44498
β-1,4-Galactosyl Transferase I human, recombinant from Saccharomyces cerevisiae
≥0.2 unit/mL
Synonym(s):
UDP-galactose-N-acetylglucosamine-β-1,4-galactosyltransferase I, human, recombinant
Product Name
β-1,4-Galactosyl Transferase I human, recombinant from Saccharomyces cerevisiae, ≥0.2 unit/mL
recombinant
expressed in Saccharomyces cerevisiae
concentration
≥0.2 unit/mL
0.5-4 mg/mL protein
impurities
≤0.1% β-galactosidase
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... GCNT1(2650)
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Biochem/physiol Actions
β-1,4-Galactosyl Transferase catalyzes the transfer of galactose from UDP-galactose to the terminal N-acetylglucosamine residues on elongating oligosaccharide chains. It is also considered to be a biosynthetic enzyme of the Golgi apparatus. β-1,4-Galactosyl Transferase can also be found on the cell surface functioning as a cell-adhesion molecule during various cellular interactions by binding to N-acetylglucosamine containing oligosaccharide substrates or ligands in the extracellular matrix.
Other Notes
1 U corresponds to the amount of enzyme which transfers 1 μmol galactose from UDP-galactose to N-Acetyl-D-glucosamine per minute at pH 7.4 and 37°C in the presence of α-Lactalbumin
contains 50% glycerol, 50 mM Tris-HCl-buffer, pH 7.5, 2 mM 2-Mercaptoethanol
Regulatory Information
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Takaomi Ito et al.
Biochemistry, 49(11), 2604-2614 (2010-02-25)
Recombinant glycosyltransferases are potential biocatalysts for the construction of a compound library of oligosaccharides, glycosphingolipids, glycopeptides, and various artificial glycoconjugates on the basis of combined chemical and enzymatic synthetic procedures. The structurally defined glycan-related compound library is a key resource
Sylvie Mugnier et al.
Reproductive biology and endocrinology : RB&E, 6, 51-51 (2008-11-19)
In human and rodents, sperm-zona pellucida binding is mediated by a sperm surface Galactosyltransferase that recognizes N-Acetylglucosamine residues on a glycoprotein ZPC. In large domestic mammals, the role of these molecules remains unclear: in bovine, they are involved in sperm-zona
Cell surface galactosyltransferase: current issues.
B D Shur et al.
Glycoconjugate journal, 15(6), 537-548 (1999-01-09)
Kazuki Mochizuki et al.
Life sciences, 86(13-14), 524-531 (2010-02-18)
We examined whether decreasing jejunal sucrase/isomaltase (S/I) activity ratio by feeding rats a high fat/carbohydrate ratio diet is regulated by changing glycosylated chains on the S-I complex. Jejunal activities of sucrase, isomaltase and beta-1,4-galactosyltransferase were examined in rats fed a
Koji Matsuoka et al.
Bioorganic & medicinal chemistry letters, 20(16), 4906-4910 (2010-07-14)
An efficient synthesis of sialyllactosamine (SiaLacNAc) clusters using carbosilanes as core scaffolds has been accomplished by means of chemical and enzymatic approaches. N-Acetyl-D-glucosamine (GlcNAc) clusters having O-glycosidic linkage or S-glycosidic linkage were chemically synthesized from known intermediates in high yields.
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