Anti-LARGE1 Purified Monoclonal Antibody

LARGE1 serves as a glycosyltransferase which participates in glycosylation of the muscle membrane protein alpha-dystroglycan. Mutations of LARGE1 lead to hypoglycosylation of alpha-dystroglycan and cause congenital muscular dystrophy (MDC1D) associated with severe mental retardation. Altered alpha-dystroglycan glycosylation may also play a role in cancer, as hypoglycosylation of the protein and loss of laminin binding have been demonstrated in invasive carcinoma cells.

Recombinant fragment of human LARGE1 (amino acids 35-142) . The mouse monoclonal antibody LARGE-02 recognizes human LARGE1, a glycosyltransferase expressed mainly in the Golgi apparatus.

Bifunctional glycosyltransferase with both xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine- beta-4- (phosphate-6-) mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1) (PubMed:22223806) . Phosphorylated O- mannosyl trisaccharid is required for binding laminin G-like domain-containing extracellular proteins with high affinity and plays a key role in skeletal muscle function and regeneration. LARGE elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure initiated by B3GNT1/B4GAT1 by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide (PubMed:25279699) .