O-GalNAc Antibody, Clone 9B9

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.

β-O-Linked N-Acetylglucosamine, O-Linked N-Acetylglucosamine, O-GlcNAc, Beta-O-Linked N-Acetylglucosamine, N-Acetylglucosamine, GlcNac, 2- (Acetylamino) -2-deoxy-D-glucose, N-acetyl-D-glucosamine, NAG, β-D- (Acetylamino) -2-deoxy-glucopyranose, beta-N-Acetylglucosamine, N-Acetylglucosamine-modified protein, β-N-Acetylglucosamine

A 1:10,000 dilution of SMC-503 was sufficient for detection of O-GalNAc in 2 µg of O-GalNAc conjugated to BSA by ECL immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary Antibody.