Streptavidin- Peroxidase from Streptomyces avidinii has been used for ELISA (enzyme linked immunosorbent assay) and Enzyme-Linked ImmunoSpot (ELISPOT).
General Description
Streptavidin is considered as a high-affinity biotin-binding agent, which shows resistance to extreme pH, detergents temperature, denaturants and enzymes, hence it is used in molecular biology and bionanotechnology.
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.
Description
This product is useful for the detection of biotinylated proteins (1,2). Conjugation of horseradish peroxidase (HRP) to streptavidin is obtained by cross linking the amino groups on streptavidin with the carbohydrate groups on HRP.
Reactivity
All
Background
Streptavidin is a 53 kDa homotetramer isolated from Streptomyces avidinii for use in isolation and detection bioassays. Each streptavidin subunit forms high affinity non-covalent bonds with the vitamin biotin. Because of its strong non-covalent interaction with biotin, streptavidin can be used to detect and isolate biotinylated proteins.Chemiluminescent detection systems have emerged as the best all-around detection method for use with western blots and ELISA. These detection assays eliminate the hazards associated with radioactive materials and toxic chromogenic substrates. The speed and sensitivity of these methods are unequalled by traditional alternatives. Streptavidin-HRP is used with biotinylated proteins and specific chemiluminescent substrates to generate light signal. Streptavidin-HRP conjugates have a very high turnover rate, coupling high sensitivity with short reaction times.
References
[1] Updyke, T.V. and Nicolson, G.L. (1984) J Immunol Methods 73, 83-95.
[2] Buckie, J.W. and Cook, G.M. (1986) Anal Biochem 156, 463-72.
[3] Chaiet, L. and Wolf, F.J. (1964) Arch Biochem Biophys 106, 1-5.
[4] Reznik, G.O. et al. (1998) Proc Natl Acad Sci USA 95, 13525-30.
