Abcam, ab131881, Recombinant Human OGT / O-Linked N-Acetylglucosamine Transferase protein

Size: 10µg
Recombinant Human OGT / O-Linked N-Acetylglucosamine Transferase protein is a Human Full Length protein, in the 1 to 1046 aa range, expressed in Wheat germ, suitable for SDS-PAGE, ELISA, WB.
Key facts
Expression system:Wheat germ,
Tags:GST tag N-Terminus,
Applications:WB, SDS-PAGE, ELISASee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Biologically active:No,
Accession:O15294,
Animal free:No,
Carrier free:No,
Species:Human,
Storage buffer:pH: 8Constituents: 0.79% Tris HCl, 0.31% Glutathione

Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--80°C, Appropriate long-term storage conditions--80°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
OGT or O-Linked N-Acetylglucosamine Transferase also known as OGT protein mechanically catalyzes the addition of N-acetylglucosamine (O-GlcNAc) onto serine or threonine residues of nuclear and cytoplasmic proteins. OGT has a molecular weight of approximately 110 kDa. It is expressed in various tissues with higher levels in the pancreas brain and spleen. This enzyme plays an important role in cellular processes by modifying proteins with O-GlcNAc.
Biological function summary
Through its transferase activity OGT regulates a wide array of cellular functions including signal transduction transcription and metabolism. It is a component of a complex involving several other proteins that facilitate its regulatory actions. OGT manages protein function and stability by influencing interactions between proteins and other cellular components.
Pathways
OGT is critical in the insulin signaling pathway and the regulation of glucose metabolism. It interacts with multiple proteins such as IRS-1 and Akt to modulate their activity and stability. The modification by OGT impacts protein phosphorylation states affecting the downstream processing of cellular signals.
OGT has a significant link to diabetes and neurodegenerative diseases like Alzheimer's. Abnormal OGT activity relates to insulin resistance contributing to diabetes pathogenesis. In Alzheimer's disease altered O-GlcNAcylation affects proteins like tau which play a central role in disease progression. Understanding OGT's role in these conditions could aid in developing targeted therapeutic strategies.