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S1638

Millipore

Streptavidin−Agarose from Streptomyces avidinii

buffered aqueous suspension

Synonym(s):

streptavidin agarose beads, streptavidin agarose resin

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About This Item

MDL number:
MFCD00082035
UNSPSC Code:
41106500
NACRES:
NA.56

form

buffered aqueous suspension

Quality Level

200

extent of labeling

≥1 mg per mL

technique(s)

affinity chromatography: suitable

matrix

4% beaded agarose

matrix activation

cyanogen bromide

matrix attachment

amino

matrix spacer

7 atoms

capacity

≥15 μg/mL binding capacity (biotin)

storage temp.

2-8°C

Related Categories

Application

Streptavidin−agarose from Streptomyces avidinii has been used:
  • to pull down biotinylated cell surface proteins during the quantification of plasma membrane transforming growth factor β (TGFβ) receptor II (TβRII) and Tβ
  • RII internalization
  • in biotinylated miRNA pull-down assay; as secondary antibodies in immunoprecipitation

Streptavidin-agarose is used in protein chromatography, affinity chromatography, and recombinant protein expression and analysis. Streptavidin-agarose has been used to study the oriented immobilization of the tobacco etch virus protease for the cleavage of fusion proteins. Streptavidin-agarose has also been used to develop a method for screening triplex DNA binders from natural plant extracts.
Used for the purification of biotin containing proteins or DNA binding proteins

Biochem/physiol Actions

Streptavidin is a homotetrameric protein, isolated from Streptomyces avidinii, which, like avidin, has a high affinity for biotin. Streptavidin is slightly anionic (pI ~ 5-6) and non-glycosylated. These properties contribute to its relatively low non-specific binding compared to egg white avidin. Streptavidin is also more resistant than avidin to dissociation into subunits by guanidinium chloride. Streptavidin-agarose can be used to immobilize or isolate various biotinylated macromolecules and complexes (proteins, antibodies, lectins, nucleic acids, receptors, and ligands). The inherent high-affinity streptavidin-biotin interaction requires harsh conditions to release biotinylated macromolecules. This feature makes streptavidin-agarose useful in a variety of affinity purification applications.

Physical form

Suspension in 0.01 M sodium phosphate, pH 7.2, containing 0.05 M NaCl and 0.02% sodium azide

Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

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Niusheng Xu et al.
Analytical chemistry, 84(5), 2562-2568 (2012-01-10)
A novel ligand fishing assay was established to screen triplex DNA binders from complicated samples by a combination of immobilization of triplex DNA on agarose beads and high-performance liquid chromatography-electrospray ionization-mass spectrometry (HPLC-ESI-MS). The biotinylated oligodeoxynucleotides were first bound to
I Gottschalk et al.
European journal of biochemistry, 267(23), 6875-6882 (2000-11-18)
Two cytochalasin B-binding states of the human red blood cell facilitative glucose transporter GLUT1 were studied, one exhibiting one cytochalasin B-binding site on every second GLUT1 monomer (state 1) and the other showing one site per monomer (state 2). Quantitative
Behrad Derakhshan et al.
Nature protocols, 2(7), 1685-1691 (2007-07-21)
Covalent addition of nitric oxide (NO) to Cys-sulfur in proteins, or S-nitrosylation, plays pervasive roles in the physiological and pathophysiological modulation of mammalian protein functions. Knowledge of the specific protein Cys residues that undergo NO addition in different biological settings
O Litzka et al.
European journal of biochemistry, 251(3), 758-767 (1998-03-07)
In Aspergillus nidulans, a DNA-binding complex, PENR1, was shown to bind to two CCAAT-box-containing DNA elements located in the promoter regions of the bidirectionally oriented penicillin biosynthesis genes acvA and ipnA, and of the aat promoter. Here, partial purification of
R Horstkorte et al.
The Journal of cell biology, 121(6), 1409-1421 (1993-06-01)
We have previously shown that the neural adhesion molecules L1 and NCAM interact with each other to form a complex which binds more avidly to L1 than L1 to L1 alone (Kadmon, G., A. Kowitz, P. Altevogt, and M. Schachner.
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