Glycosaminoglycan Library Products

The Next Frontier in Glycobiology: Precision Glycosaminoglycan (GAG) Library

Glycosaminoglycans (GAGs) are long, highly anionic polysaccharide chains and are the fundamental building blocks of the extracellular matrix (ECM). Unlike other biopolymers, GAG chains possess an astonishing degree of structural complexity, often referred to as the "Glyco-Code". This code is formed by variable sequences of sulfation and epimerization, enabling them to selectively bind to hundreds of growth factors, chemokines, adhesion molecules, and regulatory proteins. GAGs thereby orchestrate critical biological processes from neural function and inflammation to coagulation and tissue remodeling. Creative Biolabs' comprehensive GAG library is meticulously curated and chemically defined to provide researchers with the pure, structurally homogeneous GAG tools necessary to finally decode this essential molecular language. If your work involves complex cell signaling pathways, therapeutic development for chronic diseases, or the design of advanced regenerative scaffolds, access to defined GAG structures is the critical first step to discovery, reproducibility, and successful translation.

Constituent disaccharide units of the different GAGs. (OA Literature) Fig.1 The disaccharide units of different glycosaminoglycans.¹

Core Product Families Available in the Library

Our GAG library is meticulously structured to cover the full spectrum of biologically significant GAGs. By consolidating heparan sulfates (HS), chondroitin sulfates (CS), dermatan sulfates (DS), and other crucial GAGs like hyaluronic acid (HA) and keratan sulfates (KS) into this comprehensive offering, we empower researchers to conduct comparative studies with unmatched reliability. Each entry in the table below represents a gateway to understanding specific GAG-protein interactions that drive health and disease. Review the diverse families and applications below, and contact our specialists today to tailor a package that fits your precise research needs.

Table 1 Core GAG product library.

GAG Family	Product Type	Structural Focus	Significance and Application
HS & Heparin	Native HS	Broad-spectrum, heterogeneous physiological structures (GlcNAc, GlcA, IdoA).	For studying wide-ranging physiological interactions, cellular uptake, and matrix assembly in complex systems.
	Defined HS oligomers	Short, highly purified fragments (e.g., di-, tetra-, hexa-saccharides).	Essential for defining minimal protein-binding domains.
	Chemically modified HS	Variants with altered N-sulfation or specific O-sulfation profiles.	Pinpointing sulfation requirements for specific ligand binding, enabling targeted therapeutic design.
	Heparin	Highly sulfated variant of HS.	Benchmark for studies of coagulation, inflammation, and high-affinity protein binding assays.
CS & DS	CS-A (4-Sulfated) & CS-C (6-Sulfated)	Highly prevalent in cartilage/tendon.	Critical for studying osteoarthritis, joint health, tissue elasticity, and vascular functions.
	CS-D and CS-E (Di-Sulfated)	Rare, highly specialized structures.	Key tools for research into neuronal pathfinding, tumor angiogenesis, and high-affinity growth factor binding.
	DS / CS-B	Contains L-iduronic acid (IdoA).	Focuses on binding to collagen, regulating fibrin deposition, and mediating tissue remodeling/wound repair.
	Low/High-molecular-weight CS/DS	Fractionated by size.	Allows precise study of size-dependent effects on cell signaling, biomechanical properties, and bioavailability.
Other Vital GAGs	HA	Non-sulfated GAG, various molecular weights.	Crucial for cell migration, tissue hydration, viscoelasticity, and drug delivery applications.
Other Vital GAGs	KS	Unique GAG containing galactose.	Primarily used in studies of the cornea, bone development, and cartilage stability.

Key Features of Products

The dramatic biological activity of a GAG is dictated by its precise sequence and unique sulfation pattern. Generic, broad GAG preparations extracted from animal sources introduce inherent, unacceptable levels of heterogeneity and batch-to-batch variability into sensitive biological assays. Our library is specifically designed to overcome this critical challenge.

Exceptional purity and low contamination: We guarantee extremely high purity, validated against trace impurities and residual protein contaminants.
Defined structure & controlled heterogeneity: The library is a balanced collection, including:
- Naturally sourced, fractionated GAGs: Carefully size-fractionated to ensure uniform chain length and specific activity.
- Chemically and enzymatically modified variants: Designed to isolate the functional role of specific sulfation sites (N-sulfation, O-sulfation at C2, C3, C4, C6) and chain lengths, enabling structure-activity relationship studies.
Batch consistency and rigorous QC: Every lot undergoes stringent quality control using advanced analytical techniques such as high-resolution mass spectrometry and NMR spectroscopy, ensuring reliable, reproducible results across your entire research lifecycle.

Application Directions

Drug discovery and target validation

The GAG library is critical for rational drug design by enabling systematic screening to identify small molecules or peptides that selectively block or mimic high-affinity GAG-protein interactions. This includes developing safer GAG mimetics for anti-coagulation therapy and utilizing specific CS structures to study their roles in inhibiting axon regeneration after spinal cord injury or their association with amyloid plaque formation in neurodegenerative diseases like Alzheimer's and Parkinson's.

Infectious disease research

Many significant pathogens, including viruses and bacteria, exploit cell-surface GAGs as initial attachment sites, making them vital therapeutic targets. The library allows researchers to use structurally defined GAG fragments as molecular decoys for competitive inhibition, effectively preventing initial infection, which is essential for developing mechanism-based, broad-spectrum antivirals.

Tissue engineering and regenerative medicine

GAGs are foundational for advanced scaffold design due to their inherent ability to sequester, protect, and present key growth factors that direct cell fate and differentiation. Defined GAGs, such as specific CS-A/C or HS components, can be integrated into bio-scaffolds and hydrogels to mimic native ECM, thereby guiding mesenchymal stem cell (MSC) differentiation toward specific lineages like chondrocytes or osteoblasts, and accelerating tissue repair and wound healing by modulating cytokine gradients and regulating collagen fibril assembly.

Why Partner with Us?

We are a leader in glycochemistry, committed to empowering your research with the highest quality, best-characterized glycans available globally. By choosing our glycosaminoglycan library, you gain:

Accelerated discovery

Immediately access a panel of defined reagents, allowing you to bypass the complex, time-consuming, and often irreproducible steps of GAG purification and characterization.

Uncompromising reproducibility

Our strict analytical standards minimize assay variability, ensuring that your data is robust and reliable.

Integrated expertise

Partner with a team specializing in glycochemistry, glycan-protein interaction assays, and complex structural analysis, ready to support your most challenging projects.

Custom synthesis capability

If your research requires a structure not currently in the Library, we offer bespoke chemical and enzymatic synthesis services for unique, fully defined oligosaccharides.

Initiate Your High-Value Inquiry Today

The complexity of GAG structure is immense, yet it holds the fundamental key to countless biological mechanisms and therapeutic breakthroughs. Don't let structural ambiguity define your research outcomes. Define your research with Creative Biolabs' GAG Library. We offer a flexible Glycan Library, from a targeted GAG library to the N-Glycan, O-Glycan, HMO-Glycan, Mannose Glycan Libraries, etc. Please contact us today to unlock the full potential of the Glyco-Code in your laboratory.

Reference

Bayat, Parisa et al. "Comprehensive structural assignment of glycosaminoglycan oligo- and polysaccharides by protein nanopore." Nature communications vol. 13,1 5113. 30 Aug. 2022. Distributed under an Open Access license CC BY 4.0, without modification. https://doi.org/10.1038/s41467-022-32800-4