| 序号 | 专利名 | 申请号 | 申请日 | 公开（公告）号 | 公开（公告）日 | 发明人 |
|---|---|---|---|---|---|---|
| 21 | METHOD FOR RECOMBINANT PRODUCTION OF HORSESHOE CRAB FACTOR C PROTEIN IN PROTOZOA | EP13818680.4 | 2013-12-04 | EP2929025A1 | 2015-10-14 | BUCHBERGER, Bernd; MOLINARO, Sonja; GRALLERT, Holger |
| The present invention provides a novel method for the recombinant production of Factor C protein from horseshoe crab using a parasitic protozoan expressing the Factor C protein. In particular, the present invention provides a parasitic protozoan host cell harbouring a polynucleotide encoding horseshoe crab Factor C protein, and a method for producing Factor C protein comprising culturing said parasitic protozoan host cell under conditions such that the cells express the horseshoe crab Factor C protein. Furthermore, the present invention provides recombinant Factor C protein produced by the novel method and its use in the detection and/or removal of endotoxin. | ||||||
| 22 | Method for recombinant production of horseshoe crab Factor C protein in protozoa | EP12195742.7 | 2012-12-05 | EP2740791A1 | 2014-06-11 | The designation of the inventor has not yet been filed |
The present invention provides a novel method for the recombinant production of Factor C protein from horseshoe crab using a parasitic protozoan expressing the Factor C protein. In particular, the present invention provides a parasitic protozoan host cell harbouring a polynucleotide encoding horseshoe crab Factor C protein, and a method for producing Factor C protein comprising culturing said parasitic protozoan host cell under conditions such that the cells express the horseshoe crab Factor C protein. Furthermore, the present invention provides recombinant Factor C protein produced by the novel method and its use in the detection and/or removal of endotoxin.
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| 23 | SUSHI PEPTIDE MULTIMER | EP04749216.0 | 2004-07-02 | EP1644410B1 | 2009-09-09 | DING, Jeak, Ling; HO, Bow |
| Endotoxin, also known as lipopolysaccharides (LPS), is the major mediator of septic shock due to Gram-negative bacterial infection. Chemically synthesized S3 peptide, derived from Sushi3 domain of Factor C, which is the endotoxin-sensitive serine protease of the limulus coagulation cascade, binds and neutralizes LPS activity. Fluorescent tagged-S3 is shown to detect LPS-containing bacteria. For large-scale production of S3 and to mimick other pathogen-recognizing molecules, tandem multimers of the S3 gene were constructed and expressed in E. coli. Tetramer of S3 for example is shown to display an enhanced inhibitory effect on LPS-induced activities. An affinity matrix based on tetramer of S3 is also shown to be particularly efficient at removing LPS. | ||||||
| 24 | METHOD FOR RECOMBINANT PRODUCTION OF HORSESHOE CRAB FACTOR C PROTEIN IN PROTOZOA | EP13818680.4 | 2013-12-04 | EP2929025B1 | 2018-04-11 | BUCHBERGER, Bernd; MOLINARO, Sonja; GRALLERT, Holger |
| The present invention provides a novel method for the recombinant production of Factor C protein from horseshoe crab using a parasitic protozoan expressing the Factor C protein. In particular, the present invention provides a parasitic protozoan host cell harbouring a polynucleotide encoding horseshoe crab Factor C protein, and a method for producing Factor C protein comprising culturing said parasitic protozoan host cell under conditions such that the cells express the horseshoe crab Factor C protein. Furthermore, the present invention provides recombinant Factor C protein produced by the novel method and its use in the detection and/or removal of endotoxin. | ||||||
| 25 | NOVEL RECOMBINANT FACTOR C AND METHOD FOR PRODUCING SAME, AND METHOD FOR MEASURING ENDOTOXIN | EP13862466 | 2013-12-10 | EP2930241A4 | 2016-08-03 | MIZUMURA HIKARU; ODA TOSHIO; KAWABATA SHUN-ICHIRO |
| The present invention relates to methods for mitigating a reaction inhibition in endotoxin assay in the presence of a salt ion, methods for producing a water soluble horseshoe crab Factor C for use in endotoxin assay in the presence of a salt ion, and methods for measuring endotoxin in a test specimen. | ||||||
| 26 | SUSHI PEPTIDE MULTIMER | EP04749216 | 2004-07-02 | EP1644410A4 | 2006-11-02 | DING JEAK LING; HO BOW |
| Endotoxin, also known as lipopolysaccharides (LPS), is the major mediator of septic shock due to Gram-negative bacterial infection. Chemically synthesized S3 peptide, derived from Sushi3 domain of Factor C, which is the endotoxin-sensitive serine protease of the limulus coagulation cascade, binds and neutralizes LPS activity. Fluorescent tagged-S3 is shown to detect LPS-containing bacteria. For large-scale production of S3 and to mimick other pathogen-recognizing molecules, tandem multimers of the S3 gene were constructed and expressed in E. coli. Tetramer of S3 for example is shown to display an enhanced inhibitory effect on LPS-induced activities. An affinity matrix based on tetramer of S3 is also shown to be particularly efficient at removing LPS. | ||||||
| 27 | SUSHI PEPTIDE MULTIMER | EP04749216.0 | 2004-07-02 | EP1644410A1 | 2006-04-12 | DING, Jeak, Ling; HO, Bow |
| Endotoxin, also known as lipopolysaccharides (LPS), is the major mediator of septic shock due to Gram-negative bacterial infection. Chemically synthesized S3 peptide, derived from Sushi3 domain of Factor C, which is the endotoxin-sensitive serine protease of the limulus coagulation cascade, binds and neutralizes LPS activity. Fluorescent tagged-S3 is shown to detect LPS-containing bacteria. For large-scale production of S3 and to mimick other pathogen-recognizing molecules, tandem multimers of the S3 gene were constructed and expressed in E. coli. Tetramer of S3 for example is shown to display an enhanced inhibitory effect on LPS-induced activities. An affinity matrix based on tetramer of S3 is also shown to be particularly efficient at removing LPS. | ||||||
| 28 | A NOVEL GENERATION OF CLONED HORSESHOE CRAB RECOMBINANT FACTOR C FOR DETECTION AND REMOVAL OF ENDOTOXIN | EP98945748.6 | 1998-09-18 | EP1015609A1 | 2000-07-05 | .ING, Jeak, Ling,Ind. Techn. Relations Office; HO, Bow,Ind. & Techn. Relations Office |
| The horseshoe crab, Carcinoscropius rotundicauda Factor C cDNA (CrFC21) has been cloned into a shuttle baculoviral vector. The recombinant baculoviral DNA was then transfected into the insect cells for expression of recombinant Factor C. Recombinant Factor C was found to be immunoreactive and is capable of binding both free and bound/immobilized lipid A. It is enzymatically active when triggered by LPS. The rFC is probably of the two-chain form, being cleaved into the heavy and light chains after activation by Gram negative bacterial endotoxin. As low as 0.01 pg (0.001 ng/ml) of LPS was detectable by the rFC, thus, indicating its potentials as a novel generation of 'limulus amoebocyte lysate'. | ||||||
| 29 | A NOVEL GENERATION OF CLONED HORSESHOE CRAB RECOMBINANT FACTOR C FOR DETECTION AND REMOVAL OF ENDOTOXIN | PCT/SG9800073 | 1998-09-18 | WO9915676B1 | 1999-05-14 | DING JEAK LING; HO BOW |
| The horseshoe crab, Carcinoscropius rotundicauda Factor C cDNA (CrFC21) has been cloned into a shuttle baculoviral vector. The recombinant baculoviral DNA was then transfected into the insect cells for expression of recombinant Factor C. Recombinant Factor C was found to be immunoreactive and is capable of binding both free and bound/immobilized lipid A. It is enzymatically active when triggered by LPS. The rFC is probably of the two-chain form, being cleaved into the heavy and light chains after activation by Gram negative bacterial endotoxin. As low as 0.01 pg (0.001 ng/ml) of LPS was detectable by the rFC, thus, indicating its potentials as a novel generation of "limulus amoebocyte lysate". | ||||||
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