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Article provided by: bosterbio.com
Biotin streptavidin forms from the interaction between homo-tetramers and biotin. The binding of streptavidin with biotin is among the strongest in nature. When you need this vital molecule for your biological research or bionanotechnology projects, Bosterbio provides quickly.
How is biotin-streptavidin used?
Common uses of the bonded molecules include purification and the detection of various biomolecules. The pairing is incredibly strong, allowing manufacturers to offer support or chain different molecules.
In Western blotting and immunoassays, biotin-streptavidin is a building block to link biotinylated DNA molecules resulting in single-walled carbon nanotube scaffolds or complex DNA polyhedral.
Compounds created from streptavidin bound to biotin
Scientists create numerous compounds from this pairing. Applications range from western blotting to the generation of molecular force probes for atomic force microscopy studies.
Scientists and researchers generate 3DS lattices, probes, and other useful compounds while also using biotin-streptavidin as a hub for arranging proteins. The compounds often break apart without the loss of the streptavidin-biotin bond in water over 70 degrees Celsius.
Immunotherapy uses streptavidin conjugated to a monoclonal antibody in cancer treatment. Radiolabeled biotin delivers radiation only to cancer cells.
Saturation of the streptavidin and biotin sites with endogenous biotin instead of radiolabeled biotin is difficult. Doctors must also overcome a proclivity of radioactive biotin to bind to the kidneys.
What is the structure of streptavidin-biotin?
The result of binding streptavidin with biotin is a crystal structure. The structure was first discovered using multi-wavelength anomalous diffraction in 1989.
Manufacturers of the molecule process the N and C termini of the 159-residue full-length protein to improve the bonds with full removal providing the strongest bonds. Biotin binds to the secondary structure of a streptavidin monomer, a barrel-shaped structure at one end of each beta-barrel.
Why does biotin bond to streptavidin?
There is a complimentary shape between the binding pocket in streptavidin and biotin. An extensive network of hydrogen bonds forms at this site. Eight hydrogen bonds directly form at this location.
The strength of the bond exceeds the capability of hydrogen interaction. Researchers suspect that numerous Van der Waals force-mediated contacts increase the power of the combination.
Can manufacturers increase the bond between streptavidin and biotin?
The association between the molecules is already extremely powerful. Most attempts to modify streptavidin result in lower strength binding.
Recently, an increased level of understanding of how these compounds interact produced ten-fold less biotin dissociation as well as higher thermal and mechanical stability. Still, a two-fold decrease in the association rate was reported. Better procedures may improve the bond without reducing efficiency.
Can I purchase streptavidin and biotin?
Bosterbio Antibody and ELISA offers researchers, manufacturers, scientists, and doctors wishing to study the impact of the robust bond two, ten, and one-hundred milligrams of each molecule. We are cited in over 23000 publications due to a commitment to quality and fast shipping.
Many products ship within one day. Get in touch with our team or visit our website for more information.