Product Name
Streptavidin from Streptomyces avidinii, recombinant, expressed in E. coli, lyophilized powder
recombinant
expressed in E. coli
form
lyophilized powder
capacity
4 mol/mol binding capacity (Biotin)
storage temp.
−20°C
Quality Level
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Application
Streptavidin from Streptomyces avidinii has been used-
- for blocking of the AFM (atomic force microscopy) tip, during the measurement of unbinding forces in the avidin-biotin system
- for coupling of anti-HA (hemagglutinin) antibodies during cell free synthesis and assembly of proteins on a biochip
- for the coating of the gelatin flow phantoms to eventually determine the feasibility of IVUS (intravascular ultrasound) transducer for (biotinylated) microbubble-based drug delivery
- to immobilize proteins and oligonucleotides
Biochem/physiol Actions
Streptavidin is an antibiotic that functions by binding to and depleting the essential vitamin biotin from the surrounding environment. Because of its unique properties, streptavidin has found various applications in biological studies, including immunotherapy, immunoassays, hybridization assays, lymphocyte activation, antigen localization and affinity chromatography.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Streptavidin is a biotin-binding protein that is obtained from Streptomyces avidinii. It is resistant to extreme temperature, pH, detergents and proteolytic enzymes. Streptavidin has a molecular weight of 60kDa and exists as a homotetramer.
Other Notes
One unit will bind 1.0 μg biotin.
Physical form
Lyophilized from 5 mM potassium phosphate buffer
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Eduard Urich et al.
Scientific reports, 5, 14104-14104 (2015-09-29)
The blood-brain barrier and the blood-cerebrospinal fluid barrier prevent access of biotherapeutics to their targets in the central nervous system and therefore prohibit the effective treatment of neurological disorders. In an attempt to discover novel brain transport vectors in vivo
Moitrayee Bhattacharyya et al.
eLife, 9 (2020-03-10)
The many variants of human Ca2+/calmodulin-dependent protein kinase II (CaMKII) differ in the lengths and sequences of disordered linkers connecting the kinase domains to the oligomeric hubs of the holoenzyme. CaMKII activity depends on the balance between activating and inhibitory
Cell-free protein synthesis and assembly on a biochip.
Heyman Y et al
Nature Nanotechnology, 7(6), 374-378 (2012)
Polymer Nanoparticles
Progress in Molecular Biology and Translational Science, 104 (2011)
The properties of streptavidin, a biotin-binding protein produced by Streptomycetes
Louis C
Archives of Biochemistry and Biophysics, 106 (1964)
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