Glycan Release Service
Most proteins are post-translationally, and the most important modification of many secretory and membrane-related proteins in eukaryotic cells is glycosylation, that is, the attachment of one or more glycan chains. Glycan chains of glycoprotein are mainly connected to Asn residues of peptide backbone by N-glycopeptide bond or Ser / Thr residues by O-glycopeptide bond.
The glycans attached to proteins have structural diversity, and each glycosylated polypeptide is usually associated with a population of different glycan structures, which leads to the observation of considerable glycosylation heterogeneity in many glycoproteins. Current techniques generally cannot analyze the complete glycoproteins. Therefore, oligosaccharide analysis is mainly carried out after the release of the oligosaccharides from the polypeptide. Glycan release technology is based on enzyme or chemical programming. Each technology has its own advantages, and the choice of technology will depend on the type of glycosylation and the nature and quantity of samples.
CD BioGlyco stands at the forefront of glycomics research, offering a comprehensive and highly specialized glycan release service. Leveraging our expertise, we provide robust and reliable solutions that are foundational for in-depth glycan analysis. This essential preparatory step is key to unlocking the full biological potential encoded within glycosylation, ensuring the isolation of intact glycans for precise downstream characterization by advanced analytical platforms.
CD BioGlyco offers an extensive array of glycan release options, meticulously designed to cater to the diverse requirements of glycomics research and development. Our comprehensive service scope ensures that virtually any glycosylation linkage is effectively targeted and analyzed.
Our enzymatic release services leverage highly specific enzymes to ensure precise and efficient cleavage, minimizing sample degradation and preserving glycan integrity.
Utilizing PNGase F, we provide highly efficient and reproducible release of N-linked glycans from a wide range of glycoproteins. This method is the preferred choice for applications requiring intact N-glycan structures for subsequent profiling and structural elucidation.
We employ specific fucosidases to selectively cleave terminal fucose residues. This service is invaluable for studying the role of fucosylation in biological processes, such as inflammation and cancer, or for preparing glycans for further analysis by removing this common modification.
Our service includes the use of highly purified galactosidases for the enzymatic removal of terminal galactose residues. This is crucial for structural determination, especially in complex glycans, and for investigating the biological significance of galactosylation, particularly relevant in areas like blood group antigens and immune regulation.
Targeting α-N-acetylgalactosaminidase, this service enables the selective release of N-acetylgalactosamine. This is particularly useful for dissecting specific glycan linkages and for research into O-linked glycosylation pathways.
For O-linked glycans, we employ O-glycosidase and other broad-specificity enzymes to facilitate their release from various O-glycosylated proteins. This service provides a gentle yet effective way to obtain O-glycans for downstream analysis, particularly for structures amenable to enzymatic cleavage.
Focusing on one of the most common O-glycan core structures, our specialized service ensures the efficient enzymatic release of core-1 O-glycans, which are vital in cell adhesion, signaling, and disease. This targeted approach allows for focused analysis of these specific and biologically significant structures.
Using sialidases, we offer precise enzymatic removal of terminal sialic acid residues. This is essential for understanding the roles of sialylation in cellular communication, viral entry, and immune evasion, and for preparing glycans for further analysis where desialylation is required.
Our chemical release methods provide robust alternatives for glycans resistant to enzymatic digestion or for comprehensive release strategies.
Journal: Frontiers in Molecular Biosciences
IF: 4.0
Published: 2022
Results: The paper highlights the effectiveness of chemical methods for glycan release, exploring the release of protein N-glycans via effectors of a Hofmann carboxamide rearrangement. This study demonstrates that known Hofmann catalysts, such as 1,3-dichloro-5,5-dimethylhydantoin, hypervalent organoiodine compounds like diacetoxy-iodobenzene, and in-situ hypobromite generation, are all capable of releasing protein-bound N-glycans in good yield. These findings suggest that the oxidative release of N-glycans proceeds through the initial steps of a Hofmann carboxamide rearrangement. Notably, the in-situ generation of hypobromite using bromide provides a consistent and defined amount of reagent for rapid N-glycan release, suitable for both analytical and preparative applications.
Fig.1 Similarities between the hypochlorite method and the Hofmann carboxamide rearrangement. (Kasim, et al., 2022)
CD BioGlyco is committed to accelerating your research with our unparalleled glycan release service and comprehensive glycomics solutions. Please feel free to contact us our team of experienced scientists is ready to discuss your specific project needs and provide tailored recommendations.
To further support your comprehensive glycomics research and development endeavors, CD BioGlyco offers a suite of complementary services designed to provide end-to-end solutions for glycan analysis and beyond.
Reference
