Juridical Foundation the Chemo-sero-therapeutic Research Institute

Isis Pharmaceuticals, Inc.

The Chemo-sero-therapeutic Research Institute

Teijin Pharma Limited

Km Biologics Co., Ltd.

Teijin Limited

Hiroshi Nakatake

Chikateru Nozaki

Kenji Soejima

Tatsuo Eto

Kevin P Anderson

Ronnie C Hanecak

Fukusaburo Hamada

Takayuki Imamura

Tsukasa Nishihara

Ryoichi Kawamura

Shinichi Furukawa

Kazuya Hoshiko

Hitomi Togo

Arisa Maeyashiki

Thomas W Bruice

Walter F Lima

Masaki Hirashima

Hiroaki Maeda

Shoji Furusako

Nobuya Ohtomo

Hiroshi Yonemura

Keiichi Makizumi

Yoichiro Kino

Reiko Matsuyama

Wataru Morikawa

Tajayuki Imamura

Kiyotaka Suenaga

Akihiro Meta

Shoji Furasako

Hideki Takeo

A method for monomerization of MMP-7 aggregates is provided. A method for monomerization of MMP-7 aggregates which comprises treating MMP-7 aggregates with a buffer solution comprising a monovalent cation chloride (sodium chloride, potassium chloride, etc.) at a low concentration or with a buffer solution not comprising a monovalent cation chloride, a process for preparing MMP-7 which involves said method for monomerization, and a (pharmaceutical) composition comprising MMP-7 in the aforementioned buffer solution. In case that a (pharmaceutical) composition comprising MMP-7 at a low concentration is prepared, the aforementioned buffer solution comprising sugar alcohols or sugars is used.

Method for monomerizing matrix metalloproteinase 7 (MMP-7) aggregate

A process for preparing an inclusion body-forming protein is provided. A nucleic acid fragment having a nucleotide sequence coding for a modified alkaline phosphatase signal peptide (modified APSP) where leucine at the 13th position in the amino acid sequence shown in SEQ ID NO: 1 is substituted with proline and/or alanine at the 21st position is substituted with the other amino acid, downstream of which nucleotide sequence is bound a nucleotide sequence of a gene of a protein of interest is also provided.

Process for preparing inclusion body-forming protein

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 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

Antisense oligonucleotides are provided which are complementary to and hybridizable with at least a portion of HCV RNA and which are capable of inhibiting the function of the HCV RNA. These oligonucleotides can be administered to inhibit the activity of Hepatitis C virus in vivo or in vitro. These compounds can be used either prophylactically or therapeutically to reduce the severity of diseases associated with Hepatitis C virus, and for diagnosis and detection of HCV and HCV-associated diseases. Methods of using these compounds are also disclosed.

Compositions and methods for treatment of Hepatitis C virus-associated diseases

Compositions and methods for treatment of hepatitis C virus-associated diseases

A novel recombinant plasmid inserted with a herpes simplex virus gene, which comprises a plasmid vector containing a yeast DNA sequence and an Escherichia coli DNA sequence and carrying a promoter region and a herpes simplex virus gN gene (HSVgB) gene) recombined thereto under control of the promoter, said HSVgB gene lacking an N-terminal portion of the gene including a signal sequence-encoding region and optionally further lacking the region downstream therefrom, such as a gB gene lacking a DNA sequence encoding the N-terminal 30 amino acids, and a gB gene lacking a DNA sequence encoding the N-terminal 83 amino acids. The recombinant plasmid is useful for the production of transformed yeast, which is useful for the production of HSVgB proteins suitable for producing HSV vaccine and diagnostic reagents for herpes simplex virus infections.

Recombinant plasmid inserted with herpes simplex virus gene

Growing community of inventors

Kikuchi, Japan

Hiroshi Nakatake