Provided is a method for preparing genetically-modified T cells expressing chimeric antigen receptor, comprising: (i) a step of preparing non-proliferative cells holding a viral peptide antigen, which are obtained by stimulating a group of cells comprising T cells using an anti-CD3 antibody and an anti-CD28 antibody followed by culturing in the presence of the viral peptide antigen and a treatment for causing the cells to lose their proliferation capability; (ii) a step of obtaining genetically-modified T cells into which a target antigen-specific chimeric antigen receptor gene has been introduced using a transposon method; (iii) a step of mixing the non-proliferative cells prepared by step (i) with the genetically-modified T cells obtained by step (ii), and co-culturing the mixed cells; and (iv) a step of collecting the cells after culture.

The present invention relates to a method for promoting diversification of variable regions of an antibody. Specifically, the present invention relates to a method for promoting diversification of the amino acid sequences of variable regions of an antibody generated by an avian B cell population, wherein the method comprises suppressing the PI3Kα activity of each avian B cell comprised in the avian B cell population expressing the antibody.

The present disclosure relates to an isolated anti-FcRn antibody, which is an antibody binding to FcRn (stands for neonatal Fc receptor, also called FcRP, FcRB or Brambell receptor) that is a receptor with a high affinity for IgG or a fragment thereof, a method of preparing thereof, a composition for treating autoimmune disease, which comprises the antibody, and a method of treating and diagnosing autoimmune diseases using the antibody. The FcRn-specific antibody according to the present disclosure binds to FcRn non-competitively with IgG to reduce serum pathogenic auto-antibody levels, and thus can be used for the treatment of autoimmune diseases.

The present invention relates to an anti-MUC1 antibody binding specifically to Mucin 1 (MUC1) or an antigen-binding fragment thereof, an antibody-drug conjugate or bispecific antibody comprising the antibody, a pharmaceutical composition for prevention or treatment of cancer, comprising the same antibody, conjugate or bispecific antibody, and a nucleic acid encoding the same antibody, a vector and a host cell, both carrying the same nucleic acid, and a method for preparing an anti-MUC1 antibody or an antigen-binding fragment thereof, using the same vector and host cell. According to the present invention, the antibody shows outstanding affinity and binding force to MUC1 and the antibody-drug conjugate can bind specifically to a MUC1-expressing cell to specifically or selectively transfer the drug with efficacy. Therefore, the anti-MUC1 antibody and the antibody-drug conjugate according to the present invention can be usefully applied to the treatment of a MUC1-related disease, for example, cancer.

The present disclosure describes the fusogenic activity of the Myomaker protein. This polypeptide, when expressed in non-muscle cells, is able to drive fusion of the cell with a muscle cell, but not with other non-muscle cells. The use of this protein and cell expressing it in the delivery of exogenous genetic material to muscle cells also is described.

The present disclosure describes the fusogenic activity of the Myomaker protein. This polypeptide, when expressed in non-muscle cells, is able to drive fusion of the cell with a muscle cell, but not with other non-muscle cells. The use of this protein and cell expressing it in the delivery of exogenous genetic material to muscle cells also is described.

The present invention relates to an anti-MUC1 antibody binding specifically to Mucin 1 (MUC1) or an antigen-binding fragment thereof, an antibody-drug conjugate or bispecific antibody comprising the antibody, a pharmaceutical composition for prevention or treatment of cancer, comprising the same antibody, conjugate or bispecific antibody, and a nucleic acid encoding the same antibody, a vector and a host cell, both carrying the same nucleic acid, and a method for preparing an anti-MUC1 antibody or an antigen-binding fragment thereof, using the same vector and host cell. According to the present invention, the antibody shows outstanding affinity and binding force to MUC1 and the antibody-drug conjugate can bind specifically to a MUC1-expressing cell to specifically or selectively transfer the drug with efficacy. Therefore, the anti-MUC1 antibody and the antibody-drug conjugate according to the present invention can be usefully applied to the treatment of a MUC1-related disease, for example, cancer.

Immunostimulatory fusion molecules that include an immune cell targeting moiety and a cytokine molecule, pharmaceutical and formulations thereof, and methods of using and making the same, are disclosed.

Disclosed are a human serum albumin mutant that can be linked to a physiologically active protein to increase the stability of the protein in the blood, as well as a resulting protein produced by linking with the mutant. The protein produced by linking with the mutant consists of a human serum albumin mutant comprising the amino acid sequence set forth as SEQ ID NO:3 or an amino acid sequence that, in comparison with it, lacks not more than 10 amino acid residues and/or has not more than 10 amino acid residues replaced, with the proviso that the asparagine residue occurring at position 318 and the threonine at position 320 from the N-terminus of the amino acid sequence set forth as SEQ ID NO:3 are preserved and linked by peptide bonds via a single amino acid residue (X) except proline placed between those two amino acid residues, and a physiologically active protein linked to the mutant.

Disclosed are a human serum albumin mutant that can be linked to a physiologically active protein to increase the stability of the protein in the blood, as well as a resulting protein produced by linking with the mutant. The protein produced by linking with the mutant consists of a human serum albumin mutant comprising the amino acid sequence set forth as SEQ ID NO:3 or an amino acid sequence that, in comparison with it, lacks not more than 10 amino acid residues and/or has not more than 10 amino acid residues replaced, with the proviso that the asparagine residue occurring at position 318 and the threonine at position 320 from the N-terminus of the amino acid sequence set forth as SEQ ID NO:3 are preserved and linked by peptide bonds via a single amino acid residue (X) except proline placed between those two amino acid residues, and a physiologically active protein linked to the mutant.