O-Glycan Array

10611

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O-glycan microarray technology is developed to help researchers explore the interactions between O-glycans and biological samples such as proteins, antibodies, cells, cell lysate, serum, vesicles, bacteria, or viral particles. The O-glycan array features 94 distinct O-glycan structures. Each array contains 8 or 16 identical subarrays, enabling the simultaneous analysis of multiple samples. The O-Glycan array provides high-throughput and reliable glycan-binding information with a simple assay format that only requires a small sample volume. The O-glycan array can be customized to meet individual client needs. Assay services are available upon request.

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Description
Structures
Examples
Citations
Document

Description

Glycosylation is a post-translational modification in which sugar molecules are covalently attached to the protein, lipid, and nucleic acid. O-linked glycosylation adds an oligosaccharide to the oxygen (O) atom of the hydroxyl group in a serine or threonine residue. This process happens in the endoplasmic reticulum, golgi apparatus, and sometimes in the cytoplasm. O-glycosylated proteins are usually found on the cell surface and in the extracellular matrix, where they play essential roles in tissue structure support, receptor recognition, and signaling regulation.

One of the most famous examples of O-glycosylated proteins is mucin, which coats the mucosal surface of the gastrointestinal and respiratory systems. These proteins are heavily glycosylated with O-glycan structures on serine and threonine residues. Impairment of the O-glycosylation on mucins negatively affects their function. Truncated Mucin O-glycans are manifest in tumor tissues, and these abnormally expressed O-glycans promote self-tolerance and prevent the immune system from attacking the tumor cells. In Alzheimer’s disease, several changes in O-glycans of the accumulated tau protein have been detected, which escalates disease progression by promoting neuroinflammation. Identifying and understanding the respective interaction of abnormally expressed O-glycans may unveil novel molecular mechanisms for therapeutic development.

ZBiotech has developed a robust microarray platform that allows researchers to explore the interactions between O-glycans and biological samples such as proteins, antibodies, cells, cell lysate, serum, vesicles, bacteria, or viral particles. The O-glycan array features 94 distinct O-glycan structures. Each array contains 8 or 16 identical subarrays, enabling the simultaneous analysis of multiple samples. The O-Glycan array provides high-throughput and reliable glycan-binding information with a simple assay format that only requires a small sample volume. The O-glycan array can be customized to meet individual client needs. Assay services are available upon request.

Features

  • Unrivaled sensitivity and specificity;
  • Simple assay format;
  • Small sample volume;
  • Customizable (select O-glycans for a specific microarray format)
  • Assay service available;

Applications

  • Evaluate binding specificities of O-glycan interacting proteins;
  • Evaluate binding specificities of O-glycan interacting antibodies;
  • Study virus – O-glycan interactions;
  • Study bacteria – O-glycan interactions;
  • Study vesicle – O-glycan interactions;
  • Study cell – O-glycan interactions;

Structures

List of O-glycan structures on the array (download the PDF)

ID Structure
O1 GalNAcα-Ser
O2 GalNAcα-Thr
O3 Neu5Acα2-6GalNAcα-Ser
O4 Neu5Acα2-6GalNAcα-Thr
O5 Galβ1-3GalNAcα-Ser
O6 Galβ1-3GalNAcα-Thr
O7 Neu5Acα2-3Galβ1-3GalNAcα-(CH2)3NH-
O8 Neu5Gcα2-3Galβ1-3GalNAcα-(CH2)3NH-
O9 Neu5Acα2-3(GalNAcβ1-4)Galβ1-3GalNAcα-Ser
O10 Fucα1-2Galβ1-3GalNAcα-Ser
O11 GalNAcβ1-3(Fucα1-2)Galβ1-3GalNAcα-Ser
O12 Galα1-3(Fucα1-2)Galβ1-3GalNAcα-Ser
O13 GlcNAcβ1-3Galβ1-3GalNAcα-Ser
O14 Galβ1-4GlcNAcβ1-3Galβ1-3GalNAcα-Ser
O15 Galα1-3Galβ1-4GlcNAcβ1-3Galβ1-3GalNAcα-Ser
O16 Neu5Acα2-3Galβ1-4GlcNAcβ1-3Galβ1-3GalNAcα-Ser
O17 GalNAcβ1-4(Neu5Acα2-3)Galβ1-4GlcNAcβ1-3Galβ1-3GalNAcα-Ser
O18 Fucα1-2Galβ1-4GlcNAcβ1-3Galβ1-3GalNAcα-Ser
O19 Galβ1-4(Fucα1-3)GlcNAcβ1-3Galβ1-3GalNAcα-Ser
O20 Fucα1-2Galβ1-4(Fucα1-2)Galβ1-4GlcNAcβ1-3Galβ1-3GalNAcα-Ser
O21 Neu5Acα2-6(Neu5Acα2-3(GalNAcβ1-4)Galβ1-3)GalNAcα-Ser
O22 GlcNAcβ1-6(Galβ1-3)GalNAcα-Ser
O23 GlcNAcβ1-6(Galβ1-3)GalNAcα-Thr
O24 Galβ1-4GlcNAcβ1-6(Galβ1-3)GalNAcα-Ser
O25 GlcNAcβ1-3GalNAcα-Ser
O26 GlcNAcβ1-3GalNAcα-Thr
O27 Galβ1-4GlcNAcβ1-3GalNAcα-Ser
O28 Galα1-3Galβ1-4GlcNAcβ1-3GalNAcα-Ser
O29 Neu5Acα2-3Galβ1-4GlcNAcβ1-3GalNAcα-Ser
O30 Neu5Acα2-6Galβ1-4GlcNAcβ1-3GalNAcα-Ser
O31 GalNAcβ1-4(Neu5Acα2-3)Galβ1-4GlcNAcβ1-3GalNAcα-Ser
O32 Galβ1-4(Fucα1-3)GlcNAcβ1-3GalNAcα-Ser
O33 Fucα1-2Galβ1-4(Fucα1-3)GlcNAcβ1-3GalNAcα-Ser
O34 Fucα1-2Galβ1-4GlcNAcβ1-3GalNAcα-Ser
O35 GalNAcα1-3(Fucα1-2)Galb1-4GlcNAcβ1-3GalNAcα-Ser
O36 Galα1-3(Fucα1-2)Galb1-4GlcNAcβ1-3GalNAcα-Ser
O37 Neu5Acα2-6(GlcNAcβ1-3)GalNAcα-Ser
O38 Neu5Acα2-6(Galβ1-4GlcNAcβ1-3)GalNAcα-Ser
O39 GlcNAcβ1-6(GlcNAcβ1-3)GalNAcα-Thr
O40 GlcNAcβ1-6GalNAcα-Ser
O41 Galβ1-4GlcNAcβ1-6GalNAcα-Ser
O42 Galα1-3Galβ1-4GlcNAcβ1-6GalNAcα-Ser
O43 GalNAcβ1-4(Neu5Acα2-3)Galβ1-4GlcNAcβ1-6GalNAcα-Ser
O44 Galβ1-4(Fucα1-3)GlcNAcβ1-6GalNAcα-Ser
O45 Neu5Acα2-3Galβ1-4(Fucα1-3)GlcNAcβ1-6GalNAcα-Ser
O46 Fucα1-2Galβ1-4(Fucα1-3)GlcNAcβ1-6GalNAcα-Ser
O47 Fucα1-2Galβ1-4GlcNAcβ1-6GalNAcα-Ser
O48 GalNAcα 1-3(Fucα1-2)Galβ1-4GlcNAcβ1-6GalNAcα-Ser
O49 H2N-APGST*APP-NH2 (*GalNAcα)
O50 H2N-TSAPDT*RPAP-NH2 (*GalNAcα)
O51 Neu5Acα2-3Galβ1-3GalNAcα-Ser
O52 Neu5Acα2-6Galβ1-3GalNAcα-Ser
O53 Neu5Acα2-6Galβ1-4GlcNAcβ1-3Galβ1-3GalNAcα-Ser
O54 Neu5Acα2-3Galβ1-4(Fucα1-3)GlcNAcβ1-3Galβ1-3GalNAcα-Ser
O55 Neu5Acα2-3Galβ1-3(Neu5Acα2-6)GalNAcα-Ser
O56 Neu5Acα2-6Galβ1-3(Neu5Acα2-6)GalNAcα-Ser
O57 Neu5Acα2-3Galβ1-3(GlcNAcβ1-6)GalNAcα-Ser
O58 Neu5Acα2-3Galβ1-3(Galβ1-4GlcNAcβ1-6)GalNAcα-Ser
O59 Neu5Acα2-3Galβ1-4GlcNAcβ1-6(Neu5Acα2-3Galβ1-3)GalNAcα-Ser
O60 Galβ1-4(Fucα1-3)GlcNAcβ1-6(Neu5Acα2-3Galβ1-3)GalNAcα-Ser
O61 Neu5Acα2-6Galβ1-3(GlcNAcβ1-6)GalNAcα-Ser
O62 Neu5Acα2-6Galβ1-3(Galβ1-4GlcNAcβ1-6)GalNAcα-Ser
O63 Neu5Acα2-3Galβ1-4GlcNAcβ1-6(Neu5Acα2-6Galβ1-3)GalNAcα-Ser
O64 Neu5Acα2-6Galβ1-4GlcNAcβ1-6(Neu5Acα2-6Galβ1-3)GalNAcα-Ser
O65 Neu5Acα2-3(GalNAcβ1-4)Galβ1-4GlcNAcβ1-6(Neu5Acα2-6Galβ1-3)GalNAcα-Ser
O66 Galβ1-4(Fucα1-3)GlcNAcβ1-6(Neu5Acα2-6Galβ1-3)GalNAcα-Ser
O67 Fucα1-2Galβ1-4(Fucα1-3)GlcNAcβ1-6(Neu5Acα2-6Galβ1-3)GalNAcα-Ser
O68 Fucα1-2Galβ1-4GlcNAcβ1-6(Neu5Acα2-6Galβ1-3)GalNAcα-Ser
O69 Neu5Acα2-3(GalNAcβ1-4)Galβ1-3(GlcNAcβ1-6)GalNAcα-Ser
O70 Neu5Acα2-3(GalNAcβ1-4)Galβ1-3(Galβ1-4GlcNAcβ1-6)GalNAcα-Ser
O71 Neu5Acα2-3(GalNAcβ1-4)Galβ1-3(Neu5Acα2-3Galβ1-4GlcNAcβ1-6)GalNAcα-Ser
O72 Neu5Acα2-3(GalNAcβ1-4)Galβ1-4GlcNAcβ1-6(Neu5Acα2-3(GalNAcβ1-4)Galβ1-3)GalNAcα-Ser
O73 Galβ1-4(Fucα1-3)GlcNAcβ1-6(Galβ1-3)GalNAcα-Ser
O74 Fucα1-2Galβ1-3(GlcNAcβ1-6)GalNAcα-Ser
O75 Fucα1-2Galβ1-3(Galβ1-4GlcNAcβ1-6)GalNAcα-Ser
O76 Galβ1-4(Fucα1-3)GlcNAcβ1-6(Fucα1-2Galβ1-3)GalNAcα-Ser
O77 Galα1-3Galβ1-4GlcNAcβ1-6(Galβ1-3)GalNAcα-Ser
O78 Neu5Acα2-3Galβ1-4(Fucα1-3)GlcNAcβ1-3GalNAcα-Ser
O79 GalNAcβ1-4GlcNAcβ1-3GalNAcα-Ser
O80 GlcNAcβ1-6(GlcNAcβ1-3)GalNAcα-Ser
O81 Galβ1-4GlcNAcβ1-3(Galβ1-3GlcNAcβ1-6)GalNAcα-Ser
O82 Galα1-3Galβ1-4GlcNAcβ1-3(Galα1-3Galβ1-3GlcNAcβ1-6)GalNAcα-Ser
O83 Neu5Acα2-6Galβ1-4GlcNAcβ1-3(Neu5Acα2-6Galβ1-3GlcNAcβ1-6)GalNAcα-Ser
O84 Neu5Acα2-3(GalNAcβ1-4)Galβ1-3GlcNAcβ1-3(Neu5Acα2-3(GalNAcβ1-4)Galβ1-3GlcNAcβ1-6)GalNAcα-Ser
O85 Galβ1-3(Fucα1-3)GlcNAcβ1-3 (Galβ1-4(Fucα1-3)GlcNAcβ1-6)GalNAcα-Ser
O86 Neu5Acα2-3Galβ1-3(Fucα1-3)GlcNAcβ1-3(Neu5Acα2-3Galβ1-4(Fucα1-3)GlcNAcβ1-6)GalNAcα-Ser
O87 Fucα1-2Galβ1-3GlcNAcβ1-3(Fucα1-2Galβ1-4GlcNAcβ1-6)GalNAcα-Ser
O88 Fucα1-2(GalNAcα1-3)Galβ1-3GlcNAcβ1-3(Fucα1-2(GalNAcα1-3)Galβ1-4GlcNAcβ1-6)GalNAcα-Ser
O89 Fucα1-2(Galα1-3)Galβ1-3GlcNAcβ1-3(Fucα1-2(Galα1-3)Galβ1-4GlcNAcβ1-6)GalNAcα-Ser
O90 Fucα1-2Galβ1-3(Fucα1-3)GlcNAcβ1-3(Fucα1-2Galβ1-4(Fucα1-3)GlcNAcβ1-6)GalNAcα-Ser
O91 Neu5Acα2-3Galβ1-4GlcNAcβ1-6GalNAcα-Ser
O92 Neu5Acα2-6Galβ1-4GlcNAcβ1-6GalNAcα-Ser
O93 Galα1-3(Fucα1-2)Galβ1-4GlcNAcβ1-6GalNAcα-Ser
O94 GalNAcβ1-4GlcNAcβ1-6GalNAcα-Ser

Examples

Using O-glycan array to determine the binding specificity of Artocarpus integrifolia Lectin (AIA)

The O-glycan array was assayed with biotinylated Artocarpus integrifolia Lectin (AIA) (10 μg/mL), followed by streptavidin (Cy3). The array was scanned with a microarray scanner at 532nm wavelength. Positive control showed binding signals as expected. AIA binds to terminal GalNAc-containing O-glycans.

Document

List of O-glycan structures on the array (download the PDF)

Protocol & User Manual (download the manual)