产品名称
Anti-DNMT1 antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~180 kDa
species reactivity
rat, mouse, human
technique(s)
indirect immunofluorescence: 1:100-1:200 using mouse COS-7 cells
microarray: suitable
western blot: 1:1,000-1:2,000 using nuclear extracts of human HEK 293T cells
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... DNMT1(1786)
mouse ... Dnmt1(13433)
Application
Anti-DNMT1 antibody produced in rabbit has been used in western blot analysis, and staining for confocal laser scanning microscopy.
Biochem/physiol Actions
DNA methyltransferase 1 (Dnmt1) is part of different complexes; it can establish a repressive transcription complex consisting of the histone deacetylase 4 (HDAC4), DNA methyltransferase 1-associated Protein (DMAP1) and DNMT1 itself. Consistent with the role of DNA methylation in gene silencing, DNMT1 can associate with HDAC1 and MECP2 (methyl CpG binding protein 2).
DNMT1 protein is important for the maintenance of methylation, as well as for the novo methylation activities occurring in somatic cells of vertebrates. It establishes a repressive transcription complex at replication foci with histone deacetylase HDAAC4 and DMAP1.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Human DNA methyltransferase 1 (Dnmt1) is a 1616 amino acids protein; the N-terminal two-thirds of the protein is considered to be the regulatory domain, while the C-terminal region contains the catalytic domain.
In humans, the gene encodes a DNA (cytosine-5)-methyltransferase with 1616 amino acids. The N-terminal contains the regulatory domain, while the C-terminal region contains the catalytic domain. Two isoforms of DNMT1 have been isolated, DNMT1a and DNMT1b, the difference residing in 16 extra amino acids within the latter.
Immunogen
synthetic peptide corresponding to amino acids 1581-1595 of rat DNMT1, conjugated to KLH via an N-terminal added lysine residue. The sequence is conserved in human and mouse.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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存储类别
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
此项目有
Laccaic Acid A Is a Direct, DNA-competitive Inhibitor of DNA Methyltransferase 1
Fagan RL, et al.
The Journal of Biological Chemistry, 288(33), 23858-23858 (2013)
Rajiv P Sharma et al.
Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology, 35(10), 2009-2020 (2010-07-16)
The study of CpG methylation of genomic DNA in neurons has emerged from the shadow of cancer biology into a fundamental investigation of neuronal physiology. This advance began with the discovery that catalytic and receptor proteins related to the insertion
Rajiv P Sharma et al.
Epigenetics, 3(2), 74-80 (2008-06-10)
DNA methylation in post-mitotic neurons is reported to serve a variety of functions from survival during development to the consolidation of memory. Of particular interest with regards neuronal functioning is the change in site-specific methylation of a variety of gene
Depolarization induces downregulation of DNMT1 and DNMT3 in primary cortical cultures
Sharma RP, et al.
Epigenetics, 3(2), 74- 80 (2008)
Laura P Sutton et al.
Epigenetics, 14(10), 989-1002 (2019-06-19)
Many cancer therapies operate by inducing double-strand breaks (DSBs) in cancer cells, however treatment-resistant cells rapidly initiate mechanisms to repair damage enabling survival. While the DNA repair mechanisms responsible for cancer cell survival following DNA damaging treatments are becoming better
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