Abstract: The present invention relates to a polypeptide improved in protein purity and in affinity for a target antigen, a conjugate thereof with an antibody or antigen-binding fragment, and a preparation method of the polypeptide and the conjugate. The polypeptide or the conjugate thereof according to the present invention does not undergo glycosylation even when produced in a eukaryotic cell and thus has high protein purity and affinity for a target antigen, showing a very high value as a reagent for diagnosis or treatment of a disease.

Abstract: Disclosed herein are an anti-HER2 affibody and a switch molecule including a cotinine-conjugated anti-HER2 affibody. When applied in combination with Cot-sCART, the cotinine-conjugated anti-HER2 affibody reacts with HER2-positive cells to induce immune cell activity, thereby finding advantageous applications as switch molecules in sCART therapeutic agents.

Abstract: The present invention relates to a new antibody or an antigen binding fragment thereof for use in the treatment of cancer by targeting a B cell malignancy, a chimeric antigen receptor comprising the same, and a use of the same. The antibody of the present invention is an antibody for specifically binding to CD19 that is highly expressed in cancer cells (particularly, blood cancer), has very low homology to a CDR sequence thereof compared to a CDR sequence of a conventional CD19 target antibody so that the sequence thereof is unique, and specifically binds to an epitope that is different from a FMC63 antibody fragment binding to CD19 of the conventional art. A cell expressing the chimeric antigen receptor comprising an anti-CD19 antibody or the antigen binding fragment of the present invention induces immune cell activity in response to a positive cell line expressing CD19, and thus may be utilized as a CAR-immune cell therapeutic agent.

Abstract: The present invention relates to a switch molecule for activating a chimeric antigen receptor effector cell, to a polypeptide or fusion protein binding thereto, and to a chimeric antigen receptor. (i) When a switch molecule of the present invention is used, in order to improve safety of a CAR-T cell, if severe toxicity appears, a switch molecule lacking a targeting moiety can be injected to adjust activation of the CAR-T cell. (ii) When an antigen is mutated, or in order to cure various carcinomas, instead of an existing switch molecule, a switch molecule targeting a new antigen generated due to the mutation or a switch molecule targeting a different tumor associated antigen (TAA) can be injected into a patient to cure cancer more effectively.

Abstract: The present invention relates to: a novel antibody or an antigen-binding fragment thereof for use in the treatment of cancer by targeting B cell malignancies; a chimeric antigen receptor comprising the same; and uses thereof. The antibody of the present invention is an antibody specifically binding to CD19 highly expressed in cancer cells (particularly, blood cancer) and has very low homology compared to the CDR sequences of conventional CD19 target antibodies, and thus the sequence thereof is unique. In addition, cells expressing a chimeric antigen receptor comprising an anti-CD19 antibody or antigen-binding fragment of the present invention induce immune cell activity in response to a positive cell line expressing CD19, and thus can be usefully used as a therapeutic agent for CAR-immune cells.

Abstract: The present invention relates to a new antibody or an antigen binding fragment thereof for use in the treatment of cancer by targeting a B cell malignancy, a chimeric antigen receptor comprising the same, and a use of the same. The antibody of the present invention is an antibody for specifically binding to CD19 that is highly expressed in cancer cells (particularly, blood cancer), has very low homology to a CDR sequence thereof compared to a CDR sequence of a conventional CD19 target antibody so that the sequence thereof is unique, and specifically binds to an epitope that is different from a FMC63 antibody fragment binding to CD19 of the conventional art. A cell expressing the chimeric antigen receptor comprising an anti-CD19 antibody or the antigen binding fragment of the present invention induces immune cell activity in response to a positive cell line expressing CD19.

Abstract: The present invention replaces an amino acid residue of a specific region of a parent antibody so as to improve the stability of the antibody, thereby improving druggability. A variant antibody of the present invention, compared to a parent antibody hz1E11, has significantly improved stability while having nearly the same productivity and efficacy. Therefore, the variant antibody of the present invention exhibits, in the development of HER2-specific antibodies, excellent characteristics such as reduction in production costs, inhibition of efficacy reduction and reduction of side effects.

Abstract: A novel antibody against VEGFR2 for use in the prevention or treatment of macular degeneration and cancer, which are angiogenesis-related diseases. The antibody of the present invention is an antibody which specifically binds to VEGFR2 which is overexpressed in vascular endothelial cells. The antibody of the present invention has very low homology compared to the CDR sequences of conventional VEGFR2 target antibodies, and thus is unique in its sequence. Since the antibody of the present invention, when treated alone, has the ability to inhibit vascular endothelial cell growth equivalent to that of ramucirumab which is conventionally used, it is very effective to prevent or treat angiogenesis-related diseases.

Abstract: A novel antibody against VEGFR2 for use in the prevention or treatment of macular degeneration and cancer, which are angiogenesis-related diseases. The antibody of the present invention is an antibody which specifically binds to VEGFR2 which is overexpressed in vascular endothelial cells. The antibody of the present invention has very low homology compared to the CDR sequences of conventional VEGFR2 target antibodies, and thus is unique in its sequence. Since the antibody of the present invention, when treated alone, has the ability to inhibit vascular endothelial cell growth equivalent to that of ramucirumab which is conventionally used, it is very effective to prevent or treat angiogenesis-related diseases.

Abstract: The present invention relates to HER2 (Human Epidermal Growth Factor Receptor 2) antibodies to prevent or treat cancers. The antibodies of the invention binds specifically to HER2 over-expressed in cancer cells (particularly, breast cancer and stomach cancer cells), specifically to an epitope on HER2 being different from epitope for trastuzumab. The CDR sequences of the present antibodies exhibit low similarity to CDR sequences of publicly known HER2 antibodies, addressing that the CDR sequences are unique. The antibodies of the present invention in combination with trastuzumab kill cancer cells with significantly enhanced cytotoxicity and therefore very effective in therapy of cancer (particularly, breast cancer and stomach cancer). Without wishing to be bound by theory, the enhanced efficacies of the combined therapy would address that the antibodies of the present invention bind to epitope on HER2 being different from epitope for trastuzumab, and inhibit HER2 in a cooperative manner with trastuzumab.

Abstract: The present disclosure relates to complex comprising an engineered polypeptide having affinity for interleukin-6 (in the following referred to as IL-6) and an antibody or an antigen binding fragment thereof, wherein said engineered polypeptide having affinity for IL-6 belongs to a class of engineered polypeptides comprising the sequence EEX3X4AWX7EIHX11 LPNLX16X17X18QX20X21AFIX25X26LX28X29. The present disclosure also relates to the use of said complex as a therapeutic agent.

Abstract: The present invention relates to HER2 (Human Epidermal Growth Factor Receptor 2) antibodies to prevent or treat cancers. The antibodies of the invention binds specifically to HER2 over-expressed in cancer cells (particularly, breast cancer and stomach cancer cells), specifically to an epitope on HER2 being different from epitope for trastuzumab. The CDR sequences of the present antibodies exhibit low similarity to CDR sequences of publicly known HER2 antibodies, addressing that the CDR sequences are unique. The antibodies of the present invention in combination with trastuzumab kill cancer cells with significantly enhanced cytotoxicity and therefore very effective in therapy of cancer (particularly, breast cancer and stomach cancer). Without wishing to be bound by theory, the enhanced efficacies of the combined therapy would address that the antibodies of the present invention bind to epitope on HER2 being different from epitope for trastuzumab, and inhibit HER2 in a cooperative manner with trastuzumab.