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QBD10776

Sigma-Aldrich

dPEG®48-biotin acid

>90% (HPLC)

Synonym(s):

Biotin-PEG-acid, Biotin-PEG48-COOH, PEG2000 biotin acid, PEG48-biotin acid

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About This Item

Empirical Formula (Hill Notation):
C112H218N4O53S
Molecular Weight:
2500.99
UNSPSC Code:
12352106
NACRES:
NA.22

Assay

>90% (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

dPEG48 biotin acid is a 2,500 Dalton biotin acid product that contains a 157 atom (187.8 Å) dPEG spacer. Amphiphilic dPEG48 biotin acid dissolves in water or aqueous buffer and organic solvents. It does not cause aggregation or precipitation of biomolecules. Using 1-Ethyl-3-(3-dimethylaminopropyl)carbodiimide (EDC) chemistry, dPEG48 biotin acid couples 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 terminal propionic acid moiety can be functionalized with other reactive groups for coupling directly to surfaces such as glass, gold, or magnetic nanoparticles. dPEG48 biotin acid is a monodisperse equivalent of the polymeric PEG2000.

Automate your Biotin tagging with Synple Automated Synthesis Platform (SYNPLE-SC002)

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 Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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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
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
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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