Glycan Array 300 (ab272785) is the largest commercially available glycan array for screening protein-carbohydrate interactions.

This array will help researchers: 1) identify the glycans 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, 4) profile the substrate specificity of enzymes (glycosyltransferases, glycosidases, etc.); 5) profile the inflammatory 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. Galectins, which are involved in apoptosis, cell adhesion and T-cell activation suppression, function by binding beta-galactosides. 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 apoptosis. Additionally, oligosaccharides from human milk bind to microbes to promote growth of normal flora and inhibit pathogens in the gastrointestinal tract. This array provides a powerful tool for researchers in glycobiology and other fields.