Abstract: [Problem]The purpose of the present invention is to provide a bispecific antibody that is structurally stable, and can show alone a sufficient effect without the co-administration of activated lymphocyte (T-LAK). [Solution] The present invention is therefore related to a humanized highly functional bispecific antibody comprising humanized variable regions of the heavy chain (5H) and the light chain (5L) of an anti-human EGF receptor 1 antibody 528, and humanized variable regions of the heavy chain (OH) and the light chain (OL) of an anti-CD3 antibody OKT3; and having one of the following structures (i)-(vi) in Claim 1, wherein the 5H, 5L, OH and OL have an amino acid sequence represented by SEQ ID Nos 25, 26, 27 and 28, respectively.

Abstract: A structure comprises at least a porous body holding a substance releasably, comprising a capping member for keeping the substance inside the pore and/or on at least a part of the entire surface of the porous body, and a connecting member for connecting the porous body and the capping member separably, the connecting member comprising a biopolymer compound. A method for releasing a substance from the structure set forth comprises the steps of applying stimulation from outside to the structure, and cleaving at least one of the bonding between the connecting member and the capping member and the bonding between the connecting member and the porous member to make the substance releasable from the structure.

Abstract: A structure comprises at least a porous body holding a substance releasably, comprising a capping member for keeping the substance inside the pore and/or on at least a part of the entire surface of the porous body, and a connecting member for connecting the porous body and the capping member separably, the connecting member comprising a biopolymer compound. A method for releasing a substance from the structure set forth comprises the steps of applying stimulation from outside to the structure, and cleaving at least one of the bonding between the connecting member and the capping member and the bonding between the connecting member and the porous member to make the substance releasable from the structure.

Abstract: A protein utilizing an anti-gold antibody and a gold-binding side which is a part of the anti-gold antibody is constructed. This protein is capable of specifically binding to gold. This protein or a complex protein containing such a protein can be used for the detection of a target substance.

Abstract: The purpose of the present invention is to provide a diabody-type bispecific antibody, which is characterized by having low immunogenicity and high infiltrating activity into tumor tissues, and by being easily mass-produced at a low cost with use of microorganisms, and by being easily altered in function by means of genetic engineering. The diabody-type bispecific antibody shows a more remarkable effect than the conventional diabody-type bispecific antibodies and chemically synthesized bispecific antibodies even in a very low concentration and in the absence of the super antigen.

Abstract: A structure comprises at least a porous body holding a substance releasably, comprising a capping member for keeping the substance inside the pore and/or on at least a part of the entire surface of the porous body, and a connecting member for connecting the porous body and the capping member separably, the connecting member comprising a biopolymer compound. A method for releasing a substance from the structure set forth comprises the steps of applying stimulation from outside to the structure, and cleaving at least one of the bonding between the connecting member and the capping member and the bonding between the connecting member and the porous member to make the substance releasable from the structure.

Abstract: This invention provides a system for controlling the phenotypic characteristics of cells. A pair of chimeric polypeptides is anchored in the plasma membrane, each of which has a variable region sequence and an effector sequence. The polypeptides are independent in the absence of antigen, but form a stable complex with each other when antigen is provided. This drives the effector sequences together in a manner that produces a receptor activation signal, leading to a phenotypic change. By titrating the amount of antigen present in the environment, the degree of phenotypic change can be regulated. Cells bearing chimeric polypeptides can be used to measure the concentration of antigen or select cells transfected with a therapeutic gene.

Abstract: This invention provides a method for measuring an antigen concentration in a sample, which comprises: preparing VH-domain polypeptide and VL-domain polypeptide of an antibody specific to the antigen; labeling one of the polypeptides with a reporter molecule to form labeled polypeptides, and immobilizing the other polypeptide onto solid-phase to form immobilized polypeptides; contacting the antigen-containing sample and the labeled polypeptides with the solid-phase; and measuring the reporter molecule of the labeled polypeptides bound to the immobilized polypeptides. The present invention permits simpler and quicker sandwich ELISA for measurements of an antigen concentration in high sensitivity.

Abstract: This invention provides a method for measuring an antigen concentration in a sample, which comprises: preparing VH-domain polypeptide and VL-domain polypeptide of an antibody specific to the antigen; labeling one of the polypeptides with a reporter molecule to form labeled polypeptides, and immobilizing the other polypeptides onto solid-phase to form immobilized polypeptides; contacting the antigen-containing sample and the labeled polypeptides with the solid-phase; and measuring the reporter molecule of the labeled polypeptides bound to the immobilized polypeptides. The present invention permits simpler and quicker sandwich ELISA for measurements of an antigen concentration in high sensitivity.