914088
N6-((2-Azidoethoxy)carbonyl)-L-lysine hydrochloride
≥95%
Synonyme(s) :
(S)-2-amino-6-((2-azidoethoxy)carbonylamino)hexanoic acid hydrochloride, Clickable amino acid for bioconjugation, H-L-Lys(EO-N3)-OH HCl, Lysine-azide, UAA crosslinker
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A propos de cet article
Formule empirique (notation de Hill) :
C9H17N5O4 · xHCl
Numéro CAS:
Poids moléculaire :
259.26 (free base basis)
MDL number:
UNSPSC Code:
12352209
NACRES:
NA.26
Service technique
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assay
≥95%
form
powder
storage temp.
−20°C
SMILES string
[N+](=[N-])=NCCOC(=O)NCCCC[C@H](N)C(=O)O.C
InChI
1S/C9H17N5O4.CH4/c10-7(8(15)16)3-1-2-4-12-9(17)18-6-5-13-14-11;/h7H,1-6,10H2,(H,12,17)(H,15,16);1H4/t7-;/m0./s1
InChI key
LQERWAMRZNEGIE-FJXQXJEOSA-N
Application
N6-((2-Azidoethoxy)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 azide for bioorthogonal reaction with alkynes.
Other Notes
Construction of bacterial cells with an active transport system for unnatural amino acids
Semisynthesis of an Active Enzyme by Quantitative Click Ligation
A Robust and Quantitative Reporter System To Evaluate Noncanonical Amino Acid Incorporation in Yeast
An orthogonalized platform for genetic code expansion in both bacteria and eukaryotes
Semisynthesis of an Active Enzyme by Quantitative Click Ligation
A Robust and Quantitative Reporter System To Evaluate Noncanonical Amino Acid Incorporation in Yeast
An orthogonalized platform for genetic code expansion in both bacteria and eukaryotes
signalword
Danger
hcodes
Hazard Classifications
Self-react. C
Classe de stockage
5.2 - Organic peroxides and self-reacting hazardous materials
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Siqi Zheng et al.
Angewandte Chemie (International ed. in English), 53(25), 6449-6453 (2014-05-16)
Coupling the genetic code expansion technique with bioorthogonal reactions enables precise control over the conjugation site as well as the choice of fluorescent probes during protein labeling. However, the advantages of this strategy over bulky and rigid fluorescent proteins (FPs)
Chuanling Zhang et al.
Biomaterials, 80, 134-145 (2015-12-29)
Virus-based nanoparticles have shown promise as vehicles for delivering therapeutic genes. However, the rational design of viral vectors that enable selective tropism towards particular types of cells and tissues remains challenging. Here, we explored structural-functional relationships of the adeno-associated virus
Sanggil Kim et al.
Bioorganic & medicinal chemistry, 24(22), 5816-5822 (2016-10-26)
Proteins often function as complex structures in conjunction with other proteins. Because these complex structures are essential for sophisticated functions, developing protein-protein conjugates has gained research interest. In this study, site-specific protein-protein conjugation was performed by genetically incorporating an azide-containing
Numéro d'article de commerce international
| Référence | GTIN |
|---|---|
| 914088-250MG | 04061842050802 |