产品名称
DNMT1 Active human, recombinant, expressed in baculovirus infected insect cells, ≥50% (SDS-PAGE)
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)
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.
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.
Other Notes
One unit is defined as the amount of enzyme required to methylate 1 pmol of DNA substrate/min at 37°C.
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.
存储类别
12 - Non Combustible Liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
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)
Polymorphisms of the DNA Methyltransferase 1 Gene Predict Survival of Gastric Cancer Patients Receiving Tumorectomy.
Jia Z, et al.
Disease Markers (2016)
Xun Gao et al.
American journal of respiratory cell and molecular biology, 60(3), 323-334 (2018-10-18)
The factors involved in disturbing host homeostasis during sepsis are largely unknown. We sought to determine the immunopathological role of apoptosis inhibitor of macrophage (AIM)/CD5L in sepsis. Here, we show that blockade of AIM led to significantly increased survival after
Extra-coding RNAs regulate neuronal DNA methylation dynamics.
Savell KE, et al.
Nature Communications, 7:12091 (2016)
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