Function
Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids, notably by participating in biosynthesis of HNK-1 and Lewis X carbohydrate structures. Has strong activity toward lactosylceramide (LacCer) and neolactotetraosylceramide (nLc(4)Cer; paragloboside), resulting in the synthesis of Lc(3)Cer and neolactopentaosylceramide (nLc(5)Cer), respectively. Probably plays a central role in regulating neolacto-series glycolipid synthesis during embryonic development.
Biological Context
Subcellular Location: Golgi apparatus membrane (Single-pass type II membrane protein)
Tissue Specificity: Widely expressed. Highly expressed in lung, colon, placenta, testis, pituitary gland and cerebellum. Weakly expressed in brain, liver, spleen, lymph node and thymus
Pathway: Protein modification; protein glycosylation
Product Specifications
Recombinant Human UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5 (B3GNT5), partial is a recombinant protein from Homo sapiens (Human), expressed in E.coli, covering amino acids 36-378aa, with C-terminal 6xHis-tagged tag, molecular weight 46.7kDa, purity Greater than 90% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications. Explore more Enzyme proteins →
