O-GlcNAcylation: New Tools to Investigate this Important Post-Translational ModificationO-GlcNAcylation is a post-translational modification consisting of the addition of a single N-acetyl-glucosamine residue (GlcNAc) to specific serine/threonine residues of proteins. The addition of GlcNAc has been compared to phosphorylation, and there may be significant interplay between the two processes (1). Like phosphorylation, O-GlcNAcylation has putative involvement in a range of cellular activities, including the stress response, transcription, translation, cell signaling, and cell cycle regulation (2). Changes in O-GlcNAc modification have also been implicated in a host of diseases such as diabetes, Alzheimer’s disease, and cancer (3, 4). Despite potential roles in these important areas of biology, a lack of tools has hampered the understanding of O-GlcNAcylation and the advancement of therapies that might target this process. O-GlcNAcylation is regulated by a discrete set of enzymes. It was originally thought to exist solely on nuclear and cytosolic proteins catalyzed by a single O-GlcNAc transferase (OGT) (5). However, O-GlcNAcylation has recently been discovered on extracellular proteins, where O-GlcNAc addition is catalyzed by extracellular OGT (EOGT) (6). O-GlcNAc is removed by a single O-GlcNAcase (OGA) (7). Recombinant OGT (New), Recombinant EOGT (New), and Recombinant OGA are part of our extensive portfolio of glycobiology reagents. Our offering also includes a line of ancillary reagents that can be utilized for labeling and detection of O-GlcNAc modification (Table 1). Figure 1 demonstrates the results of an assay used for the detection of OGT-specific targets.
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