StreptaClick® Technology -
aggregation-free streptavidin
Streptavidin and Biotin: A powerful Interaction for many applications
Streptavidin is a 53 kDa tetrameric protein derived from Streptomyces avidinii, known for its ability to bind biotin with exceptional strength. This binding interaction is one of the strongest non-covalent interactions found in nature. Each streptavidin molecule is tetravalent, meaning it contains four binding sites for biotin.
Biotin is a small vitamin (B7) that can be easily conjugated to a wide array of molecules, including proteins, antibodies, nucleic acids, lipids, and other biomolecules. This versatility allows the biotin-streptavidin binding to be used in diverse applications, such as protein purification, immunoassays, molecular imaging, among others. However, the tetravalency of streptavidin can also cause unwanted aggregation of biotinylated molecules, which limits its use in many applications.
To address this challenge, Kromnigon has developed StreptaClick®, an modified tetrameric streptavidin with monovalent binding properties that prevents aggregation of biotinylated proteins.
The StreptaClick® Technology — Much more than streptavidin
The patented StreptaClick® technology provides monovalent binding of streptavidin to biotinylated proteins. StreptaClick® is a modified form of tetrameric streptavidin with conserved high binding affinity for biotin. This is in contrast to monomeric monovalent streptavidin that consist of only one streptavidin subunit and has a poor biotin binding, 1 000 000 times weaker than StreptaClick®
The monovalent properties of StreptaClick® makes it suitable for multiplexing with biotinylated antibodies. StreptaClick® can simply be pre-mixed with biotinylated antibodies before applying them to the sample. This feature is utilized in our immunohistochemistry (IHC) kits, where StreptaClick® with fluorochromes or enzymes are attached to biotinylated antibodies before use in an IHC protocol.
The StreptaClick® molecule works as a scaffold to which different types of reporter molecules can be attached. Whether it is a fluorochrome as in StreptaClick® Color, an enzyme as in StreptaClick® HRP, or any other biomolecule you choose to attach via click chemistry as in StreptaClick® Precision, the flexibility StreptaClick® offers is truly remarkable.
StreptaClick® Precision - Conjugate with your own molecule of choice
Easily conjugate exactly one reporter of your choice to aggregation-free streptavidin by click chemistry (DBCO or azide). StreptaClick® Precision is a unique cis divalent streptavidin that ensures no aggregation when mixed with biotinylated proteins. With two clustered biotin binding pockets, StreptaClick® Precision is the most robust monovalently binding streptavidin on the market. Moreover, StreptaClick® Precision is engineered to have one side for site-specific conjugation through click chemistry and the opposite side for biotin binding. Together, these features make StreptaClick® Precision ideal for precise conjugation of bulky molecules such as DNA oligonucleotides and lipid nanoparticles (LNPs), without compromising the binding capacity to biotinylated molecules, such as antibodies, antigens or surfaces.
Possible applications include antibody-oligonucleotide based immunoassays and targeting antibodies conjugated to delivery systems such as lipid nanoparticles in the development of advanced therapies and medicinal products (ATMPs).
If you wish to explore novel applications using StreptaClick® Precision please do not hesitate to get in touch with us.
