Disclosed are a natural killer (NK) cell expressing an anti-cotinine chimeric antigen receptor (CAR) specifically binding to cotinine, and a cell therapeutic agent containing the NK cell. The CAR-expressing NK cell which specifically binds cotinine, can effectively move to tumor tissue, regardless of the kind of cancer, depending on the binding substance bound to cotinine. Therefore, the natural killer cell can be usefully employed as a gene therapy exhibiting a highly efficient anticancer effect.

Disclosed are a natural killer (NK) cell expressing an anti-cotinine chimeric antigen receptor (CAR) specifically binding to cotinine, and a cell therapeutic agent containing the NK cell. The CAR-expressing NK cell which specifically binds cotinine, can effectively move to tumor tissue, regardless of the kind of cancer, depending on the binding substance bound to cotinine. Therefore, the natural killer cell can be usefully employed as a gene therapy exhibiting a highly efficient anticancer effect.

The present disclosure is directed to human monoclonal IgE antibodies, and IgG antibodies engineered therefrom. Such engineered antibodies can be used to blunt pathologic IgE responses in subjects, such as in the treatment or prevention of allergies.

The present disclosure is directed to human monoclonal IgE antibodies, and IgG antibodies engineered therefrom. Such engineered antibodies can be used to blunt pathologic IgE responses in subjects, such as in the treatment or prevention of allergies.

The present disclosure is directed to human monoclonal IgE antibodies, and IgG antibodies engineered therefrom. Such engineered antibodies can be used to blunt pathologic IgE responses in subjects, such as in the treatment or prevention of allergies.

The present disclosure is directed to human monoclonal IgE antibodies, and IgG antibodies engineered therefrom. Such engineered antibodies can be used to blunt pathologic IgE responses in subjects, such as in the treatment or prevention of allergies.

In one embodiment, the present disclosure provides a combination of recombinant Ara h 1 and Ara h 2 variant polypeptides lacking at least one epitope recognized by anti-Ara h 1 antibodies and anti-Ara h 2 antibodies, respectively, thereby having reduced or abolished antibody binding to the peanut allergen. These peanut allergen variants may be used in methods of treating subjects allergic to peanuts and reducing the severity of their allergy.

In one embodiment, the present disclosure provides a combination of recombinant Ara h 1 and Ara h 2 variant polypeptides lacking at least one epitope recognized by anti-Ara h 1 antibodies and anti-Ara h 2 antibodies, respectively, thereby having reduced or abolished antibody binding to the peanut allergen. These peanut allergen variants may be used in methods of treating subjects allergic to peanuts and reducing the severity of their allergy.

The present invention provides multispecific antigen-binding molecules and uses thereof. The multispecific antigen-binding molecules comprise a first antigen-binding domain that specifically binds a target molecule, and a second antigen-binding domain that specifically binds an internalizing effector protein. The multispecific antigen-binding molecules of the present invention can, in some embodiments, be bispecific antibodies that are capable of binding both a target molecule and an internalizing effector protein. In certain embodiments of the invention, the simultaneous binding of the target molecule and the internalizing effector protein by the multispecific antigen-binding molecule of the present invention results in the attenuation of the activity of the target molecule to a greater extent than the binding of the target molecule alone. In other embodiments of the invention, the target molecule is a tumor associated antigen, and the simultaneous binding of the tumor associated antigen and the internalizing effector protein by the multispecific antigen-binding molecule of the present invention causes or facilitates the targeted killing of tumor cells.

An anti-equol antibody composition, containing an anti-equol antibody or antibody fragment thereof containing, as an immunoglobulin heavy chain variable region, hypervariable regions CDR1, CDR2, and CDR3 respectively including amino acid sequences represented by SEQ ID NO: 1-3, and as an immunoglobulin light chain variable region, hypervariable regions CDR1, CDR2, and CDR3 respectively including amino acid sequences represented by SEQ ID NO: 4-6; and an anti-equol antibody or antibody fragment thereof containing, as an immunoglobulin heavy chain variable region, hypervariable regions CDR1, CDR2, and CDR3 respectively including amino acid sequences represented by SEQ ID NO: 1-3, and as an immunoglobulin light chain variable region, hypervariable regions CDR1, CDR2, and CDR3 respectively including amino acid sequences represented by SEQ ID NO: 7-9.