Examples of streptavidin

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The surface density of streptavidin molecules was sufficiently small that each of the pinning sites represented a single streptavidin-biotin cross-bridge.
Once the particles are trapped, streptavidin is introduced in solution at the trap location and bond with the biotin on the particles.
These molecules are not fluorescent, but are imaged after fixation with a fluorescent streptavidin derivative.
The separated proteins were transblotted onto nitrocellulose membranes and protein spots bound to streptavidin were detected as described above.
The hybridized product is held on streptavidin-coated microtitre plates.
The streptavidin measurements show that this is even the case for bonds with very high affinities that are usually considered to be very strong.
The other end of the molecule is tethered to a magnetic bead coated with streptavidin.
In these simulations, the spring constant increased at a given rate, thus forcing the biotin out of the streptavidin binding pocket.
In the single-channel record (b), streptavidin was already present in the trans compartment.
After the experiments, the injected cells were visualized with fluorescent streptavidin and photographed on a confocal microscope.
Sensing discrete streptavidin-biotin interactions with atomic force microscopy.
In this study, two membranes containing biotin-lipid conjugates were cross-linked by streptavidin.
The linker is biotin when using streptavidin coated polystyrene particles and thiol when using gold particles.
For visualization of the biotinylated standard (high molecular weight protein standard), horseradish peroxidase-conjugated streptavidin was used.
Biotin-labelled probes are first localized with antibodies, or more commonly, with avidin and streptavidin.

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