IL93660A - DNA that encodes the b-chain of a 2 IL receptor, prepares it and coordinates stores that contain it - Google Patents

DNA that encodes the b-chain of a 2 IL receptor, prepares it and coordinates stores that contain it

Info

Publication number: IL93660A
Authority: IL; Israel
Prior art keywords: ctg; gag; ccc; ctc; gcc
Prior art date: 1989-03-07

Application number

IL9366090A

Other languages

English (en)

Hebrew (he)

Other versions

IL93660A0 (en

Original Assignee

Boehringer Ingelheim Int

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1989-03-07

Filing date

1990-03-06

Publication date

2001-11-25

1989-03-07 Priority claimed from EP89104023A external-priority patent/EP0386289A1/de

1989-07-20 Priority claimed from EP89113310A external-priority patent/EP0408790A1/de

1990-03-06 Application filed by Boehringer Ingelheim Int filed Critical Boehringer Ingelheim Int

1990-12-23 Publication of IL93660A0 publication Critical patent/IL93660A0/xx

2001-11-25 Publication of IL93660A publication Critical patent/IL93660A/en

Links

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108040006849 interleukin-2 receptor activity proteins Proteins 0.000 claims abstract description 11
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108020004414 DNA Proteins 0.000 claims description 30
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102000053602 DNA Human genes 0.000 claims description 16
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108091026890 Coding region Proteins 0.000 claims description 4
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PIDRBUDUWHBYSR-UHFFFAOYSA-N 1-[2-[[2-[(2-amino-4-methylpentanoyl)amino]-4-methylpentanoyl]amino]-4-methylpentanoyl]pyrrolidine-2-carboxylic acid Chemical compound CC(C)CC(N)C(=O)NC(CC(C)C)C(=O)NC(CC(C)C)C(=O)N1CCCC1C(O)=O PIDRBUDUWHBYSR-UHFFFAOYSA-N 0.000 claims 1
CXRCVCURMBFFOL-FXQIFTODSA-N Ala-Ala-Pro Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(O)=O CXRCVCURMBFFOL-FXQIFTODSA-N 0.000 claims 1
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SOBIAADAMRHGKH-CIUDSAMLSA-N Ala-Leu-Ser Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(O)=O SOBIAADAMRHGKH-CIUDSAMLSA-N 0.000 claims 1
UCDOXFBTMLKASE-HERUPUMHSA-N Ala-Ser-Trp Chemical compound C[C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC1=CNC2=CC=CC=C21)C(=O)O)N UCDOXFBTMLKASE-HERUPUMHSA-N 0.000 claims 1
DFCIPNHFKOQAME-FXQIFTODSA-N Arg-Ala-Asn Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(N)=O)C(O)=O DFCIPNHFKOQAME-FXQIFTODSA-N 0.000 claims 1
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PBSOQGZLPFVXPU-YUMQZZPRSA-N Arg-Glu-Gly Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(O)=O PBSOQGZLPFVXPU-YUMQZZPRSA-N 0.000 claims 1
NLRJGXZWTKXRHP-DCAQKATOSA-N Asn-Leu-Arg Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O NLRJGXZWTKXRHP-DCAQKATOSA-N 0.000 claims 1
DTNUIAJCPRMNBT-WHFBIAKZSA-N Asp-Gly-Ala Chemical compound [H]N[C@@H](CC(O)=O)C(=O)NCC(=O)N[C@@H](C)C(O)=O DTNUIAJCPRMNBT-WHFBIAKZSA-N 0.000 claims 1
JUWISGAGWSDGDH-KKUMJFAQSA-N Asp-Phe-Lys Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC(O)=O)CC1=CC=CC=C1 JUWISGAGWSDGDH-KKUMJFAQSA-N 0.000 claims 1
GCACQYDBDHRVGE-LKXGYXEUSA-N Asp-Thr-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H]([C@H](O)C)NC(=O)[C@@H](N)CC(O)=O GCACQYDBDHRVGE-LKXGYXEUSA-N 0.000 claims 1
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MWMJCGBSIORNCD-AVGNSLFASA-N Glu-Leu-Leu Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(O)=O MWMJCGBSIORNCD-AVGNSLFASA-N 0.000 claims 1
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MGBRZXXGQBAULP-DRZSPHRISA-N Phe-Glu-Ala Chemical compound OC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](N)CC1=CC=CC=C1 MGBRZXXGQBAULP-DRZSPHRISA-N 0.000 claims 1
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Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/715—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons
- C07K14/7155—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons for interleukins [IL]

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Health & Medical Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Zoology (AREA)
Molecular Biology (AREA)
Gastroenterology & Hepatology (AREA)
Immunology (AREA)
Biochemistry (AREA)
Biophysics (AREA)
General Health & Medical Sciences (AREA)
Genetics & Genomics (AREA)
Medicinal Chemistry (AREA)
Toxicology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Cell Biology (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Peptides Or Proteins (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Steroid Compounds (AREA)

IL9366090A 1989-03-07 1990-03-06 DNA that encodes the b-chain of a 2 IL receptor, prepares it and coordinates stores that contain it IL93660A (en)

Applications Claiming Priority (3)

Application Number	Priority Date	Filing Date	Title
EP89104023A EP0386289A1 (de)	1989-03-07	1989-03-07	Rekombinanter Interleukin-2-Rezeptor
EP89109656A EP0386304A1 (de)	1989-03-07	1989-05-29	Rekombinanter Interleukin-2-Rezeptor
EP89113310A EP0408790A1 (de)	1989-07-20	1989-07-20	Rekombinanter Proteinrezeptor

Publications (2)

Publication Number	Publication Date
IL93660A0 IL93660A0 (en)	1990-12-23
IL93660A true IL93660A (en)	2001-11-25

Family

ID=27232332

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
IL9366090A IL93660A (en)	1989-03-07	1990-03-06	DNA that encodes the b-chain of a 2 IL receptor, prepares it and coordinates stores that contain it

Country Status (16)

Country	Link
US (1)	US5198359A (de)
EP (1)	EP0395853B1 (de)
JP (1)	JP3339855B2 (de)
AT (1)	ATE166921T1 (de)
AU (1)	AU639226B2 (de)
CA (1)	CA2011450C (de)
DE (1)	DE69032357T2 (de)
DK (1)	DK0395853T3 (de)
ES (1)	ES2117623T3 (de)
FI (1)	FI104188B1 (de)
HU (1)	HUT57827A (de)
IE (1)	IE81125B1 (de)
IL (1)	IL93660A (de)
NO (1)	NO306624B1 (de)
NZ (1)	NZ232832A (de)
PT (1)	PT93345B (de)

Families Citing this family (24)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CA1341588C (en) *	1988-01-26	2009-01-06	Michel Revel	Human ifn-beta2/i1-6, its purification and use
US20040049014A1 (en) *	1988-12-28	2004-03-11	Protein Design Labs, Inc.	Humanized immunoglobulins
US5530101A (en)	1988-12-28	1996-06-25	Protein Design Labs, Inc.	Humanized immunoglobulins
US6552170B1 (en)	1990-04-06	2003-04-22	Amgen Inc.	PEGylation reagents and compounds formed therewith
JP3024311B2 (ja) *	1991-10-03	2000-03-21	味の素株式会社	Ｉｌ−２受容体重鎖に結合するポリペプチド
US5776755A (en) *	1992-10-09	1998-07-07	Helsinki University Licensing, Ltd.	FLT4, a receptor tyrosine kinase
US6107046A (en) *	1992-10-09	2000-08-22	Orion Corporation	Antibodies to Flt4, a receptor tyrosine kinase and uses thereof
US6824777B1 (en)	1992-10-09	2004-11-30	Licentia Ltd.	Flt4 (VEGFR-3) as a target for tumor imaging and anti-tumor therapy
US5536657A (en) *	1993-07-19	1996-07-16	Hoffmann-La Roche Inc.	Recombinant DNA encoding human receptor for interleukin-12
US6074642A (en)	1994-05-02	2000-06-13	Alexion Pharmaceuticals, Inc.	Use of antibodies specific to human complement component C5 for the treatment of glomerulonephritis
US5650295A (en) *	1995-06-02	1997-07-22	Human Genone Sciences, Inc.	Macrophage migration inhibitory factor-3
US5635597A (en) *	1994-05-27	1997-06-03	Affymax Technologies, N.V.	Peptides that bind IL-2 receptors
US6297028B1 (en) *	1995-01-09	2001-10-02	Boehringer Ingelheim International Gmbh	IL-2R-associated polypeptide and DNA molecules coding therefor
TW555765B (en)	1996-07-09	2003-10-01	Amgen Inc	Low molecular weight soluble tumor necrosis factor type-I and type-II proteins
ATE489108T1 (de) *	1998-10-09	2010-12-15	Vegenics Ltd	Flt4 (vegfr-3) als ziel für tumornachweis (imaging) und antitumortherapie
US6660843B1 (en)	1998-10-23	2003-12-09	Amgen Inc.	Modified peptides as therapeutic agents
EP1230368A2 (de) *	1999-11-18	2002-08-14	Schering Corporation	Rezeptorproteine aus säugetieren; verwandte reagenzien und verfahren
CA2435503C (en) *	2001-01-19	2011-02-22	Ludwig Institute For Cancer Research	Flt4(vegfr-3) as a target for tumor imaging and anti-tumor therapy
US7175988B2 (en) *	2001-02-09	2007-02-13	Human Genome Sciences, Inc.	Human G-protein Chemokine Receptor (CCR5) HDGNR10
EP1251531B1 (de)	2001-04-20	2010-10-27	Yazaki Corporation	Ausschaltvorrichtung
US20060147945A1 (en) *	2005-01-06	2006-07-06	Edmonds Brian T	Novel secreted proteins and their uses
US20080283557A1 (en) *	2007-05-17	2008-11-20	Julianne Desautels	Spout for food stuff container
US20100298163A1 (en) *	2008-01-04	2010-11-25	The Royal Institution For The Advancement Of Learning/Mcgill University	Microfluidic microarray system and method for the multiplexed analysis of biomolecules
WO2021113577A1 (en) *	2019-12-05	2021-06-10	Immune Targeting Inc.	Interleukin 15 fusion proteins and prodrugs, and compositions and methods thereof

Family Cites Families (3)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CA1339269C (en) *	1984-05-21	1997-08-12	Douglas P. Cerretti	Purification of and cloning of the gene for interleukin-2 receptor
US4707443A (en) *	1985-04-19	1987-11-17	The United States Of America As Represented By The Secretary Of The Department Of Health And Human Services	Soluble interleukin-2 receptor as a disease indicator and a method of assaying the same
AU1992388A (en) *	1987-06-29	1989-01-30	United States of America, as represented by the Secretary, U.S. Department of Commerce, The	Novel interleukin-2 receptor and applications thereof

1990
- 1990-03-05 CA CA002011450A patent/CA2011450C/en not_active Expired - Lifetime
- 1990-03-05 US US07/487,059 patent/US5198359A/en not_active Expired - Lifetime
- 1990-03-06 AT AT90104246T patent/ATE166921T1/de not_active IP Right Cessation
- 1990-03-06 EP EP90104246A patent/EP0395853B1/de not_active Expired - Lifetime
- 1990-03-06 DK DK90104246T patent/DK0395853T3/da active
- 1990-03-06 ES ES90104246T patent/ES2117623T3/es not_active Expired - Lifetime
- 1990-03-06 FI FI901124A patent/FI104188B1/fi active IP Right Grant
- 1990-03-06 AU AU50726/90A patent/AU639226B2/en not_active Expired
- 1990-03-06 JP JP05483190A patent/JP3339855B2/ja not_active Expired - Lifetime
- 1990-03-06 HU HU901326A patent/HUT57827A/hu unknown
- 1990-03-06 DE DE69032357T patent/DE69032357T2/de not_active Expired - Lifetime
- 1990-03-06 NO NO901046A patent/NO306624B1/no not_active IP Right Cessation
- 1990-03-06 IL IL9366090A patent/IL93660A/en not_active IP Right Cessation
- 1990-03-06 IE IE79390A patent/IE81125B1/en not_active IP Right Cessation
- 1990-03-06 PT PT93345A patent/PT93345B/pt not_active IP Right Cessation
- 1990-03-07 NZ NZ232832A patent/NZ232832A/xx unknown

Also Published As

Publication number	Publication date
NZ232832A (en)	1991-11-26
NO901046D0 (no)	1990-03-06
PT93345B (pt)	1996-02-29
AU639226B2 (en)	1993-07-22
JP3339855B2 (ja)	2002-10-28
FI901124A0 (fi)	1990-03-06
FI104188B (fi)	1999-11-30
ATE166921T1 (de)	1998-06-15
IE81125B1 (en)	2000-03-22
NO306624B1 (no)	1999-11-29
EP0395853A1 (de)	1990-11-07
IL93660A0 (en)	1990-12-23
EP0395853B1 (de)	1998-06-03
DK0395853T3 (da)	1999-02-15
ES2117623T3 (es)	1998-08-16
CA2011450A1 (en)	1990-09-07
HUT57827A (en)	1991-12-30
DE69032357D1 (de)	1998-07-09
US5198359A (en)	1993-03-30
FI104188B1 (fi)	1999-11-30
JPH0367588A (ja)	1991-03-22
AU5072690A (en)	1990-09-13
DE69032357T2 (de)	1998-10-29
IE900793L (en)	1990-09-07
HU901326D0 (en)	1990-05-28
NO901046L (no)	1990-09-10
PT93345A (pt)	1990-11-07
CA2011450C (en)	2002-06-04

Legal Events

Date	Code	Title
2002-09-12	KB	Patent renewed
2004-06-01	KB	Patent renewed
2008-04-13	KB	Patent renewed
2010-12-30	EXP	Patent expired

Publication	Publication Date	Title
EP0395853B1 (de)	1998-06-03	Rekombinanter Interleukin-2-Rezeptor
Hatakeyama et al.	1989	Interleukin-2 receptor β chain gene: generation of three receptor forms by cloned human α and β chain cDNA's
Takatsu	1992	Interleukin-5
Fukunaga et al.	1993	Growth and differentiation signals mediated by different regions in the cytoplasmic domain of granulocyte colony-stimulating factor receptor
EP0760857B9 (de)	2006-09-06	Onkostatin- m rezeptor
US5912172A (en)	1999-06-15	Endowing lymphocytes with antibody specificity
CA2345109C (en)	2012-12-18	Receptor based antagonists and methods of making and using
EP0475746B1 (de)	2000-07-12	Menschlicher und Murin-Interleukin-5-Rezeptor
EP0693084A4 (de)	1999-06-02	Chimäre cytokinrezeptoren in lymphozyten
WO1990008822A1 (en)	1990-08-09	Erythropoietin receptor
Bamford et al.	1996	IL‐15: the role of translational regulation in their expression
JP2002514079A (ja)	2002-05-14	キメラｏｐｇポリペプチド
WO2022179545A1 (zh)	2022-09-01	针对cd19和cd22的双靶点star
US7008781B1 (en)	2006-03-07	Method of enhancing the biological activity of ligands
US20090010872A1 (en)	2009-01-08	Chimeric soluble hyper il-11 and use thereof
Mori et al.	1991	Signal transduction by interleukin 2 receptor β chain: importance of the structural integrity as revealed by site-directed mutagenesis and generation of chimeric receptors
EP0386289A1 (de)	1990-09-12	Rekombinanter Interleukin-2-Rezeptor
KR0172123B1 (ko)	1999-02-01	재조합 단백질 수용체
EP0408790A1 (de)	1991-01-23	Rekombinanter Proteinrezeptor
US7083949B2 (en)	2006-08-01	Receptor based antagonists and methods of making and using
Taniguchi et al.	1989	Interleukin-2 Receptor β Chain: Molecular Cloning and Functional Expression of the Human cDNA
Muto et al.	1995	CYTOPLASMIC DOMAIN OF THE ß SUBUNIT BUT NOT THE o SUBUNIT
森寿	1991	Signal transduction by interleukin 2 receptor β