H-L-Lys(2-N3-Z)-OH

Nom chimique: N6-(((2-azidobenzyl)oxy)carbonyl)-L-lysine // Synonymes: H-Lys(2-N3-Z), H-Lys(Z(2-N3))-OH, o-Az-Z-Lys, oAzZLys, H-Lys(Z-2-N3)-OH, N-epsilon-o-azidobenzyloxycarbonyl lysine, N-epsilon-(o-azidobenzyloxycarbonyl)-L-lysine, OABK,(2S)-6-(2-Azido-benzyloxycarbo nylamino)-2-amino-hexanoic acid

  • n° Art.:HAA9380
  • n° CAS:1131963-69-3
  • Formule:C14H19N5O4
  • Masse moléculaire:321,34 g/mol
  • Pureté:min.98%
  • Pureté Énantiomérique:min.99,7%

Starting at 132,00 €

Grouped product items
Nombre Unité de vente Prix SKU
100 mg
132,00 €
HAA9380.0100
250 mg
220,00 €
HAA9380.0250
500 mg
396,00 €
HAA9380.0500
1 g
616,00 €
HAA9380.1000
5 g
2 200,00 €
HAA9380.5000
description

Modified Lysine containing an Azide moiety as a bioorthogonal ligation handle. This Lysine derivative can be incorporated into proteins for further modification using Click-chemistry or Staudinger ligation (Lysine decaging).

references

Multistep Engineering of Pyrrolysyl-tRNA Synthetase to Genetically Encode N-epsilon-(o-Azidobenzyloxycarbonyl) lysine for Site-Specific Protein Modification; T. Yanagisawa, R. Ishii, R. Fukunaga, T. Kobayashi, K. Sakamoto, S. Yokoyama; Chem. Biol. 2008, 15: 1187–1197. https://doi.org/10.1016/j.chembiol.2008.10.004

Genetic-code evolution for protein synthesis with non-natural amino acids; T. Mukai, T. Yanagisawa, K. Ohtake, M. Wakamori, J. Adachi, N. Hino, A. Sato, T. Kobayashi, A. Hayashi, M. Shirouzu, T. Umehara, S. Yokoyama, K. Sakamoto; Biochem. Biophys. Res. Commun. 2011, 411(4): 757-61. https://doi.org/10.1016/j.bbrc.2011.07.020

Genetic Code Expansion in Zebrafish Embryos and Its Application to Optical Control of Cell Signaling; J. Liu, J. Hemphill, S. Samanta, M. Tsang, A. Deiters; J. Am. Chem. Soc. 2017, 139(27): 9100–9103. https://doi.org/10.1021/jacs.7b02145

Extensive Survey of Antibody Invariant Positions for Efficient Chemical Conjugation Using Expanded Genetic Codes; A. Kato, M. Kuratani, T. Yanagisawa, K. Ohtake, A. Hayashi, Y. Amano, K. Kimura, S. Yokoyama, K. Sakamoto, Y. Shiraishi; Bioconjugate Chem. 2017, 28(8): 2099–2108. https://doi.org/10.1021/acs.bioconjchem.7b00265

Small-molecule control of protein function through Staudinger reduction; J. Luo, Q. Liu, K. Morihiro, A. Deiters; Nat. Chem. 2016, (8): 1027–1034. https://doi.org/10.1038/nchem.2573

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