The remarkably strong interaction between the small molecule biotin and the proteins streptavidin or (neutr)avidin is widely exploited in biological research 1. Biotin-binding proteins have been ...

Receptor–ligand interactions are essential for biological function and their binding strength is commonly explained in terms of static lock-and-key models based on molecular complementarity. However, ...

A team of researchers from the University at Buffalo in Amherst, NY have successfully engineered a novel variant of streptavidin that forms a stable monomer and is capable of monovalent biotin ...

A novel streptavidin variant with improved biotin binding characteristics allows stable monovalent detection of biotinylated targets for imaging applications and can be recombinantly fused to ...

Biotin can amplify signals by forming complexes of large size with avidin or streptavidin. There are several techniques that use biotinylated secondary antibodies for this purpose, which are dealt ...

Recent research by Rafael C. Bernardi at the University of Illinois, Urbana-Champaign examines why a common tool in biotechnology -- the binding of streptavidin to biotin -- shows different mechanical ...

Quantum Dot Corporation (QDC) has announced a new addition to its nanocrystal-based family of fluorescent labels: the Qdot 705 streptavidin conjugate for ultra-bright, near infra-red bio-detection.

Sera-Mag™ Streptavidin-Coated Magnetic Beads and SpeedBeads exhibit high affinity and sensitivity for biotinylated target molecules, along with fast reaction kinetics, increasing throughput and ...

The term biotinylation refers to the process of binding biotin to either a protein or a nucleic acid, or in some cases to another type of molecule. An antibody is one of these potential targets, a ...

A team of researchers from the University at Buffalo in Amherst, NY have successfully engineered a novel variant of streptavidin that forms a stable monomer and is capable of monovalent biotin ...