推薦產品
product name
Dansyl-L-alanine cyclohexylammonium salt, fluorescent amino acid
化驗
≥98% (TLC)
形狀
powder
技術
protein expression: suitable
儲存溫度
−20°C
SMILES 字串
NC1CCCCC1.C[C@H](NS(=O)(=O)c2cccc3c(cccc23)N(C)C)C(O)=O
InChI
1S/C15H18N2O4S.C6H13N/c1-10(15(18)19)16-22(20,21)14-9-5-6-11-12(14)7-4-8-13(11)17(2)3;7-6-4-2-1-3-5-6/h4-10,16H,1-3H3,(H,18,19);6H,1-5,7H2/t10-;/m0./s1
InChI 密鑰
CZUBQNQWSOLSJH-PPHPATTJSA-N
相關類別
應用
Alanine conjugated to the fluorophore 5-(dimethylamino)naphthalene-1-sulfonyl (dansyl). The unnatural amino acid has been incorporated into expressed proteins by use of a mutated aminoacyl-tRNA synthetase specific for dansylalanine.
生化/生理作用
Dansyl-L-alanine contains an N-terminal fluorophore (dansyl) making it useful as a fluorescent marker/probe. Dansylalanine can be incorporated into proteins by newly developing techniques that expand the genetic code.
儲存類別代碼
11 - Combustible Solids
水污染物質分類(WGK)
WGK 3
閃點(°F)
Not applicable
閃點(°C)
Not applicable
分析證明 (COA)
輸入產品批次/批號來搜索 分析證明 (COA)。在產品’s標籤上找到批次和批號,寫有 ‘Lot’或‘Batch’.。
Journal of the American Chemical Society, 131(36), 12921-12923 (2009-08-26)
Here, we report that the fluorescent amino acid, 3-(6-acetylnaphthalen-2-ylamino)-2-aminopropanoic acid (Anap), can be genetically incorporated into proteins in yeast with excellent selectivity and efficiency by means of an orthogonal tRNA/aminoacyl-tRNA synthetase pair. This small, environmentally sensitive fluorophore was site-specifically incorporated
Esterification of an unnatural amino acid structurally deviating from canonical amino acids promotes its uptake and incorporation into proteins in mammalian cells.
Chembiochem : a European journal of chemical biology, 11(16), 2268-2272 (2010-09-28)
Nature neuroscience, 10(8), 1063-1072 (2007-07-03)
Proteins participate in various biological processes and can be harnessed to probe and control biological events selectively and reproducibly, but the genetic code limits the building block to 20 common amino acids for protein manipulation in living cells. The genetic
Proceedings of the National Academy of Sciences of the United States of America, 103(26), 9785-9789 (2006-06-21)
The ability to introduce fluorophores selectively into proteins provides a powerful tool to study protein structure, dynamics, localization, and biomolecular interactions both in vitro and in vivo. Here, we report a strategy for the selective and efficient biosynthetic incorporation of
A genetically encoded fluorescent amino acid.
Proceedings of the National Academy of Sciences of the USA, 108, 9785-9789 (2006)
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