Abstract: An apparatus for manufacturing an electrode according to an embodiment of the present invention includes a pattern formation mechanism configured to form a pattern groove in an electrode, the electrode including an electrode collector and a coating part made of an electrode active material applied on at least one surface of the electrode collector. The pattern formation mechanism presses a surface of the coating part to form the pattern groove, the pattern groove being an intaglio pattern in the coating part. Related methods for manufacturing the electrode and the electrode manufactured thereby are provided.

Abstract: The present invention provides a sealing process for a secondary battery of the present invention, which thermally fuses and seals a sealing portion that extends along an edge surface of a battery case, the sealing process comprising: an arrangement operation of disposing the sealing portion of the battery case between an anvil and a horn; a first region-fixing operation of pressing and fixing a first region of the sealing portion through the anvil and the horn; and a first region-primary sealing operation of applying an ultrasonic wave to the first region of the sealing portion through the horn at a set frequency and a set amplitude for a set time, thereby thermally fusing the first region of the sealing portion.

Abstract: A PD-L1 mutant having improved binding affinity for PD-1 is disclosed. A method for preparing the PD-L1 variant and a method for screening the PD-L1 variant are also disclosed. The PD-L1 variant produced by substituting some amino acids in the sequence of wild-type PD-L1 with other optimal amino acids, achieving greatly improved affinity for PD-1. In addition, the possibility of immunogenicity can be reduced by the smallest possible number of the mutation sites.

Abstract: The present disclosure relates to a novel human antibody or an antigen-binding fragment thereof that recognizes the SMO (smoothened) protein as an antigen and binds specifically thereto. The antibody of the present disclosure binds specifically to the SMO protein, which is directly involved in major cancer progression processes such as proliferation, migration, invasion and metastasis of cancer cells, and blocks the progression those processes. Therefore, it can be usefully used as a therapeutic agent for various cancers such as colon cancer, etc., resistant cancer, metastatic cancer, or recurrent cancer.

Abstract: Provided are Fc variants having improved half-life by binding to and unbinding from FcRn in a pH-dependent manner, which have improved capacity to selectively bind to Fc? receptors. The human Fc domain variants have lower capacity to bind to immune-inhibiting receptor Fc?RIIb and have higher capacity to bind to immune activating receptor Fc?RIIIa (increased A/I ratio) than a wild-type human antibody Fc domain and conventional antibodies approved as antibody therapeutic agents, thereby having remarkably improved ADCC induction ability and having maximized half-life in blood in which excellent pH-selective FcRn binding and unbinding capacity is exhibited, and thus bind to numerous peptide drug therapeutics having a low half-life and retention time in the body to enable the peptide drug therapeutics to have an increased blood half-life and exhibit long-term drug efficacy, and can maximize the immune mechanism of therapeutic protein drugs to be effectively used as an improved antibody drug.

Abstract: The present disclosure relates to an anti-CD20 asymmetric antibody including a single-chain variable fragment (scFv) on one side and an antigen-binding fragment (Fab) on the other side. Compared to an antibody having a symmetric structure, the asymmetric antibody of the present disclosure effectively activates complements and exhibits significantly improved complement-dependent cytotoxicity (CDC), and thus can be advantageously used as an effective therapeutic agent or therapeutic adjuvant for treating cancer.

Abstract: The present invention relates to a human antibody against a novel coronavirus and a variant thereof, or an immunologically active fragment of the human antibody. The human antibody against a novel coronavirus and a variant thereof, or an immunologically active fragment of the human antibody can effectively keep COVID-19 virus from infecting a host by binding with high affinity to an RBD region of a spike protein of COVID-19 virus or a variant thereof, may be utilized for preventing or treating COVID-19 virus infection by binding to a variety of all variants of COVID-19 virus with high affinity, and may be advantageously utilized in diagnosis and epidemiological surveys of highly infectious covid-19 virus by enabling rapid diagnosis (detection) of various types of COVID-19 virus.

Abstract: The present invention relates to an antibody having enhanced binding affinity for human Fc alpha receptor and a technique for maximizing a mechanism of antibody action by using same. Antibodies specific for Fc alpha receptors or immunologically active fragments thereof according to the present invention are in the form of IgG and bind to Fc alpha receptors of effector cells, especially, neutrophils, which are most abundant in mammals, thereby overcoming the disadvantages of conventional IgA antibodies and maximizing an effector function in various antibody therapeutic agents, which leads to maximizing the mechanism of antibody action (ADCC and ADCP). Thus, various Fc-fused protein therapeutic agents using same can be advantageously utilized as antibody drugs with enhanced effector functions.

Abstract: The present disclosure relates to PD-1 variants having minimal mutations for enhancing binding ability to PD-L1. The PD-1 variants of the present disclosure have fewer mutations than existing PD-1 and PD-1 variants and have significantly increased binding ability to PD-L1 compared to the existing variants, thereby solving the problem of immunogenicity. In addition, since these variants are very small-sized proteins as compared to existing antibody therapeutic agents, PD-1/PD-L1 binding of tumors and immune cells in a tumor micro-environment can be effectively inhibited, and since the problem of low binding ability of PD-L1 to existing PD-1 has been solved, the therapeutic effect thereof as a therapeutic agent can be significantly improved. These variants can also be used as an imaging agent for detecting the expression level of PD-L1.

Abstract: The present disclosure relates to a polypeptide including an Fc-gamma receptor mutant. The Fc-gamma receptor mutant of the present disclosure is optimized by substituting a part of an amino acid sequence of an Fc-gamma receptor with a different amino acid sequence, so as to provide an excellent selective binding ability to immunoglobulins. Therefore, it can be usefully used for increasing in vivo half-life of drugs, detecting and purifying immunoglobulins, inhibiting organ transplant rejections, or preventing or treating autoimmune diseases.

Abstract: The present disclosure pertains to an Fc variant having an improved half-life due to pH-dependent association and dissociation from FcRn. The Fc variant has a maximized blood half-life and exhibits a pH-sensitive FcRn association and dissociation ability superior to those of conventional blood half-life-improved Fc variants. Thus, the Fc variant can bind to numerous peptide drug therapeutics having a low half-life and retention time in the body, thereby enabling the peptide drug therapeutics to have an increased blood half-life and exhibit long-term drug efficacy. Accordingly, the dosage and frequency of administration of antibodies and biopharmaceuticals can be drastically reduced, and there is an effect of reducing the cost of new drug development and greatly improving the possibility of developing new drugs.

Abstract: The present invention relates to a polypeptide including an Fc variant produced by substituting a portion of the amino acid sequence of the Fc domain of a human antibody with a different amino acid sequence. The present invention also relates to an antibody including the polypeptide. The Fc variant can find application in a wide range of antibodies and Fc-fusion constructs. In one aspect, the antibody or Fc fusion construct of the present invention is a therapeutic, diagnostic or laboratory reagent, preferably a therapeutic reagent. The Fc variant is suitable for use in the treatment of cancer because its in vivo half-life can be maximized by optimization of the portion of the amino acid sequence. The antibody or Fc fusion construct of the present invention is used to kill target cells that bear a target antigen, for example cancer cells. Alternatively, the antibody or Fc fusion construct of the present invention is used to block, antagonize or agonize a target antigen.

Abstract: The present disclosure relates to a PD-1 variant having improved binding affinity to PD-L1. In addition, the present disclosure relates to a method for preparing the PD-1 variant and a method for screening the PD-1 variant. The PD-1 variant of the present disclosure effectively inhibits the binding between wild-type PD-1 and PD-L1, and thus is expected to have significantly higher penetration ability and anticancer effect by immune cells or therapeutic effect for infectious diseases as compared to existing immune checkpoint inhibitors. At the same time, the possibility of immunogenicity can be minimized. In addition, the convenience of developing biomedicine may be promoted through aglycosylation.

Abstract: The present invention relates to a polypeptide including an Fc variant produced by substituting a portion of the amino acid sequence of the Fc domain of a human antibody with a different amino acid sequence. The present invention also relates to an antibody including the polypeptide. The Fc variant can find application in a wide range of antibodies and Fc-fusion constructs. In one aspect, the antibody or Fc fusion construct of the present invention is a therapeutic, diagnostic or laboratory reagent, preferably a therapeutic reagent. The Fc variant is suitable for use in the treatment of cancer because its in vivo half-life can be maximized by optimization of the portion of the amino acid sequence. The antibody or Fc fusion construct of the present invention is used to kill target cells that bear a target antigen, for example cancer cells. Alternatively, the antibody or Fc fusion construct of the present invention is used to block, antagonize or agonize a target antigen.

Abstract: The present disclosure relates to a polypeptide containing an Fc domain in which a part of an amino acid sequence of a human antibody Fc domain is substituted with another amino acid sequence, or an aglycosylated antibody containing the same. The Fc domain of the present disclosure is optimized by substituting a part of an amino acid sequence of a wild-type Fc domain with another amino acid sequence. Therefore, it is useful in treatment of cancer due to superior selective binding ability to Fc?RIIIa among Fc receptors, and can be prepared as a homogeneous aglycosylated antibody through bacterial culture.

Abstract: The present invention relates to flavoprotein improved LOV (iLOV) variants that exhibit enhanced fluorescence intensity compared to iLOV. The present invention also relates to a method for screening any of the iLOV variants. The iLOV variants of the present invention are useful in determining whether target proteins are expressed, irrespective of the presence of oxygen, and isolating and purifying the expressed target proteins due to their enhanced fluorescence intensity and quantum yield compared to existing LOV or iLOV proteins.

Abstract: The present disclosure relates to a polypeptide containing an Fc domain in which a part of an amino acid sequence of a human antibody Fc domain is substituted with another amino acid sequence, or an aglycosylated antibody containing the same. The Fc domain of the present disclosure is optimized by substituting a part of an amino acid sequence of a wild-type Fc domain with another amino acid sequence. Therefore, it is useful in treatment of cancer due to superior selective binding ability to Fc?RIIIa among Fc receptors, and can be prepared as a homogeneous aglycosylated antibody through bacterial culture.

Abstract: The present invention relates to an antibody or an antigen-binding fragment thereof that has improved binding affinity for endothelin receptor type A. The present invention also relates to an antibody or an antigen-binding fragment thereof that has improved productivity. The antibody developed in the present invention is suitable for use in the treatment and diagnosis of diseases associated with endothelin receptor type A due to its remarkably improved binding affinity for the antigen and high productivity compared to conventional antibodies.

Abstract: The present invention relates to a monoclonal antibody or a fragment thereof that recognizes and binds specifically to the extracellular domain of endothelin receptor type A as an antigen. The monoclonal antibody of the present invention is suitable for use in a therapeutic agent for hypertension or cancer associated with endothelin receptor type A.

Abstract: A PD-L1 mutant having improved binding affinity for PD-1 is disclosed. A method for preparing the PD-L1 variant and a method for screening the PD-L1 variant are also disclosed. The PD-L1 variant produced by substituting some amino acids in the sequence of wild-type PD-L1 with other optimal amino acids, achieving greatly improved affinity for PD-1. In addition, the possibility of immunogenicity can be reduced by the smallest possible number of the mutation sites.