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Sigma-Aldrich

Fmoc-L-photo-methionine

≥95%, for peptide synthesis

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Synonym(s):
(S)-2-(((9H-Fluoren-9-yl)methoxy)carbonylamino)-4-(3-methyl-3H-diazirin-3-yl)butanoic acid, (S)-2-(Fmoc-amino)-4-(3H-diazirin-3-yl)pentanoic acid, Diazirine amino acid, Photo-Met, Photo-crosslinking amino acid, Photoprobe building block
Empirical Formula (Hill Notation):
C21H21N3O4
CAS Number:
Molecular Weight:
379.41
UNSPSC Code:
12352209
NACRES:
NA.22

Assay

≥95%

form

powder

reaction suitability

reaction type: Fmoc solid-phase peptide synthesis

application(s)

peptide synthesis

functional group

Fmoc

storage temp.

−20°C

Application

Fmoc-L-photo-methionine is a diazirine-containing, Fmoc-protected methionine amino acid and multifunctional photo-crosslinker. Its incorporation into peptides or small-molecule probes and tools allows for photoaffinity labeling of cellular targets and protein-protein interactions upon UV light (∼360 nm) irradiation to form a covalent bond. This and other multifunctional probe building blocks will continue to accelerate drug discovery research for probing cellular mechanisms, target ID/validation, and understanding traditionally undruggable targets. An unprotected version is also available as 907375.

Product can be used with our line of photoreactors: Including Penn PhD (Z744035) & SynLED 2.0 (Z744080)

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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Tangpo Yang et al.
Chemical science, 6(2), 1011-1017 (2015-02-01)
Post translational modifications (PTMs, e.g., phosphorylation, acetylation and methylation) of histone play important roles in regulating many fundamental cellular processes such as gene transcription, DNA replication and damage repair. While 'writer' and 'eraser' enzymes modify histones by catalyzing the addition
Covalent capture of phospho-dependent protein oligomerization by site-specific incorporation of a diazirine photo-cross-linker.
Miquel Vila-Perelló et al.
Journal of the American Chemical Society, 129(26), 8068-8069 (2007-06-15)
Haibin Shi et al.
Chemical communications (Cambridge, England), 47(40), 11306-11308 (2011-09-17)
A clickable, affinity-based probe (AfBP), which was modified from staurosporine (a natural product kinase inhibitor), has been synthesized and used in situ for activity-based proteome profiling of potential cellular targets of staurosporine in HepG2 cancer cells.

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