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Merck

907278

Sigma-Aldrich

H-L-Photo-leucine HCl

≥98%

Synonim(y):

(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

Wzór empiryczny (zapis Hilla):
C5H10ClN3O2
Masa cząsteczkowa:
179.60
Kod UNSPSC:
12352209

Próba

≥98%

Postać

solid

przydatność reakcji

reaction type: solution phase peptide synthesis

dostępność

available only in USA

Zastosowanie

peptide synthesis

temp. przechowywania

−20°C

Zastosowanie

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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produkt powiązany

Numer produktu
Opis
Cennik

Piktogramy

Flame

Hasło ostrzegawcze

Danger

Zwroty wskazujące rodzaj zagrożenia

Zwroty wskazujące środki ostrożności

Klasyfikacja zagrożeń

Self-react. C

Kod klasy składowania

5.2 - Organic peroxides and self-reacting hazardous materials

Klasa zagrożenia wodnego (WGK)

WGK 3


Certyfikaty analizy (CoA)

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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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
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
Chanelle C Jumper et al.
Analytical chemistry, 84(10), 4411-4418 (2012-04-07)
Carbene chemistry has been used recently in structural mass spectrometry as a labeling method for mapping protein surfaces. The current study presents a method for quantitating label distribution at the amino acid level and explores the nature and basis for
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
Chanelle C Jumper et al.
Analytical chemistry, 83(8), 2913-2920 (2011-03-24)
We report a protein labeling method using nonselective carbene reactions of sufficiently high efficiency to permit detection by mass spectrometric methods. The approach uses a diazirine-modified amino acid (l-2-amino-4,4'-azipentanoic acid, "photoleucine") as a label source, which is converted to a

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