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San Francisco, CA, United States

Patent
Five Prime Therapeutics | Date: 2014-04-30

Antibodies that bind CSF1R are provided. Antibody heavy chains and light chains that are capable of forming antibodies that bind CSF1R are also provided. Polynucleotides encoding antibodies to CSF1R are provided. Polynucleotides encoding antibody heavy chains and lights chains are also provided. Methods of treatment using antibodies to CSF1R are provided. Such methods include, but are not limited to, methods of treating rheumatoid arthritis, bone loss, and multiple sclerosis.


Patent
Five Prime Therapeutics | Date: 2014-07-31

The present invention provides antibodies that bind FGFR2IIIb, wherein the antibodies are afucosylated. The present invention provides compositions comprising antibodies that bind FGFR2IIIb, wherein at least 95% of the antibodies in the composition are afucosylated. In some embodiments, methods of treating cancer comprising administering afucosylated anti-FGFR2IIIb antibodies are provided.


Patent
Five Prime Therapeutics and Glaxosmithkline | Date: 2014-05-22

Methods of treating cancers comprising administering a fibroblast growth factor receptor 1 (FGFR1) extracellular domain (ECD) and/or an FGFR1 ECD fusion molecule are provided. Methods of treating cancers comprising administering a fibroblast growth factor receptor 1 (FGFR1) extracellular domain (ECD) and/or an FGFR1 ECD fusion molecule and at least one anti-angiogenic agent are provided.


Patent
Five Prime Therapeutics | Date: 2014-02-20

The present invention relates to a method of promoting hair growth comprising administering a fibroblast growth factor receptor 3 (FGFR3) extracellular domain (ECD), including native FGFR3 ECDs, variants, fragments, and fusion molecules, to a subject in an amount sufficient to promote hair growth.


Patent
Five Prime Therapeutics | Date: 2015-10-07

The invention provides FGFR fusion proteins, methods of making them, and methods of using them to treat proliferative disorders, including cancers and disorders of angiogenesis. The FGFR fusion molecules can be made in CHO cells and may comprise deletion mutations in the extracellular domains of the FGFRs which improve their stability. These fusion proteins inhibit the growth and viability of cancer cells in vitro and in vivo. The combination of the relatively high affinity of these receptors for their ligand FGFs and the demonstrated ability of these decoy receptors to inhibit tumor growth is an indication of the clinical value of the compositions and methods provided herein.

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