Innovative Biochemical Analysis Solutions
Glycosaminoglycan Microarray on 8 subarray format. A subarray assayed with antithrombin-III (10 μg/ml), followed by anti-antithrombin-III antibody (2 μg/ml), and finally anti-mouse IgG-AlexaFluoro555 (10 μg/ml) (sandwich assay format). The array was scanned with a microarray scanner at 532nm wavelength. The positive control 3 (mouse IgG) shows binding as expected.
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The pathogenesis of Alzheimer’s Disease involves ubiquitous, linear polysaccharide molecules called glycosaminoglycans (GAGs) in the genesis of senile plaques and neuronal uptake of toxic tau protein aggregates. GAG interactions are largely electrostatic, and the GAG heparin – having the highest negative charge density of any known biological molecule – promotes tau protein aggregation by affecting its conformation and interprotein electrostatic repulsion. These protein aggregates can then bind to GAGs on neurons to gain entry to the cell. GAGs are also involved in many other biological processes from skin aging to tumor progression. Characterizing their roles, concentrations and configurations in relation to physiological stimuli could provide new approaches to disease prevention and regression.
Glycosaminoglycans are highly heterogeneous due to their varying conformations, molecular mass, and electrostatic potential, and their specific composition is determined by cell type. Their expression has been shown to change with age, ultraviolet radiation exposure, and at sites of injury, diseased tissues, and tumor growth. Further studies using new glycomic technologies are needed to help understand the presence of certain GAGs and their roles.
This Gycosaminoglycan Microarray compiles several varieties of GAGs in varying lengths, degrees of sulfation, and disaccharide sequences to aid in the efficient study of the functions and specific interactions of GAGs. Researchers can use this array to test molecules designed as inhibitory agents or disease, scar or injury-targeting therapeutics. This array can be used to investigate the GAG-binding specificity of viruses or VLPs, or determine the presence of specific GAG binders in sera, cerebrospinal fluid, or other biological samples.