Microarray-based Glycoproteomics Service
As a trusted supplier in the field of microarrays, CD BioGlyco is committed to designing and developing various effective biological microarray products and providing corresponding testing services. Our microarray detection platform provides a full range of microarray-based analysis services to help our customers reduce costs while using advanced technologies for related research. We are confident to provide you with high-quality products and high-quality services to accelerate the output of research results.
Carbohydrate post-translational modifications on proteins are important determinants of protein function in normal and disease biology. Protein glycosylation is the enzymatic addition of sugars or oligosaccharides to proteins. Altered glycosylation usually occurs in the early stages of disease development. For example, certain tumor-associated glycans have been shown to be expressed in the precursor lesions of different types of cancer and have become powerful early diagnostic markers. A variety of lectins can be used as detection probes, and each probe is directed to a different glycan group to establish a lectin binding profile for the capture protein. The antibody array used for glycan detection is very effective for analyzing the variation of specific glycans on a variety of proteins. The main goal of the high-throughput analysis is usually related to the identification of novel biomarkers with therapeutic and/or diagnostic value. Lectin microarray technology is expected to become an important tool for glycosylation research and identification of tumor cell surface markers. Efficient and multiple studies are performed on the glycans of a single protein in a complex mixture. The antibody microarrays of multiple proteins are used to capture, and then lectin or glycan-binding antibodies are used for detection.
Lectin microarrays constitute foundational elements within our analytical platform. We deploy an expansive array of lectins – carbohydrate-binding proteins exhibiting discrete specificity for defined glycotopes – to interrogate intricate glycan topologies within a singular, multiplexed assay. This methodology facilitates the concurrent, expeditious interrogation of manifold lectin-glycan recognition events, furnishing an exhaustive representation of a specimen's glycomic signature. Lectin microarrays prove exceptionally potent for expansive screening initiatives and discerning pathological glycoform aberrations.
Protein microarrays complement our analytical arsenal. These substrates, arrayed with multitudinous distinct probes encompassing antibodies and lectins, facilitate the selective sequestration of discrete glycoproteins from convoluted biological matrices. This targeted capture mechanism enables focused scrutiny of protein-glycan interplay. This replicable, highly parallelized paradigm confers inestimable utility for extensive biomarker verification campaigns and the systematic evaluation of voluminous sample cohorts.
MS augments our microarray-centric paradigm. Ensuing enrichment and microarray-mediated capture, specimens routinely undergo MS-based deconstruction. This delivers granular architectural intelligence concerning glycan configurations and their precise loci of adduction. This synergistic strategy guarantees clients procure not merely a panoramic glycosylation profile, but concurrently, profound, site-resolved structural intelligence – a duality paramount for substantive scientific elucidation.
We provide customers with glycan microarray services to study the binding properties of potential glycan-binding proteins. We have the ability to analyze cells using high-throughput lectin microarrays, and can also be used to analyze the glycosylation characteristics of samples of interest. Our lectin microarrays include custom and semi-custom. Customized lectin microarray services use non-contact multi-channel printing equipment. The advantage of our customized service is that we can customize microarray products with a specific layout, size or substrate type. You can choose whether we can provide a glass slide substrate suitable for your sample, provide a customized substrate coating, or print directly on the substrate provided by the customer. You can choose probe samples from our internal glycan or lectin library, or provide your own samples as probes. After the microarray is made, you can also choose our microarray detection service, including sample pretreatment, hybridization, cleaning and data analysis.
The microarray-based glycoproteomics service is executed through a streamlined, multi-step process to ensure a high level of quality and data integrity. Our typical workflow includes:
The process begins with the careful preparation of client samples, such as serum, cell lysates, or tissue extracts. Glycoproteins are often digested with proteases to generate a mixture of glycopeptides, which are more amenable to downstream analysis.
To focus the analysis, we enrich for glycoproteins or glycopeptides from the complex sample matrix. This is a critical step that removes non-glycosylated proteins, allowing for a deeper and more targeted analysis of the glycosylated components.
The enriched samples are then applied to our custom-designed lectin or protein microarrays. The labeled glycoproteins or glycopeptides bind to the immobilized probes (lectins, antibodies), and the resulting binding signals are detected and quantified using a high-sensitivity scanner.
Following microarray analysis, the captured molecules can be further analyzed by mass spectrometry to determine the exact glycan structures and their corresponding protein sites. This provides unparalleled depth and confidence in the results.
The raw data from the microarray and mass spectrometer are meticulously processed and analyzed. We use advanced bioinformatics tools to provide comprehensive reports, including glycan profiles, differential expression analysis, and structural annotations.
DOI.: 10.1016/j.mcpro.2022.100433 External Link
Journal: Molecular & Cellular Proteomics
Published: 2022
Results: This research employed multi-lectin affinity chromatography and HILIC enrichment coupled with LC-MS/MS to profile the N-glycoproteome across normal, asymptomatic, and symptomatic Alzheimer's disease (AD) human brains. The study identified >300 glycoproteins and ~1,900 glycoforms, revealing that brain glycans are predominantly high-mannose structures (notably Man5, >20% of glycoforms) and bisected/fucosylated complex glycans, with minimal sialylation (<9%). Critically, site-specific glycosylation alterations were observed across AD stages, including changes in fucosylation frequency, bisection, and antennae number (e.g., increased branching in symptomatic AD). These findings highlight how glycoproteomics uncovers AD-associated glycan dysregulation, providing insights into disease mechanisms and potential biomarkers.
Microarray-based glycoproteomics service delivers high-resolution mapping of site-specific glycosylation across complex biological samples—revealing glycoform heterogeneity critical for biomarker discovery and therapeutic monitoring. To extend this structural precision into dynamic functional studies of glycan-mediated interactions, we offer the Liquid Glycan Display Array (LiGA) platform, which engineers fluidic membrane environments to mimic native cell-surface conditions. This integrated approach enables:
CD BioGlyco provides glycoproteomics services based on microarrays. We have a large team of scientists with a solid academic foundation and cooperate with researchers in basic biology and biomedical projects from all over the world. The advantage of choosing an analytical testing outsourcing testing service is that there is no need to consider any other costs (such as equipment and laboratory space), and it saves supervision or management. This advanced technology can quickly turn around and provide reliable results, thereby saving valuable time and resources. Please contact us for more detailed information.
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