Abstract: An anti-HBs monoclonal antibody is described herein. This antibody can bind to the following: (i) a wild type HBsAg; (ii) at least one mutant HBsAg selected from the group consisting of a first mutant HBsAg and a second mutant HBsAg; and (iii) at least one mutant HBsAg selected from the group consisting of a third mutant HBsAg and a fourth mutant HBsAg. The first mutant HBsAg has a mutation at position 120. The second mutant HBsAg has a mutation at position 141. The third mutant HBsAg has a substitution to a lysine at position 118. The fourth mutant HBsAg has only one mutation at position 144 and an amino acid at the position 144 is substituted by a glutamic acid.

Abstract: The present invention provides a method for measuring SARS virus nucleocapsid protein (SARS-NP) using first and second antibodies both binding specifically to SARS-NP, wherein the first or second antibody is an antibody recognizing an epitope located in a region (Region C) of amino acid 283 to 422 from the N-terminus of the amino acid sequence of SARS-NP.

Abstract: The object of the present invention is to provide a method for more accurately assaying the enzyme activities of mCK isozymes and a method for separately assaying the enzyme activities of CK isozymes by separately assaying the enzyme activities of ubiquitous mCK (umCK) and sarcomeric mCK (smCK). The above object is attained by an assay using an antibody that specifically recognizes umCK protein. In addition, other anti-mCK antibodies (e.g., anti-smCK antibody) and/or anti-human CK-M-inhibiting antibody can also be used. The above antibody is a polyclonal antibody or a monoclonal antibody. As a result of these antibodies, a monoclonal antibody (U1-1881) that is capable of specifically recognizing human umCK and is produced by a hybridoma having a deposition number of FERM BP-8342 is provided.

Abstract: An anti-HBs monoclonal antibody is described herein. This antibody can bind to the following: (i) a wild type HBsAg; (ii) at least one mutant HBsAg selected from the group consisting of a first mutant HBsAg and a second mutant HBsAg; and (iii) at least one mutant HBsAg selected from the group consisting of a third mutant HBsAg and a fourth mutant HBsAg. The first mutant HBsAg has a mutation at position 120. The second mutant HBsAg has a mutation at position 141. The third mutant HBsAg has a substitution to a lysine at position 118. The fourth mutant HBsAg has only one mutation at position 144 and an amino acid at the position 144 is substituted by a glutamic acid.

Abstract: The present invention provides a process and regent for analyzing annexin-V, wherein the measurement of a concentration of annexin-V can be easily carried out without need for addition of chemicals for inhibiting the bonding of various proteins with calcium ion and for adjusting a specimen solution to the specimen at a measuring stage, and a process and medicine for diagnosing an internal organ disorder based on the analyzing process and regent. A urine is brought into contact with an anti-annexin-V monoclonal antibody to perform an antigen-antibody reaction of annexin-V in the urine with the anti-annexin-V monoclonal antibody, thereby forming an annexin-V antigen/anti-annexin-V monoclonal antibody complex, and the amount of the formed annexin-V antigen/anti-annexin-V monoclonal antibody complex is quantitatively measured.

Abstract: The object of the present invention is to provide a method for more accurately assaying the enzyme activities of mCK isozymes and a method for separately assaying the enzyme activities of CK isozymes by separately assaying the enzyme activities of ubiquitous mCK (umCK) and sarcomeric mCK (smCK).

Abstract: A method for measuring the activity of creatine kinase MB (CK-MB) isozyme which is accurate, high in specificity, convenient, by inhibiting the activity of a mitochondria-localized creatine kinase (mCK) isozyme to avoid the influence of mCK and a measurement reagent therefor are provided.

Abstract: The present invention provides a process and regent for analyzing annexin-V, wherein the measurement of a concentration of annexin-V can be easily carried out without need for addition of chemicals for inhibiting the bonding of various proteins with calcium ion and for adjusting a specimen solution to the specimen at a measuring stage, and a process and medicine for diagnosing an internal organ disorder based on the analyzing process and regent. A urine is brought into contact with an anti-annexin-V monoclonal antibody to perform an antigen-antibody reaction of annexin-V in the urine with the anti-annexin-V monoclonal antibody, thereby forming an annexin-V antigen/anti-annexin-V monoclonal antibody complex, and the amount of the formed annexin-V antigen/anti-annexin-V monoclonal antibody complex is quantitatively measured.

Abstract: A method for measuring the activity of creatine kinase MB (CK-MB) isozyme which is accurate, high in specificity, convenient, by inhibiting the activity of a mitochondria localized creatine kinase (mCK) isozyme to avoid the influence of mCK and a measurement reagent therefor.

Abstract: The present invention provides a process and regent for analyzing annexin-V, wherein the measurement of a concentration of annexin-V can be easily carried out without need for addition of chemicals for inhibiting the bonding of various proteins with calcium ion and for adjusting a specimen solution to the specimen at a measuring stage, and a process and medicine for diagnosing an internal organ disorder based on the analyzing process and regent. A urine is brought into contact with an anti-annexin-V monoclonal antibody to perform an antigen-antibody reaction of annexin-V in the urine with the anti-annexin-V monoclonal antibody, thereby forming an annexin-V antigen/anti-annexin-V monoclonal antibody complex, and the amount of the formed annexin-V antigen/anti-annexin-V monoclonal antibody complex is quantitatively measured.

Abstract: This invention concerns a monoclonal antibody having binding specificity for an antigenic determinant site on core structural protein from Non-A,Non-B hepatitis virus (NANBV); a hybridoma cell line capable of producing the monoclonal antibody; a process for the preparation of the monoclonal antibody; an immunoassay of NANBV-related antigens by use of the monoclonal antibody; and a test kit for use in the immunoassay. The preferred monoclonal antibody is 5E3, 5F11, 515S or 1080S. The monoclonal antibody can specifically recognize the NANBV core structural protein in sera from patients with Non-A,Non-B hepatitis thereby being served extensively as an antibody in various immunological reagents for definitive diagnosis of Non-A, Non-B hepatitis.

Abstract: Using human annexin-V or human annexin-V plus dog annexin-V as antigen(s), hybridoma cell lines are prepared which are capable of producing anti-annexin-V monoclonal antibodies having a binding specificity to antigenic determinant site on annexin-V as antigenic protein and belonging to immunoglobulin G class. By the hybridoma cell lines are produced the anti-annexin-V monoclonal antibodies, with which a diagnostic agent is provided for diagnosis of myocardial infarction and angina pectoris.