| Description | Our Europium (Eu) Streptavidin conjugates are manufactured using covalent attachment of Streptavidin to the specially treated surface of 200nm Eu particles. The surface treatment of the particles makes the conjugates resistant to aggregation, while the extremely broad Stokes shift of the Eu chelate particle allows to reach a higher sensitivity in any immunoassay, preventing non-specific fluorescence interference. Streptavidin is a tetrameric biotin-binding protein that is isolated from Streptomyces avidinii. It is composed of identical subunits, with the tetramer having a molecular weight of approximately 53kDa. Each subunit binds one biotin molecule with a very high degree of specificity and affinity. The streptavidin-biotin complex is the strongest known non-covalent interaction (Kd = 10-15M) between a protein and a ligand. The combination between the Eu fluorescence properties and the specific interaction of streptavidin with biotin makes our conjugate a useful tool in designing detection systems with excellent sensitivity. Features and Benefits of Europium-Streptavidin conjugates:
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| Application Notes | When excited with UV light, the Eu chelate particle shows a maximal absorbance at 365nm and emits at 610 nm. The large Stokes shift leads to a low background signal and makes the conjugated particles ideal for immunochromatographic assay as well as a microwell-based assay. Thanks to the extended lifetime of approximately 0.5 milliseconds, the 200nm Eu Streptavidin conjugate can be used in a wide range of time-resolved fluorescence application for the indirect detection of antigens and DNA targets in many biotin/streptavidin interaction based assays. |
| Storage | Storage of components varies. See protocol for specific instructions. |