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914088

Sigma-Aldrich

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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About This Item

Formule empirique (notation de Hill):
C9H17N5O4 · xHCl
Numéro CAS:
1994331-17-7
Poids moléculaire :
259.26 (free base basis)
Code UNSPSC :
12352209

Niveau de qualité

100

Pureté

≥95%

Forme

powder

Température de stockage

−20°C

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.

Autres remarques

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

Produit(s) apparenté(s)

Réf. du produit
Description
Tarif

Pictogrammes

Flame
GHS02

Mention d'avertissement

Danger

Mentions de danger

H242

Classification des risques

Self-react. C

Code de la classe de stockage

5.2 - Organic peroxides and self-reacting hazardous materials

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

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
Michael P VanBrunt et al.
Bioconjugate chemistry, 26(11), 2249-2260 (2015-09-04)
Antibody-drug conjugates (ADC) have emerged as potent antitumor drugs that provide increased efficacy, specificity, and tolerability over chemotherapy for the treatment of cancer. ADCs generated by targeting cysteines and lysines on the antibody have shown efficacy, but these products are
Yiming Wu et al.
Bioconjugate chemistry, 27(10), 2460-2468 (2016-10-21)
Radioimmunotherapy (RIT) delivers radioisotopes to antigen-expressing cells via monoantibodies for the imaging of lesions or medical therapy. The chelates are typically conjugated to the antibody through cysteine or lysine residues, resulting in heterogeneous chelate-to-antibody ratios and various conjugation sites. To
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