What is Streptavidin PE?

What is Streptavidin PE?

PE Streptavidin is a second-step reagent useful when detecting biotinylated antibodies in indirect staining protocols. Streptavidin is a nonglycosylated biotin-binding protein that is bacterially derived. Like avidin, it binds to biotin with high affinity but displays less nonspecific binding.

What is molecular weight of Streptavidin?

The molecular weight of streptavidin is 55,000 daltons. The protein is composed of 4 essentially identical polypeptide chains (homotetramer).

How does streptavidin bind biotin?

Streptavidin is a tetramer and each subunit binds biotin with equal affinity. Multivalency is an advantage in applications like MHC tetramer staining, where avidity effects improve the ability of MHC molecules attached to streptavidin to detect specific T cells.

What is streptavidin used for?

Streptavidin is widely used in Western blotting and immunoassays conjugated to some reporter molecule, such as horseradish peroxidase. Streptavidin has also been used in the developing field of Nanobiotechnology, the use of biological molecules such as proteins or lipids to create nanoscale devices/structures.

What is the size of streptavidin?

Streptavidin is a 60 KDa tetrameric protein with a globular subunit organization of 5 nm in size (Kuzuya et al., 2008)—a large and bulky linker compared to alternative techniques.

What is the function of streptavidin?

Like Avidin, Streptavidin is thought to function as an antibiotic and has a very high affinity for biotin (Kd = 10-14 to -15M). Unlike Avidin, Streptavidin has no carbohydrate and has an acidic isoelectric point (pI = 5) that gives Streptavidin a significantly lower solubility than Avidin.

Does streptavidin denature?

However, it has previously been impossible to re-use any streptavidin solid support, since the conditions needed to break the interaction with biotin has led to the denaturation of the streptavidin. Both biotin and the streptavidin remain active after dissociation and both molecules can therefore be re-used.

Which amino acids can be biotinylated?

Chemical structure of biotin. The molecule is comprised of a ureido ring joined with a tetrahydrothiophene ring. A coenzyme for carboxylase enzymes, biotin is required for the synthesis of fatty acids, isoleucine and valine.

How is streptavidin used in flow cytometry?

The streptavidin fluorochrome conjugates are commonly used in indirect staining protocols to detect biotinylated primary antibodies in flow cytometry. Streptavidin binds to biotin with high affinity. For Research Use Only. Not for use in diagnostic procedures.

When to use streptavidin fluorochrome PE conjugates?

The streptavidin fluorochrome conjugates are commonly used in indirect staining protocols to detect biotinylated primary antibodies in flow cytometry. Streptavidin binds to biotin with high affinity. Laser. Blue Laser, Green Laser, Yellow-Green Laser.

How is the inguinal lymph node stained for streptavidin?

To separate SA-specific and OVA-specific GC B cells, inguinal lymph nodes were first stained with streptavidin-APC (to detect SA-specific B cells and to block SA-specific binding of subsequent tetramers) and then stained with OVA-PE tetramers.