MGEA5/OGA (E9C5U) Rabbit Monoclonal Antibody #60406

O-GlcNAcylation is a post-translational modification where β-D-N-acetylglucosamine (GlcNAc) is covalently linked to cytoplasmic and nuclear proteins at serine or threonine residues (1,2). This modification is important in many cellular processes, including metabolism, cell growth and morphogenesis, apoptosis, and transcription (2,3). The reversible protein modification by O-GlcNAc, which has been suggested to be a nutrient and stress sensor, is catalyzed by two highly conserved enzymes, O-GlcNAc transferase (OGT) and human meningioma-expressed antigen 5 (MGEA5)/O-GlcNAcase (OGA) (4). Research studies have implicated O-GlcNAcylation in cancer (1). This modification has also been proposed to have protective effects against the production and aggregation of toxic protein species associated with neurodegenerative diseases, including amyloid β (Aβ) and tau (Alzheimer's disease), and α-synuclein (Parkinson's disease) (5-7).