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Dear Customer:

The current international situation is complex and volatile, and the tariff policy remains unclear, which may have a certain impact on the prices of our products. Under these circumstances, we hope to have a friendly communication with you regarding the order matters.

Given the current uncertainties, if you choose to place an order during this period, we reserve the right to adjust the price based on the actual situation. At the same time, we understand that the market changes may bring you some inconvenience. Therefore, if there is a significant price fluctuation due to changes in the tariff policy before the actual delivery of the order, Merck will negotiate with you and adjust or cancel the order as the situation requires.

Merck
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主要文件

安全信息

44498

Sigma-Aldrich

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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About This Item

CAS号:
MDL编号:
UNSPSC代码:
12352204

价格与库存信息目前不能提供

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
SAB1300288HPA031151SAE0093
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.

Q02742

UniProt accession no.

Q02742

UniProt accession no.

Q02742

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

  • 历史批次信息供参考:

    分析证书(COA)

    Lot/Batch Number

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    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
    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
    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

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