Glycosyltransferase-like protein LARGE2 (gyltl1b) Recombinant Protein | gyltl1b recombinant protein

Recombinant Danio rerio Glycosyltransferase-like protein LARGE2 (gyltl1b), partial

• Gene Names: large2; gyltl1b; si:ch211-206g24.1; si:ch211-282n12.1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Glycosyltransferase-like protein LARGE2 (gyltl1b); Recombinant Danio rerio Glycosyltransferase-like protein LARGE2 (gyltl1b); partial; gyltl1b recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Length: 750

• Species: Zebrafish
• Preparation and Storage: Store at -20 degrees C. For long-term storage, store at -20 degrees C or -80 degrees C. Store working aliquots at 4 degrees C for up to one week. Repeated freezing and thawing is not recommended.

NCBI and Uniprot Product Information

• NCBI GI #: 52218928
• NCBI GeneID: 446214
• NCBI Accession #: NP_001004538.1
• NCBI GenBank Nucleotide #: NM_001004538.1
• UniProt Accession #: Q66PG1; Q1LUJ7; Q1LV71
• Molecular Weight: 86,987 Da
• NCBI Official Full Name: LARGE xylosyl- and glucuronyltransferase 2
• NCBI Official Synonym Full Names: LARGE xylosyl- and glucuronyltransferase 2
• NCBI Official Symbol: large2
• NCBI Official Synonym Symbols: gyltl1b; si:ch211-206g24.1; si:ch211-282n12.1
• NCBI Protein Information: LARGE xylosyl- and glucuronyltransferase 2
• UniProt Protein Name: LARGE xylosyl- and glucuronyltransferase 2
• UniProt Gene Name: large2

Uniprot Description

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). Phosphorylated O-mannosyl trisaccharid is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide. Has a higher activity toward alpha-dystroglycan than LARGE.