Beta-1,4-Galactosyltransferase 3 (B4GALT3) Antibody – Rabbit Polyclonal

This gene is one of seven beta-1,4-galactosyltransferase (beta4GalT) genes. They encode type II membrane-bound glycoproteins that appear to have exclusive specificity for the donor substrate UDP-galactose; all transfer galactose in a beta1,4 linkage to similar acceptor sugars: GlcNAc, Glc, and Xyl. Each beta4GalT has a distinct function in the biosynthesis of different glycoconjugates and saccharide structures. As type II membrane proteins, they have an N-terminal hydrophobic signal sequence that directs the protein to the Golgi apparatus and which then remains uncleaved to function as a transmembrane anchor. By sequence similarity, the beta4GalTs form four groups: beta4GalT1 and beta4GalT2, beta4GalT3 and beta4GalT4, beta4GalT5 and beta4GalT6, and beta4GalT7. This gene encodes an enzyme that may be mainly involved in the synthesis of the first N-acetyllactosamine unit of poly-N-acetyllactosamine chains. Multiple alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Dec 2010]

B4GALT3: Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. Belongs to the glycosyltransferase 7 family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Glycan Metabolism - N-glycan biosynthesis; Glycan Metabolism - keratan sulfate biosynthesis; EC 2.4.1.90; EC 2.4.1.38; Glycan Metabolism - glycosphingolipid biosynthesis - lacto and neolacto series; Transferase; Membrane protein, integral

Chromosomal Location of Human Ortholog: 1q23.3

Cellular Component: cytoplasm; Golgi apparatus; Golgi membrane; integral to membrane

Molecular Function: beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity; galactosyltransferase activity; metal ion binding; N-acetyllactosamine synthase activity

Biological Process: carbohydrate metabolic process; cellular protein metabolic process; glycosaminoglycan metabolic process; keratan sulfate biosynthetic process; keratan sulfate metabolic process; post-translational protein modification; protein amino acid N-linked glycosylation via asparagine