117196
(2-溴乙基)三甲基溴化铵
98%
别名:
Bromocholine Bromide
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关于此项目
线性分子式:
BrCH2CH2N(CH3)3Br
化学文摘社编号:
分子量:
246.97
EC 号:
MDL编号:
UNSPSC代码:
12352101
PubChem化学物质编号:
NACRES:
NA.22
质量水平
方案
98%
mp
244 °C (dec.) (lit.)
SMILES字符串
[Br-].C[N+](C)(C)CCBr
InChI
1S/C5H13BrN.BrH/c1-7(2,3)5-4-6;/h4-5H2,1-3H3;1H/q+1;/p-1
InChI key
OINMNSFDYTYXEQ-UHFFFAOYSA-M
警示用语:
Danger
危险分类
Acute Tox. 3 Dermal - Acute Tox. 3 Inhalation - Acute Tox. 3 Oral - Eye Dam. 1 - Skin Corr. 1B
储存分类代码
6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Faceshields, Gloves, type P2 (EN 143) respirator cartridges, type P3 (EN 143) respirator cartridges
Haibo Wang et al.
Nature structural & molecular biology, 27(1), 8-13 (2019-12-11)
Recognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies revealed how reader domains bind modified histone peptides, it is unclear how reader domains interact with modified nucleosomes. Here, we report the cryo-electron
Caitlin I Stoddard et al.
Molecular cell, 73(1), 73-83 (2018-11-13)
DNA methylation and H3K9me are hallmarks of heterochromatin in plants and mammals, and are successfully maintained across generations. The biochemical and structural basis for this maintenance is poorly understood. The maintenance DNA methyltransferase from Zea mays, ZMET2, recognizes dimethylation of
Francesca Munari et al.
PloS one, 8(4), e60887-e60887 (2013-04-16)
As essential components of the molecular machine assembling heterochromatin in eukaryotes, HP1 (Heterochromatin Protein 1) proteins are key regulators of genome function. While several high-resolution structures of the two globular regions of HP1, chromo and chromoshadow domains, in their free
Phillip A Dumesic et al.
Molecular cell, 79(1), 127-139 (2020-05-22)
C.neoformans Dnmt5 is an unusually specific maintenance-type CpG methyltransferase (DNMT) that mediates long-term epigenome evolution. It harbors a DNMT domain and SNF2 ATPase domain. We find that the SNF2 domain couples substrate specificity to an ATPase step essential for DNA
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