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Sulfated Glycan Library Products

Comprehensive Sulfated Glycan Libraries for Precision Biomarker and Drug Discovery

Sulfation is one of the most crucial and tightly regulated post-translational modifications in the glycocalyx, profoundly influencing the biological function of proteins and lipids. Sulfated glycans, characterized by the attachment of sulfate groups (OSO3-) to hydroxyl groups on specific sugar residues, dictate molecular shape and charge, acting as high-affinity ligands for various receptors and proteins. These charged carbohydrate epitopes are central regulators in a vast array of physiological and pathological processes, including:

  • Immune response & inflammation: Sulfated structures, such as those found on high endothelial venules, are essential for leukocyte extravasation via interactions with selectins. Abnormal sulfation can drive chronic inflammatory diseases.
  • Cell-cell communication: They serve as recognition motifs, mediating cell adhesion, migration, and signaling cascades crucial for embryonic development and tissue maintenance.
  • Viral and pathogen entry: Specific sulfated glycans often function as cellular receptors or co-receptors, utilized by viruses and bacteria to gain entry into host cells.
  • Disease markers: Alterations in sulfotransferase and sulfatase activity result in aberrant sulfation patterns that are distinct signatures of numerous diseases, most notably advanced-stage cancers, chronic inflammatory conditions, and neurodegenerative disorders.

Sulfated N-glycans identified in IgG. (OA Literature)Fig.1 The structure of sulfated N-glycans identified in human serum IgG.1

Our sulfated glycan library is not merely a collection of compounds; it is a gateway to decoding the sulfation landscape, offering unparalleled structural definition for accelerating fundamental research and translational efforts. Accurate, reproducible, and translational studies demand high-purity glycan standards for rigorous assay development and reliable data interpretation. Our Glycan Libraries are specifically engineered to resolve these analytical constraints by providing:

Absolute structural purity and specificity

We utilize advanced chemical and enzymatic synthesis pathways to ensure that the precise location of the sulfate group and glycosidic linkages are defined. Each lot is rigorously analyzed to confirm purity and its exact linkage and sulfation position, eliminating the ambiguity inherent in naturally extracted samples.

Traceability and quantitative method validation

The standards serve as essential reference points for generating calibration curves, determining limits of detection and limits of quantification, and validating analytical methods such as LC-MS and capillary electrophoresis.

Access to rare and biologically relevant epitopes

Many critical sulfated epitopes are present in minuscule amounts in natural sources or are challenging to isolate. Our library provides ready access to these complex, functional structures, allowing researchers to study molecules critical for specific disease pathways (e.g., specific sulfated Lewis antigens).

Sulfated Glycan Library Structure and Composition

The future of clinical glycomics relies on robust, quantitative assays. While MS-based techniques offer high sensitivity, matrix effects and ionization suppression can compromise accuracy. Our isotope-labeled sulfated glycan standards represent a paradigm shift by providing a solution for absolute, high-precision quantification. We are developing a library of standards labeled with stable isotopes, such as the C-13 labeled glycan standards. These standards are chemically identical to their native (unlabeled) counterparts but possess a predictable mass shift, allowing them to be measured simultaneously and distinguished from the endogenous target molecule within the same LC-MS/MS run.

In addition, our library is meticulously curated, focusing on the functional significance of specific sulfation patterns and core glycan structures, providing researchers with the exact tools needed for targeted investigation.

N-glycan motifs

Covers a spectrum from high-mannose to complex and hybrid structures featuring terminal sulfation. Examples include sulfated LacNAc repeats or terminal GalNAc-6-S residues found on specific membrane glycoproteins, often implicated in cell adhesion and inflammatory signaling.

O-glycan motifs

Features core 1, 2, 3, and 4 O-glycans, the fundamental structures of mucins. The library contains crucial modifications like sulfated GalNAc at the O-linkage point and Gal sulfation at C4 or C6 positions, critical components of the tumor microenvironment.

Glycolipid & specialized epitopes

This includes oligosaccharides that mimic structures found on sulfatides and specific signaling lipids. Key specialized epitopes include various sulfated Lewis antigens, which are highly associated with GI tract malignancies.

The location of the sulfate group is as important as its presence. Our library guarantees positional specificity, essential for functional studies.

Table 1 Types and applications of sulfated glycan library.

Sulfation Position Example Epitope & Biological Role Relevant Core Structures Applications
C6-Sulfation GlcNAc-6-S & Gal-6-S: Essential for L-selectin ligand binding, facilitating lymphocyte homing to lymph nodes and sites of inflammation. N-Glycans, O-Glycans Immuno-oncology, Chronic Inflammation
C4-Sulfation GalNAc-4-S: A distinctive feature of certain pituitary hormones and specialized O-glycans that influence protein stability and turnover. Mucin-type O-Glycans Hormone Signaling, Protein Stability
C3-Sulfation Gal-3-S & GlcNAc-3-S: A key feature of sulfatides found in the nervous system, and certain sulfated Lewis antigens linked to cancer progression. Glycolipids, N/O-Glycans Neurobiology, Pancreatic Cancer Biomarkers
Multiple/Disulfation Structures containing disulfated or trisulfated residues. High charge density structures are often involved in high-affinity protein binding. Complex N-Glycans, O-Glycans High-Affinity Ligand Screening, Drug Targeting

We offer a tiered product line tailored to every phase of glycomics research, from initial screening to clinical method validation.

  • Unlabeled Sulfated Glycan Library

Available as individual standards or pre-plated libraries in 96-well formats. Provides the broadest structural diversity of unique sulfated epitopes and is available in high-volume, bulk formats suitable for large-scale screening and initial binding affinity studies.

  • Isotope-Labeled Sulfated Glycan Standards

Chemically synthesized and validated to serve as certified reference materials for quantitative glycoproteomics.

De novo synthesis of specific sulfation patterns on bespoke core structures (N-linked, O-linked, or synthetic scaffolds). We also provide functionalization with biotin, various Fluorescent Probes (e.g., APTS, 2-AB), photoaffinity labels, or conjugation to carrier proteins (BSA, KLH) for immunogenicity studies and immunoassays.

  • Other Glycan Library

We provide various glycan libraries to support your project, such as N-Glycan Libraries, O-Glycan Libraries, Mannose Glycan Libraries, Glycosaminoglycan Libraries, Methylated Glycan Libraries, etc.

Standardize Your Glycomics, Accelerate Your Discovery.

Creative Biolabs provides structurally defined, high-purity, and quantitatively labeled glycan standards. We offer the definitive solution for reliable glycomics and accelerate your biomarker and therapeutic discoveries with the industry-leading sulfated glycan library. Please contact our scientific team today for a consultation.

Reference

  1. Wang, Jing-Rong et al. "A method to identify trace sulfated IgG N-glycans as biomarkers for rheumatoid arthritis." Nature Communications vol. 8,1 631. 20 Sep. 2017. Distributed under an Open Access license CC BY 4.0, Fig. 4a is unmodified. https://doi.org/10.1038/s41467-017-00662-w
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