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重组
expressed in Saccharomyces cerevisiae
浓度
≥0.2 unit/mL
0.5-4 mg/mL protein
杂质
≤0.1% β-galactosidase
UniProt登记号
储存温度
−20°C
基因信息
human ... GCNT1(2650)
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生化/生理作用
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.
组分
contains 50% glycerol, 50 mM Tris-HCl-buffer, pH 7.5, 2 mM 2-Mercaptoethanol
单位定义
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
法规信息
新产品
Boopathy Ramakrishnan et al.
The Journal of biological chemistry, 285(20), 15619-15626 (2010-03-20)
The beta1,4-galactosyltransferase-7 (beta4Gal-T7) enzyme, one of seven members of the beta4Gal-T family, transfers in the presence of manganese Gal from UDP-Gal to an acceptor sugar (xylose) that is attached to a side chain hydroxyl group of Ser/Thr residues of proteoglycan
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
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
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.
Cell surface galactosyltransferase: current issues.
B D Shur et al.
Glycoconjugate journal, 15(6), 537-548 (1999-01-09)
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