Abstract: Provided are Fc variants having improved half-life by binding to and unbinding from FcRn in a pH-dependent manner and which have improved selective binding 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?RIIa (increased A/I ratio) than a wild-type human antibody Fc domain and conventional antibodies approved as antibody therapeutic agents, thereby having remarkably improved ADCP 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 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 a glycosylated Fc variant with improved selective binding affinity to Fc?RIIIa. Novel human antibody Fc domain variants of the present invention have reduced binding affinity to Fc?RIIIb, which is an immuno-inhibitory receptor, compared to antibodies approved as conventional antibody therapeutic agents, and have improved binding affinity to Fc?RIIIa (an increase in the A/I ratio), which is an immuno-activating receptor, and thus have a significantly improved ability to induce ADCC, and have the effect of maximizing the immune action mechanism of therapeutic protein drugs, and thus can be effectively used as antibody drugs.

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 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 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 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 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 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.