Recombinant Human Protein O-GlcNAcase (OGA) Fragment (60-336) is a high-purity, enzymatically active protein designed for studying O-GlcNAc hydrolysis. This fragment encompasses the full GH84 domain, offering researchers a precise tool to investigate O-GlcNAcase function, substrate specificity, and regulatory mechanisms in cellular signaling pathways.

Protein O-GlcNAcase (OGA) is a key enzyme in human cells that selectively cleaves O-linked N-acetylglucosamine (GlcNAc) modifications from serine and threonine residues of proteins. It plays a crucial role in regulating diverse cellular processes by deglycosylating numerous substrates, including CRYAB, ELK1, GSDMD, LMNB1, and TAB1, thereby influencing protein stability, activity, and localization. Isoform 1, the primary cytoplasmic form, exhibits strict substrate specificity for beta-GlcNAc and does not possess acetyltransferase activity. O-GlcNAcylation is a dynamic post-translational modification involved in nutrient sensing, stress response, and gene