| Patent application number | Description | Published |
| 20080226632 | AMPHIREGULIN ANTIBODIES AND THEIR USE TO TREAT CANCER AND PSORIASIS - The present invention is directed to anti-AR antibodies, preferably humanized monoclonal antibodies having the amino acid sequences disclosed herein. The present invention includes a pharmaceutical composition comprising such antibodies. The present invention includes a method of inhibiting cancer cell growth comprising administering such antibodies into a subject. The present invention also provides a method of treating cancer or psoriasis in a subject in need of such a treatment by administering such antibodies to said subject in a pharmaceutically effective amount. | 09-18-2008 |
| 20080287657 | Alteration of Fc-fusion protein serum half-lives by mutagenesis - The present invention provides for a modified Fc-fusion protein in which at least one amino acid from the heavy chain constant region selected from the group consisting of amino acid residues 250, 314, and 428 is substituted with another amino acid which is different from that present in the unmodified Fc-fusion protein, thereby altering the binding affinity for FcRn and/or the serum half-life in comparison to the unmodified Fc-fusion protein. | 11-20-2008 |
| 20090175847 | HUMANIZED ANTIBODIES TO AB (20-42) GLOBULOMER AND USES THEREOF - The present invention relates to binding proteins and, in particular, humanized antibodies that may be used, for example, in the diagnosis, treatment and prevention of Alzheimer's Disease and related conditions. | 07-09-2009 |
| 20090232801 | Humanized Antibodies Which Bind To AB (1-42) Globulomer And Uses Thereof - The present invention relates to binding proteins and, in particular, humanized antibodies that may be used, for example, in the diagnosis, treatment and prevention of Alzheimer's Disease and related conditions. | 09-17-2009 |
| 20100047245 | IL-12/P40 BINDING PROTEINS - The present invention encompasses IL-12 | 02-25-2010 |
| 20100196315 | IL-12/p40 BINDING PROTEINS - The present invention encompasses IL-12p40 binding proteins, particularly antibodies that bind human interleukin-12 (hIL-12) and/or human IL-23 (hIL-23). Specifically, the invention relates to antibodies that are chimeric, CDR grafted and humanized antibodies. Preferred antibodies have high affinity for hIL-12 and/or hIL-23 and neutralize h IL-12 and/or hIL-23 activity in vitro and in vivo. An antibody of the invention can be a full-length antibody or an antigen-binding portion thereof. Method of making and method of using the antibodies of the invention are also provided. The antibodies, or antibody portions, of the invention are useful for detecting hIL-12 and/or hIL-23 and for inhibiting hIL-12 and/or hIL-23 activity, e.g., in a human subject suffering from a disorder in which hIL-12 and/or hIL-23 activity is detrimental. | 08-05-2010 |
| 20110165066 | INTERLEUKIN-13 BINDING PROTEINS - The present invention encompasses IL-13 binding proteins. Specifically, the invention relates to antibodies that are chimeric, CDR grafted and humanized antibodies. Preferred antibodies have high affinity for hIL-13 and neutralize hIL-13 activity in vitro and in vivo. An antibody of the invention can be a full-length antibody or an antigen-binding portion thereof. Method of making and method of using the antibodies of the invention are also provided. The antibodies, or antibody portions, of the invention are useful for detecting hIL-13 and for inhibiting hIL-13 activity, e.g., in a human subject suffering from a disorder in which hIL-13 activity is detrimental. | 07-07-2011 |
| 20110183412 | ALTERATION OF FC-FUSION PROTEIN SERUM HALF-LIVES BY MUTAGENESIS - The present invention provides for a modified Fc-fusion protein in which at least one amino acid from the heavy chain constant region selected from the group consisting of amino acid residues 250, 314, and 428 is substituted with another amino acid which is different from that present in the unmodified Fc-fusion protein, thereby altering the binding affinity for FcRn and/or the serum half-life in comparison to the unmodified Fc-fusion protein. | 07-28-2011 |