AU613022B2 - Bifunctional proteins - Google Patents
Bifunctional proteins Download PDFInfo
- Publication number
- AU613022B2 AU613022B2 AU14661/88A AU1466188A AU613022B2 AU 613022 B2 AU613022 B2 AU 613022B2 AU 14661/88 A AU14661/88 A AU 14661/88A AU 1466188 A AU1466188 A AU 1466188A AU 613022 B2 AU613022 B2 AU 613022B2
- Authority
- AU
- Australia
- Prior art keywords
- protein
- asp
- thr
- pro
- constituent
- 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
- 108090000623 proteins and genes Proteins 0.000 title claims description 38
- 102000004169 proteins and genes Human genes 0.000 title claims description 35
- 230000001588 bifunctional effect Effects 0.000 title claims description 16
- 102100020873 Interleukin-2 Human genes 0.000 claims description 23
- 108010002350 Interleukin-2 Proteins 0.000 claims description 23
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 claims description 17
- 150000001413 amino acids Chemical class 0.000 claims description 14
- 239000000470 constituent Substances 0.000 claims description 14
- 210000004027 cell Anatomy 0.000 claims description 8
- 238000002360 preparation method Methods 0.000 claims description 7
- 239000003814 drug Substances 0.000 claims description 4
- 238000000034 method Methods 0.000 claims description 4
- GRIUMVXCJDKVPI-IZPVPAKOSA-N Thr-Thr-Tyr Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=C(O)C=C1)C(O)=O GRIUMVXCJDKVPI-IZPVPAKOSA-N 0.000 claims description 3
- 108010093581 aspartyl-proline Proteins 0.000 claims description 3
- WXERCAHAIKMTKX-ZLUOBGJFSA-N Ala-Asp-Asp Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O WXERCAHAIKMTKX-ZLUOBGJFSA-N 0.000 claims description 2
- 206010028980 Neoplasm Diseases 0.000 claims description 2
- ZJXXCGZFYQQETF-CYDGBPFRSA-N Pro-Met-Ile Chemical compound CC[C@H](C)[C@@H](C(=O)O)NC(=O)[C@H](CCSC)NC(=O)[C@@H]1CCCN1 ZJXXCGZFYQQETF-CYDGBPFRSA-N 0.000 claims description 2
- NADLKBTYNKUJEP-KATARQTJSA-N Ser-Thr-Leu Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(C)C)C(O)=O NADLKBTYNKUJEP-KATARQTJSA-N 0.000 claims description 2
- 201000011510 cancer Diseases 0.000 claims description 2
- 238000010276 construction Methods 0.000 claims description 2
- 102000004457 Granulocyte-Macrophage Colony-Stimulating Factor Human genes 0.000 claims 5
- 101100428021 Candida albicans (strain SC5314 / ATCC MYA-2876) UTR2 gene Proteins 0.000 claims 1
- 235000009917 Crataegus X brevipes Nutrition 0.000 claims 1
- 235000013204 Crataegus X haemacarpa Nutrition 0.000 claims 1
- 235000009685 Crataegus X maligna Nutrition 0.000 claims 1
- 235000009444 Crataegus X rubrocarnea Nutrition 0.000 claims 1
- 235000009486 Crataegus bullatus Nutrition 0.000 claims 1
- 235000017181 Crataegus chrysocarpa Nutrition 0.000 claims 1
- 235000009682 Crataegus limnophila Nutrition 0.000 claims 1
- 235000004423 Crataegus monogyna Nutrition 0.000 claims 1
- 240000000171 Crataegus monogyna Species 0.000 claims 1
- 235000002313 Crataegus paludosa Nutrition 0.000 claims 1
- 235000009840 Crataegus x incaedua Nutrition 0.000 claims 1
- 108010054576 Deoxyribonuclease EcoRI Proteins 0.000 claims 1
- 239000002253 acid Substances 0.000 claims 1
- 150000007513 acids Chemical class 0.000 claims 1
- 210000004899 c-terminal region Anatomy 0.000 claims 1
- 210000002837 heart atrium Anatomy 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 description 23
- 239000013612 plasmid Substances 0.000 description 17
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 11
- 235000001014 amino acid Nutrition 0.000 description 9
- 238000003776 cleavage reaction Methods 0.000 description 7
- 230000007017 scission Effects 0.000 description 7
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- 108091034117 Oligonucleotide Proteins 0.000 description 6
- 108020001507 fusion proteins Proteins 0.000 description 5
- 102000037865 fusion proteins Human genes 0.000 description 5
- 241000894006 Bacteria Species 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 239000002299 complementary DNA Substances 0.000 description 4
- 108020004414 DNA Proteins 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 239000013613 expression plasmid Substances 0.000 description 3
- 230000004048 modification Effects 0.000 description 3
- 238000012986 modification Methods 0.000 description 3
- 239000013049 sediment Substances 0.000 description 3
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 241001302584 Escherichia coli str. K-12 substr. W3110 Species 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 210000003714 granulocyte Anatomy 0.000 description 2
- 210000002540 macrophage Anatomy 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- 239000013598 vector Substances 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- VPSHHQXIWLGVDD-ZLUOBGJFSA-N Asp-Asp-Asp Chemical compound OC(=O)C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(O)=O)C(O)=O VPSHHQXIWLGVDD-ZLUOBGJFSA-N 0.000 description 1
- LKIYSIYBKYLKPU-BIIVOSGPSA-N Asp-Asp-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(=O)O)N)C(=O)O LKIYSIYBKYLKPU-BIIVOSGPSA-N 0.000 description 1
- LGGHQRZIJSYRHA-GUBZILKMSA-N Asp-Pro-Met Chemical compound CSCC[C@@H](C(=O)O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(=O)O)N LGGHQRZIJSYRHA-GUBZILKMSA-N 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108060002716 Exonuclease Proteins 0.000 description 1
- PFPUFNLHBXKPHY-HTFCKZLJSA-N Ile-Ile-Ser Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CO)C(=O)O)N PFPUFNLHBXKPHY-HTFCKZLJSA-N 0.000 description 1
- 108010054278 Lac Repressors Proteins 0.000 description 1
- WIDZHJTYKYBLSR-DCAQKATOSA-N Leu-Glu-Glu Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O WIDZHJTYKYBLSR-DCAQKATOSA-N 0.000 description 1
- LJBVRCDPWOJOEK-PPCPHDFISA-N Leu-Thr-Ile Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O LJBVRCDPWOJOEK-PPCPHDFISA-N 0.000 description 1
- XNQCXEBZBVDKAL-UHFFFAOYSA-N OSSS Chemical compound OSSS XNQCXEBZBVDKAL-UHFFFAOYSA-N 0.000 description 1
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 1
- 241000607715 Serratia marcescens Species 0.000 description 1
- 241000702208 Shigella phage SfX Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 108700005078 Synthetic Genes Proteins 0.000 description 1
- RRRRCRYTLZVCEN-HJGDQZAQSA-N Thr-Leu-Asp Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(O)=O RRRRCRYTLZVCEN-HJGDQZAQSA-N 0.000 description 1
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 1
- 238000007792 addition Methods 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000031018 biological processes and functions Effects 0.000 description 1
- 229960000074 biopharmaceutical Drugs 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 210000001185 bone marrow Anatomy 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 238000001516 cell proliferation assay Methods 0.000 description 1
- 230000003196 chaotropic effect Effects 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 239000000824 cytostatic agent Substances 0.000 description 1
- 230000001085 cytostatic effect Effects 0.000 description 1
- 231100000433 cytotoxic Toxicity 0.000 description 1
- 230000001472 cytotoxic effect Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 102000013165 exonuclease Human genes 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 239000013604 expression vector Substances 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- 230000002607 hemopoietic effect Effects 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 230000007775 late Effects 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- OJMIONKXNSYLSR-UHFFFAOYSA-N phosphorous acid Chemical compound OP(O)O OJMIONKXNSYLSR-UHFFFAOYSA-N 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000002953 preparative HPLC Methods 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 239000003643 water by type Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/62—DNA sequences coding for fusion proteins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/53—Colony-stimulating factor [CSF]
- C07K14/535—Granulocyte CSF; Granulocyte-macrophage CSF
-
- 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
- C07K14/55—IL-2
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/70—Fusion polypeptide containing domain for protein-protein interaction
- C07K2319/74—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor
- C07K2319/75—Fusion polypeptide containing domain for protein-protein interaction containing a fusion for binding to a cell surface receptor containing a fusion for activation of a cell surface receptor, e.g. thrombopoeitin, NPY and other peptide hormones
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- Biotechnology (AREA)
- General Health & Medical Sciences (AREA)
- General Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Physics & Mathematics (AREA)
- Medicinal Chemistry (AREA)
- Microbiology (AREA)
- Plant Pathology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Immunology (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- General Chemical & Material Sciences (AREA)
- Public Health (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE3712985 | 1987-04-16 | ||
| DE19873712985 DE3712985A1 (de) | 1987-04-16 | 1987-04-16 | Bifunktionelle proteine |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU1466188A AU1466188A (en) | 1988-10-20 |
| AU613022B2 true AU613022B2 (en) | 1991-07-25 |
Family
ID=6325799
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU14661/88A Ceased AU613022B2 (en) | 1987-04-16 | 1988-04-15 | Bifunctional proteins |
Country Status (20)
Families Citing this family (27)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5662896A (en) * | 1988-03-21 | 1997-09-02 | Chiron Viagene, Inc. | Compositions and methods for cancer immunotherapy |
| US5116964A (en) * | 1989-02-23 | 1992-05-26 | Genentech, Inc. | Hybrid immunoglobulins |
| US5225538A (en) * | 1989-02-23 | 1993-07-06 | Genentech, Inc. | Lymphocyte homing receptor/immunoglobulin fusion proteins |
| US6406697B1 (en) | 1989-02-23 | 2002-06-18 | Genentech, Inc. | Hybrid immunoglobulins |
| AU5355790A (en) * | 1989-04-19 | 1990-11-16 | Cetus Corporation | Multifunctional m-csf proteins and genes encoding therefor |
| US5108910A (en) * | 1989-08-22 | 1992-04-28 | Immunex Corporation | DNA sequences encoding fusion proteins comprising GM-CSF and IL-3 |
| US5073627A (en) * | 1989-08-22 | 1991-12-17 | Immunex Corporation | Fusion proteins comprising GM-CSF and IL-3 |
| WO1991002754A1 (en) * | 1989-08-22 | 1991-03-07 | Immunex Corporation | Fusion proteins comprising gm-csf and il-3 |
| US5376367A (en) * | 1991-11-22 | 1994-12-27 | Immunex Corporation | Fusion proteins comprising MGF and IL-3 |
| US5723125A (en) * | 1995-12-28 | 1998-03-03 | Tanox Biosystems, Inc. | Hybrid with interferon-alpha and an immunoglobulin Fc linked through a non-immunogenic peptide |
| JP4336452B2 (ja) | 1997-12-08 | 2009-09-30 | メルク パテント ゲーエムベーハー | 標的化免疫治療および一般の免疫刺激に対して有用である二量体融合タンパク質 |
| SK782002A3 (en) | 1999-07-21 | 2003-08-05 | Lexigen Pharm Corp | FC fusion proteins for enhancing the immunogenicity of protein and peptide antigens |
| 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 |
| EP1200479B1 (en) | 1999-08-09 | 2006-02-01 | Lexigen Pharmaceuticals Corp. | Multiple cytokine-antibody complexes |
| WO2001036489A2 (en) | 1999-11-12 | 2001-05-25 | Merck Patent Gmbh | Erythropoietin forms with improved properties |
| JP4553290B2 (ja) * | 1999-11-30 | 2010-09-29 | 塩野義製薬株式会社 | ケモカインｓｌｃ−ｉｌ２融合タンパク質とその遺伝子 |
| AU4314801A (en) | 2000-02-11 | 2001-08-20 | Lexigen Pharm Corp | Enhancing the circulating half-life of antibody-based fusion proteins |
| SK982003A3 (en) | 2000-06-29 | 2004-05-04 | Merck Patent Gmbh | Enhancement of antibody-cytokine fusion protein mediated immune responses by combined treatment with immunocytokine uptake enhancing agents |
| RU2003129528A (ru) | 2001-03-07 | 2005-04-10 | Мерк Патент ГмбХ (DE) | Способ экспрессии белков, содержащих в качестве компонента гибридный изотип антитела |
| US6992174B2 (en) | 2001-03-30 | 2006-01-31 | Emd Lexigen Research Center Corp. | Reducing the immunogenicity of fusion proteins |
| ES2361664T3 (es) | 2001-05-03 | 2011-06-21 | Merck Patent Gmbh | Anticuerpo recombinante para tumor específico y su utilización. |
| EP2305314B1 (en) | 2001-10-10 | 2015-12-23 | ratiopharm GmbH | Remodelling and glycoconjugation of antibodies |
| DK1454138T3 (da) | 2001-12-04 | 2012-02-13 | Merck Patent Gmbh | Immunocytokiner med moduleret selektivitet |
| US7169904B2 (en) | 2002-12-17 | 2007-01-30 | Emd Lexigen Research Center Corp. | Immunocytokine sequences and uses thereof |
| ATE500267T1 (de) * | 2003-07-21 | 2011-03-15 | Transgene Sa | Multifunktionelle cytokine |
| DE602004031341D1 (de) | 2003-07-21 | 2011-03-24 | Transgene Sa | Multifunktionelle cytokine |
| WO2010001414A1 (en) * | 2008-07-03 | 2010-01-07 | Lupin Limited | Expression of heterologous proteins in bacterial system using a gm-csf fusion tag |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0136489A1 (en) * | 1983-08-10 | 1985-04-10 | Amgen Inc. | Analogs of human interleukin II and their preparation |
| EP0183350A2 (en) * | 1984-10-29 | 1986-06-04 | Immunex Corporation | DNA Encoding human colony stimulating factor, peptide encoded thereby,vectors and transformed hosts containing such DNA, and the production of all thereof |
| AU6675686A (en) * | 1985-12-21 | 1987-06-25 | Hoechst Aktiengesellschaft | GM-CSF protein, its derivatives, the preparation of proteins of this type, and their use |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB8327880D0 (en) * | 1983-10-18 | 1983-11-16 | Ajinomoto Kk | Saccharomyces cerevisiae |
| EP0158198A1 (en) * | 1984-03-29 | 1985-10-16 | Takeda Chemical Industries, Ltd. | DNA and use thereof |
| WO1985004673A1 (en) * | 1984-04-10 | 1985-10-24 | Takeda Chemical Industries, Ltd. | Novel dna and its use |
| DE3419995A1 (de) * | 1984-05-29 | 1985-12-05 | Hoechst Ag, 6230 Frankfurt | Gentechnologisches verfahren zur herstellung von human-interleukin-2 und mittel zur durchfuehrung dieses verfahrens |
| JPS61128889A (ja) * | 1984-11-27 | 1986-06-16 | Green Cross Corp:The | 組換えｄｎａ及び該ｄｎａによる形質転換体 |
| JPH0646957B2 (ja) * | 1985-03-11 | 1994-06-22 | 武田薬品工業株式会社 | インタ−ロイキン−２の製造方法 |
| WO1987002060A1 (en) * | 1985-10-03 | 1987-04-09 | Biogen N.V. | Human granulocyte-macrophage colony stimulating factor-like polypeptides and processes for producing them in high yields in microbial cells |
| DE3541856A1 (de) * | 1985-11-27 | 1987-06-04 | Hoechst Ag | Eukaryotische fusionsproteine, ihre herstellung und verwendung sowie mittel zur durchfuehrung des verfahrens |
-
1987
- 1987-04-16 DE DE19873712985 patent/DE3712985A1/de not_active Withdrawn
-
1988
- 1988-04-09 EP EP88105693A patent/EP0288809B1/de not_active Expired - Lifetime
- 1988-04-09 DE DE8888105693T patent/DE3873397D1/de not_active Expired - Fee Related
- 1988-04-09 AT AT88105693T patent/ATE79135T1/de not_active IP Right Cessation
- 1988-04-09 ES ES198888105693T patent/ES2033981T3/es not_active Expired - Lifetime
- 1988-04-14 PT PT87237A patent/PT87237B/pt active IP Right Grant
- 1988-04-14 FI FI881743A patent/FI98830C/fi not_active IP Right Cessation
- 1988-04-14 NZ NZ224247A patent/NZ224247A/en unknown
- 1988-04-15 AU AU14661/88A patent/AU613022B2/en not_active Ceased
- 1988-04-15 ZA ZA882659A patent/ZA882659B/xx unknown
- 1988-04-15 IE IE114688A patent/IE61574B1/en not_active IP Right Cessation
- 1988-04-15 CA CA000564322A patent/CA1322157C/en not_active Expired - Fee Related
- 1988-04-15 IL IL8608688A patent/IL86086A/en not_active IP Right Cessation
- 1988-04-15 JP JP63093321A patent/JP2667193B2/ja not_active Expired - Fee Related
- 1988-04-15 AR AR88310585A patent/AR242991A1/es active
- 1988-04-15 NO NO881658A patent/NO176922C/no not_active IP Right Cessation
- 1988-04-15 HU HU881966A patent/HU204303B/hu not_active IP Right Cessation
- 1988-04-15 DK DK209188A patent/DK170741B1/da not_active IP Right Cessation
- 1988-04-16 KR KR1019880004345A patent/KR970000187B1/ko not_active Expired - Fee Related
-
1989
- 1989-04-14 PH PH36799A patent/PH25327A/en unknown
-
1992
- 1992-11-04 GR GR920402185T patent/GR3006141T3/el unknown
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0136489A1 (en) * | 1983-08-10 | 1985-04-10 | Amgen Inc. | Analogs of human interleukin II and their preparation |
| EP0183350A2 (en) * | 1984-10-29 | 1986-06-04 | Immunex Corporation | DNA Encoding human colony stimulating factor, peptide encoded thereby,vectors and transformed hosts containing such DNA, and the production of all thereof |
| AU6675686A (en) * | 1985-12-21 | 1987-06-25 | Hoechst Aktiengesellschaft | GM-CSF protein, its derivatives, the preparation of proteins of this type, and their use |
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| MK14 | Patent ceased section 143(a) (annual fees not paid) or expired |