Recombinant PGLT1 protein (His tag)

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Recombinant Human Protein O-glucosyltransferase 1 (POGLUT1) Fragment (residues 24-392) is a highly purified, stable protein designed for structural and biochemical studies. This 369-amino acid fragment retains key functional domains, enabling researchers to investigate its dual glycosyltransferase activity in Notch signaling and other critical pathways.

Protein O-glucosyltransferase 1 (POGLUT1) is a dual-specificity glycosyltransferase that catalyzes the transfer of glucose and xylose from UDP-sugar donors to serine residues within the consensus sequence C-X-S-X-P-C of extracellular EGF repeats. It plays essential roles in Notch signaling by mediating O-glucosylation of Notch receptors, thereby regulating muscle development without affecting ligand binding. POGLUT1 also targets other proteins including CRB2, F7, and F9, and is required for proper CRB2 membrane localization during gastrulation. The enzyme localizes to the endoplasmic reticulum lumen, where it performs its glycosylation functions on client proteins.