The present invention relates to peptides, proteins, nucleic acids and cells for use in immunotherapeutic methods. In particular, the present invention relates to the immunotherapy of cancer. The present invention furthermore relates to tumor-associated T-cell peptide epitopes, alone or in combination with other tumor-associated peptides that can for example serve as active pharmaceutical ingredients of vaccine compositions that stimulate anti-tumor immune responses, or to stimulate T cells ex vivo and transfer into patients. Peptides bound to molecules of the major histocompatibility complex (MHC), or peptides as such, can also be targets of antibodies, soluble T-cell receptors, and other binding molecules.

The invention disclosed herein relates to improved methods for expanding cell populations, particularly B cell populations. The invention further relates to improved B-cell expansion media, compositions comprising expanded B cells and methods of using such expanded B cells. The invention further relates to methods of treating diseases or disorders wherein a population of B cells is obtained and cultured, and wherein said B cells are engineered to express a payload and/or a chimeric receptor, and wherein said B cells are administered to a subject.

Disclosed herein are methods of treating a subject exhibiting a solid tumor that expresses Glypican-3 (GPC3). The methods typically utilize g GPC3 chimeric antigen receptor immunoresponsive cells to a subject in need thereof to effect killing of tumor cells.

The present invention relates to a substance interacting with C terminal fragment of the STIM1 fraction localized to the plasma membrane of the cells, for its use in the treatment of cancers. The present invention further relates to a pharmaceutical composition comprising at least one substance interacting with C terminal fragment of the STIM1 fraction localized to the plasma membrane of cells, and at least one pharmaceutically acceptable excipient. The invention also refers to the use of isolated C terminal fragment of the STIM1 fraction localized to the plasma membrane of cells in a method for screening candidate molecules for treating cancers, especially pancreatic, colon, breast, Burkitt lymphoma or chronic Lymphocytic Leukaemia. The present invention also relates to a process for predicting the progression and/or monitoring the progression of a cancer, comprising the in vitro detection of the expression of STIM1 in a sample of the tumour of the subject.

The present disclosure describes combination therapies comprising an antagonist of Programmed Death 1 receptor (PD-1) and a VEGFR inhibitor, and the use of the combination therapies for the treatment of cancer, and in particular for treating cancers that express PD-L1.

The present disclosure provides a pharmaceutical composition comprising an antibody having ADCC activity, a T cell-redirecting antibody, or a cell expressing a chimeric receptor, for use in combination with the administration of an antigen binding molecule capable of binding to a target antigen, wherein the primary molecule comprises a linker that is cleaved by protease, the antigen binding molecule obtained through the cleavage of the linker has the ability to bind to the target antigen, variable regions of the antibody having ADCC activity or the T cell-redirecting antibody, and an extracellular binding domain of the chimeric receptor bind to a cell expressing the target antigen via binding to the antigen binding molecule resulting from the cleavage of the cleavable linker.

Methods of culturing cells capable of producing desired proteins to obtain the proteins by use of a medium from which biological components are excluded as much as possible are provided. Specifically, a culture method characterized by culturing while maintaining a specific amino acid in a culture solution at a high concentration, and a cell culture fed-batch medium for use in the method are provided.

Provided herein are antibodies and related polypeptides that bind specifically to CEACAM6. The antibodies and/or polypeptides can be configured as bispecific T cell engagers. The antibodies and/or polypeptides can also be configured as chimeric antigen receptors. Also provided are methods of detection and treatment of cancer, for example, pancreatic cancer, using the antibodies and related polypeptides herein.

The present invention aims to provide a CAR that contains a single-chain antibody capable of specifically binding to GPC3 localized in the cell membrane and is useful for cancer immunotherapy using a CAR-T cell; and an immunocompetent cell expressing such a CAR. A gene encoding a CAR containing: a single-chain antibody that contains specific heavy-chain CDR1 to CDR3 and specific light-chain CDR1 to CDR3, as defined in claim 1, and specifically binds to a human-derived GPC3 polypeptide; a transmembrane region fused to a carboxyl terminus of the single-chain antibody; and an immunocompetent cell activation signaling transduction region fused to a carboxyl terminus of the transmembrane region is produced, and the gene is introduced into an immunocompetent cell. Thereby, a CAR-expressing immunocompetent cell having excellent cytotoxic activity on cancer cells and interferon gamma (IFN-γ) producibility can be produced.

A tetravalent, homodimer-type bispecific antibody molecule that simultaneously targets immune effector cell antigen CD3 and human epidermal growth factor receptor 2 (Her2); the bispecific antibody molecule comprises, from in sequence from N-terminus to C-terminus, a first single-chain Fv capable of specifically binding to Her2, a second single-chain Fv capable of specifically binding to CD3, and an Fc fragment; the first and second single-chain Fv are connected by means of a connection peptide, and the second single-chain Fv is connected to the Fc directly fragment or is connected by means of a connection peptide; the Fc fragment does not have effector functions such as CDC, ADCC and ADCP. The bispecific antibody may significantly inhibit or kill tumor cells, and has controlled toxic side effects that may be caused by excessive activation of effector cells. The maximum safe starting dose in preclinical toxicology evaluation tests is significantly higher than other doses having the same target, and no systemic immunotoxicity occurs, suggesting that the drug administration safety window for the bispecific antibody is wide; in addition, said bispecific antibody is a homodimer that does not experience the problem of heavy chain and light chain mismatching; the steps of purification are simple and efficient, expression is high, and the physicochemical and in vivo stability of the antibody are significantly improved.