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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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此商品 | SAB1300288 | HPA031151 | SAE0093 |
|---|---|---|---|
| Gene Information human ... GCNT1(2650) | Gene Information human ... GCNT1(2650) | Gene Information human ... GCNT1(2650) | Gene Information - |
| recombinant expressed in Saccharomyces cerevisiae | recombinant - | recombinant - | recombinant expressed in HEK 293 cells |
| concentration ≥0.2 unit/mL, 0.5-4 mg/mL protein | concentration - | concentration - | concentration - |
| UniProt accession no. | UniProt accession no. | UniProt accession no. | UniProt accession no. - |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
| impurities ≤0.1% β-galactosidase | impurities - | impurities - | impurities - |
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.[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]
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
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
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
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
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
Kar Kheng Yeoh et al.
Carbohydrate research, 344(5), 586-591 (2009-02-24)
A series of potential UDP-sugar mimics were readily synthesised by copper(I) catalysed modified Huisgen cycloaddition of the corresponding alpha-propargyl glycosides with 5-azido uridine in aqueous solution. None of the compounds accessed displayed significant inhibitory activity at concentrations of up to
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