Native Streptav*din

Store desiccated at -20C. 18 months.

Streptavidin is a protein produced by Streptomyces avidinii and isolated by purification from fermentation broth. It consists of 4 identical subunits, each bearing an active binding site for Biotin. It is stable over a wide range of pH and decomposes only in the presence of SDS at temperatures >60 C. The neutral isoelectric point (5-6) of Streptavidin is in the same area where many biological interactions occur. Further, the high affinity of the Biotin:Streptavidin interaction results in a very quick reaction with a high signal to noise ratio. Streptavidin is non- or very low charged, around pH 7, reducing non-specific binding to charged molecules to a very limited level. It binds 4 moles of Biotin per mole of protein with a very high affinity. Streptavidin is non-glycosylated and does not react non-specifically with endogenous Lectins when used in assays on cells and tissues.

Reconstitute in distilled water containing 0.05 M NaCl, pH 9.0 (or preferred alternate buffer) to a concentration of 10 mg/mL.