form
buffered aqueous suspension
Quality Level
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
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
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
常规特殊物品
This item has
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Related Content
利用亲和力、GST pull-down、TAP 和共免疫沉淀方法,通过Pull-Down研究体外蛋白质互作。
Investigate in vitro protein-protein interactions with pull-down assays, utilizing affinity, GST pull-down, TAP, and co-immunoprecipitation methods.
Find protein research tools to prepare, isolate, and analyze proteins. Organized by how to extract, protect, purify, enrich, modify, and quantify proteins.
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
Global Trade Item Number
| SKU | GTIN |
|---|---|
| S1638-1ML | 04061836911799 |
| S1638-5ML | 04061836911829 |