Anti-O-Linked N-Acetylglucosamine Mouse mAb

Primary Antibodies

Pan PTM Antibodies

Store at -20°C. Avoid freeze/thaw cycles.

Stable for 12 months from date of receipt/reconstitution.

O-Linked β-N-acetylglucosamine modification (GlcNAcylation) is a glycosylation in which the monosaccharide β-N-acetylglucosamine (GlcNAc) attaches to serine/threonine residues via an O-linked glycosidic bond and is found mostly within the cytoplasm or nucleoplasm. GlcNAcylation regulates several important cellular processes, such as signal transduction, protein expression, degradation, embryonic stem cell pluripotency and trafficking. This post-translational modification is regulated by OGT and O-GlcNAcase (β-N-acetylglucosaminidase) enzymes, whereas OGT catalyzes the attachment and O-GlcNAcase catalyzes the removal of O-GlcNAc to proteins. O-GlcNAc modification has been observed on histones: H2A at T101, H2B at S36 and S112, H3 at S10 and T32, and H4 at S47.

PBS, Glycerol, BSA

Ser, Thr

O-Linked β-N-acetylglucosamine modification (GlcNAcylation) is a glycosylation in which the monosaccharide β-N-acetylglucosamine (GlcNAc) attaches to serine/threonine residues via an O-linked glycosidic bond and is found mostly within the cytoplasm or nucleoplasm. GlcNAcylation regulates several important cellular processes, such as signal transduction, protein expression, degradation, embryonic stem cell pluripotency and trafficking. This post-translational modification is regulated by OGT and O-GlcNAcase (β-N-acetylglucos-aminidase) enzymes, whereas OGT catalyzes the attachment and O-GlcNAcase catalyzes the removal of O-GlcNAc to proteins. O-GlcNAc modification has been observed on histones: H2A at T101, H2B at S36 and S112, H3 at S10 and T32, and H4 at S47.