Glycosaminoglycan Microarray

Glycosaminoglycans (GAGs) play critical roles in many cellular processes, ranging from viral invasion and angiogenesis to spinal cord injury. Glycosaminoglycan microarray provides a high-throughput method to elucidate glycosaminoglycan-protein interactions which just requires a few GAGs sample. Creative Biolabs offers high-quality services in Glycosaminoglycan Microarray. We can provide commercial, customized and semi-customized microarray services of GAGs. Combined with various kinds of support technologies such as Lectin Microarray, MALDI-TOF MS, SPRi, TLC, and Flow Cytometry, we can provide comprehensive service of glycosaminoglycan-protein research. Moreover, we also provide general or customized Heparin Sulfate Microarray service to support more specific studies furtherly. With a large and well-equipped scientist team, we are dedicated to collaborating with our clients around the world to meet your requirements.

Fig.1 Glycosaminoglycan structure. (van Golen, 2014)

Introduction of Glycosaminoglycan Microarray

Glycosaminoglycans are extracellular matrix and cell surface sulfated glycans crucial to the regulation of various signaling proteins whose functions are essential in many pathophysiologycal systems. GAGs are structurally composed of alternating hexosamine and uronic acid or galactose. Assembled from repeating disaccharide units, GAGs display diverse patterns of sulfation, which contribute to the high structure flexibility of GAGs. According to the type of monosaccharides and glycosidic bonds, GAGs are classified to heparin, heparan sulfate, chondroitin sulfate, dermatan sulfate, hyaluronan or hyaluronic acid, keratan sulfate and so on.

Recent researches suggested that GAGs take part in numerous biological processes by binding to protein molecules and functionally regulating protein-ligand interactions. Because structural heterogeneity is high in GAG chains and purification is difficult, the use of structurally defined GAG oligosaccharides from natural sources as molecular models in both biophysical and pharmacological assays is limited. Therefore, the establishment of glycosaminoglycan microarray platform with synthetic GAG oligosaccharides is a novel approach to overcome this obstacle and serve as useful molecular tools in studies of GAG-protein interactions.

Applications of Glycosaminoglycan Microarray

Fig.2 Patterns of a GAG microarray. (Takada, 2013)

Because of GAGs extracellular location, high anionic character and rich structural diversity, GAGs are capable of interacting with and regulating many proteins whose functions are essential to pathophysiology. In particular, GAGs are known to modulate wound repair, coagulation, thrombosis, cancer growth and metastasis, inflammation, neovascularization, tissue regeneration and repair, cellular growth and migration. Since the first report of dedicated GAG microarray created using synthetic GAG oligosaccharides appeared in 2006, many novel immobilization methods are used to build glycosaminoglycan microarray chips. Nowadays, the application of glycosaminoglycan microarray to discover new interactions between proteins and GAGs is widely accepted in the immunology field. Creative Biolabs also established a mature glycosaminoglycan microarray platform in Tumor Glyco-diag, glycoprotein vaccine development and Anti-Glycoprotein Antibody Development. Particularly, because of the importance of heparin sulfate (HS) in vivo, we specially launched Heparin Sulfate Microarray service based on general glycosaminoglycan microarray.

Glycosaminoglycan microarray overcame the difficulties of traditional methods and provide a rapid and low-cost way to research GAG-protein interactions. If you are interested in our Glycosaminoglycan Microarray services or learn more about our Heparin Sulfate Microarray service, please contact us for more details.

References

1. van Golen, G. F.; et al. The mechanisms and physiological relevance of glycocalyx degradation in hepatic ischemia/ reperfusion injury. Antioxidants & redox signaling. 2014, 21(7), 1098-1118.
2. Takada, W.; et al. A sulfated glycosaminoglycan array for molecular interactions between glycosaminoglycans and growth factors or anti-glycosaminoglycan antibodies. Analytical biochemistry. 2013, 435(2), 123-130.

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