Strands of sugars and proteins, collectively termed the “glycocalyx” (sugar coat), surround the cell surface and play a fundamental role in cellular events such as embryonic development, cell adhesion, and viral and bacterial infections. The RayBio Glycobiology Arrays designed for the detection of glycans or glycan-protein interaction are available in three different formats. All 3 formats feature glass slide supports with fluorescent detection.
The glycans featured in the RayBio Glycan Arrays are the most frequently identified structures showing important binding function in literature. The glycans are spotted on the array, capturing glycan-binding proteins, for example the influenza virus, which binds to a variety of sialosides with a serotype-specific pattern. Another example are Galectins, which are involved in apoptosis, cell adhesion and T-cell activation suppression and function by binding beta-galactosides. The RayBio Glycan Arrays can be used with either a label-based method or with a sandwich-based method.
The RayBio Glycome Arrays allow researchers to efficiently obtain glycosylation profiles of several proteins in their samples. Capture antibodies which bind known glycosylated proteins are printed onto glass slides. After incubation with the samples, five unique biotin-labeled lectins are incubated with the array to allow binding to the glycans from the captured target proteins. Streptavidin-conjugated fluorescent dye (Cy3 equivalent) is then added to the array. Laser fluorescence scanning is used to visualize the signals. These signals are then compared to the array map to identify glycosylated proteins present in the samples.
For the RayBio Lectin Arrays, each well of a standard glass slide is spotted with 40 different lectins. The slides come with an 8-well removable gasket which allows for the process of 8 samples using one slide. Each lectin, together with the positive controls, is arrayed in duplicate. The RayBio Lectin Arrays provide a powerful tool for glycosylation determination, drug discovery and biomarker development; all with limited samples volumes required. They can be used with either a label-based method or with a sandwich-based method.