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907375

Sigma-Aldrich

H-L-Photo-methionine HCl

≥95%

Synonym(s):

(S)-2-Amino-4-(3-methyl-3H-diazirin-3-yl)butanoic acid hydrochloride, (S)-2-Amino-4-(3H-diazirin-3-yl)pentanoic acid hydrochloride, Diazirine amino acid, Photo-Met, Photo-crosslinking amino acid, Photoprobe building block

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About This Item

Empirical Formula (Hill Notation):
C6H12ClN3O2
CAS Number:
Molecular Weight:
193.63
UNSPSC Code:
12352209

Assay

≥95%

form

powder

reaction suitability

reaction type: solution phase peptide synthesis

availability

available only in USA

application(s)

peptide synthesis

storage temp.

2-8°C

Application

H-L-Photo-Methionine HCl is a diazirine-containing 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 Fmoc-protected version is also available as 907367.

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

Pictograms

Flame

Signal Word

Danger

Hazard Statements

Hazard Classifications

Self-react. C

Storage Class Code

5.2 - Organic peroxides and self-reacting hazardous materials

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Proceedings of the National Academy of Sciences of the United States of America, 113(13), 3615-3620 (2016-03-16)
Thiopeptides are a subclass of ribosomally synthesized and posttranslationally modified peptides (RiPPs) with complex molecular architectures and an array of biological activities, including potent antimicrobial activity. Here we report the generation of thiopeptides containing noncanonical amino acids (ncAAs) by introducing
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Analytical chemistry, 90(4), 2805-2809 (2018-01-30)
A major challenge in cross-linking/mass spectrometry (MS) is targeting carboxyl functions in proteins under physiological conditions that do not disturb the protein's conformation. Cross-linking of glutamic acid and aspartic acid residues in proteins will greatly expand the scope of structural
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Proceedings of the National Academy of Sciences of the United States of America, 114(46), E9903-E9912 (2017-11-01)
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