Morphosys Further Strengthens U.S. Patent Position on Core Technologies
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MorphoSys AG has announced that the US Patent and Trademark Office (USPTO) has granted a new patent providing extended protection for the company's CysDisplay technology.
The new patent (US 7,785,859) covers the host cells used in this enhanced phage display technology. Currently, the company is prosecuting more than 35 different proprietary patent families worldwide, in addition to about the same number of patent families being pursued in cooperation with its partners.
“Today’s news marks yet another step in extending our strong intellectual property portfolio in key pharmaceutical markets like the US,” commented Dr. Marlies Sproll, Chief Scientific Officer of MorphoSys AG. “We are committed to maximizing the patent protection on our core technologies, as these are essential value-drivers for the company.”
CysDisplay is an improved version of phage display in which an antibody is linked to the surface of a bacteriophage via a disulphide bond. Recovery of the antibodies following screening of a library is then effected by reductive cleavage of the disulphide bond, ensuring that all specific binders are eluted independent of their binding affinity to the antigen.
The new patent (US 7,785,859) covers the host cells used in this enhanced phage display technology. Currently, the company is prosecuting more than 35 different proprietary patent families worldwide, in addition to about the same number of patent families being pursued in cooperation with its partners.
“Today’s news marks yet another step in extending our strong intellectual property portfolio in key pharmaceutical markets like the US,” commented Dr. Marlies Sproll, Chief Scientific Officer of MorphoSys AG. “We are committed to maximizing the patent protection on our core technologies, as these are essential value-drivers for the company.”
CysDisplay is an improved version of phage display in which an antibody is linked to the surface of a bacteriophage via a disulphide bond. Recovery of the antibodies following screening of a library is then effected by reductive cleavage of the disulphide bond, ensuring that all specific binders are eluted independent of their binding affinity to the antigen.
