Antibodies to O-GlcNAc

O-glycosylation on the serine and threonine of proteins by a single -N-acetyl-D-glucosamine moiety (O-GlcNAc) is a post-translational modification that is highly dynamic and fluctuates in response to a wide range of stimuli. This type of glycosylation has been found on hundreds of human proteins and is thought to be nearly as wide-spread as protein phosphorylation.   Interestingly, multiple reports have demonstrated a reciprocal regulatory relationship between O-GlcNAc and phosphorylation, which occupy the same or adjacent serine/threonine sites on proteins, share extensive crosstalk, and contribute to many different human disease mechanisms. 

To facilitate the study of this modification and its dynamics, we developed a range of site-specific antibodies that have a high preference for the O-GlcNAcylated species, we refer to this as glycophilic antibodies.  We have also generated antibodies that recognize the site with or without the O-GlcNAc.  The combination of these antibodies lets one determine changes in the extent of occupancy.    We also can provide peptide/glycopeptides as controls for these experiments.

a-Synuclein (Mus musculus)

NMDA 2B/NR2B (Mus musculus)

Histone H2A

Histone H2B

Histone H3

Histone H4


Insulin Receptor Substrate 2

Ten-eleven translocation methylcytosine dioxygenase (TET) (Mus musculus)