Description_x000D_ General description_x000D_ O-GlcNAc transferase (OGT) catalyzes the addition of an N-acetylglucosamine residue to the amino acids serine or threonine. The enzyme is an homotrimer consisting of three subunits of 110 kDa each, with multiple tetratricopeptide (TPR) repeats._x000D_ Immunogen_x000D_ synthetic peptide corresponding to amino acids 1024-1037 of human O-GlcNAc transferase, conjugated to KLH via an N-terminal added cysteine residue._x000D_ Application_x000D_ Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below._x000D_ Immunofluorescence (1 paper)_x000D_ Physical form_x000D_ Solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide._x000D_ Disclaimer_x000D_ Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals._x000D_ Biochem/physiol Actions_x000D_ O-linked β-N-acetyl glycosamine (O-GlcNAc) is involved in repressing transcription. O-GlcNAc transferase (OGT) interacts with a histone deacetylase complex by binding to the co repressor Sin3A. This interaction leads to the repression of transcription, after transcription factors and RNA polymerase II are modified by addition of O-GlcNAc. O-GlcNAc modification reversibly inhibits proteosomal function in an ubiquitin-independent fashion.