M9317
Anti-MeCP2 antibody produced in rabbit
~0.6 mg/mL, affinity isolated antibody, buffered aqueous solution
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~75 kDa
species reactivity
human
concentration
~0.6 mg/mL
technique(s)
microarray: suitable, western blot: 0.5-1 μg/mL using nuclear extracts of the MCF7 breast carcinoma cell line.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... MECP2(4204)
mouse ... Mecp2(17257)
rat ... Mecp2(29386)
General description
Methyl-CpG binding protein 2 (MeCP2) possesses a methyl-CpG-binding domain (MBD) and a transcriptional repression domain.
Immunogen
synthetic peptide corresponding to the C-terminus of human MeCP2 (amino acids 465-478) conjugated to KLH. The sequence is conserved in rat and mouse.
Biochem/physiol Actions
MeCP2 can bind to a single symmetrically methylated CpG pair. It is also capable of binding to chromosomes at sites known to have methylated DNA. MeCP2 silences transcription by recruiting the histone deacetylase (HDAC) repressive machinery via recruitment of the Sin 3A corepressor thus removing acetyl groups from histones and consequently silencing genes.
Methyl-CpG binding protein 2 (MeCP2) has been shown be crucial for brain development. It is part of the methyl-CpG-binding proteins, which are involved in repression of gene expression by binding to methylated DNA. Mutations in the gene encoding MeCP2 have been associated with Rett syndrome (RTT).
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.
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.
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存储类别
10 - Combustible liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
低风险生物材料
常规特殊物品
此项目有
Joseph R Kurian et al.
Epigenetics, 2(3), 173-178 (2007-10-30)
Pervasive developmental disorder is a classification covering five related conditions including the neurodevelopmental disorder Rett syndrome (RTT) and autism. Of these five conditions, only RTT has a known genetic cause with mutations in Methyl-CpG-binding protein 2 (MeCP2), a global repressor
Gilda Stefanelli et al.
Scientific reports, 6, 28295-28295 (2016-06-22)
MeCP2 is a transcriptional regulator whose functional alterations are responsible for several autism spectrum and mental disorders. Post-translational modifications (PTMs), and particularly differential phosphorylation, modulate MeCP2 function in response to diverse stimuli. Understanding the detailed role of MeCP2 phosphorylation is
David P Stuss et al.
Nucleic acids research, 41(9), 4888-4900 (2013-04-06)
MeCP2 is a methyl-CpG-binding protein that is a main component of brain chromatin in vertebrates. In vitro studies have determined that in addition to its specific methyl-CpG-binding domain (MBD) MeCP2 also has several chromatin association domains. However, the specific interactions
Romana Tomasoni et al.
eLife, 6 (2017-03-30)
Inflammation modifies risk and/or severity of a variety of brain diseases through still elusive molecular mechanisms. Here we show that hyperactivation of the interleukin 1 pathway, through either ablation of the interleukin 1 receptor 8 (IL-1R8, also known as SIGIRR
Tugba G Kucukkal et al.
Biochemistry, 54(41), 6357-6368 (2015-09-30)
Rett syndrome causing missense mutations in the methyl-CpG-binding domain (MBD) of methyl CpG-binding protein 2 (MeCP2) were investigated both in silico and in vitro to reveal their effect on protein stability. It is demonstrated that the vast majority of frequently
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