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O-Glycan Library Products

The Critical Role of O-Glycans in Biology and Disease

Glycosylation is one of the most common and complex post-translational modifications, and O-linked glycosylation, in particular, plays an indispensable role in maintaining cellular functions and mediating intercellular communication. Understanding these Glycan Structures is the next frontier in biological research and drug development. O-glycans (primarily O-GalNAc, or mucin-type, initiated by GalNAc attachment, but also including O-GlcNAc) are dynamic structures attached to serine (Ser) or threonine (Thr) residues of proteins. Their complexity, which often involves branched and sialylated terminal structures, and structural diversity make them a crucial area of study:

Cell signaling and receptor function

O-glycans often shield or expose underlying protein domains, regulating the binding affinity and activation of receptors. The reciprocal O-GlcNAc modification acts as a crucial nutrient sensor, regulating protein stability, localization, and transcriptional activity in metabolic diseases and neurodegeneration.

Immune response and inflammation

Mucin-type O-glycans are heavily expressed on mucosal surfaces, acting as a crucial defense layer. Changes in their structures (e.g., expression of T antigen, Tn antigen) are critical markers in autoimmune conditions and tumor-mediated immune evasion, directly influencing innate and adaptive immune cell interactions.

Cancer biomarkers and therapeutics

Aberrant O-glycosylation is a hallmark of cancer, leading to the expression of truncated or novel structures like the sialyl-Tn antigen and structures displayed on MUC1 mucins. These specific O-glycan structures serve as high-potential biomarkers for tumor progression and metastasis, and are emerging targets for next-generation immunotherapies and diagnostics.

Workflow for O-linked glycan profiling. (OA Literature)Fig.1 Analytical procedures for O-linked glycans.1

O-Glycan Structural Diversity

Common O-glycan Structures
CAT#: GLJF-1125-HX367 CAT#: GLJF-1125-HX368 CAT#: GLJF-1125-HX369
CAT#: GLJF-1125-HX370 CAT#: GLJF-1125-HX371 CAT#: GLJF-1125-HX372
CAT#: GLJF-1125-HX373 CAT#: GLJF-1125-HX374 CAT#: GLJF-1125-HX375
CAT#: GLJF-1125-HX376 CAT#: GLJF-1125-HX377 CAT#: GLJF-1125-HX378
CAT#: GLJF-1125-HX379 CAT#: GLJF-1125-HX380 CAT#: GLJF-1125-HX381

For more structures, please refer to our O-Glycan Library Catalog.

Introducing Our Comprehensive O-Glycan Library

Our O-glycan library is meticulously assembled to provide researchers with the broadest possible range of defined, biologically relevant O-glycan structures. Designed for maximum flexibility and immediate use, our library supports discovery, validation, and high-throughput screening across proteomics, immunology, oncology, and neuroscience fields, accelerating the drug discovery pipeline.

Table 1 The core features and benefits of the O-glycan library.

Feature Description Advantage
Broad Coverage & Complexity Includes all O-glycan core structures, major tumor-associated antigens (Tn, sTn), blood group antigens, and highly complex, branched, sulfated, or fucosylated structures derived from cell lines and tissues. Maximize target identification, providing comprehensive coverage to minimize false negatives and ensure true biological relevance in screening assays.
Exceptional Purity & Validation Every compound is rigorously purified and structurally validated via multiple orthogonal analytical techniques, including NMR spectroscopy, Mass Spectrometry (MS), and UPLC/HPLC analysis. Ensure assay specificity, reproducibility, and compliance, eliminating ambiguity and batch variability from your most critical experiments.
Versatile Formats Available as purified free glycans, synthetic glycopeptides with defined peptide backbones, and pre-printed high-density microarrays, alongside custom solid-phase resin conjugates. Seamless integration into diverse experimental workflows across drug discovery, diagnostics, and fundamental research.
Scalability & Customization Available in both research-scale quantities and bulk supply for industrial-scale. Supports projects from initial pilot studies, through dose-response optimization, to large-scale reagent production and late-stage drug development.

Diverse O-Glycan Product Portfolio

We offer several product categories to meet the specific needs of various research platforms, ensuring we have the right format for your assay.

  • Purified O-Glycan Standards (Free Glycans)

These are chemically or enzymatically released and meticulously purified glycan chains, ideal for use as quantitative internal standards and highly accurate mass spectrometry references.

  • Synthetic O-Glycopeptides (Defined Backbone)

This category features synthetically linked O-glycan structures attached to a defined peptide sequence (Ser/Thr), precisely mimicking the natural, site-specific presentation of glycosylation on a protein. This format is crucial for studying protein-glycan interactions that are context-dependent and site-specific.

  • O-Glycan Microarrays (High-Throughput Screening)

Our high-density O-glycan arrays present hundreds of unique, structurally defined glycan compounds simultaneously on a single, functionalized glass slide. This state-of-the-art tool allows for rapid, parallel, and quantitative screening of the specificity of antibodies, lectins, and endogenous glycan-binding proteins.

  • Tagged and Derivatized O-Glycan Derivatives

To maximize experimental flexibility and facilitate robust detection and immobilization across various platforms, we offer O-glycans modified with versatile tags:

  • Biotinylated glycans: Essential for high-sensitivity detection using streptavidin systems in ELISA, Western Blots, and for efficient pull-down assays and surface plasmon resonance (SPR) immobilization.
  • Fluorescently labeled glycans: Perfect for real-time visualization, high-content screening, confocal microscopy, and flow cytometry assays.
  • Amino- or thiol-functionalized glycans: Provide reactive handles for robust, site-specific conjugation to resins, beads, liposomes, nanocarriers, or custom surfaces.

Our Technological Advantages

Cutting-edge chemical and enzymatic synthesis

We utilize proprietary, cutting-edge synthetic methodologies, including solid-phase and solution-phase techniques, combined with specialized enzymatic approaches. This strategy enables us to create structures that are often inaccessible through natural isolation and to handle challenging glycosidic linkages with guaranteed high purity and homogeneity, minimizing process-related contaminants.

State-of-the-art quality control (QC)

Every synthesized batch undergoes rigorous, multi-faceted quality checks. We provide full documentation on lot-to-lot consistency and perform absolute structural confirmation via high-resolution mass spectrometry, advanced 2D-NMR spectroscopy, and UPLC/HPLC analysis with diode array detection. We are committed to transparency in purity reporting.

Dedicated custom synthesis services

Cannot find the exact structure, label, or quantity you need? Our team of expert glyco-chemists specializes in bespoke synthesis of unique, rare, or highly challenging O-glycan structures and glycopeptides. This includes synthesis of isotopically labeled glycans for advanced MS studies and novel glycan linker chemistries for proprietary platforms.

Request a Quote & Product Consultation

Whether you are targeting a specific cancer antigen, profiling global protein glycosylation, or developing a novel diagnostic tool, Creative Biolabs' comprehensive O-glycan library is the essential resource for precision and reliability. In addition, we also provide other specialized glycan libraries that can support your research, such as N-Glycan, HMO-Glycan, Mannose Glycan, Glycosaminoglycan, Tag based Glycan Libraries, etc. Please contact our specialist team today to receive detailed technical specifications, our complete catalog, transparent pricing information, or to discuss custom synthesis inquiries tailored to your project goals.

Reference

  1. Hu, Xinyue et al. "Analysis Strategy for Identifying the O-Linked Glycan Profile and O-glycosylation Sites on Recombinant Human Follicle Stimulating Hormone-C-terminal Peptide (rhFSH-CTP)." Molecules (Basel, Switzerland) vol. 30,10 2141. 13 May. 2025. Distributed under an Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/molecules30102141
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