B0519
Biotin−Agarose
PBS suspension
Synonym(s):
Vitamin H Agarose
form
PBS suspension
extent of labeling
≥30 mg avidin per mL packed resin, 2-6 μmol per mL
matrix
4% beaded agarose
matrix activation
epoxy
matrix attachment
carboxy (amide linkage); resin remains relatively uncharged over wide pH range
matrix spacer
13 atoms
application(s)
life science and biopharma
storage temp.
2-8°C
Quality Level
Application
Biotin contains a high affinity for binding to avidin or streptavidin. It has been widely used in biochemistry and molecular biology for detecting and labeling proteins.
Physical form
Suspension in phosphate buffered saline containing 0.02% sodium azide
Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Biotinylated CdSe/ZnSe nanocrystals for specific fluorescent labeling.
Charvet, N., et al.
Journal of Materials Chemistry, 14, 2638-2642 (2004)
Dietmar Eberbeck et al.
Journal of nanobiotechnology, 6, 4-4 (2008-03-13)
The binding reaction of the biomolecules streptavidin and anti-biotin antibody, both labelled by magnetic nanoparticles (MNP), to biotin coated on agarose beads, was quantified by magnetorelaxometry (MRX). Highly sensitive SQUID-based MRX revealed the immobilization of the MNP caused by the
P A Smith et al.
Nucleic acids research, 26(6), 1414-1420 (1998-04-29)
The high affinity binding interaction of biotin to avidin or streptavidin has been used widely in biochemistry and molecular biology, often in sensitive protein detection or protein capture applications. However, in vitro chemical techniques for protein biotinylation are not always
Emrah Celik et al.
Journal of molecular recognition : JMR, 25(1), 53-56 (2012-01-04)
Sample-probe contact duration (dwell time) and loading force are two important parameters for the atomic force microscopy (AFM) force spectroscopy measurements of ligand-receptor interaction. A prolonged contact time may be required to initiate ligand-receptor binding as a result of slow
K J Airenne et al.
Gene, 144(1), 75-80 (1994-06-24)
A recombinant avidin (re-Avd), containing amino acids (aa) 1-123 of the native chicken egg-white Avd, was produced in Escherichia coli. When cells were grown at 37 degrees C production was over 1 microgram/ml, due to altering the codon preference of
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