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Merck

907278

Sigma-Aldrich

H-L-Photo-leucine HCl

≥98%

Sinónimos:

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

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About This Item

Fórmula empírica (notación de Hill):
C5H10ClN3O2
Peso molecular:
179.60
UNSPSC Code:
12352209

assay

≥98%

form

solid

reaction suitability

reaction type: solution phase peptide synthesis

availability

available only in USA

application(s)

peptide synthesis

storage temp.

−20°C

Application

H-L-Photo-leucine HCl is a diazirine-containing leucine 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 907391.

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Referencia del producto
Descripción
Precios

pictograms

Flame

signalword

Danger

hcodes

Hazard Classifications

Self-react. C

Storage Class

5.2 - Organic peroxides and self-reacting hazardous materials

wgk_germany

WGK 3


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Bojie Zhang et al.
Journal of the American Society for Mass Spectrometry, 27(3), 552-555 (2015-12-19)
Protein footprinting combined with mass spectrometry provides a method to study protein structures and interactions. To improve further current protein footprinting methods, we adapted the fast photochemical oxidation of proteins (FPOP) platform to utilize carbenes as the footprinting reagent. A
Christopher J Shaffer et al.
Journal of the American Society for Mass Spectrometry, 27(4), 633-645 (2016-01-29)
Noncovalent complexes of hydrophobic peptides GLLLG and GLLLK with photoleucine (L*) tagged peptides G(L* n L m )K (n = 1,3, m = 2,0) were generated as singly charged ions in the gas phase and probed by photodissociation at 355
Christopher J Shaffer et al.
Journal of the American Society for Mass Spectrometry, 27(7), 1176-1185 (2016-04-10)
We report a combined experimental and computational study aimed at elucidating the structure of N-terminal fragment ions of the c type produced by electron transfer dissociation of photo-leucine (L*) peptide ions GL*GGKX. The c 4 ion from GL*GGK is found
Andrew L MacKinnon et al.
Journal of the American Chemical Society, 129(47), 14560-14561 (2007-11-07)
Photoaffinity labeling is a powerful tool to identify protein targets of biologically active small molecules, yet is often limited by the size, chemical properties, and availability of photoreactive groups. We report an improved synthesis of photo-leucine, a diazirine-based photoreactive analogue
Lavanya K Iyer et al.
Molecular pharmaceutics, 10(12), 4629-4639 (2013-10-16)
Local side-chain interactions in lyophilized protein formulations were mapped using solid-state photolytic labeling-mass spectrometry (ssPL-MS). Photoactive amino acid analogues (PAAs) were used as probes and either added to the lyophilized matrix or incorporated within the amino acid sequence of a

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