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质量水平
方案
≥97% (TLC)
表单
powder
包含
salts and water as balance
组成
Amino acid content, ~75%
技术
LC/MS: suitable
颜色
white
储存温度
−20°C
SMILES字符串
[Cl-].C[N+](C)(C)CCCC[C@H](N)C(O)=O
InChI
1S/C9H20N2O2.ClH/c1-11(2,3)7-5-4-6-8(10)9(12)13;/h8H,4-7,10H2,1-3H3;1H/t8-;/m0./s1
InChI key
ZKIJKCHCMFGMCM-QRPNPIFTSA-N
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, type N95 (US)
Jean-François Couture et al.
The Journal of biological chemistry, 281(28), 19280-19287 (2006-05-10)
SET domain enzymes represent a distinct family of protein lysine methyltransferases in eukaryotes. Recent studies have yielded significant insights into the structural basis of substrate recognition and the product specificities of these enzymes. However, the mechanism by which SET domain
Importance of charge independent effects in readout of the trimethyllysine mark by HP1 chromodomain.
Zhenyu Lu et al.
Journal of the American Chemical Society, 131(41), 14928-14931 (2009-10-01)
Histone modifications are implicated in epigenetic inheritance and are of central importance in regulating chromatin structure and gene expression. A prototype example is the trimethylation (Me3) of lysine 9 on histone 3 (H3), which is a readout by an aromatic
Naomi van Vlies et al.
Analytical biochemistry, 354(1), 132-139 (2006-05-19)
Although the mouse frequently is used to study metabolism and deficiencies therein, little is known about carnitine biosynthesis in this animal. To this point, only laborious procedures have been described to measure the activity of carnitine biosynthesis enzymes using subcellular
Lynnette M A Dirk et al.
Biochemistry, 46(12), 3905-3915 (2007-03-07)
Processive versus distributive methyl group transfer was assessed for pea Rubisco large subunit methyltransferase, a SET domain protein lysine methyltransferase catalyzing the formation of trimethyllysine-14 in the large subunit of Rubisco. Catalytically competent complexes between an immobilized form of des(methyl)
Yasunori Tokuda et al.
Journal of bioscience and bioengineering, 111(4), 402-407 (2011-01-11)
The preparation of posttranslationally modified proteins is required to investigate the function and structure of modified proteins. However, homogeneously modified proteins are not easily isolated from natural sources or prepared using modification enzymes. Non-natural amino acid mutagenesis has enabled us
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