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Beta-1, 4-galactosyltransferase 1 (B4GALT1), one of seven beta-1, 4-galactosyltransferases, is commonly found in trans-Golgi complexes and transfers galactose to oligosaccharides. According to sequence similarity, B4GALTs can be divided into 4 groups: B4GALT1 and B4GALT2, B4GALT3 and B4GALT4, B4GALT5 and B4GALT6, and B4GALT7. Of these seven enzymes, B4GALT1 is unique in that it can be expressed as a membrane-bound or secreted form. The secreted form exists only in lactating mammary gland tissue, where the enzyme forms a heterodimer with α-lactalbumin, which catalyzes the synthesis of lactose. The membrane-bound form resides either in the Golgi apparatus, where the enzyme adds galactose to N-acetylglucosamine residues, or on the cell surface, during a variety of cell-cell and cell-matrix interactions, The enzyme functions as a recognition molecule by binding to specific oligosaccharide ligands on opposing cells or the extracellular matrix. These two enzyme forms arise from alternate transcription initiation sites and post-translational processing. Loss of B4GALT1 causes an inborn error of 2D-type glycosylation.