910007
20-Azido-3,6,9,12,15,18-hexaoxaicosanoic acid
95%
Synonym(s):
Azido-PEG6-CH2CO2H, Azido-PEG6-acid, N3-PEG6-CH2COOH
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About This Item
Empirical Formula (Hill Notation):
C14H27N3O8
CAS Number:
Molecular Weight:
365.38
UNSPSC Code:
12352106
Assay:
95%
Form:
(Liquid or Semi-Solid or Paste or Solid)
assay
95%
form
(Liquid or Semi-Solid or Paste or Solid)
reaction suitability
reaction type: click chemistry, reagent type: cross-linking reagent
functional group
azide, carboxylic acid
storage temp.
2-8°C
SMILES string
OC(COCCOCCOCCOCCOCCOCCN=[N+]=[N-])=O
Application
This heterobifunctional, PEGylated crosslinker 20-Azido-3,6,9,12,15,18-hexaoxaicosanoic acid features a carboxyl group at one end and azide at the other. The hydrophillic PEG linker facilitates solubility in biological applications. This azido-PEG6-acid linker can be used for bioconjugation or as a building block for synthesis of small molecules, conjugates of small molecules and/or biomolecules, or other tool compounds for chemical biology and medicinal chemistry that require ligation. Examples of applications include its synthetic incorporation into antibody-drug conjugates or proteolysis-targeting chimeras (PROTAC® molecules) for targeted protein degradation.
Legal Information
PROTAC is a registered trademark of Arvinas Operations, Inc., and is used under license
Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Yong Ma et al.
Bioconjugate chemistry, 21(11), 1994-1999 (2010-10-14)
A surface-bound cytomimetic assembly based on chemically selective and biocompatible immobilization and further modification of intact liposome is described. Liposomes carrying PEG-triphenylphosphine were chemoselectively immobilized onto azide-modified glass slides through Staudinger ligation, followed by modification with azide-modified lactose as a
Towards potential nanoparticle contrast agents: Synthesis of new functionalized PEG bisphosphonates.
Souad Kachbi-Khelfallah et al.
Beilstein journal of organic chemistry, 12, 1366-1371 (2016-08-26)
The use of nanotechnologies for biomedical applications took a real development during these last years. To allow an effective targeting for biomedical imaging applications, the adsorption of plasmatic proteins on the surface of nanoparticles must be prevented to reduce the
Ryota Sato et al.
Journal of the American Chemical Society, 139(48), 17397-17404 (2017-11-10)
Single-molecule imaging (SMI) has been widely utilized to investigate biomolecular dynamics and protein-protein interactions in living cells. However, multicolor SMI of intracellular proteins is challenging because of high background signals and other limitations of current fluorescence labeling approaches. To achieve