O-GlcNAc Western Blot Detection Kit
from
Thermo Scientific Pierce Protein Research Products
Description
Glycosylation and phosphorylation are two of the most extensively studied post-translational modifications because of their important role in the signaling pathways that regulate cellular response.
O-glycosidically linked modifications of serine or threonine residues are found in the protein from essentially all eukaryotic cells. Proteins in both the cytoplasm and nucleus can be found with this specific posttranslational modification. Although not precisely known, the function of the b-O-linked N-acetylglucosamine (O-GlcNAc) modification may serve as an alternative to phosphorylation, as a modulator of protein interactions in multimeric complexes or as a fortification against proteolytic attack.
The O-GlcNAc modification is seemingly related to phosphorylation in many respects. Notably, the modification is controlled similarly to that of phosphorylation. All O-GlcNAc-modified proteins currently known are also phosphoproteins. In addition, there is an apparent reciprocal relationship between these two important posttranslational modifications within a single protein. Therefore, there is considerable interest in the O-GlcNAc modification.
The new Pierce O-GlcNAc Western Blot Detection Kit contains the most highly specific mouse monoclonal antibody available for the detection of the O-GlcNAc posttranslational modification on a membrane. Reaction of the monoclonal antibody in this Western Blotting kit is confined to the b-O-linked serine or threonine GlcNAc modification. There is no cross-reactivity with the a-O-GlcNAc linkage, the a/b-O-GalNAc modification or the other N-linked oligosaccharides.
OGT
(O-linked N-acetylglucosamine transferase)