Purified anti-OGT Antibody, OGT, W20094A,BioLegend,603551

UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (OGT) catalyzes the transfer of N-acetyl glucosamine (GlcNAc) post-translational modification to serine, threonine, and cysteine residues of proteins. Serine and threonine residues are modified by O-glycosidic linkage, while cysteine is modified by S-glycosidic linkage. Since the amino acids utilized for O-GlcNAcylation are identical to those used for protein phosphorylation, OGT competes with kinases for modification of those sites. Numerous functions for GlcNAcylation have been reported in regulating protein-protein interactions, and OGT plays diverse roles in the regulation of the cell cycle, transcription, and cellular stress. Dysregulation of O-GlcNAcylation plays a role in the pathology of Alzheimer’s disease, cancer and diabetes. OGT activity is regulated by glucose availability, and plays a role in regulating glycolysis by glycosylation of phosphofructokinase.