| 序号 | 专利名 | 申请号 | 申请日 | 公开（公告）号 | 公开（公告）日 | 发明人 |
|---|---|---|---|---|---|---|
| 1 | 一种基因重组表达中国鲎C因子特异性检测内毒素增强比浊法 | CN201610515205.2 | 2016-07-04 | CN106119271A | 2016-11-16 | 于源华; 郭瑞; 张昊; 张彬; 张起莹; 张洋; 徐蕾; 丁秋雨; 赵玉环; 沈洁 |
| 一种基因重组表达中国鲎C因子特异性检测内毒素增强比浊法，属于生物检测技术领域，其方法是：将基因片段克隆到表达载体上，从大肠杆菌细胞株中筛选出基因工程菌株。诱导重组SSCrFCES表达，确定优化的表达条件是：培养基PH 6.0，培养温度27‑29℃，诱导时菌体浓度OD600为1.3，诱导时间为48小时。通过亲和层析纯化，电泳，纯度到95％以上。回收率达到40％。乳胶微球偶联，使样品浊度发生变化；在340nm波长的光线通过该反应混合物时，检测体系的吸光值增大，当重组蛋白浓度固定时，绘制标准曲线，从而测出未知内毒素的含量。有益效果是：利用比浊法对内毒素进行测定，可广泛应用在检测真菌感染，食品，药品以及医疗器械检测等领域。 | ||||||
| 2 | 新重组因子C、其制造方法、及内毒素的测定法 | CN201380064649.3 | 2013-12-10 | CN104919046A | 2015-09-16 | 水村光; 小田俊男; 川畑俊一郞 |
| 本发明提供一种制造鲎的重组因子C的方法。将CHO DG44及HEK293等哺乳类细胞用作宿主细胞而表达鲎的因子C，从而制造鲎的重组因子C。 | ||||||
| 3 | Method for recombinant production of horseshoe crab factor C protein in protozoa | US14649765 | 2013-12-04 | US09725706B2 | 2017-08-08 | Bernd Buchberger; Holger Grallert; Sonja Molinaro |
| 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 harboring 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. | ||||||
| 4 | Cloned factor C cDNA of the Singapore horseshoe crab, Carcinoscorpius rotundicauda and purification of factor C proenzyme | US296014 | 1994-08-19 | US5716834A | 1998-02-10 | Jeak Ling Ding; Bow Ho |
| Full-length and deletion subclones of cDNAs for Factor C of Carcinoscorpius rotundicauda are provided. These cDNAs have been cloned into .lambda.gt 22 and pGEM 11Zf(+). Further manipulations of the 5' and 3' ends of these cDNAs have been carried out, and these cDNAs have been further subcloned into other expression vectors such as pGEMEX-1, pET 3b, and the yeast shuttle vectors YEpsec 1 and pEMBLyex 4, and pPIC 9 and pHIL D2. Also provided are host cells transformed with expression vectors containing DNA molecules encoding proteins having Factor C-like enzymatic activity, methods of producing such proteins, methods for purifying Factor C zymogens, and methods for protecting Factor C zymogens from autoactivation by Gram negative bacterial endotoxin while the proenzyme is being purified and/or processed from amoebocyte lysates or from recombinant clones, or during storage or subsequent handling. This protection is afforded by the addition of 5-30% Me.sub.2 SO, which reversibly inhibits the Factor C zymogen. | ||||||
| 5 | 原生動物におけるカブトガニC因子タンパク質の組み換え生産方法 | JP2015545998 | 2013-12-04 | JP6410727B2 | 2018-10-24 | ブーフベルガー ベルント; グラーレアト ホルガー; モリナーロ ゾーニャ |
| 6 | A NOVEL GENERATION OF CLONED HORSESHOE CRAB RECOMBINANT FACTOR C FOR DETECTION AND REMOVAL OF ENDOTOXIN | EP98945748.6 | 1998-09-18 | EP1015609B1 | 2004-09-01 | DING, Jeak, Ling, Ind. Techn. Relations Office; HO, Bow, Ind. & Techn. Relations Office |
| 7 | NOVEL RECOMBINANT FACTOR C AND METHOD FOR PRODUCING THE SAME, AND METHOD FOR MEASURING ENDOTOXIN | US15983725 | 2018-05-18 | US20180258414A1 | 2018-09-13 | Hikaru Mizumura; Toshio Oda; Shun-ichiro Kawabata |
| To provide a method for producing a horseshoe crab recombinant Factor C. The horseshoe crab recombinant Factor C is produced through expression thereof by use of mammalian cells such as CHO DG44 and HEK293 as host cells. | ||||||
| 8 | METHOD FOR RECOMBINANT PRODUCTION OF HORSESHOE CRAB FACTOR C PROTEIN IN PROTOZOA | US15635301 | 2017-06-28 | US20170306315A1 | 2017-10-26 | Bernd BUCHBERGER; Holger GRALLERT; Sonja MOLINARO |
| 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. | ||||||
| 9 | Expression of carcinoscorpius rotundicauda factor C in eukaryotes | US596405 | 1996-02-02 | US5858706A | 1999-01-12 | Jeak Ling Ding; Bow Ho |
| CrFC21 cDNA was cloned into two mammalian vectors: pCIneo and pCDNAI, both of which carry the strong CMV promoter for expression in mammalian cell lines. Various CrFC cDNA constructs transformed into P. pastoris and S. cerevisiae were expressed to yield full-length recombinant Factor C (rCrFC) protein of .about.130 kDa which is immunoreactive. The rCrFC is expressed in an intracellular, insoluble form. Intracellular localization of the nascent protein provides protection from premature digestion by proteases secreted by the host cell. Subsequent to its synthesis, rCrFC is solubilized and purified under pyrogen-free conditions. Using established protocols, the protein can be denatured and renatured to recover its biological functionality. By manipulation of the 5' end of CrFC26, truncated constructs containing this cDNA are expressed by S. cerevisiae to give immunoreactive rCrFC. The rCrFC produced from both CrFC21 and CrFC26 constructs, solubilized by Triton X-100 or SDS, is found to be immunoreactive. Solubilized rCrFC was purified as a proenzyme and reversibly protected from activation by addition of Me.sub.2 SO. | ||||||
| 10 | 新規組換えファクターＣ、その製造法、およびエンドトキシンの測定法 | JP2014552048 | 2013-12-10 | JPWO2014092079A1 | 2017-01-12 | 光 水村; 俊男 小田; 俊一郎 川畑 |
| カブトガニの組換えファクターCを製造する方法を提供する。CHO DG44およびHEK293等の哺乳類細胞を宿主細胞として用いてカブトガニのファクターCを発現することにより、カブトガニの組換えファクターCを製造する。 | ||||||
| 11 | 原生動物におけるカブトガニＣ因子タンパク質の組み換え生産方法 | JP2015545998 | 2013-12-04 | JP2015536158A | 2015-12-21 | ベルント ブーフベルガー; ホルガー グラーレアト; ゾーニャ モリナーロ |
| 本発明は、カブトガニ由来のC因子タンパク質をC因子タンパク質発現寄生性原生動物を用いて組み換え生産するための新規の方法を提供する。特に、本発明は、カブトガニC因子タンパク質をコードするポリヌクレオチドを有する寄生性原生動物宿主細胞、および前記寄生性原生動物宿主細胞を、前記細胞がカブトガニC因子タンパク質を発現する条件下で培養する工程を含むC因子タンパク質を生産する方法を提供する。さらに、本発明は、前記新規の方法によって生産される組み換えC因子タンパク質、ならびに内毒素の検出および/または除去におけるその使用を提供する。 | ||||||
| 12 | Recombinant Factor C and method for producing the same, and method for measuring endotoxin | US14650767 | 2013-12-10 | US10144923B2 | 2018-12-04 | Hikaru Mizumura; Toshio Oda; Shun-ichiro Kawabata |
| To provide a method for producing a horseshoe crab recombinant Factor C. The horseshoe crab recombinant Factor C is produced through expression thereof by use of mammalian cells such as CHO DG44 and HEK293 as host cells. | ||||||
| 13 | NOVEL RECOMBINANT FACTOR C AND METHOD FOR PRODUCING THE SAME, AND METHOD FOR MEASURING ENDOTOXIN | US14650767 | 2013-12-10 | US20150307864A1 | 2015-10-29 | Hikaru MIZUMURA; Toshio ODA; Shun-ichiro KAWABATA |
| To provide a method for producing a horseshoe crab recombinant Factor C. The horseshoe crab recombinant Factor C is produced through expression thereof by use of mammalian cells such as CHO DG44 and HEK293 as host cells. | ||||||
| 14 | METHOD FOR RECOMBINANT PRODUCTION OF HORSESHOE CRAB FACTOR C PROTEIN IN PROTOZOA | US14649765 | 2013-12-04 | US20150299684A1 | 2015-10-22 | Bernd BUCHBERGER; Holger GRALLERT; Sonja MOLINARO |
| 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. | ||||||
| 15 | Sushi peptide multimer | US10563551 | 2004-07-02 | US07763704B2 | 2010-07-27 | Jeak Ling Ding; Bow Ho |
| 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 mimic 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. | ||||||
| 16 | Sushi Peptide Multimer | US10563551 | 2004-07-02 | US20080113906A1 | 2008-05-15 | Jeak Ling Ding; Bow Ho |
| 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 mimic 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. | ||||||
| 17 | Expression of Carcinoscorpius rotundicauda Factor C in eukaryotes | US877620 | 1997-06-18 | US5985590A | 1999-11-16 | Jeak Ling Ding; Bow Ho |
| CrFC21 cDNA was cloned into two mammalian vectors: pCIneo and pCDNAI, both of which carry the strong CMV promoter for expression in mammalian cell lines. Various CrFC cDNA constructs transformed into P. pastoris and S. cerevisiae were expressed to yield full-length recombinant Factor C (rCrFC) protein of .about.130 kDa which is immunoreactive. The rCrFC is expressed in an intracellular, insoluble form. Intracellular localization of the nascent protein provides protection from premature digestion by proteases secreted by the host cell. Subsequent to its synthesis, rCrFC is solubilized and purified under pyrogen-free conditions. Using established protocols, the protein can be denatured and renatured to recover its biological functionality. By manipulation of the 5' end of CrFC26, truncated constructs containing this cDNA are expressed by S. cerevisiae to give immunoreactive rCrFC. The rCrFC produced from both CrFC21 and CrFC26 constructs, solubilized by Triton X-100 or SDS, is found to be immunoreactive. Solubilized rCrFC was purified as a proenzyme and reversibly protected from activation by addition of Me.sub.2 SO. | ||||||
| 18 | Cloned factor C cDNA of the Singapore Horseshoe Crab, Carcinoscorpius rotundicauda and purification of Factor C proenzyme | US460521 | 1995-06-02 | US5712144A | 1998-01-27 | Jeak Ling Ding; Bow Ho |
| Full-length and deletion subclones of cDNAs for Factor C of Carcinoscorpius rotundicauda are provided. These cDNAs have been cloned into .lambda.gt 22 and pGEM 11Zf(+). Further manipulations of the 5' and 3' ends of these cDNAs have been carried out, and these cDNAs have been further subcloned into other expression vectors such as pGEMEX-1, pET 3b, and the yeast shuttle vectors YEpsec 1 and pEMBLyex 4, and pPIC 9 and pHIL D2. Also provided are host cells transformed with expression vectors containing DNA molecules encoding proteins having Factor C-like enzymatic activity, methods of producing such proteins, methods for purifying Factor C zymogens, and methods for protecting Factor C zymogens from autoactivation by Gram negative bacterial endotoxin while the proenzyme is being purified and/or processed from amoebocyte lysates or from recombinant clones, or during storage or subsequent handling. This protection is afforded by the addition of 5-30% Me.sub.2 SO, which reversibly inhibits the Factor C zymogen. | ||||||
| 19 | 원생동물 중 참게 인자 C 단백질의 재조합 생산을 위한 방법 | KR1020157017635 | 2013-12-04 | KR1020150091499A | 2015-08-11 | 부흐베르거베른트; 그랄레르트홀거; 몰리나로손야 |
| 본 발명은 인자 C 단백질을 발현하는 기생성 원생동물을 사용하여, 참게로부터 인자 C 단백질의 재조합 생산을 위한 신규한 방법을 제공한다. 구체적으로, 본 발명은 참게 인자 C 단백질을 코딩하는 폴리뉴클레오티드를 갖는 기생성 원생동물 숙주 세포, 및 상기 세포가 상기 참게 인자 C 단백질을 발현하는 조건에서 상기 기생성 원생동물 숙주 세포를 배양하는 단계를 포함하는 인자 C 단백질을 생산하는 방법을 제공한다. 또한, 본 발명은 상기 신규한 방법에 의해 생산된 재조합 인자 C 단백질, 및 그의 내독소의 검출 및/또는 제거에서의 용도를 제공한다.
|
||||||
| 20 | NOVEL RECOMBINANT FACTOR C AND METHOD FOR PRODUCING SAME, AND METHOD FOR MEASURING ENDOTOXIN | EP13862466.3 | 2013-12-10 | EP2930241A1 | 2015-10-14 | MIZUMURA, Hikaru; ODA, Toshio; KAWABATA, Shun-ichiro |
To provide a method for producing a horseshoe crab recombinant Factor C. The horseshoe crab recombinant Factor C is produced through expression thereof by use of mammalian cells such as CHO DG44 and HEK293 as host cells. |
||||||
QQ群二维码
意见反馈
意见反馈