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QBD10773

Sigma-Aldrich

dPEG®24-biotin acid

>95% (HPLC)

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Synonym(s):
Biotin-PEG-acid, Biotin-PEG24-COOH, PEG1000 biotin acid, PEG24-biotin acid
Empirical Formula (Hill Notation):
C61H117N3O28S
Molecular Weight:
1372.65
MDL number:

assay

>95% (HPLC)

form

solid or viscous liquid

reaction suitability

reaction type: Biotinylations
reaction type: Pegylations

polymer architecture

shape: linear
functionality: monofunctional

shipped in

ambient

storage temp.

−20°C

Features and Benefits

dPEG24 biotin acid consists of a biotin molecule conjugated to a single molecular weight polyethylene glycol chain of discrete length (dPEG). The dPEG chain is 76 atoms (90.1 Å) long. The distal end of the dPEG chain terminates with a propionic acid group. The terminal acid is available for direct conjugation to free amines or functionalization as an active ester. Amphiphilic dPEG24 biotin acid can be dissolved both in water or aqueous buffer and in organic solvent. It does not cause aggregation or precipitation of biomolecules. Using 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) chemistry, dPEG24 biotin acid can be coupled directly to free primary amines in aqueous media. These free amines can be on a protein, peptide, or the treated surface of a nanoparticle. Moreover, the acid moiety can be functionalized with other reactive groups for coupling directly to surfaces such as glass, gold, or magnetic nanoparticles. The linker length of dPEG24 biotin acid is much longer than the linker lengths of LC-biotin and of LC-LC-biotin and is a monodisperse equivalent of a PEG1000. The performance characteristics of dPEG24-biotin acid are quite superior to both LC-biotin and LC-LC-biotin.

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Legal Information

Products Protected under U.S. Patent #s 7,888,536 & 8,637,711 and European Patent #s 1,594,440 & 2,750,681
dPEG is a registered trademark of Quanta BioDesign

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Veronica C Ardi et al.
ACS chemical biology, 6(12), 1357-1366 (2011-09-29)
Heat shock protein 90 (Hsp90) accounts for 1-2% of the total proteins in normal cells and functions as a molecular chaperone that folds, assembles, and stabilizes client proteins. Hsp90 is overexpressed (3- to 6-fold increase) in stressed cells, including cancer
Thurid Boetel et al.
Biochemical and biophysical research communications, 349(1), 296-302 (2006-08-29)
The biological function of prion protein (PrP) and the physiological relevance of its truncated subtypes and glycoforms is still enigmatic. In this paper, we adduce evidence that recombinant murine PrP fragment 90-231 (mPrP90-231) contains a biotin-mimicking sequence motif that causes
Alexander Kuzmin et al.
Bioconjugate chemistry, 21(11), 2076-2085 (2010-10-23)
The utility of catalyst-free azide-alkyne [3 + 2] cycloaddition for the immobilization of a variety of molecules onto a solid surface and microbeads was demonstrated. In this process, the surfaces are derivatized with aza-dibenzocyclooctyne (ADIBO) for the immobilization of azide-tagged
Amir Syahir et al.
Chemistry, an Asian journal, 7(8), 1867-1874 (2012-05-29)
The need to develop label-free biosensing devices that enable rapid analyses of interactions between small molecules/peptides and proteins for post-genomic studies has increased significantly. We report a simple metal-insulator-metal (MIM) geometry for fabricating a highly sensitive detection platform for biosensing.

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