Streptavidinbased

Streptavidinbased refers to molecules or systems that utilize streptavidin, a protein found in the bacterium Streptomyces avidinii, as a key component. Streptavidin is renowned for its exceptionally high affinity for biotin, a small molecule vitamin also known as vitamin B7 or vitamin H. This binding interaction is one of the strongest known non-covalent biological interactions, with a dissociation constant in the femtomolar range.

This strong and specific binding property makes streptavidin a valuable tool in various scientific and diagnostic applications. Streptavidinbased systems are frequently employed in techniques such as enzyme-linked immunosorbent assays (ELISAs), Western blotting, immunohistochemistry, and flow cytometry. In these contexts, biotinylated molecules (e.g., antibodies, DNA probes, or enzymes) are attached to the target of interest. Subsequently, streptavidin, often conjugated to a detectable label like an enzyme or a fluorescent dye, is used to bind to the biotinylated target. This allows for the sensitive detection and quantification of the target molecule.

The use of streptavidinbased systems offers several advantages, including high sensitivity, low background noise, and versatility. The robust nature of the streptavidin-biotin interaction ensures that even small amounts of target can be reliably detected. Furthermore, the biotinylation process can be applied to a wide range of biomolecules, making streptavidinbased detection methods adaptable to diverse research and clinical needs. While the term is broad, it specifically highlights the functional utilization of the streptavidin-biotin conjugate in mediating molecular recognition and detection.