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Merck

914827

Sigma-Aldrich

N6-((Prop-2-yn-1-yloxy)carbonyl)-L-lysine hydrochloride

≥98%

别名:

(S)-Amino-6-((prop-2-ynyloxy)carbonylamino)hexanoic acid hydrochloride, Clickable amino acid for bioconjugation, H-L-Lys(Poc)-OH HCl, Lysine-alkyne, Plk, Propargyl-derivatized lysize, UAA crosslinker

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About This Item

经验公式(希尔记法):
C10H16N2O4 · xHCl
分子量:
228.25 (free base basis)
分類程式碼代碼:
12352200

化驗

≥98%

形狀

powder

儲存溫度

2-8°C

儲存類別代碼

11 - Combustible Solids

水污染物質分類(WGK)

WGK 3

閃點(°F)

Not applicable

閃點(°C)

Not applicable


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Ivana Nikić et al.
Angewandte Chemie (International ed. in English), 53(8), 2245-2249 (2014-01-30)
The growing demands of advanced fluorescence and super-resolution microscopy benefit from the development of small and highly photostable fluorescent probes. Techniques developed to expand the genetic code permit the residue-specific encoding of unnatural amino acids (UAAs) armed with novel clickable
Claudio Zambaldo et al.
Journal of the American Chemical Society, 139(34), 11646-11649 (2017-08-16)
Nisin is a complex lanthipeptide that has broad spectrum antibacterial activity. In efforts to broaden the structural diversity of this ribosomally synthesized lantibiotic, we now report the recombinant expression of Nisin variants that incorporate noncanonical amino acids (ncAAs) at discrete
Yiming Li et al.
Organic & biomolecular chemistry, 11(16), 2624-2629 (2013-03-02)
Three alkyne-containing pyrrolysine derivatives were synthesized and genetically encoded into proteins by a mutant PylRS-tRNA pair with high efficiencies. With these alkyne handles, site-specific dual labeling of proteins can be achieved via a bioorthogonal thiol-yne ligation reaction.
K W Swiderska et al.
Bioorganic & medicinal chemistry, 25(14), 3685-3693 (2017-05-20)
Recent advances in site-specific protein modification include the increasingly popular incorporation of unnatural amino acid(s) using amber codon, a method developed by Schultz and coworkers. In this study, we employ this technique to introduce propargyllysine (PrK) in human fibroblast growth
Tatjana Schneider et al.
Angewandte Chemie (International ed. in English), 53(47), 12925-12929 (2014-09-10)
Ubiquitylation is a complex posttranslational protein modification and deregulation of this pathway has been associated with different human disorders. Ubiquitylation comes in different flavors: Besides mono-ubiquitylation, ubiquitin chains of various topologies are formed on substrate proteins. The fate of ubiquitylated

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