914827
N6-((Prop-2-yn-1-yloxy)carbonyl)-L-lysine hydrochloride
≥98%
Synonym(s):
(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
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Assay
≥98%
form
powder
storage temp.
2-8°C
Application
N6-((Prop-2-yn-1-yloxy)carbonyl)-L-lysine hydrochloride is a clickable amino acid derivative for site-specific incorporation into recombinant proteins or synthesis of chemical probes and tools for biological applications. This non-canonical lysine possesses an alkyne for bioorthogonal reaction with azides.
Other Notes
Site-Specific Encoding of Photoactivity in Antibodies Enables Light-Mediated Antibody-Antigen Binding on Live Cells Quick View Other Sources
PEGylated polylysine derived copolymers with reduction-responsive side chains for anticancer drug delivery
Construction of bacterial cells with an active transport system for unnatural amino acids
Semisynthesis of an Active Enzyme by Quantitative Click Ligation
Combined Use of Unnatural Amino Acids Enables Dual-Color Super-Resolution Imaging of Proteins via Click Chemistry
PEGylated polylysine derived copolymers with reduction-responsive side chains for anticancer drug delivery
Construction of bacterial cells with an active transport system for unnatural amino acids
Semisynthesis of an Active Enzyme by Quantitative Click Ligation
Combined Use of Unnatural Amino Acids Enables Dual-Color Super-Resolution Imaging of Proteins via Click Chemistry
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Product No.
Description
Pricing
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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ACS chemical biology, 13(9), 2472-2483 (2018-08-01)
Single-molecule techniques allow unique insights into biological systems as they provide unrivaled access to structural dynamics and conformational heterogeneity. One major bottleneck for reliable single-molecule Förster resonance energy transfer (smFRET) analysis is the identification of suitable fluorophore labeling sites that
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
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
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
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.
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