N-Glycan Array

 

 

N-glycosylation is a post-translational modification in which sugar molecules are covalently attached to the specific asparagine residues of a protein. N-linked glycans are attached to nitrogen (N) atoms in asparagine residues of particular amino acid sequences. These sequences include Asn–X–Ser, Asn–X–Thr, or in rare instances, Asn–X–Cys, where X can be any amino acid except proline. All eukaryotic N-glycans begin with a GlcNAc–Asn unit which is further extended with varieties of sugar molecules to form high-mannose, complex, and hybrid N-glycans.

 

N-glycans play essential roles in eukaryotic cells. Intrinsically, N-glycans maintain protein stability and solubility under different temperatures and pHs. They are also critical structural components of the cell barrier. Extrinsic effects of N-glycans are related to protein trafficking and cell signaling. Although N-glycans are crucial for maintaining normal physiological homeostasis, alterations of N-glycan expression are manifest in various pathological conditions. For example, aberrant N-glycosylation is observed in multiple types of cancers. Abnormally expressed N-glycans have been linked to specific autoimmune diseases. Mutation of critical enzymes for N-glycosylation contributes to the congenital disorders of glycosylation. Identifying and understanding the respective interaction of abnormally expressed N-glycans may unveil novel molecular mechanisms for therapeutic development.

 

ZBiotech has developed a robust microarray platform that allows researchers to explore the interactions between 114 structurally – defined N-glycans and biological samples, such as proteins, antibodies, cells, cell lysate, serum, vesicles, bacteria, or viral particles. Each array contains 8 or 16 identical subarrays, enabling the simultaneous analysis of multiple samples. The N-glycan array provides high-throughput and reliable glycan-binding information with a simple assay format that only requires a small sample volume. Results can be obtained in only a few hours, making investigating N-glycan binding easy and efficient. The N-glycan array can be customized to meet individual client needs. Assay services are available upon request.

 

 

Features

•  114 distinct N-glycan structures

•  Unrivaled sensitivity and specificity;

•  Simple assay format;

•  Small sample volume;

•  Customizable (select N-glycans for a specific microarray format)

•  Assay service available;

 

Applications

•  Evaluate binding specificities of N-glycan interacting proteins

•  Evaluate binding specificities of N-glycan interacting antibodies

•  Study virus – N-glycan interactions

•  Study bacteria – N-glycan interactions

•  Study vesicle – N-glycan interactions

•  Study cell – N-glycan interactions

 

 

 

Using N-glycan array to determine the binding specificity of Hippeastrum hybrid Lectin (HHL)

 

The N-glycan array was assayed with biotinylated Hippeastrum hybrid Lectin (HHL) (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. HHL binds to high-mannose and complex N-glycans.

 

 

 

 

 

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

 

 

 

 

 

 

10602-8S         N-Glycan Array Slide (8 samples)

10602-16S        N-Glycan Array Slide (16 samples)

10602-8K         N-Glycan Array *Assay Kit (8 samples)

10602-16K        N-Glycan Array *Assay Kit (16 samples)

 

* The assay kit contains a microarray slide, a bottle of blocking buffer, a bottle of assay buffer, a hybridization chamber, and sealing films. The hybridization chamber is a device that holds the array slide, assay buffer, and samples to be analyzed. 

 

 

 

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

Protocol & User Manual (download the manual)