Provided are a method of efficiently producing an sIL-2R antigen in an amount necessary for antibody generation, and a method of producing an anti-sIL-2R antibody using the antigen. Specifically, provided are a method of producing soluble interleukin-2 receptor, including culturing SCC-3 cells and recovering soluble interleukin-2 receptor from a culture of the cells, and a method of producing an anti-soluble interleukin-2 receptor antibody, including immunizing an animal with sIL-2R produced by the method.

Provided are a method of efficiently producing an sIL-2R antigen in an amount necessary for antibody generation, and a method of producing an anti-sIL-2R antibody using the antigen. Specifically, provided are a method of producing soluble interleukin-2 receptor, including culturing SCC-3 cells and recovering soluble interleukin-2 receptor from a culture of the cells, and a method of producing an anti-soluble interleukin-2 receptor antibody, including immunizing an animal with sIL-2R produced by the method.

Provided are an anti-CD40 antibody, an antigen binding fragment thereof, and a medical use thereof. Also provided are a chimeric antibody and a humanized antibody including a CDR region of the anti-CD40 antibody, a pharmaceutical composition including the human anti-CD40 antibody and the antigen binding fragment thereof, and an application thereof as an anti-cancer drug. In particular, provided are a humanized anti-CD40 antibody, and an application thereof in preparation of a drug to treat a CD40-mediated disease or disorder.

Systems and methods to characterize dimerization interfaces at the subdomain level of a protein are provided. An exemplary method includes digesting a protein dimer sample into subdomains, labeling the digested protein sample, isolating labeled dimeric and monomeric subdomain fragments, and peptide mapping the labeled sample to determine where the dimer fragments are labeled and where the dimer fragments are not labeled. Regions that show decreased labeling extents in the dimer fraction than that in the monomer fraction are likely involved or in close proximity to the dimerization interface.

Systems and methods to characterize dimerization interfaces at the subdomain level of a protein are provided. An exemplary method includes digesting a protein dimer sample into subdomains, labeling the digested protein sample, isolating labeled dimeric and monomeric subdomain fragments, and peptide mapping the labeled sample to determine where the dimer fragments are labeled and where the dimer fragments are not labeled. Regions that show decreased labeling extents in the dimer fraction than that in the monomer fraction are likely involved or in close proximity to the dimerization interface.

The present invention belongs to the fields of tumor therapy and molecular immunology. The present invention relates to an anti-CTLA4 antibody, pharmaceutical composition and use thereof. The anti-CTLA4 antibody of the present invention can specifically bind CTLA4, and can very effectively block the binding of CLTA4 to B7.

The present invention belongs to the fields of tumor therapy and molecular immunology. The present invention relates to an anti-CTLA4 antibody, pharmaceutical composition and use thereof. The anti-CTLA4 antibody of the present invention can specifically bind CTLA4, and can very effectively block the binding of CLTA4 to B7.

The invention relates to monoclonal antibodies, in particular against a peptide of the BAMBI protein, as well as the uses thereof and methods comprising same. Preferably, the antibodies are used for the treatment of autoimmune diseases.

This disclosure relates to nanoparticles coated with fusion proteins comprising a domain that binds a cancer marker and a domain comprising a toxic polypeptide. In certain embodiments, the targeted cancer marker is urokinase plasminogen activator receptor (uPAR) insulin-like growth factor 1 receptor (IGF1R), EGFR, HER2, and/or other member of the ErbB family of receptors. In certain embodiments, the molecule that binds a cancer marker is an amino terminal fragment of uPA or variant capable of binding uPAR and/or IGF1 or variant capable of binding IGF1R. In certain embodiments, the toxic polypeptide is a bacterial exotoxin.

Fusion proteins containing a half-life extension protein, a linker, and a GDF15 protein are described. Also described are nucleic acids encoding the fusion proteins, recombinant cells thereof, compositions comprising the fusion proteins, and methods of using the fusion proteins for treating or preventing metabolic diseases, disorders or conditions.