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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Boopathy Ramakrishnan et al.
Current opinion in structural biology, 20(5), 536-542 (2010-08-14)
Cell surface glycans play important cellular functions and are synthesized by glycosyltransferases. Structure and function studies show that the donor sugar specificity of the invertebrate β1,4-N-acetyl-glactosaminyltransferase (β4GalNAc-T) and the vertebrate β1,4-galactosyltransferase I (β4Gal-T1) are related by a single amino acid
Mateja Erdani Kreft et al.
Biology of the cell, 102(11), 593-607 (2010-08-26)
The GA (Golgi apparatus) has an essential role in membrane trafficking, determining the assembly and delivery of UPs (uroplakins) to the APM (apical plasma membrane) of superficial UCs (uroepithelial cells) of urinary bladder. UPs are synchronously and uniformly delivered from
Yeon Tae Jeong et al.
Journal of microbiology and biotechnology, 18(12), 1945-1952 (2009-01-10)
Sialylation, the attachment of sialic acid residues to a protein, can affect the biological activity and in vivo circulatory half-life of glycoproteins. Human alpha2,3- sialyltransferase (alpha2,3-ST) and beta1,4-galactosyltransferase (beta1,4-GT) are responsible for terminal sialylation and galactosylation, respectively. Enhanced sialylation of
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
Cell surface galactosyltransferase: current issues.
B D Shur et al.
Glycoconjugate journal, 15(6), 537-548 (1999-01-09)
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