Described herein are compositions and methods relating to LAP-binding agents, including, for example, anti-LAP antibodies, and to their use in methods of treatment of cancer. LAP-binding agents affected both systemic and intra-tumor immunity and were shown effective to treat a broad spectrum of cancer types.

The present invention relates to methods of treating hematologic cancers using a combination of inhibitors of PD-1 or PD-L1 and TIM-3, LAG-3 or CTLA4.

Disclosed are antigen binding polypeptides and antigen binding polypeptide complexes (e.g., antibodies and antigen binding fragments thereof) having certain structural features. Also disclosed are polynucleotides and vectors encoding such polypeptides and polypeptide complexes; chimeric antigen receptors (CARs), cells, pharmaceutical compositions and kits containing such polypeptides and polypeptide complexes; and methods of using such polypeptides and polypeptide complexes.

Antibodies binding to human claudin 18.2 (CLDN 18.2) and bispecific antibodies binding to both human CLDN 18.2 and PD-L1, pharmaceutical compositions comprising such, and methods of using such for treating target diseases such as cancer.

Disclosed are antigen binding polypeptides and antigen binding polypeptide complexes (e.g., antibodies and antigen binding fragments thereof) having certain structural features. Also disclosed are polynucleotides and vectors encoding such polypeptides and polypeptide complexes; host cells; chimeric antigen receptors (CARs); immune cells; pharmaceutical compositions and kits containing such polypeptides and polypeptide complexes; and methods of using such polypeptides and polypeptide complexes.

Herein is reported an anti-transferrin receptor antibody that specifically binds to human transferrin receptor and cynomolgus transferrin receptor, which comprises i) a humanized heavy chain variable domain derived from the heavy chain variable domain of SEQ ID NO: 01, and ii) a humanized light chain variable domain derived from the light chain variable domain of SEQ ID NO: 26, wherein the antibody has an off-rate for the human transferrin receptor that is equal to or less than (i.e. at most) the off-rate of the anti-transferrin receptor antibody 128.1 for the cynomolgus transferrin receptor, whereby the off-rates are determined by surface plasmon resonance, and whereby the anti-transferrin receptor antibody 128.1 has a heavy chain variable domain of SEQ ID NO: 64 and a light chain variable domain of SEQ ID NO: 65.

The present invention relates to Tri-Specific Binding Molecules, which are multi-chain polypeptide molecules that possess three Binding Domains and are thus capable of mediating coordinated binding to three epitopes. The Tri-Specific Binding Molecule is preferably characterized in possessing binding domains that permit it to immunospecifically bind to: (1) an epitope of a first Cancer Antigen, (2) an epitope of a second Cancer Antigen, and (3) an epitope of a molecule that is expressed on the surface of an immune system effector cell, and are thus capable of localizing an immune system effector cell to a cell that expresses a Cancer Antigen, so as to thereby facilitate the killing of such cancer cell.

The invention provides a method for the treatment of EGFRvIII-positive cancer or glioblastoma, comprising administering to a subject in need thereof an initial dose of between about 15 μg/day to about 6000 μg/day of an anti-EGFRvIII agent. Diagnostic methods for assessing EGFRvIII expression are also provided.

The invention relates to an anti-CD16A antigen binding protein for use in NK cell-based immunotherapy, wherein the anti-CD16A antigen binding protein is to be administered intermittently and in combination with a cytokine. In certain embodiments the antigen binding protein is a tetravalent and bispecific CD30/CD16A tandem diabody.

This disclosure belongs to the field of biomedical technology, and particularly refers to a trifunctional molecule and the application thereof. The structure of the trifunctional molecule includes a first functional domain, a second functional domain and a third functional domain. These domains are capable of simultaneously binding to CD19, CD3, and T cell positive (negative) costimulatory factors, thereby producing the first and second signal required for T cell activation. The trifunctional molecule is a recombinant protein peptide chain, which can be produced by a eukaryotic cell expression system. The product has a single structure, simple purification process, high protein yield, and preparation process and product stability. The trifunctional molecule is superior to the anti-CD19/anti-CD3 BiTE bispecific antibody in killing CD19-positive target cells. Compared with the CAR-T technology targeting CD19, the trifunctional molecule is more convenient to use, the dose is controllable, and the side effects of CAR-T are avoided.