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Merck
CN

44498

人体 β-1,4-半乳糖转移酶 I 重组体 来源于酿酒酵母

≥0.2 unit/mL

别名:

人体 UDP-半乳糖-N-乙酰胺基葡萄糖-β-1,4-半乳糖转移酶·I 重组体

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关于此项目

化学文摘社编号:
UNSPSC Code:
12352204
MDL number:
Recombinant:
expressed in Saccharomyces cerevisiae
Concentration:
≥0.2 unit/mL, 0.5-4 mg/mL protein
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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

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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
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
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
Cell surface beta 1,4 galactosyltransferase: twenty years later.
B D Shur
Glycobiology, 1(6), 563-575 (1991-12-01)

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