Anti Streptavidin mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant Streptavidin amino acids 25-183 purified from E. coli.
Streptavidin is a tetrameric protein derived from the bacterium Streptomyces avidinii. It is known for its high affinity binding to biotin (vitamin B7), with a dissociation constant (Kd) of approximately (10^{-14}) mol/L . This strong binding affinity has made streptavidin a crucial component in various biochemical and diagnostic applications.
Streptavidin consists of four identical subunits, each capable of binding one biotin molecule. This tetrameric structure allows for multiple biotin-binding events, making it highly effective in applications requiring signal amplification. The protein’s high stability and resistance to denaturation under extreme pH and temperature conditions further enhance its utility in laboratory settings .
Mouse antibodies against streptavidin are monoclonal antibodies produced by hybridizing mouse myeloma cells with spleen cells from immunized mice. These antibodies are highly specific to streptavidin and do not cross-react with avidin, a similar protein found in egg whites . The monoclonal nature of these antibodies ensures consistent performance in various assays.
The production of mouse anti-streptavidin antibodies involves several steps: