SRP0127
DNMT2 Active human
recombinant, expressed in baculovirus infected insect cells, ≥80% (SDS-PAGE)
Synonym(s):
DNA (cytosine-5-)-methyltransferase 2, PUMET, RNMT1, tRNA (cytosine-5-)-methyltransferas, tRNA aspartic acid methyltransferase 1
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About This Item
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biological source
human
recombinant
expressed in baculovirus infected insect cells
assay
≥80% (SDS-PAGE)
form
aqueous solution
mol wt
71 kDa
packaging
pkg of 10 μg
concentration
>0.02 mg/mL
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... TRDMT1(1787)
General description
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.
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Biochem/physiol Actions
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.
Physical form
Formulated in 25 mM Tris-HCl, pH 8.0, 100 mM NaCl, 0.05% Tween-20 and 10% glycerol.
Preparation Note
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.
Certificates of Analysis (COA)
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Azacytidine Inhibits RNA Methylation at DNMT2 Target Sites in Human Cancer Cell Lines
Cancer Research, 69(20) (2009)
Human DNMT2 methylates tRNAAsp molecules using a DNA methyltransferase-like catalytic mechanism
RNA, 14(8), 1663-1670 (2008)
Assignment1 of candidate DNA methyltransferase gene (DNMT2) to human chromosome band 10p15.1 by in situ hybridization
Cytogenetic and genome research, 82 (1998)
Mapping the tRNA binding site on the surface of human DNMT2 methyltransferase.
Biochemistry, 51(22), 4438-4444 (2012)
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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