Lectin Array

Description

Glycosylation is one of the most abundant posttranslational modifications in eukaryotic cells. It is a complex process in which multiple glycosyltransferases work together to covalently add carbohydrate structures to proteins, lipids, or ribonucleic acids. Glycosylation is an intracellular process essential to all eukaryotic cells. The carbohydrate structures stabilize proteins to ensure proper folding for optimal activities. They also involve cellular signaling regulation to enforce tissue homeostasis. Determining the chemistry and biology of glycosylation is indispensable for understanding the biology of living organisms.

The discovery of ricin by Stillmark in 1888 marked the beginning of lectinology, a discipline dedicated to studying lectins’ chemical and biological functions. In 1952, Watkins and Morgan found that adding sugars can block the agglutination of erythrocytes caused by lectins. This milestone discovery unveiled the carbohydrate-binding specificity of lectins. Since then, hundreds of lectins have been purified and studied from plants, microorganisms, and animals. Lectins are now defined as carbohydrate-binding proteins, and each lectin recognizes a unique repertoire of carbohydrate structures.

For example, SNA (Sambucus Nigra lectin), MAL1 (Maackia Amurensis Lectin I), and MAL2 (Maackia Amurensis Lectin II) are sialoglycan-specific lectins. SNA recognizes terminal α-2,6 sialic acids (either Neu5Ac or Neu5Gc). In stark contrast, MAL1 and MAL2 preferentially recognize terminal α-2,3 sialic acids (either Neu5Ac or Neu5Gc). Another example is Calsepa (Calystegia Sepium lectin). Calsepa generally binds with all N-linked glycans without differentiating a specific subtype of N-glycans with or without terminal sialic acids. Compared with Calsepa, BanLec (Musa Paradisiaca lectin) preferentially recognizes high-mannose N-glycans and hybrid N-glycans without terminal sialic acids.

Lectins have been widely used to detect glycosylation because of their unique carbohydrate-recognizing properties. ZBiotech has developed a robust microarray platform that allows researchers to simultaneously profile glycosylation by multiple lectins. The lectin array utilizes a panel of 37 plant-based lectins immobilized on the array surface for high-throughput glycosylation analysis. Each lectin has been validated by glycan microarrays to ensure binding specificity. The proprietary coating substrate of this array outperforms other substrates with exceptional sensitivity without compromising specificity. Each lectin array contains 8 or 16 identical subarrays, enabling the analysis of multiple samples simultaneously and facilitating rapid results in a simple and easy-to-use format. Varieties of biological samples can be analyzed by the array. For example, proteins, antibodies, cells, cell lysate, serum, vesicles, bacteria, and viral particles. The Lectin array can be customized to meet individual client needs. Assay services are available upon request.

Features

• 37 lectins (validated by glycan microarrays)
• Unrivaled sensitivity and specificity;
• Simple assay format;
• Small sample volume;
• Customizable (select lectins for a specific microarray format)
• Assay service available;

Applications

• Evaluate glycosylation of proteins;
• Evaluate glycosylation of antibodies;
• Evaluate glycosylation of viral particles;
• Evaluate glycosylation of bacteria;
• Evaluate glycosylation of cells;
• Evaluate glycosylation of vesicles;