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SRP0416

Sigma-Aldrich

T4 Beta-glucosyltransferase

recombinant, expressed in E. coli, ≥83% (SDS-PAGE)

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Synonym(s):
T4-phage beta-glucosyltransferase, UDP glucose-DNA ?-glucosyltransferase, hydroxymethyl cytosine
UNSPSC Code:
12352200
NACRES:
NA.32

biological source

Escherichia coli

recombinant

expressed in E. coli

Assay

≥83% (SDS-PAGE)

form

aqueous solution

mol wt

41.6 kDa

packaging

pkg of 100 μg

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

bacteriophage T4 ... B-GT(1258765)

General description

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.

Application

Useful for the differentiation of hydroxymethylcytosine (HMC) from methylcytosine in DNA, via glucosylating HMC and protecting HMC from endonuclease cleavage.

Biochem/physiol Actions

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.

Physical form

Formulated in 200 mM imidazole and 20% glycerol.

Pictograms

Health hazardExclamation mark

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

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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)
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
Bacteriophage T4 genome.
Miller ES
Microbiology and Molecular Biology Reviews, 67(1), 86-156 (2003)
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)
T4 phage beta-glucosyltransferase: substrate binding and proposed catalytic mechanism.
Morera S
Journal of Molecular Biology, 292(3), 717-730 (1999)

Articles

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