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主要文件

安全信息

SRP0127

Sigma-Aldrich

DNMT2 Active human

recombinant, expressed in baculovirus infected insect cells, ≥80% (SDS-PAGE)

别名:

DNA (cytosine-5-)-methyltransferase 2, PUMET, RNMT1, tRNA (cytosine-5-)-methyltransferas, tRNA aspartic acid methyltransferase 1

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About This Item

UNSPSC代码:
12352200
NACRES:
NA.32

生物来源

human

重组

expressed in baculovirus infected insect cells

方案

≥80% (SDS-PAGE)

表单

aqueous solution

分子量

71 kDa

包装

pkg of 10 μg

浓度

>0.02 mg/mL

NCBI登记号

UniProt登记号

运输

dry ice

储存温度

−70°C

基因信息

human ... TRDMT1(1787)

一般描述

DNA (cytosine-5-)-methyltransferase 2 (DNMT2) is a highly conserved protein which is part of the DNA methyltransferase family. It possesses a conserved cysteine residue in its catalytic pocket. The gene encoding it is localized on human chromosome 10p14->p12.

应用

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

生化/生理作用

DNA (cytosine-5-)-methyltransferase 2 (DNMT2) methylates the cytosine-38 residue of the aspartic acid transfer RNA (tRNA-Asp). It has been shown to interact with the anticodon stem and loop. The protein also functions in cellular physiology and stress response. It is significantly expressed in cancers.

外形

Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20 and 10% glycerol.

制备说明

Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.

法规信息

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访问文档库

Azacytidine Inhibits RNA Methylation at DNMT2 Target Sites in Human Cancer Cell Lines
Matthias Schaefer
Cancer Research, 69(20) (2009)
Mapping the tRNA binding site on the surface of human DNMT2 methyltransferase.
Jurkowski TP
Biochemistry, 51(22), 4438-4444 (2012)
Assignment1 of candidate DNA methyltransferase gene (DNMT2) to human chromosome band 10p15.1 by in situ hybridization
Vilain A
Cytogenetic and genome research, 82 (1998)
Human DNMT2 methylates tRNAAsp molecules using a DNA methyltransferase-like catalytic mechanism
Tomasz P. Jurkowski
RNA, 14(8), 1663-1670 (2008)
Winfried Elhardt et al.
Biochimie, 112, 66-72 (2015-03-10)
Methylation of tRNA is an important post-transcriptional modification and aberrations in tRNA modification has been implicated in cancer. The DNMT2 protein methylates C38 of tRNA-Asp and it has a role in cellular physiology and stress response and its expression levels

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