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
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关于此项目
经验公式（希尔记法）:
C16H21N3O8
化学文摘社编号:
分子量:
383.35
UNSPSC Code:
12352209
NACRES:
NA.22
MDL number:
Assay:
≥95%
Form:
powder
SMILES string
[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
assay
≥95%
form
powder
storage temp.
−20°C
Quality Level
Application
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)
Other Notes
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
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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
Sarah B Erickson et al.
Angewandte Chemie (International ed. in English), 56(15), 4234-4237 (2017-03-16)
Viruses utilize distinct binding interactions with a variety of host factors to gain entry into host cells. A chemical strategy is described to precisely perturb a specific molecular interaction between adeno-associated virus and its host cell, which can be rapidly
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.
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
Gong Zhang et al.
ACS central science, 2(5), 325-331 (2016-06-10)
Selective manipulation of protein kinases under living conditions is highly desirable yet extremely challenging, particularly in a gain-of-function fashion. Here we employ our recently developed bioorthogonal cleavage reaction as a general strategy for intracellular activation of individual kinases. Site-specific incorporation
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