Mouse Anti-O-GalNAc (β-O-Linked N-Acetylgalactosamine) (Clone 9H6) Monoclonal IgM Antibody
O-GlcNAcylation is a reversible post-translational modification involving the attachment of N-acetylglucosamine (GlcNAc) to serine and threonine residues of nuclear and cytoplasmic proteins. This modification, catalyzed by O-GlcNAc transferase (OGT) and removed by O-GlcNAcase (OGA), plays a critical role in neuronal signaling, transcriptional regulation, and proteostasis.
In the central nervous system, O-GlcNAcylation modulates synaptic plasticity, axonal transport, and stress responses. It acts as a nutrient and stress sensor, integrating metabolic status with cellular function. Dysregulation of O-GlcNAc cycling has been implicated in several neurodegenerative diseases, including Alzheimer’s, Parkinson’s, and Huntington’s disease.
In Alzheimer’s disease, reduced O-GlcNAcylation correlates with increased tau hyperphosphorylation and aggregation, contributing to neurofibrillary tangle formation. Enhancing O-GlcNAc levels has been shown to reduce tau pathology and improve cognitive function in preclinical models. Similarly, in Parkinson’s disease, O-GlcNAcylation influences α-synuclein aggregation and mitochondrial function.
Given its broad regulatory scope and neuroprotective potential, O-GlcNAcylation is emerging as a promising therapeutic target. Pharmacological modulation of OGT and OGA activity is under investigation for restoring proteostasis and mitigating neurodegenerative progression.
As a dynamic and responsive signaling mechanism, O-GlcNAcylation bridges metabolism, stress adaptation, and neuronal health—making it a focal point in the search for disease-modifying interventions in neurodegeneration.
This Mouse Anti-O-GalNAc (β-O-Linked N-Acetylgalactosamine) (Clone 9H6) Monoclonal IgM Antibody is manufactured in Canada by StressMarq.
