Product Overview
Streptavidin, DyLight350-conjugated
Purity
Purified streptavidin was covalently conjugated to R-Phycoerythrin (R-PE) and the conjugate isolated by size exclusion chromatography. with a DL350 to protein molar ratio of 9.6.
Concentration
OA/HRP molar ratio - approximately 3:1
Buffer
50 mM Sodium Phosphate pH 7.5, 100 mM Potassium Chloride, 150 mM NaCl, 5% Glycerol, 0.2% BSA, 0.04% NaN3 (as a preservative).
Preservative
0.04% Sodium Azide
Storage
2-8°C short term, -20°C long term
Introduction
Streptavidin 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.
Citations
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