Streptavidin, FITC-conjugated, synthetic
Ficoll prepared human peripheral blood lymphocytes, CEM, HPB-MLT, Nalm-6, Jurkat, U-937, Molt-4, Raji, Daudi and KG-1 (cells expressing Fc receptors were pre-blocked with human IgG).
Purified streptavidin was covalently conjugated to FITC and the conjugate isolated by size exclusion chromatography. with a FITC to protein molar ratio of 9.0.
50 mM Sodium Phosphate pH 7.5, 100 mM Potassium Chloride, 150mM NaCl, 5% Glycerol, 0.2% BSA, 0.04% NaN3 (as a preservative).
2-8°C short term, -20°C long term
Streptavidin /?str?p?t?v?d?n/ is a 52.8 kDa protein purified from the bacterium Streptomyces avidinii. Streptavidin homo-tetramers have an extraordinarily high affinity for biotin (also known as vitamin B7 or vitamin H). With a dissociation constant (Kd) on the order of ≈10?14 mol/L, the binding of biotin to streptavidin is one of the strongest non-covalent interactions known in nature. Streptavidin is used extensively in molecular biology and bionanotechnology due to the streptavidin-biotin complex's resistance to organic solvents, denaturants (e.g. guanidinium chloride), detergents (e.g. SDS, Triton), proteolytic enzymes, and extremes of temperature and pH.