WO2000068376B1 - Novel chimpanzee erythropoietin (chepo) polypeptides and nucleic acids encoding the same - Google Patents
Novel chimpanzee erythropoietin (chepo) polypeptides and nucleic acids encoding the sameInfo
- Publication number
- WO2000068376B1 WO2000068376B1 PCT/US2000/012370 US0012370W WO0068376B1 WO 2000068376 B1 WO2000068376 B1 WO 2000068376B1 US 0012370 W US0012370 W US 0012370W WO 0068376 B1 WO0068376 B1 WO 0068376B1
- Authority
- WO
- WIPO (PCT)
- Prior art keywords
- seq
- tfrklfrvysnflrgklklytgeacrtgdr
- amino acid
- polypeptide
- sequence
- Prior art date
- Legal status (The legal status 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 status listed.)
- Ceased
Links
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
- C07K14/475—Growth factors; Growth regulators
- C07K14/505—Erythropoietin [EPO]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/06—Antianaemics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K48/00—Medicinal preparations containing genetic material which is inserted into cells of the living body to treat genetic diseases; Gene therapy
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Toxicology (AREA)
- Hematology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Diabetes (AREA)
- Pharmacology & Pharmacy (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Animal Behavior & Ethology (AREA)
- Engineering & Computer Science (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
The present invention is directed to novel chimpanzee erythropoietin polypeptides and to nucleic acid molecules encoding those polypeptides. Also provided herein are vectors and host cells comprising those nucleic acid sequences, chimeric polypeptide molecules comprising the polypeptides of the present invention fused to heterologous polypeptide sequences, antibodies which bind to the polypeptides of the present invention and to methods for producing the polypeptides of the present invention.
Claims
AMENDED CLAIMS
[received by the International Bureau on 7 November 2000 (07.11.00); original claims 2-4 and 34 amended; original claims 1, 5-8, 16, 18-21 and 28-33 cancelled; new claims 39-42 added; remaining claims unchanged (5 pages)]
2. An isolated nucleic acid molecule comprising nucleotides 1 or about 82 to about 579 of Figure 2 (SEQ
ID N0:3).
3. An isolated nucleic acid molecule comprising the nucleotide sequence of Figure 2 (SEQ ID N0:3).
4. An isolated nucleic acid molecule comprising a nuclεotide sequence that encodes the sequence of amino acid residues from about 1 or about 26 to about 193 of Figure 2 (SEQ ID N0:2).
9. A vector comprising the nucleic acid molecule of any one of Claims 2, 3, 4, 9 or 42.
10. The vector of Claim 9, wherein said nucleic acid molecule is operablγ linked to control sequences recognized by a host cell transformed with the vector.
1 1. A host cell comprising the vector of Claim 9.
12. The host ceil of Claim 11, wherein said cell is a CHO cell.
1 . The host cell of Claim 11 , wherein said ceil is an £ coli.
14. The host cell αf Claim 11, wherein said cell is a yeast cell.
15. A process or producing a polypeptide comprising cuituring the host cell of Claim 11 under conditions suitable for expression of said polypeptide and recovering said polypeptide from the cell culture.
17. An isolated polypeptide comprising amino acid residues 1 or about 28 to about 193 of Figure 2 (SEQ ID N0:2).
22. A chimeric molecule comprising the polypeptide of any one of Claims 17, 40 or 41 fused to a heterologous amino acid sequence.
23. The chimeric molecule of Claim 22, wherein said heterologous amino acid sequence is an epitope tag sequence.
24. The chimeric molecule of Claim 22, wherein said heterologous amino acid sequence is a Fc region of an irπrπuπoglobulin.
98
25. An antibody which specifically binds to the polypeptide of any one of Claims 17, Q or 41.
26. The antibody of Claim 24, wherein said antibody is a monoclonal antibody.
27. The antibody of Claim 24, wherein said antibody is a humanized antibody.
34. A polypeptide comprising an amino acid sequence selected from the group consisting of:
(1) APPRLICDSRVL£RY> KEAENiπGCAEHCSLNENrτVPDTW^ NSSWWEPLlTljWDKAVSGLRSLmLRALGAM
GDR (SEQ ID NO: 18);
(2) APPRLICDSRVLERYLLEAKEAENiπGCAEHCSu ENITVPDTKVNFYAW RNXSXQQAVEVWQG LLSEAVLRGQALLV NSSDPWEPLQLHVD AVSGLRSLπLLRALGAKKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRGKL LYTGEACRT GDR (SEQ ID NO: 19); (3) APPRLlCDSRVLERYLL EAENrπGCAEHCSLNENITvPD™
NSSQPWEPLQLHVDKAVSGLRSLπLLRALGAQ EAISPPDAASAAPLRTITAmTRKLFRVYSNFLRG L LYTGEACRT GDR {SEQ ID NQ:2Q);
(4) APPRLICDSRVLERYLLEAKEAENiπGCAEHCSLNENlTVPDTKVNFYAW RNXTXQl^VEVWQGl^ SEAVLRGriALLV NSSQPWEPLQLHVDKAVSGIΛSLπLLRALGAKKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRG LKLYTGEACRT GDR (SEQ ID N0:21);
(5) APPRUCDSRVlIRY KEAENrπGCAEHCSLNENr^ VNSSQP EPLQLHVDKAVSGLRSLπLLRALGAQKEAISPPDAASAAPLRTlTADTFRKLFRVYSNFLRGKLKLπGEACR TGDR (SEQ ID I\I0:22);
(6) APPHUCDSRiilERYllEAKEAENiTTGCAEM^ VNSSQPWEPLQLHVDKAVSGLRSLπLLRALGA KEAlSPPDAASAAPLRTlTADTFRKLFRVYSrJFLRGKLKLYTGEACR
TGDR (SEQ ID N0:23); (7| APPRLICDSRVLERYLLEAKEAENiπGCAEHCSLNENITVPDTKVNFYAWKR NXTXωVEVWQGLALLSEAVLRGQALL
VNSSrjTWEPLQLHVDKAVSGLRSLπLLRALGAK EAlSPPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACR
TGDR (SEQ ID N0:25); (S) APPRLICDSRVLERYUEAKEAENiπGCAEHCSLNENiWD ^
VNSSQPWEPLQLHVDKAVSGLRSLπLLRALGAQKEAISPPDAASAAPLRTlTADTFRKLFRVYSNFLRGKLKLYTGEACR
TGDR (SEQ ID l\IO:26); (9) APPRLICDSRVLERYLLEAKEAENiπGCAEHCSLNENITVPDT VNFYA KR ENXSXAVEVWQGLALLSEAVLRGQALL
VNSSiOPWEPLQLHVDKAVSGlΛSLT RALGAKKEAISPPDAASAAPl^TITADTFRKLFRnSNrlRGKLKLYTGEACR TGDR (SEQ ID rJ0 7);
99
do) APPRLICDSRVLERYLLEA EAENΓΓTGCAEHCSLNENITVPD
VNSSuTWEPLrjlHVD AVSGi TTLi GAQ TGDR (SEQ ID N0:2B);
(11) APPRLICDSRVLERYLLEAKEAENiπGCAEHCSl-NENlTVPDTKVNFYAWKRMENXTXAVEvmGULL VNSSQPWEPLQLHVDKAVSGLRSLπLLRALGA KEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACR
TGDR (SEQ ID N0:29);
( 12) APPRLICDSRVLIRYLLEAKEAENiπGCAEHCSLNENITVPDTKVNFYAWKRMEVNXSXVEVWQG WL1SEAVLRGQA V NSSr WEPLQIHVDKAVSGLRSLnLLRALGAriKEAISPPnAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRT GDR (SEQ ID NQ:30); (13) APPRLICDSRVLERYLLEAKEAENIHGCAEHCSilj ENI PDTKVNFYAWKRMEVI^SXVEVWQGLAllSEAVLRGQALLV NSSfJ WEPLQLHVDKAVSG SLπLLRALGAKKEAISPPDAASAAPLRmADTFRKLFRVYSNFLRGKLKLYTGEACRT GDR (SEQ ID PJQ:31); and (14) APPRLICDSRVLERYLLEAKEA£NiπGCAEHCSU\IENITVPDT
NSSQPWEPLQLHVDKAVSGLRSLπLLRALGAKKEAISPPDAASAAPLRTITADTFRKLFRVYSNFLRG L LYTGEACRT GDR (SEQ ID NQ:33), wherein X is any amino acid except for proline,
35. The polypeptide according to Claim 34, which comprises an amino acid sequence selected from the group consisting of:
(1) MGVHECPAWLWLllSllSLPLGLPVLGAPPRUCDSRVLERYLLEAKEAENiπGCAEHCSLNENITVPDTKVN AWKRNX SXQriAVEWOGUlLLSEAV Gi ALLVNSSQP EPLQLHVOKAVSGLRSLnLLRALGAQKEAISPPDAASAAPI JTrrAD
TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID N0:34);
(2) GVHECPAWL LLLS SLPLGLPVLGAPPRUCDSRVLERYLLEAKEAENiπGCAEHCSLNENIWPDTKVNi^AW RNX SXQQAVEVWQGLALLSEAV RGQALLVNSSQPWEPLfii IVDKAVSGLRSLTULRALGAK EAISPPDAASMPLRTITAD TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID ND:35); (3) MGVHECPAWLWLUSLLSlJLGLPVLGAPPRLICDSRVLERYLLEAKEAENiπGCAEHCSLNENITVPDTKVNrΥAWKRNX
TXQQAVEVWQGiLALLSEAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLπLLRALGAQKEAISPPDAASAAPLRTITAD TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID N0:36); (4| GVHECPAWLWLLLSLLSLPLGLPVLGAPPRLICDSRVLERYLLEAKEAENITTGCAEHCSLNENITVPDTKVNFYAWKRNX
TXQQAVEVWQGLALLSEAVLRGQAI VNSSQPWEPLflLHVDKAVSGLRSLπLLRALGAKKEAISPPDAASAAPLRTrrAD TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID N0:37);
(5) MGVHECPAWLWLLLSLLSLPLGLPVLGAPPRLICDSRVLERYLLEAKEAENITTGCAEHCSLNENiπPDTKVNFYAWKRMN XSXQAVEVWQGULLSEAVLRGQALLVNSSQPWEPL LHVDKAVSGLRSLπLLRALGAQKEAISPPDAASAAPLRTITAD TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID N0:38);
(6) MGVHECPAWLWLLLSLLSLPLGLPVLGAPPRLICDSRVLERYLIiAKEAENiπGCAEHCSLNENITVPDTKVNFYAWKRMN XSXWVETOQGLALLSEAV GClALLVNSSi PWEPLu HVDKAVSGLRSLπL ALGAKKEAISPPDAASAAPLRTITAD
TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID N0:39);
100
(7) MGVHECPA LWLllSLLSLPLGlJ^VLGAPPRLICDSRVLERYLl-EAKEAENiπGCAEHCSLNENITVPDTKVNFYAWKRMN
XTXMVEVWQGLALLSEAVLRGij VNSSQPWEPLαW
TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID N0:4Q); (θ) MGVHECPAWL LLLSLLSI-PLGIfVLGAPPRLICDSRVlJ RYLLEAKEAENiπGCAEHCSLi NENrrVPDTIWNFYAWKR XTXWVEVWQG LLSEAVLRGMLLVNSSQP EPLQLHVDKAVSGLRSLπLLRALGAKKEAISPPDAASAAPLRTITAD
TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID N0:41); (9) MGVHECPAWLWU -SLLSIJLGLPVLGAPPRLICDSRVLERYLLEAKEAENiπGCAEHCSLNENITVPDTKVNFYA KRME
NXSXAVEVWQGLALLSEAVLRGQALLVNSSQP EPLQLHVDKAVSGLRSLTTLLRALGAQKEAISPPDAASAAPLRTITAD
TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID ND:42); (10) MGVHECPAWLWLLLSLLSLPLGLPVLGAPPRLICDSRVLERYLLEAKEAENiπGCAEHCSLNENITVPDTKVNFYAWKRME
NXSXAVEVWQGLALLSEAVLRGQALLVNSSQP EPLQLHVDKAVSGLRSLπLLRALGAKKEAISPPDAASAAPLRTITAD
TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID N0;43);
(11) MGVHECPAWLWllLSLLSLPLGLPVLGAPPRLICDSRVLERYLLEAKEAENiπGCAEHCSLNENITVPDTKVNFYAWKRME NXTXAVEVWQG LLSEAVLRGMLLVNSSriPWEPLQLHVDKAVSGLRSLπLLRALGAQKEAISPPDAASAAPLRτiTAD TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID N0:44);
(12) GVHECPAWLWIlLSLI^LPLGLPVLGAPPRLICDSRVIiRYLLEAKEAENiπGCAEHCSLNENITVPDTKVNFYAWKRME NXTXAVEVWQGLALLSEAVLRGQALLVNSSrj WEPLQLHVDKAVSGLRSLTTLLRALGAKKEAISPPDAASAAPLRTITAD TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID NQ:45);
(13) MGVHECPAWLWllLSLI^LPLGLPVLGAPPRLICDSRVLERYLLEAKEAENinGCAEHCSLNENITVPDTKVNFYAWKRiME VNXSXVEVWQG LLSEAVLRGOAllVNSSQPWEPLrjLHVDKAVSG SLπLLRALGAQKEAISPPDAASAAPLRTITAD
TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID N0:46);
( 14) MGVHECPAWLWLLLSLLSLPLGLPVLGAPPRLICDSRVLERYLLEAKEAENiπGCAEHCSLNENITVPDTKVNFYAWKRME VNXSXVEVWQGLALLSEAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAKKEAISPPDAASAAPLRTiTAD TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID N0;47); (15) MGVHECPAWLWLLLSLLSLPLGLPVLGAPPRUCDSRVLERYLLEAKEAENIHGC AEHCSLNENrrVPDTKVNFYAWKR E
VNXTXVi VWQGULI^EAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAISPPDAASAAPLRTITAD
TFRKLFRVYSNFLRGKLKLYTGEACRTGDR (SEQ ID N0:48); and
(16) MGVHECPAWL LLLSLLSLPLGLPVLGAPPRLICDSRVLERYLLEAKEAENiπGCAEHCSLNENITVPDTKVNFYA KRME
VNXTXVEVWQG LLSEAVLRGQALLVNSSQPWEPLQLHVDKAVSGLRSLπLLRALGAKKEAISPPDAASAAPLRTITAD TFRKLFRVYSNFLR GKLKLYTGEACRTGDR (SEQ ID N0:49), wherein X is any amino acid except for proiine.
36. A chimeric molecule comprising a polypeptide of Claim 34 or 35 fused to a heterologous amino acid sequence.
37. The chimeric molecule of Claim 36, wherein said heterologous amino acid sequence is an epitope tag sequence.
101
AMENDED.SHEET (ARTICLE 19)
38. The chimeric molecule of Claim 36, wherein said heterologous amino acid sequence is a Fc region of an immunoglobulin.
39. An isolated nucleic acid molecule consisting of the nucleotide sequence of Figure 2 (SEQ ID NQ:3).
40. An isolated polypeptide consisting of amino acid residues 1 or about 28 to about 1 3 of Figure 2 (SEQ ID N0:2).
41. An isolated polypeptide encoded by nucleotides 1 or about 82 to about 579 of Figure 2 (SEQ ID NQ:3).
42. An isolated nudeic acid molecule comprising a nudeic add sequence that encodes the chimeric molecule of any one of Claims 22, 23, 24, 36, 7 or 38.
102
Priority Applications (7)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| KR10-2001-7014133A KR100524041B1 (en) | 1999-05-07 | 2000-05-05 | Novel Chimpanzee Erythropoietin (CHEPO) Polypeptides and Nucleic Acids Encoding the Same |
| IL14578500A IL145785A0 (en) | 1999-05-07 | 2000-05-05 | Novel chimpanzee erythropoietin (chepo) polypeptides and nucleic acids encoding the same |
| MXPA01011264A MXPA01011264A (en) | 1999-05-07 | 2000-05-05 | Novel chimpanzee erythropoietin (chepo) polypeptides and nucleic acids encoding the same. |
| AU47047/00A AU766507B2 (en) | 1999-05-07 | 2000-05-05 | Novel chimpanzee erythropoietin (CHEPO) polypeptides and nucleic acids encoding the same |
| CA002369605A CA2369605A1 (en) | 1999-05-07 | 2000-05-05 | Novel chimpanzee erythropoietin (chepo) polypeptides and nucleic acids encoding the same |
| EP00928879A EP1177285A1 (en) | 1999-05-07 | 2000-05-05 | Chimpanzee erythropoietin (chepo) polypeptides and nucleic acids encoding the same |
| JP2000616342A JP3660880B2 (en) | 1999-05-07 | 2000-05-05 | Novel chimpanzee erythropoietin (CHEPO) polypeptide and nucleic acid encoding the same |
Applications Claiming Priority (6)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US28759400P | 1999-05-07 | 1999-05-07 | |
| US30730799A | 1999-05-07 | 1999-05-07 | |
| US09/307,307 | 1999-05-07 | ||
| US60/287,594 | 2000-03-28 | ||
| US09/552,265 US6555343B1 (en) | 1999-05-07 | 2000-04-19 | Chimpanzee erythropoietin (CHEPO) polypeptides and nucleic acids encoding the same |
| US09/552,265 | 2000-04-19 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| WO2000068376A1 WO2000068376A1 (en) | 2000-11-16 |
| WO2000068376B1 true WO2000068376B1 (en) | 2001-02-15 |
| WO2000068376A8 WO2000068376A8 (en) | 2002-02-07 |
Family
ID=27403728
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| PCT/US2000/012370 Ceased WO2000068376A1 (en) | 1999-05-07 | 2000-05-05 | Novel chimpanzee erythropoietin (chepo) polypeptides and nucleic acids encoding the same |
Country Status (6)
| Country | Link |
|---|---|
| EP (1) | EP1177285A1 (en) |
| JP (1) | JP3660880B2 (en) |
| AU (1) | AU766507B2 (en) |
| IL (1) | IL145785A0 (en) |
| MX (1) | MXPA01011264A (en) |
| WO (1) | WO2000068376A1 (en) |
Cited By (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6838260B2 (en) | 1997-12-08 | 2005-01-04 | Emd Lexigen Research Center Corp. | Heterodimeric fusion proteins useful for targeted immune therapy and general immune stimulation |
| US6969517B2 (en) | 2001-05-03 | 2005-11-29 | Emd Lexigen Research Center Corp. | Recombinant tumor specific antibody and use thereof |
| US6992174B2 (en) | 2001-03-30 | 2006-01-31 | Emd Lexigen Research Center Corp. | Reducing the immunogenicity of fusion proteins |
| US7067110B1 (en) | 1999-07-21 | 2006-06-27 | Emd Lexigen Research Center Corp. | Fc fusion proteins for enhancing the immunogenicity of protein and peptide antigens |
| US7091321B2 (en) | 2000-02-11 | 2006-08-15 | Emd Lexigen Research Center Corp. | Enhancing the circulating half-life of antibody-based fusion proteins |
| US7141651B2 (en) | 1999-08-09 | 2006-11-28 | Emd Lexigen Research Center Corp. | Multiple cytokine protein complexes |
| US7148321B2 (en) | 2001-03-07 | 2006-12-12 | Emd Lexigen Research Center Corp. | Expression technology for proteins containing a hybrid isotype antibody moiety |
| US7169904B2 (en) | 2002-12-17 | 2007-01-30 | Emd Lexigen Research Center Corp. | Immunocytokine sequences and uses thereof |
| US7186804B2 (en) | 2001-12-04 | 2007-03-06 | Emd Lexigen Research Center Corp. | IL-2 fusion proteins with modulated selectivity |
| US7211253B1 (en) | 1999-11-12 | 2007-05-01 | Merck Patentgesellschaft Mit Beschrankter Haftung | Erythropoietin forms with improved properties |
| US7465447B2 (en) | 2003-12-31 | 2008-12-16 | Merck Patent Gmbh | Fc-erythropoietin fusion protein with improved pharmacokinetics |
| US7517526B2 (en) | 2000-06-29 | 2009-04-14 | Merck Patent Gmbh | Enhancement of antibody-cytokine fusion protein mediated immune responses by combined treatment with immunocytokine uptake enhancing agents |
Families Citing this family (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6831060B2 (en) * | 1999-05-07 | 2004-12-14 | Genentech, Inc. | Chimpanzee erythropoietin (CHEPO) polypeptides and nucleic acids encoding the same |
| DE60232870D1 (en) * | 2001-04-04 | 2009-08-20 | Genodyssee | NEW POLYNUCLEOTIDES AND POLYPEPTIDES OF ERYTHROPOIETING |
| CA2521273A1 (en) * | 2003-04-02 | 2004-10-21 | Epimmune Inc. | Peptides, polypeptides, and proteins of reduced immunogenicity and methods for their production |
Family Cites Families (9)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| NZ210501A (en) * | 1983-12-13 | 1991-08-27 | Kirin Amgen Inc | Erythropoietin produced by procaryotic or eucaryotic expression of an exogenous dna sequence |
| DE3924746A1 (en) * | 1989-07-26 | 1991-01-31 | Behringwerke Ag | ERTHROPOIETIN (EPO) PEPTIDES AND ANTIBODIES THEREFOR |
| DK0464533T3 (en) * | 1990-06-28 | 1999-04-26 | Gen Hospital Corp | Fusion proteins with immunoglobulin moieties, their preparation and use |
| WO1994024160A2 (en) * | 1993-04-21 | 1994-10-27 | Brigham And Women's Hospital | Erythropoietin muteins with enhanced activity |
| ZA946122B (en) * | 1993-08-17 | 1995-03-20 | Amgen Inc | Erythropoietin analogs |
| WO1995013376A1 (en) * | 1993-11-10 | 1995-05-18 | Amgen Inc. | Gene therapy vector for the treatment of low or defective red blood cell production |
| GB9511935D0 (en) * | 1995-06-13 | 1995-08-09 | Smithkline Beecham Plc | Novel compound |
| WO1999002709A1 (en) * | 1997-07-10 | 1999-01-21 | Beth Israel Deaconess Medical Center | Recombinant erythropoietin / immunoglobulin fusion proteins |
| JP4809977B2 (en) * | 1998-10-23 | 2011-11-09 | アムジエン・インコーポレーテツド | Methods and compositions for the prevention and treatment of anemia |
-
2000
- 2000-05-05 MX MXPA01011264A patent/MXPA01011264A/en active IP Right Grant
- 2000-05-05 IL IL14578500A patent/IL145785A0/en unknown
- 2000-05-05 AU AU47047/00A patent/AU766507B2/en not_active Ceased
- 2000-05-05 WO PCT/US2000/012370 patent/WO2000068376A1/en not_active Ceased
- 2000-05-05 JP JP2000616342A patent/JP3660880B2/en not_active Expired - Fee Related
- 2000-05-05 EP EP00928879A patent/EP1177285A1/en not_active Withdrawn
Cited By (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6838260B2 (en) | 1997-12-08 | 2005-01-04 | Emd Lexigen Research Center Corp. | Heterodimeric fusion proteins useful for targeted immune therapy and general immune stimulation |
| US7576193B2 (en) | 1997-12-08 | 2009-08-18 | Merck Patent Gmbh | Heterodimeric fusion proteins useful for targeted immune therapy and general immune stimulation |
| US7226998B2 (en) | 1997-12-08 | 2007-06-05 | Emd Lexigen Research Center Corp. | Heterodimeric fusion proteins useful for targeted immune therapy and general immune stimulation |
| US7067110B1 (en) | 1999-07-21 | 2006-06-27 | Emd Lexigen Research Center Corp. | Fc fusion proteins for enhancing the immunogenicity of protein and peptide antigens |
| US7582288B2 (en) | 1999-08-09 | 2009-09-01 | Merck Patent Gmbh | Methods of targeting multiple cytokines |
| US7141651B2 (en) | 1999-08-09 | 2006-11-28 | Emd Lexigen Research Center Corp. | Multiple cytokine protein complexes |
| US7211253B1 (en) | 1999-11-12 | 2007-05-01 | Merck Patentgesellschaft Mit Beschrankter Haftung | Erythropoietin forms with improved properties |
| US7091321B2 (en) | 2000-02-11 | 2006-08-15 | Emd Lexigen Research Center Corp. | Enhancing the circulating half-life of antibody-based fusion proteins |
| US7507406B2 (en) | 2000-02-11 | 2009-03-24 | Emd Serono Research Center, Inc. | Enhancing the circulating half-life of antibody-based fusion proteins |
| US7517526B2 (en) | 2000-06-29 | 2009-04-14 | Merck Patent Gmbh | Enhancement of antibody-cytokine fusion protein mediated immune responses by combined treatment with immunocytokine uptake enhancing agents |
| US7148321B2 (en) | 2001-03-07 | 2006-12-12 | Emd Lexigen Research Center Corp. | Expression technology for proteins containing a hybrid isotype antibody moiety |
| US7601814B2 (en) | 2001-03-30 | 2009-10-13 | Merck Patent Gmbh | Reducing the immunogenicity of fusion proteins |
| US6992174B2 (en) | 2001-03-30 | 2006-01-31 | Emd Lexigen Research Center Corp. | Reducing the immunogenicity of fusion proteins |
| US7459538B2 (en) | 2001-05-03 | 2008-12-02 | Merck Patent Gmbh | Recombinant tumor specific antibody and use thereof |
| US6969517B2 (en) | 2001-05-03 | 2005-11-29 | Emd Lexigen Research Center Corp. | Recombinant tumor specific antibody and use thereof |
| US7186804B2 (en) | 2001-12-04 | 2007-03-06 | Emd Lexigen Research Center Corp. | IL-2 fusion proteins with modulated selectivity |
| US7462350B2 (en) | 2001-12-04 | 2008-12-09 | Emd Serono Research Center, Inc. | Cancer treatments including administering IL-2 fusion proteins with modulated selectivity |
| US7169904B2 (en) | 2002-12-17 | 2007-01-30 | Emd Lexigen Research Center Corp. | Immunocytokine sequences and uses thereof |
| US7465447B2 (en) | 2003-12-31 | 2008-12-16 | Merck Patent Gmbh | Fc-erythropoietin fusion protein with improved pharmacokinetics |
Also Published As
| Publication number | Publication date |
|---|---|
| WO2000068376A1 (en) | 2000-11-16 |
| AU4704700A (en) | 2000-11-21 |
| JP3660880B2 (en) | 2005-06-15 |
| AU766507B2 (en) | 2003-10-16 |
| EP1177285A1 (en) | 2002-02-06 |
| JP2002543784A (en) | 2002-12-24 |
| IL145785A0 (en) | 2002-07-25 |
| MXPA01011264A (en) | 2002-07-02 |
| WO2000068376A8 (en) | 2002-02-07 |
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