Abstract: A secondary battery includes an electrode assembly having a positive electrode provided with a positive electrode tab, a separator, and a negative electrode provided with a negative electrode tab, the positive electrode, the separator, and the negative electrode being wound, the electrode assembly having a core part at a center thereof; a can configured to receive the electrode assembly therein, the negative electrode tab being connected to the can; a cap assembly coupled to an opening of the can, the positive electrode tab being connected to the cap assembly; and a reinforcing member provided on an end of the separator exposed beyond the positive electrode or the negative electrode to prevent heat of the positive electrode tab or the negative electrode tab from being transferred to the separator.

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.

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: Methods and composition for the screening and isolation of aglycosylated antibody Fc domain polypeptides. For example, in certain aspects methods for identifying aglycosylated Fc domains that bind to Fc receptors or preferentially bind to particular Fc receptors are described. Furthermore, the invention provides aglycosylated Fc domains that bind to Fc receptors with high affinity. Enhanced methods and media for prokaryotic based interaction screening are also provided.

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: Methods and compositions involving polypeptides having an aglycosylated antibody Fc domain. In certain embodiments, polypeptides have an aglycosylated Fc domain that contains one or more substitutions compared to a native Fc domain. Additionally, some embodiments involve an Fc domain that is binds some Fc receptors but not others. For example, polypeptides are provided with an aglycosylated Fc domain that selectively binds Fc?RIIa, but that is significantly reduced for binding to the highly homologous Fc?RIIb receptors. Furthermore, methods and compositions are provided for promoting antibody-dependent cell-mediated toxicity (ADCC) using a polypeptide having a modified aglycosylated Fc domain and a second non-Fc binding domain, which can be an antigen binding region of an antibody or a non-antigen binding region. Some embodiments concern antibodies with such polypeptides, which may have the same or different non-Fc binding domain.

Abstract: Methods and compositions involving polypeptides having an aglycosylated antibody Fc domain. In certain embodiments, polypeptides have an aglycosylated Fc domain that contains one or more substitutions compared to a native Fc domain. Additionally, some embodiments involve an Fc domain that is binds some Fc receptors but not others. For example, polypeptides are provided with an aglycosylated Fc domain that selectively binds Fc?RIIa, but that is significantly reduced for binding to the highly homologous Fc?RIIb receptors. Furthermore, methods and compositions are provided for promoting antibody-dependent cell-mediated toxicity (ADCC) using a polypeptide having a modified aglycosylated Fc domain and a second non-Fc binding domain, which can be an antigen binding region of an antibody or a non-antigen binding region. Some embodiments concern antibodies with such polypeptides, which may have the same or different non-Fc binding domain.