Cell Surface Glycosylphosphatidylinositol (GPI) Anchor Glycoengineering Service
Diversity of GPI Anchor Structure and Function
Unlike general post-translational modifications, the structure of GPI anchors is complex. Its core sugar chain can be modified to different degrees. It has been found that GPI anchors are diverse in different species and cells. This diversity stems from its complex structure on the one hand and the diversity of proteins it anchors on the other. Its synthesis and its attachment to protein chains are found to be highly regulated. Blockage of the biosynthetic pathway of the human GPI anchor leads to different diseases. The diversity of structures creates a diversity of functions. GPI anchor proteins (GPI-AP) signals through interactions with glycosphingolipids, G proteins, etc.
Fig.1 Structure and biosynthesis of mammalian GPI-APs. (Fujita & Kinoshita, 2012)
Cell Surface GPI Anchor Glycoengineering Service at CD BioGlyco
CD BioGlyco is equipped with a specialized research team and state-of-the-art technology for Cell Surface Glycoengineering. GPI anchors play a role in signaling, cell adhesion, protein translocation, immune response, and more. We offer comprehensive cell surface GPI anchor glycoengineering services. Our services involve free GPI molecules, GPI-anchored glycoproteins, etc.
Fig.2 Types of cell surface GPI anchor glycoengineering. (CD BioGlyco)
- Targeted introduction and modification of cell surface GPI anchor
We introduce and modify cell surface GPI anchors by Gene Editing to introduce or modify cell surface GPI anchors of different structures. The biosynthesis of GPI-anchored proteins is very complex. By knocking out the relevant genes involved in the biosynthesis of GPI-anchored proteins, we can also explore the effects of different GPI structures on the cell surface expression of GPI-anchored proteins.
- GPI anchor structure analysis service
We use a combination of nuclear magnetic resonance spectroscopy (NMR), mass spectrometry (MS), chemical modification, exoglycosidase digestion, etc., to analyze GPI anchors. The analysis includes monosaccharide composition, glycosidic bond type, side chain structure, modification sites, etc. Samples from animals, plants, yeast, etc., can be analyzed.
- GPI anchor service
We have a mature experimental platform and are experienced in protein expression, phage display systems, antibody preparation, and so on. We customize the experimental plan according to the client's requirements. Anchoring of multiple proteins with GPI in different species can be realized.
Applications
- The diversity of GPI anchors is related to their complex structure and the types of proteins. GPI anchor glycoengineering is used to study its function in organisms.
- The biosynthesis of GPI anchors in fungi is not identical to that in human cells. GPI anchor glycoengineering provides the basis for the development of antifungal therapies.
- Certain GPI-APs are associated with tumor invasion and growth. The GPI anchor proteins on the surface of tumors are also of great interest. GPI anchor glycoengineering is used to study the mechanisms of tumorigenesis.
Advantages
- GPI anchor glycoengineering services are less restrictive, reproducible, and time-consuming, and can be customized to fit different needs.
- Using a combination of highly efficient enrichment and highly sensitive mass spectrometry, it can rapidly and comprehensively identify glycosylation sites, separate glycopeptides, and identify the glycosides attached to the sites.
- Our GPI anchor glycoengineering plays a role in oncology research, helping researchers find GPI-APs that can be used as diagnostic markers for lung cancer.
CD BioGlyco is committed to accurate and comprehensive GPI anchor glycoengineering services for a wide range of substances. Please feel free to contact us. All you need to do is tell us your requirements. We will complete all the steps from experiment development to completion.
Reference
- Fujita, M.; Kinoshita, T. GPI-anchor remodeling: potential functions of GPI-anchors in intracellular trafficking and membrane dynamics. Biochim Biophys Acta. 2012, 1821(8): 1050-1058.
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