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
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
Recommended Products
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.[1][2] It is also considered to be a biosynthetic enzyme of the Golgi apparatus.[3] 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.[4]
Components
contains 50% glycerol, 50 mM Tris-HCl-buffer, pH 7.5, 2 mM 2-Mercaptoethanol
Unit Definition
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
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Kam Lau et al.
Chemical communications (Cambridge, England), 46(33), 6066-6068 (2010-07-14)
Two bacterial beta1-4-galactosyltransferases, NmLgtB and Hp1-4GalT, exhibit promiscuous and complementary acceptor substrate specificity. They have been used in an efficient one-pot multienzyme system to synthesize LacNAc, lactose, and their derivatives including those containing negatively charged 6-O-sulfated GlcNAc and C2-substituted GlcNAc
Huiguang Yang et al.
Inflammation, 32(5), 279-286 (2009-06-24)
beta4 Galactosylation of glycoproteins is one of the most important post-translational modifications. Recent studies have demonstrated that aberrant galactosylation associates with some inflammation diseases. beta-1,4-galactosyltransferase-I (beta-1,4-GalT-I), which transfers galactose to the terminal N-acetylglucosamine of N- and O-linked glycans in a
Cell surface beta 1,4 galactosyltransferase: twenty years later.
B D Shur
Glycobiology, 1(6), 563-575 (1991-12-01)
Sungjin Park et al.
Methods in molecular biology (Clifton, N.J.), 669, 195-208 (2010-09-22)
Microarray technology has received considerable attention for rapid analysis of biomolecular interactions and high-throughput screening to identify binding partners. An efficient and selective immobilization technique of substances on the surface is essential for successful construction of microarrays. Although a variety
A Varki
Glycobiology, 3(2), 97-130 (1993-04-01)
Many different theories have been advanced concerning the biological roles of the oligosaccharide units of individual classes of glycoconjugates. Analysis of the evidence indicates that while all of these theories are correct, exceptions to each can also be found. The
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