Glycosphingolipid Microarray
To satisfy our customers' scientific needs in exploring the structures of glycosphingolipids (GSLs), CD BioGlyco's dedicated research teams have developed GSLs microarray analysis techniques to help customers analyze multiple samples simultaneously and provide valuable glycan-binding information. Our efficient and professional services will help our clients accelerate their research progress.
GSLs are ubiquitous glycoconjugates found on cell membranes and they have important functions in many biological processes such as signal transduction, cell adhesion, embryonic development, and carcinogenesis. Understanding the role and immunological interactions of abnormally expressed glycolipids may be critical for the development of therapeutic agents for cancer and neurological diseases. However, identifying unknown GSL-glycan structures remains a major challenge.
Over the past few years, developments in MS-based technologies have offered valuable insights into the structural analysis of GSLs through the combination of efficient separation techniques and high-resolution MS. However, the complexities of biosynthesis, structure, and function of GSL increase the difficulty of GSL structural analysis.
Our GSL microarray integrates a structurally defined, curated collection of GSLs covalently immobilized onto solid surfaces, including glass substrates, forming dense, multiplexed arrays. This platform facilitates simultaneous, high-throughput screening of target molecule binding specificities across diverse GSL architectures. Engineered for exceptional specificity and sensitivity, the arrays detect subtle variations in glycan recognition events. The methodology remains compatible with orthogonal analytical techniques—notably mass spectrometry—delivering structural validation and granular analysis of GSL glycans. Rigorous immobilization chemistry ensures reproducible ligand presentation, enabling robust interrogation of glycan-protein interactions.
We offer a comprehensive suite of services centered around the GSL microarray. We accommodate various sample types, including purified proteins, antibodies, and complex biological fluids such as serum, plasma, or cell lysates. Our services include the determination of glycan-binding specificity, glycan-binding affinity, and the identification of novel GSL-binding partners. Our platform is well-suited for a wide range of applications, from fundamental research to preclinical and clinical studies. We are committed to working closely with clients to design the most effective experimental plan to achieve their research goals.
Our streamlined workflow is designed to provide a seamless experience, guiding your project from initial sample submission to the delivery of actionable data.
Your sample, which can be a purified protein, antibody, or complex mixture such as serum, is prepared and labeled with a fluorescent tag. This ensures that any binding events on the array can be accurately detected by a scanner.
The labeled sample is incubated on the GSL microarray slide under optimized conditions. During this step, any GSL-binding proteins or molecules in your sample will bind specifically to their corresponding glycans on the array.
Non-specifically bound molecules are washed away, and the microarray is scanned with a high-sensitivity fluorescent scanner. This generates a raw data image of the binding signals.
The raw image data is processed using specialized bioinformatics software. This involves quantifying the binding intensity for each GSL spot, normalizing the data, and performing statistical analysis to identify significant binding interactions.
We deliver a detailed report that includes the raw data, processed results, and a clear visualization of the binding profile. Our expert team is available to help you interpret the findings and discuss their biological implications.
DOI.: 10.1038/s41467-017-02747-y
Journal: Nature Communications
Published: 2018
IF: 14.7
Results: This study introduces a multiplex glycan bead array platform for high-throughput analysis of glycan-binding proteins. The authors covalently conjugated 184 diverse glycans to spectrally coded Luminex beads, enabling simultaneous screening of glycan-binding protein interactions across 384 samples per assay. They validated MGBA's specificity using 39 plant lectins (e.g., RCA-I binding to Gal-β4-GlcNAc motifs), 13 recombinant antibodies, and mammalian glycan-binding proteins (e.g., siglec-5, E-selectin), demonstrating reproducible glycan recognition profiles. The platform's utility was highlighted by profiling natural anti-glycan antibodies in 961 human sera, revealing IgM clusters associated with blood group antigens (e.g., anti-BGH antibodies). Crucially, MGBA identified ovarian cancer biomarkers, showing that elevated IgG against glycan #11 (Gal-α3-Gal-β4-Glc) correlated with poor survival (HR=4.12, p=0.002), while anti-blood group-A antibodies (#54) predicted better outcomes. This scalable technology bridges glycomics and clinical research by enabling population-scale glycan-binding protein studies.
While our GSL microarray analysis service provides critical insights into aberrant glycan expression patterns, translating these findings into actionable therapeutic strategies often requires targeting the underlying glycosylation machinery. This is where our specialized suite of Metabolic Interconversion Inhibitor Development Services becomes invaluable. We develop targeted agents against key nucleotide sugar transporters and metabolizing enzymes, including inhibitors for:
CD BioGlyco is committed to technological innovation and development in the field of glycobiology. Our GSL microarray analysis service allows for simultaneous large-scale analysis, providing glycan patterns and detailed linkage information of GSL-glycans. Please contact us directly if you need technical support, we will try our best to provide you with the best solution.
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