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生物来源
Escherichia coli
重组
expressed in E. coli
方案
≥83% (SDS-PAGE)
表单
aqueous solution
分子量
41.6 kDa
包装
pkg of 100 μg
NCBI登记号
UniProt登记号
运输
dry ice
储存温度
−70°C
基因信息
bacteriophage T4 ... B-GT(1258765)
一般描述
T4-phage β−glucosyltransferase, also known as UDP glucose-DNA β-glucosyltransferase, (Genbank Accession No. NP_049658) amino acids 1-351(end) with C-terminal His-tag, MW= 41.6 kDa, expressed in Escherichia coli.
应用
Useful for the differentiation of hydroxymethylcytosine (HMC) from methylcytosine in DNA, via glucosylating HMC and protecting HMC from endonuclease cleavage.
生化/生理作用
T4-phage β-glucosyltransferase is involved in the transfer of glucose from uridine diphosphoglucose (UDP-Glc) to 5-hydroxymethylcytosine (5-HMC) in double-stranded DNA of the T4-phage. Ions such as Mg2+, Mn2+ and Ca2+ activate this enzyme.
外形
Formulated in 200 mM imidazole and 20% glycerol.
警示用语：
Danger
危险声明
危险分类
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
储存分类代码
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
历史批次信息供参考:
Chun-Xiao Song et al.
Nature biotechnology, 29(1), 68-72 (2010-12-15)
In contrast to 5-methylcytosine (5-mC), which has been studied extensively, little is known about 5-hydroxymethylcytosine (5-hmC), a recently identified epigenetic modification present in substantial amounts in certain mammalian cell types. Here we present a method for determining the genome-wide distribution
High resolution crystal structures of T4 phage beta-glucosyltransferase: induced fit and effect of substrate and metal binding.
Morera S
Journal of Molecular Biology, 311(3), 569-577 (2001)
Glucosylation of deoxyribonucleic acid by enzymes from bacteriophage-infected Escherichia coli.
S R KORNBERG et al.
The Journal of biological chemistry, 236, 1487-1493 (1961-05-01)
Bacteriophage T4 genome.
Miller ES
Microbiology and Molecular Biology Reviews, 67(1), 86-156 (2003)
T4 phage beta-glucosyltransferase: substrate binding and proposed catalytic mechanism.
Morera S
Journal of Molecular Biology, 292(3), 717-730 (1999)
商品
Explore tools for glycosyltransferase synthesis and modification of glycans, such as glycosyltransferases and nucleotide sugar donors.
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