NWB-CMS Brassica oleracea has cytoplasmic male sterility. It relates to NWB-CMS cabbage plant having cytoplasmic male sterility derived from NWB-CMS cabbage line produced by fusion between protoplast of NWB-CMS radish line plant derived from callus of NWB-CMS radish line having cytoplasmic male sterility with inactivated nucleus and protoplast of male fertile cabbage plant with inactivated cytoplasm and a seed thereof, a plant of NWB-CMS Brassica oleracea line having cytoplasmic male sterility produced by breeding of a male fertile Brassica oleracea as a subject for introduction with the NWB-CMS cabbage plant as a breeding line and a seed thereof, a method for producing a hybrid seed of NWB-CMS Brassica oleracea line having cytoplasmic male sterility comprising breeding of a male fertile Brassica oleracea as a subject for introduction with the NWB-CMS cabbage plant as a breeding line, and a hybrid seed of NWB-CMS Brassica oleracea line produced by the method.

A monoclonal antibody to KIR2DS1 or a fragment containing an antigen-binding region thereof has VL having an amino acid sequence of SEQ ID NO: 1 or an amino acid sequence having the same amino acid sequence as the amino acid sequence except that one or several amino acids are conservatively substituted as CDR1, having an amino acid sequence of SEQ ID NO: 2 or an amino acid sequence having the same amino acid sequence as the amino acid sequence except that one or several amino acids are conservatively substituted as CDR2, and having an amino acid sequence of SEQ ID NO: 3 or an amino acid sequence having the same amino acid sequence as the amino acid sequence except that one or several amino acids are conservatively substituted as CDR3; and VH having an amino acid sequence of SEQ ID NO: 4 or SEQ ID NO: 5 or an amino acid sequence having the same amino acid sequence as the amino acid sequence except that one or several amino acids are conservatively substituted as CDR1, having an amino acid sequence of SEQ ID NO: 6 or an amino acid sequence having the same amino acid sequence as the amino acid sequence except that one or several amino acids are conservatively substituted as CDR2, and having an amino acid sequence of any one selected from the group consisting of SEQ ID NO: 7, SEQ ID NO: 8, and SEQ ID NO: 9 or an amino acid sequence having the same amino acid sequence as the amino acid sequence except that one or several amino acids are conservatively substituted as CDR3.

Provided are an IL-5 antibody, an antigen binding fragment thereof, and a medical application therefor. The present invention comprises a mouse-derived antibody containing an IL-5 antibody CDR region, a chimeric antibody, a humanized antibody, and a pharmaceutical composition comprising said IL-5 antibody and said antigen binding fragment thereof, as well as the use of the pharmaceutical composition as a drug.

The present invention relates to a method to modulate the level of activation of an engineered immune cell (such as a Chimeric Antigen Receptor T-cell) for immunotherapy. The present invention also relates to cells obtained by the present method, preferably comprising said modulable/tunable chimeric antigen receptors for use in therapeutic or prophylactic treatment.

The present invention relates to a method to modulate the level of activation of an engineered immune cell (such as a Chimeric Antigen Receptor T-cell) for immunotherapy. The present invention also relates to cells obtained by the present method, preferably comprising said modulable/tunable chimeric antigen receptors for use in therapeutic or prophylactic treatment.

Disclosed is an antibody which binds to olanzapine, which can be used to detect olanzapine in a sample such as in a competitive immunoassay method. The antibody can be used in a lateral flow assay device for point-of-care detection of olanzapine, including multiplex detection of aripiprazole, olanzapine, quetiapine, and risperidone in a single lateral flow assay device.

Disclosed is an antibody which binds to olanzapine, which can be used to detect olanzapine in a sample such as in a competitive immunoassay method. The antibody can be used in a lateral flow assay device for point-of-care detection of olanzapine, including multiplex detection of aripiprazole, olanzapine, quetiapine, and risperidone in a single lateral flow assay device.

The purpose of the present invention is to provide a specific antibody applicable to immunochromatographic detection of Mycoplasma pneumoniae infections, and a detection reagent using the same, among others. Provided are a Mycoplasma pneumoniae detection reagent and kit that include a specific antibody against the P30 protein of Mycoplasma pneumoniae, and an immunochromatographic test device.

[Problem] Provided is an anti-human Igβ antibody which crosslinks BCR and FcγRIIb and has an immunosuppressive function more enhanced than that of an antibody in the prior art.

[Means for Solution] An anti-human Igβ antibody comprising a heavy chain variable region comprising CDR1 consisting of the amino acid sequence of amino acid numbers 31 to 35 of SEQ ID NO: 2, CDR2 consisting of the amino acid sequence of amino acid numbers 50 to 65 of SEQ ID NO: 2, and CDR3 consisting of the amino acid sequence of amino acid numbers 98 to 108 of SEQ ID NO: 2, a light chain variable region comprising CDR1 consisting of the amino acid sequence of amino acid numbers 24 to 38 of SEQ ID NO: 4, CDR2 consisting of the amino acid sequence of amino acid numbers 54 to 60 of SEQ ID NO: 4, and CDR3 consisting of the amino acid sequence of amino acid numbers 93 to 101 of SEQ ID NO: 4, and a heavy chain constant region which is a human Igγ1 constant region having amino acid mutations of S239D, H268D, and L328W.

The purpose of the present invention is to provide a monoclonal antibody that is useful in specifically assaying tartrate resistant acid phosphatase 5b (TRACP-5b). A hybridoma producing a monoclonal antibody against TRACP-5b, said monoclonal antibody showing higher reactivity with TRACP-5b than with tartrate resistant acid phosphatase 5a (TRACP-5a) and, therefore, being specific to TRACP-5b, is obtained by cell fusion using, as an antigen, human recombinant TRACP-5b purified from silkworm silk gland. By using this monoclonal antibody, TRACP-5b in a specimen can be highly sensitively and specifically detected.