915793
Methyl-o-nitropiperonyllysine
≥95%
别名:
N6-((1-(6-Nitrobenzo[d][1,3]dioxol-5-yl)ethoxy)carbonyl)-L-lysine, Light-triggered decaging Lys, Photo-controlled amino acid, Photocaged amino acid, Photocleavable lysine derivative, mNPK
质量水平
方案
≥95%
表单
powder
储存温度
−20°C
SMILES字符串
[N+](=O)([O-])c1cc2c(cc1C(OC(=O)NCCCC[C@H](N)C(=O)O)C)OCO2
InChI
1S/C16H21N3O8/c1-9(27-16(22)18-5-3-2-4-11(17)15(20)21)10-6-13-14(26-8-25-13)7-12(10)19(23)24/h6-7,9,11H,2-5,8,17H2,1H3,(H,18,22)(H,20,21)/t9?,11-/m0/s1
InChI key
ZXXFKVZFDGUTQW-UMJHXOGRSA-N
应用
Methyl-o-nitropiperonyllysine (mNPK) trifluoroacetic acid is a photo-responsive unnatural amino acid (UAA) for spatiotemporal control of biological molecules or processes as reported by Kneuttinger et al. Irradiation with UV light decages the Lys amino acid, freeing the residue or protein for biological activity. Tools such as mNPK will find wide utility in light regulation of activity, allostery, and enzyme pathways.
Product can be used with our line of photoreactors: Including Penn PhD (Z744035) & SynLED 2.0 (Z744080)
Product can be used with our line of photoreactors: Including Penn PhD (Z744035) & SynLED 2.0 (Z744080)
其他说明
Light Regulation of Enzyme Allostery through Photoresponsive Unnatural Amino Acids
Precise Photoremovable Perturbation of a Virus-Host Interaction
Genetic code expansion in the mouse brain
Genetically encoded optical activation of DNA recombination in human cells
Bioorthogonal Chemical Activation of Kinases in Living Systems
Precise Photoremovable Perturbation of a Virus-Host Interaction
Genetic code expansion in the mouse brain
Genetically encoded optical activation of DNA recombination in human cells
Bioorthogonal Chemical Activation of Kinases in Living Systems
储存分类代码
11 - Combustible Solids
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
Olivia S Walker et al.
Journal of the American Chemical Society, 138(3), 718-721 (2016-01-14)
Isocitrate dehydrogenase is mutated at a key active site arginine residue (Arg172 in IDH2) in many cancers, leading to the synthesis of the oncometabolite (R)-2-hydroxyglutarate (2HG). To investigate the early events following acquisition of this mutation in mammalian cells we
James Hemphill et al.
Journal of the American Chemical Society, 135(36), 13433-13439 (2013-08-13)
Photocaging provides a method to spatially and temporally control biological function and gene expression with high resolution. Proteins can be photochemically controlled through the site-specific installation of caging groups on amino acid side chains that are essential for protein function.
Arnaud Gautier et al.
Journal of the American Chemical Society, 132(12), 4086-4088 (2010-03-12)
Precise photochemical control of protein function can be achieved through the site-specific introduction of caging groups. Chemical and enzymatic methods, including in vitro translation and chemical ligation, have been used to photocage proteins in vitro. These methods have been extended
Arnaud Gautier et al.
Journal of the American Chemical Society, 133(7), 2124-2127 (2011-01-29)
We report a general strategy for creating protein kinases in mammalian cells that are poised for very rapid activation by light. By photoactivating a caged version of MEK1, we demonstrate the specific, rapid, and receptor independent activation of an artificial
Hanna Engelke et al.
ACS synthetic biology, 3(10), 731-736 (2014-06-17)
Controlled manipulation of proteins and their function is important in almost all biological disciplines. Here, we demonstrate control of protein activity with light. We present two different applications-light-triggered transcription and light-triggered protease cleavage-both based on the same concept of protein
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