The dynamic modification of cytoplasmic and nuclear proteins by O-linked N-acetylglucosamine (O-GlcNAc) addition and removal on serine and threonine residues is catalyzed by OGT (MIM 300255), which adds O-GlcNAc, and MGEA5, a glycosidase that removes O-GlcNAc modifications (Gao et al., 2001 [PubMed 11148210]). Human meningioma-expressed antigen 5 (MGEA5) has two putative domains including protein O-GlcNAcase domain and histone acetyltransferase domain, therefore it is often called bifunctional protein NCOAT. Three isoforms of MEGE5 are produced by alternative splicing. MGEA5 was found to be regulated to reduce the state of glycosylation of transcitpional activators while increasing the acetylation of histones to allow for the concerted activation of eukaryotic gene transcription, for instance, acetylation of Lys8 of histone H4 and Lys 14 of histone H3 are resulted from acetyltransferase activity. In addition, single nucleotide polymorphism in MGE5A is associated with type 2 diabetes in Mexican Americans. Two bands at 130kDa and 75 kDa could be detected using the present rabbit polyclonal antibody 14711-1-AP, which is consistent with results in a related reference.