Juridical Foundation the Chemo-sero-therapeutic Research Institute

The Chemo-sero-therapeutic Research Institute

Km Biologics Co., Ltd.

Kumamoto University

Mitsubishi Kagaku Iatron, Inc.

Mitsubishi Chemical Medience Corporation

National University Corporation Kumamoto University

Kenji Soejima

Chikateru Nozaki

Tomohiro Nakagaki

Hiroaki Maeda

Toshihiro Nakashima

Masaharu Torikai

Hiroshi Nakatake

Takayoshi Hamamoto

Noriko Mimura

Takayuki Imamura

Ryoichi Kawamura

Yukio Ando

Hirofumi Jono

Yu Su

Akihiko Hosoi

Masayo Ueno

Arisa Maeyashiki

Hitomi Togo

Tomoyo Takeo

Mineyuki Mizuguchi

Hiroyuki Shimizu

Masanori Matsumoto

Masaki Hirashima

Hirofumi Higuchi

Hiroshi Yonemura

Tomoko Ono

Miyuki Matsumoto

Wataru Morikawa

Yoshihiro Fujimura

Yoichi Sakata

Tajayuki Imamura

Tomohiro; c/o Kikuchi Research Center Nakagaki

A human antibody which comprises a complementarity determining region of an H chain consisting of the amino acid sequence as shown in SEQ ID NOs: 1 to 3 and a complementarity determining region of an L chain consisting of the amino acid sequence as shown in SEQ ID NOs: 4 to 6. The human antibody of the present invention has the activity to specifically bind to transthyretin (TTR) with structural change and the activity to inhibit fibrillization of TTR and is a human antibody suitable for application to human body.

Anti-transthyretin human antibody

A humanized antibody which comprises a complementarity determining region of an H chain consisting of the amino acid sequence as shown in SEQ ID NOs: 1 to 3 and a complementarity determining region of an L chain consisting of the amino acid sequence as shown in SEQ ID NOs: 4 to 6. The humanized antibody of the present invention has the activity to specifically bind to transthyretin (TTR) with structural change and the activity to inhibit fibrillization of TTR and is a humanized antibody suitable for application to human body.

Anti-transthyretin humanized antibody

The present invention relates to a human anti-human IL-18 antibody which reacts with human interleukin-18 (human IL-18) and does not react with a K53A variant of human IL-18.

Human antibody against IL-18

An enhanced disintegrin-like domain, and metalloprotease, with an isolated human thrombospondin type 1 motif, member 13 (ADAMTS-13) that includes substitutions at one or more positions in the isolated human ADAMTS-13.

ADAMTS-13 mutant

A method of enhancing an enzymatic activity of a disintegrin-like domain, and metalloprotease, with an isolated human thrombospondin type 1 motif, member 13 (ADAMTS-13) by substituting on or more positions in the isolated human ADAMTS-13.

A Factor X (hereinafter referred to as 'FX') with a high activity is provided. The present invention relates to a method for efficiently preparing a recombinant, two-chain FX which comprises intervening glycosylation at such an amino acid sequence that is essential for glycosylation in FX to thereby allow for expression of a recombinant FX with no glycosylation, and the recombinant FX with no glycosylation obtained by said method.

Recombinant factor X with no glycosylation and method for preparing the same

Recombinant Factor X with no glycosylation and method for preparing the same

A method of detecting thrombosis or the degree of thrombophilia by measuring a von Willebrand factor cleaving protease, and a kit for detecting thrombosis or the degree of thrombophilia, comprising an antibody or a fragment thereof specifically binding to a von Willebrand factor-cleaving protease, are disclosed. The detection method and the detection kit have an excellent convenience, rapidity, and specificity.

Method of detecting thrombosis by measuring von Willenbrand factor-cleaving protease

This invention is intended to isolate and identify a vWF-specific cleaving protease. The vWF-specific cleaving protease cleaves a bond between residues Tyr 842 and Met 843 of vWF and comprises a polypeptide chain having Leu-Leu-Val-Ala-Val (SEQ ID NO: 1) as a partial sequence, and more preferably comprises a polypeptide chain having the partial N-terminal amino acid sequence of a mature protein, Ala-Ala-Gly-Gly-Ile-Leu-His-Leu-Glu-Leu-Leu-Val-Ala-Val (SEQ ID NO: 2), and having a molecular weight of 105 to 160 kDa in SDS-PAGE under reducing or non-reducing conditions. Isolation and identification of this vWF-specific cleaving protease have led to the possibility of replacement therapy for patients having diseases resulting from a deficiency of the protease, such as thrombotic thrombocytopenic purpura.

Von Willebrand factor (vWF)-cleaving protease

A genetic recombinant human thrombin is provided. Human thrombin is efficiently prepared by the genetic engineering technique comprising the steps: (1) culturing a transfectant animal cell transfected with an expression vector in which a gene encoding human prethrombin is incorporated to the downstream of a promoter so as to produce and accumulate prethrombin in culture supernatant and recovering the produced human prethrombin; (2) treating a solution containing human prethrombin recovered in step (1) with ecarin so as to convert human prethrombin into human thrombin; and (3) purifying the solution obtained after the above activation process to obtain purified human thrombin. The present invention allows for provision of human thrombin in a large scale in a safe and economical manner due to exclusion of blood-derived components.

Process for producing human thrombin by gene modification technique

It is intended to provide an antibody showing immunoreactivity selectively to ADAMTS-13 and applications of this antibody in epitope analysis or diagnosis of an ADAMTS-13 autoantibody-positive patient. Alternatively, it is intended to provide a process for producing and use of a modified ADAMTS-13 molecule partially deleted aiming at the application in pharmaceutical products. An antibody specific for ADAMTS-13 which can be obtained from a warm-blooded animal immunized and sensitized with a polypeptide containing a part or the whole of ADAMTS-13 amino acid sequence; a process for producing an antibody comprising a step of immunizing and sensitizing a warm-blooded animal with a polypeptide containing a part or the whole of ADAMTS-13 amino acid sequence; use of the above-described antibody including a method of detecting and purifying ADAMTS-13; and a modified ADAMTS-13 molecule partially deleted are provided.

Antibody against von Willebrand factor cleaving enzyme and assay system using the same

The present invention provides an epitope recognized by an antibody (hereinafter, also referred to as an anti-ADAMTS-13 antibody) against a cleaving protease (hereinafter, also referred to as ADAMTS-13) specific to von Willebrand factor (hereinafter, also referred to as vWF), and a polypeptide comprising the epitope region. The present invention also provides a polypeptide located in a region from position 449 to position 687 in an amino acid sequence composing the ADAMTS-13, which is recognized by the anti-ADAMTS-13 antibody, or a peptide fragment derived from the polypeptide.

Construct comprising recognition domain of antibody against von Willebrand factor-specific cleaving enzyme

Growing community of inventors

Kumamoto, Japan

Kenji Soejima