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Merck
CN

907278

Sigma-Aldrich

H-L-Photo-leucine HCl

≥98%

别名:

(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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关于此项目

经验公式(希尔记法):
C5H10ClN3O2
分子量:
179.60
UNSPSC代码:
12352209
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方案

≥98%

表单

solid

反应适用性

reaction type: solution phase peptide synthesis

存货情况

available only in USA

应用

peptide synthesis

储存温度

−20°C

应用

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.

象形图

Flame

警示用语:

Danger

危险声明

危险分类

Self-react. C

储存分类代码

5.2 - Organic peroxides and self-reacting hazardous materials

WGK

WGK 3


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Nicholas Vance et al.
Bioconjugate chemistry, 30(1), 148-160 (2018-12-20)
Site-specific conjugation of small molecules to antibodies represents an attractive goal for the development of more homogeneous targeted therapies and diagnostics. Most site-specific conjugation strategies require modification or removal of antibody glycans or interchain disulfide bonds or engineering of an
Yuan Gao et al.
Chemical communications (Cambridge, England), 48(67), 8404-8406 (2012-07-18)
Here we report the first example of the use of supramolecular hydrogels to discover the protein targets of aggregates of small molecules.
Balakrishnan S Moorthy et al.
Journal of visualized experiments : JoVE, (98), 52503-52503 (2015-05-06)
Amide hydrogen/deuterium exchange (ssHDX-MS) and side-chain photolytic labeling (ssPL-MS) followed by mass spectrometric analysis can be valuable for characterizing lyophilized formulations of protein therapeutics. Labeling followed by suitable proteolytic digestion allows the protein structure and interactions to be mapped with
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
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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