Kobayashi J.,Kanazawa Medical University |
Miyashita K.,Immuno Biological Laboratories Co. |
Nakajima K.,Gunma University |
Mabuchi H.,Kanazawa University
Journal of Atherosclerosis and Thrombosis | Year: 2015
Hepatic lipase (HL) is a key enzyme catalyzing the hydrolysis of triglycerides (TG) and phospholipids (PLs) in several lipoproteins. It is generally recognized that HL is involved in the remodeling of remnant, low-density lipoprotein (LDL), high-density lipoprotein (HDL) and the production of small, dense low-density lipoproteins (sd-LDLs). On the other hand, it is unclear whether HL accelerates or retards atherosclerosis. From the clinical point of view, HL deficiency may provide useful information on answering this question, but the rarity of this disease makes it impossible to conduct epidemiological study. In this review, we describe a comprehensive and updated view of the clinical significance of HL on lipid and lipoprotein metabolism. © 2015, Japan Atherosclerosis Society. All rights reserved.
Tomita M.,Immuno Biological Laboratories Co.
Biotechnology Letters | Year: 2011
As a result of breeding for more than 4,000 years, the silkworm, Bombyx mori, has acquired the ability to synthesize bulk amounts of silk proteins in its silk glands. To utilize this capacity for mass production of useful proteins, transgenic silkworms were generated that synthesized recombinant proteins in the silk gland and secreted them into the silk cocoon. The silk gland is classified into two main regions: the posterior (PSG) and the middle silk gland (MSG). By controlling the expressed regions of the recombinant protein gene in the silk gland, we were able to control the localization of the synthesized protein in the silk thread. Expression in the PSG or MSG led to localization in the insoluble fibroin core or hydrophilic outer sericin layer, respectively. This review focuses on the expression of recombinant protein in the MSG of transgenic silkworms. The recombinant protein secreted in the sericin layer is extractable from the cocoon with only a small amount of endogenous silk protein contamination by soaking the cocoon in mild aqueous solutions. The possibility of utilizing transgenic silkworms as a valuable tool for the mass production of therapeutic and industrially relevant recombinant proteins is discussed. © 2010 Springer Science+Business Media B.V.
Immuno Biological Laboratories Co. | Date: 2011-05-11
The purpose of the invention is to provide an antibody which recognizes OPN N-half but does not recognize the full-length OPN, and its use. A monoclonal antibody which is characterized in that it recognizes a protein or polypeptide in which the C-terminal amino acid sequence is YGLR (SEQ ID NO: 1) and it substantially does not recognize a protein or polypeptide which has an amino acid sequence of YGLR outside of the C-terminal, as well as a method for measuring OPN N-half utilizing the said antibody, a method for diagnosing diseases relating to OPN N-half, a method for judging the severity of said disease, and a method for treating said diseases, are provided.
Noguchi Institute and Immuno Biological Laboratories Co. | Date: 2015-04-17
The present invention is aimed to provide a method for preparing an acceptor that is N-glycan hydrolyzed antibody or a Fc fragment thereof used for producing antibody having a homogeneous N-glycan structure; a method for determining a combination of endoglycosidases for use in said preparation; and a method for measuring N-glycans linked to an antibody. The present invention is directed to a method for producing a N-glycan hydrolyzed antibody or Fc fragment thereof, comprising reacting the antibody or the Fc fragment thereof with several endoglycosidases; and a method for determining quantitative information of an objective N-glycan with a desired structure linked to an antibody or a Fc thereof, comprising a protease treatment step and a glycopeptide measurement step, etc.
Immuno Biological Laboratories Co. | Date: 2012-03-02
Disclosed is a novel means that enables mass production of highly safe fibrinogen at low cost. The transgenic silkworm of the present invention expresses the fibrinogen subunit A, B and chains in the silk gland cells and produces fibrinogen having coagulation activity in the cocoon filament. Preferably, the transgenic silkworm expresses the subunits in the middle silk gland cells and produces fibrinogen in the sericin layer of the cocoon filament. By recovering fibrinogen from the cocoon of the transgenic silkworm of the present invention, highly safe fibrinogen can be mass-produced at low cost.