Introduction

Glycocalyx, literally meaning ‘sugar coat’, is an extracellular polymeric coating surrounding many prokaryotic and eukaryotic cells consisting of glycoproteins, glycolipids, proteoglycans and glycosaminoglycans. The constituents of the glycocalyx play an important role in the process of protein folding and trafficking, cell signaling and intercellular interactions, cell pathogen interactions, and immunity. However, detection tools for the research of glycobiology are currently in very limited supply.

Raybiotech has pioneered the development of antibody arrays which are now widely applied in the research community with thousands of peer reviewed publications, including in Cell and Nature. Taking advantage of advancements in microarray technology developed for antibody arrays, we have developed a new generation glycan array, the Glycan-300, soon after previously launching the Glycan-100. The Glycan-300 is currently the largest commercially available glycan array for screening protein-carbohydrate interactions. This array will help researchers:

1. Identify glycan binding partners in biological samples
2. Identify whether target proteins are carbohydrate binding proteins
3. Probe binding of pathogens including bacteria, viruses and whole cells to glycans^1-3
4. Profile the substrate specificity of enzymes (glycosyltransferases, glycosidases, etc.)^4-6
5. Profile the inflammatory and/or immune response.

The 300 synthetic glycans featured in the new generation Glycan Glycan-300 array consists of four groups of targets including the 100 glycans from the Raybio Glycan-100 array and an additional 80 N-glycans, 50 glycolipid glycans, and 50 human milk oligosaccharide glycans. The included glycans have been frequently identified as structures showing important binding functions in the literature. For example, a variety of sialosides have been shown to bind to the influenza virus with a serotype-specific pattern.^7-9 Galectins, which are involved in apoptosis, cell adhesion and T-cell activation suppression, function by binding beta-galactosides.^10-12 Glycosphingolipids interact with growth factor receptors to modify signal transduction or with bacterial toxin subunits, such as Vero(Shiga) toxin, cholera toxin, and the heat labile E.coli toxins, to induce cell apoptosis¹³. Additionally, oligosaccharides from human milk bind to microbes to promote growth of normal flora and inhibit pathogens in the gastrointestinal tract¹⁴. This array provides a powerful tool for researchers in glycobiology and other fields.

Glycan Names: Download Full Glycan List | Download Glycan Structures

Application Data

Storage/Stability

References