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Merck
CN

907375

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
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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

signalword

Danger

hcodes

Hazard Classifications

Self-react. C

Storage Class

5.2 - Organic peroxides and self-reacting hazardous materials

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

Regulatory Information

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Claudio Iacobucci et al.
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
Yeolin Lee et al.
Analytical chemistry, 88(19), 9503-9509 (2016-09-01)
Fc-specific antibody binding proteins (FcBPs) with the minimal domain of protein G are widely used for immobilization of well-oriented antibodies onto solid surfaces, but the noncovalently bound antibodies to FcBPs are unstable in sera containing large amounts of antibodies. Here
Knut Kölbel et al.
Angewandte Chemie (International ed. in English), 51(50), 12602-12605 (2012-10-31)
Photochemical cross-linking was applied to trap intramolecular interactions in peptides. The incorporation of diazirine-labeled amino acid analogues in combination with high-resolution mass spectrometry made it possible to catch reverse-turn conformations within peptides, exactly map their self-interacting surfaces, and discriminate between



Global Trade Item Number

SKUGTIN
907375-100MG04022536044675