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Key Documents

S1638

Millipore

Streptavidin−Agarose from Streptomyces avidinii

buffered aqueous suspension

Synonyme(s) :

streptavidin agarose beads, streptavidin agarose resin

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About This Item

Numéro MDL:
Code UNSPSC :
41106500
Nomenclature NACRES :
NA.56

Forme

buffered aqueous suspension

Niveau de qualité

Ampleur du marquage

≥1 mg per mL

Technique(s)

affinity chromatography: suitable

Matrice

4% beaded agarose

Activation de la matrice

cyanogen bromide

Fixation de matrice

amino

Espaceur de matrice

7 atoms

Capacité

≥15 μg/mL binding capacity (biotin)

Température de stockage

2-8°C

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

Actions biochimiques/physiologiques

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.

Forme physique

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

Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

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
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
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
S W Rogers et al.
The Plant journal : for cell and molecular biology, 11(6), 1359-1368 (1997-06-01)
Barley aleurain is contained within a specific type of vacuole characterized by acidic pH and the presence of other hydrolytic enzymes. The aleurain-containing vacuole is distinct from protein storage vacuoles, and anti-aleurain antibodies serve as markers for this organelle in
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

Contenu apparenté

Tests, réactifs et protocoles permettant d'étudier les interactions protéines/protéines in vitro par différentes méthodes : pull-down ou GST pull-down, purification par affinité en tandem (TAP pour "Tandem Affinity Purification") et co-immunoprécipitation.

Pull-down assays, reagents, and protocols for investigating in vitro protein-protein interactions using affinity or GST pull-down, tandem affinity purification (TAP), and co-immunoprecipitation methods.

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