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Key Documents

915793

Sigma-Aldrich

Methyl-o-nitropiperonyllysine

≥95%

Synonym(s):

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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About This Item

Empirical Formula (Hill Notation):
C16H21N3O8
CAS Number:
Molecular Weight:
383.35
MDL number:
UNSPSC Code:
12352209
NACRES:
NA.22

Quality Level

Assay

≥95%

form

powder

storage temp.

−20°C

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)

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
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
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
J Luo et al.
Chemical communications (Cambridge, England), 52(55), 8529-8532 (2016-06-10)
We developed two tightly regulated, light-activated Cre recombinase enzymes through site-specific incorporation of two genetically-encoded photocaged amino acids in human cells. Excellent optical off to on switching of DNA recombination was achieved. Furthermore, we demonstrated precise spatial control of Cre
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.

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