EOGT Mouse
Description
Product Specs
Product Science Overview
EGF Domain-Specific O-Linked N-Acetylglucosamine Transferase (EOGT) is an enzyme that plays a crucial role in the post-translational modification of proteins. This enzyme is responsible for the addition of N-acetylglucosamine (GlcNAc) to serine or threonine residues within the epidermal growth factor (EGF)-like domains of extracellular proteins. The mouse recombinant version of this enzyme is often used in research to study its function and role in various biological processes.
EOGT is a glycosyltransferase that catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins. This modification results in the formation of a beta-linked N-acetylglucosamine (O-GlcNAc) on the target protein . The enzyme specifically glycosylates the threonine residue located between the fifth and sixth conserved cysteines of folded EGF-like domains .
The modification of proteins by O-GlcNAc is essential for various cellular processes, including intracellular signaling, endocytosis, transcription, and protein stability . EOGT’s activity is particularly important in the regulation of developmental signaling pathways. For instance, it modifies the Notch receptor, which is involved in cell differentiation, proliferation, and apoptosis .
The EOGT gene is located on chromosome 3p14.1 and encodes a protein that is 527 amino acids long . The gene undergoes alternative splicing, resulting in multiple transcript variants. Mutations in the EOGT gene have been associated with Adams-Oliver Syndrome 4, a genetic disorder characterized by congenital limb defects and scalp abnormalities .
The mouse recombinant version of EOGT is widely used in research to study its enzymatic activity and role in various biological processes. Researchers utilize this enzyme to investigate the mechanisms of protein glycosylation and its impact on cellular functions. Additionally, studies on EOGT can provide insights into the development of therapeutic strategies for diseases associated with glycosylation defects.
