S1638
Streptavidin−Agarose from Streptomyces avidinii
buffered aqueous suspension
동의어(들):
streptavidin agarose beads, streptavidin agarose resin
form
buffered aqueous suspension
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
Quality Level
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
저장 등급
10 - Combustible liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
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
Veronica Ramberg et al.
Journal of neuroinflammation, 8, 34-34 (2011-04-16)
The transcription factors CCAAT/enhancer binding proteins (C/EBP) α, β and δ have been shown to be expressed in brain and to be involved in regulation of inflammatory genes in concert with nuclear factor κB (NF-κB). In general, C/EBPα is down-regulated
Angel Guerra-Moreno et al.
Science signaling, 12(609) (2019-11-28)
The yeast stress-activated protein kinase Hog1 is best known for its role in mediating the response to osmotic stress, but it is also activated by various mechanistically distinct environmental stressors, including heat shock, endoplasmic reticulum stress, and arsenic. In the
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
관련 콘텐츠
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.
친화성, GST 풀다운, TAP, 공동 면역 침전법을 활용한 풀다운 분석을 통해 in vitro 단백질-단백질 상호작용을 분석합니다.
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