Multiple technology platforms
  • High mass accuracy and varied fragmentation modes
  • One-stop services

CD BioGlyco provides a variety of comprehensive glycosylation research technology platforms to meet customers research needs. For a scientific research project, we guarantee one-stop service and maintain transparency in the whole process.

Customers can contact our employees directly and we will respond promptly. If you are interested in our services, please contact us for more detailed information.

References:

  1. Mulagapati, S.; et al. Decoding of O-linked glycosylation by Mass Spectrometry. Biochemistry. 2017, 56(9): 1218-1226.
  2. Hua, S.; et al. Site-specific protein glycosylation analysis with glycan isomer differentiation. Anal Bioanal Chem. 2012, 403: 1291-1302.
This service is for Research Use Only, not intended for any clinical use.

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