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About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
biological source
human
recombinant
expressed in baculovirus infected insect cells
tag
GST tagged (N-terminal)
Assay
≥50% (SDS-PAGE)
form
aqueous solution
potency
≥50
mol wt
211 kDa
packaging
pkg of 10 μg
manufacturer/tradename
Sigma-Aldrich
storage condition
avoid repeated freeze/thaw cycles
concentration
0.12 mg/mL
technique(s)
inhibition assay: suitable
NCBI accession no.
UniProt accession no.
application(s)
life science and biopharma
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... DNMT1(1786)
General description
Research area: Cell cycle
DNMT1 (DNA methyltransferase 1) is a member of the DNMT enzyme family which also includes DNMT2, DNMT3A, and DNMT3B. It is a multidomain protein composed of 1616 amino acids. It has a methyltransferase domain in its C-terminal, which shows sequence homology to bacterial methyltransferases. The DNMT1 gene is mapped to human chromosome 19p13.2.
DNMT1 (DNA methyltransferase 1) is a member of the DNMT enzyme family which also includes DNMT2, DNMT3A, and DNMT3B. It is a multidomain protein composed of 1616 amino acids. It has a methyltransferase domain in its C-terminal, which shows sequence homology to bacterial methyltransferases. The DNMT1 gene is mapped to human chromosome 19p13.2.
The DNMT1 gene is mapped to human chromosome 19p13.2.
Application
DNMT1 (DNA methyltransferase 1) has been used for RNA electrophoretic mobility shift assay (REMSA) to determine the role of extra-coding RNAs (ecRNAs) in controlling neuronal DNA methylation, through interaction with DNA methyltransferases.
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Biochem/physiol Actions
DNMT1 (DNA methyltransferase 1) is the predominant enzyme that is responsible for maintaining the level of DNA methylation. It is responsible for replicating CpG methylation patterns from parent to daughter DNA strands, thus, creating heritable methylation signatures through cell division. It, therefore, maintains epigenetic state of DNA. Abnormalities in the expression of this protein are linked with the progression and prognosis of multiple cancers, such as hepatocellular carcinoma, pancreatic, lung and bladder cancers. Up-regulation of this protein in GC (gastric cancer) with less differentiation, advanced stage and increased rate of mortality. Upregulation of the DNMT1 gene indicates poor prognosis in malignant cancers including renal cell carcinoma, lymphoma, pancreatic and and bladder cancer.
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.
Other Notes
One unit is defined as the amount of enzyme required to methylate 1 pmol of DNA substrate/min at 37°C.
Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Epigenetic regulation of DNA methyltransferases: DNMT1 and DNMT3B in gliomas.
Rajendran G, et al.
Journal of Neuro-Oncology, 104(2), 483-494 (2011)
Differential expression of the epigenetic methylation-related protein DNMT1 by breast cancer molecular subtype and stromal histology.
Shin E, et al.
Journal of Translational Medicine, 14:87 (2016)
Extra-coding RNAs regulate neuronal DNA methylation dynamics.
Savell KE, et al.
Nature Communications, 7:12091 (2016)
Xun Gao et al.
American journal of respiratory cell and molecular biology, 60(3), 323-334 (2018-10-18)
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Journal of peptide science : an official publication of the European Peptide Society, 25(9), e3200-e3200 (2019-07-17)
Posttranslational modifications of histone proteins, which form nucleosome cores, play an important role in gene regulation. Ubiquitination is one such modification. We previously reported on the synthesis of ubiquitinated histone H3 with an isopeptide mimetic structure. In this report, we
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