AU780810B2 - Recombinant stable cell clone, its production and use thereof - Google Patents
Recombinant stable cell clone, its production and use thereof Download PDFInfo
- Publication number
- AU780810B2 AU780810B2 AU53636/99A AU5363699A AU780810B2 AU 780810 B2 AU780810 B2 AU 780810B2 AU 53636/99 A AU53636/99 A AU 53636/99A AU 5363699 A AU5363699 A AU 5363699A AU 780810 B2 AU780810 B2 AU 780810B2
- Authority
- AU
- Australia
- Prior art keywords
- protein
- cell
- recombinant
- serum
- stable
- 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.)
- Expired
Links
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 39
- 210000002966 serum Anatomy 0.000 claims abstract description 33
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 24
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 21
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 claims abstract description 15
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 claims abstract description 15
- 210000004027 cell Anatomy 0.000 claims description 216
- 238000004113 cell culture Methods 0.000 claims description 48
- 238000000034 method Methods 0.000 claims description 37
- 238000012258 culturing Methods 0.000 claims description 26
- 239000000047 product Substances 0.000 claims description 26
- 210000004978 chinese hamster ovary cell Anatomy 0.000 claims description 23
- 238000002360 preparation method Methods 0.000 claims description 22
- 108010054218 Factor VIII Proteins 0.000 claims description 12
- 102000001690 Factor VIII Human genes 0.000 claims description 12
- 229960000301 factor viii Drugs 0.000 claims description 12
- 238000010367 cloning Methods 0.000 claims description 9
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 8
- 238000012360 testing method Methods 0.000 claims description 8
- 108010047303 von Willebrand Factor Proteins 0.000 claims description 8
- 229960000182 blood factors Drugs 0.000 claims description 7
- 210000004962 mammalian cell Anatomy 0.000 claims description 7
- 229920001184 polypeptide Polymers 0.000 claims description 7
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 7
- 102100022641 Coagulation factor IX Human genes 0.000 claims description 5
- 108010076282 Factor IX Proteins 0.000 claims description 5
- 108010094028 Prothrombin Proteins 0.000 claims description 5
- AGVAZMGAQJOSFJ-WZHZPDAFSA-M cobalt(2+);[(2r,3s,4r,5s)-5-(5,6-dimethylbenzimidazol-1-yl)-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl] [(2r)-1-[3-[(1r,2r,3r,4z,7s,9z,12s,13s,14z,17s,18s,19r)-2,13,18-tris(2-amino-2-oxoethyl)-7,12,17-tris(3-amino-3-oxopropyl)-3,5,8,8,13,15,18,19-octamethyl-2 Chemical compound [Co+2].N#[C-].[N-]([C@@H]1[C@H](CC(N)=O)[C@@]2(C)CCC(=O)NC[C@@H](C)OP(O)(=O)O[C@H]3[C@H]([C@H](O[C@@H]3CO)N3C4=CC(C)=C(C)C=C4N=C3)O)\C2=C(C)/C([C@H](C\2(C)C)CCC(N)=O)=N/C/2=C\C([C@H]([C@@]/2(CC(N)=O)C)CCC(N)=O)=N\C\2=C(C)/C2=N[C@]1(C)[C@@](C)(CC(N)=O)[C@@H]2CCC(N)=O AGVAZMGAQJOSFJ-WZHZPDAFSA-M 0.000 claims description 5
- 229960004222 factor ix Drugs 0.000 claims description 5
- 238000009776 industrial production Methods 0.000 claims description 5
- 238000002955 isolation Methods 0.000 claims description 5
- 229920000858 Cyclodextrin Polymers 0.000 claims description 4
- HFHDHCJBZVLPGP-UHFFFAOYSA-N schardinger α-dextrin Chemical compound O1C(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC(C(O)C2O)C(CO)OC2OC(C(C2O)O)C(CO)OC2OC2C(O)C(O)C1OC2CO HFHDHCJBZVLPGP-UHFFFAOYSA-N 0.000 claims description 4
- 102100023804 Coagulation factor VII Human genes 0.000 claims description 2
- 108010014172 Factor V Proteins 0.000 claims description 2
- 108010023321 Factor VII Proteins 0.000 claims description 2
- 108010014173 Factor X Proteins 0.000 claims description 2
- 108010074864 Factor XI Proteins 0.000 claims description 2
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 claims description 2
- 101800004937 Protein C Proteins 0.000 claims description 2
- 102000017975 Protein C Human genes 0.000 claims description 2
- 108010066124 Protein S Proteins 0.000 claims description 2
- 229940096437 Protein S Drugs 0.000 claims description 2
- 102000029301 Protein S Human genes 0.000 claims description 2
- 101800001700 Saposin-D Proteins 0.000 claims description 2
- 239000012228 culture supernatant Substances 0.000 claims description 2
- 239000000284 extract Substances 0.000 claims description 2
- 229940012413 factor vii Drugs 0.000 claims description 2
- 229940012426 factor x Drugs 0.000 claims description 2
- 238000003306 harvesting Methods 0.000 claims description 2
- 108020004707 nucleic acids Proteins 0.000 claims description 2
- 102000039446 nucleic acids Human genes 0.000 claims description 2
- 150000007523 nucleic acids Chemical class 0.000 claims description 2
- 239000000137 peptide hydrolase inhibitor Substances 0.000 claims description 2
- 229960000856 protein c Drugs 0.000 claims description 2
- 238000001890 transfection Methods 0.000 claims description 2
- 241000237519 Bivalvia Species 0.000 claims 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims 1
- 235000020639 clam Nutrition 0.000 claims 1
- 239000002028 Biomass Substances 0.000 abstract description 9
- 239000002609 medium Substances 0.000 description 66
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 12
- 230000010412 perfusion Effects 0.000 description 12
- 238000013411 master cell bank Methods 0.000 description 8
- 238000010166 immunofluorescence Methods 0.000 description 7
- 102000004877 Insulin Human genes 0.000 description 6
- 239000000654 additive Substances 0.000 description 6
- 230000000694 effects Effects 0.000 description 6
- 230000012010 growth Effects 0.000 description 6
- 229940125396 insulin Drugs 0.000 description 6
- 102100036537 von Willebrand factor Human genes 0.000 description 6
- 108090001061 Insulin Proteins 0.000 description 5
- 102000004338 Transferrin Human genes 0.000 description 5
- 230000007423 decrease Effects 0.000 description 5
- 230000014509 gene expression Effects 0.000 description 5
- 239000003550 marker Substances 0.000 description 5
- 239000012581 transferrin Substances 0.000 description 5
- 102100026735 Coagulation factor VIII Human genes 0.000 description 4
- 101000911390 Homo sapiens Coagulation factor VIII Proteins 0.000 description 4
- 108090000901 Transferrin Proteins 0.000 description 4
- 230000001464 adherent effect Effects 0.000 description 4
- 239000002736 nonionic surfactant Substances 0.000 description 4
- 239000003708 ampul Substances 0.000 description 3
- 238000011109 contamination Methods 0.000 description 3
- 230000001419 dependent effect Effects 0.000 description 3
- AIUDWMLXCFRVDR-UHFFFAOYSA-N dimethyl 2-(3-ethyl-3-methylpentyl)propanedioate Chemical compound CCC(C)(CC)CCC(C(=O)OC)C(=O)OC AIUDWMLXCFRVDR-UHFFFAOYSA-N 0.000 description 3
- 238000000855 fermentation Methods 0.000 description 3
- 230000004151 fermentation Effects 0.000 description 3
- 239000003102 growth factor Substances 0.000 description 3
- 229920001983 poloxamer Polymers 0.000 description 3
- 230000000644 propagated effect Effects 0.000 description 3
- 239000012679 serum free medium Substances 0.000 description 3
- 239000004017 serum-free culture medium Substances 0.000 description 3
- 238000004114 suspension culture Methods 0.000 description 3
- HZAXFHJVJLSVMW-UHFFFAOYSA-N 2-Aminoethan-1-ol Chemical compound NCCO HZAXFHJVJLSVMW-UHFFFAOYSA-N 0.000 description 2
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 2
- 101000976075 Homo sapiens Insulin Proteins 0.000 description 2
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 2
- RVGRUAULSDPKGF-UHFFFAOYSA-N Poloxamer Chemical compound C1CO1.CC1CO1 RVGRUAULSDPKGF-UHFFFAOYSA-N 0.000 description 2
- 108010009736 Protein Hydrolysates Proteins 0.000 description 2
- 230000006978 adaptation Effects 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 230000003321 amplification Effects 0.000 description 2
- 230000010261 cell growth Effects 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 238000010924 continuous production Methods 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 238000011156 evaluation Methods 0.000 description 2
- -1 for example Proteins 0.000 description 2
- 239000012737 fresh medium Substances 0.000 description 2
- 238000003199 nucleic acid amplification method Methods 0.000 description 2
- 244000052769 pathogen Species 0.000 description 2
- 239000003531 protein hydrolysate Substances 0.000 description 2
- 210000003501 vero cell Anatomy 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- FERIUCNNQQJTOY-UHFFFAOYSA-M Butyrate Chemical compound CCCC([O-])=O FERIUCNNQQJTOY-UHFFFAOYSA-M 0.000 description 1
- FERIUCNNQQJTOY-UHFFFAOYSA-N Butyric acid Natural products CCCC(O)=O FERIUCNNQQJTOY-UHFFFAOYSA-N 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 102100037362 Fibronectin Human genes 0.000 description 1
- 108010067306 Fibronectins Proteins 0.000 description 1
- CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 0.000 description 1
- 229930182566 Gentamicin Natural products 0.000 description 1
- 101000766306 Homo sapiens Serotransferrin Proteins 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 108010070716 Intercellular Signaling Peptides and Proteins Proteins 0.000 description 1
- 102000005755 Intercellular Signaling Peptides and Proteins Human genes 0.000 description 1
- 229930182816 L-glutamine Natural products 0.000 description 1
- WHXSMMKQMYFTQS-UHFFFAOYSA-N Lithium Chemical compound [Li] WHXSMMKQMYFTQS-UHFFFAOYSA-N 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- GKWTZACONBQTNK-IVIZKJKWSA-N N-benzyl-7H-purin-6-amine (1R,2R,5R,8R,9S,10R,12S)-12-hydroxy-11-methyl-6-methylidene-16-oxo-15-oxapentacyclo[9.3.2.15,8.01,10.02,8]heptadecane-9-carboxylic acid (1R,2R,5R,8R,9S,10R,12S)-12-hydroxy-11-methyl-6-methylidene-16-oxo-15-oxapentacyclo[9.3.2.15,8.01,10.02,8]heptadec-13-ene-9-carboxylic acid Chemical compound C(Nc1ncnc2nc[nH]c12)c1ccccc1.CC12[C@H]3[C@H](C(O)=O)[C@@]45C[C@@H](CC[C@H]4[C@@]3(CC[C@@H]1O)OC2=O)C(=C)C5.CC12[C@H]3[C@H](C(O)=O)[C@@]45C[C@@H](CC[C@H]4[C@]3(OC1=O)C=C[C@@H]2O)C(=C)C5 GKWTZACONBQTNK-IVIZKJKWSA-N 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 101100208039 Rattus norvegicus Trpv5 gene Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 238000005273 aeration Methods 0.000 description 1
- 239000002518 antifoaming agent Substances 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 230000001174 ascending effect Effects 0.000 description 1
- 229960005070 ascorbic acid Drugs 0.000 description 1
- 235000010323 ascorbic acid Nutrition 0.000 description 1
- 239000011668 ascorbic acid Substances 0.000 description 1
- 230000009172 bursting Effects 0.000 description 1
- 229940041514 candida albicans extract Drugs 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 210000001728 clone cell Anatomy 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
- 239000012894 fetal calf serum Substances 0.000 description 1
- 229960002518 gentamicin Drugs 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 210000001822 immobilized cell Anatomy 0.000 description 1
- PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 description 1
- 229910052744 lithium Inorganic materials 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 230000002101 lytic effect Effects 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 239000006151 minimal media Substances 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 230000001717 pathogenic effect Effects 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 229920001993 poloxamer 188 Polymers 0.000 description 1
- 229920001451 polypropylene glycol Polymers 0.000 description 1
- 108010012557 prothrombin complex concentrates Proteins 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 229940082569 selenite Drugs 0.000 description 1
- MCAHWIHFGHIESP-UHFFFAOYSA-L selenite(2-) Chemical compound [O-][Se]([O-])=O MCAHWIHFGHIESP-UHFFFAOYSA-L 0.000 description 1
- 239000003001 serine protease inhibitor Substances 0.000 description 1
- 239000002356 single layer Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 230000010473 stable expression Effects 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 230000000381 tumorigenic effect Effects 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 239000012138 yeast extract Substances 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/647—Blood coagulation factors not provided for in a preceding group or according to more than one of the proceeding groups
-
- 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
- C07K14/745—Blood coagulation or fibrinolysis factors
- C07K14/755—Factors VIII, e.g. factor VIII C (AHF), factor VIII Ag (VWF)
-
- 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
- C12N5/00—Undifferentiated human, animal or plant cells, e.g. cell lines; Tissues; Cultivation or maintenance thereof; Culture media therefor
- C12N5/0018—Culture media for cell or tissue culture
- C12N5/005—Protein-free medium
-
- 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
- C12N2500/00—Specific components of cell culture medium
- C12N2500/70—Undefined extracts
- C12N2500/76—Undefined extracts from plants
-
- 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
- C12N2510/00—Genetically modified cells
- C12N2510/02—Cells for production
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Biomedical Technology (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biotechnology (AREA)
- Wood Science & Technology (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Microbiology (AREA)
- General Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Hematology (AREA)
- Biophysics (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Cell Biology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| PCT/AT1999/000197 WO2001011021A1 (de) | 1999-08-05 | 1999-08-05 | Rekombinanter stabiler zellklon, seine herstellung und verwendung |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU5363699A AU5363699A (en) | 2001-03-05 |
| AU780810B2 true AU780810B2 (en) | 2005-04-21 |
Family
ID=3683861
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU53636/99A Expired AU780810B2 (en) | 1999-08-05 | 1999-08-05 | Recombinant stable cell clone, its production and use thereof |
Country Status (11)
| Country | Link |
|---|---|
| EP (1) | EP1200561B1 (https=) |
| JP (1) | JP2003506077A (https=) |
| AT (1) | ATE330003T1 (https=) |
| AU (1) | AU780810B2 (https=) |
| CA (1) | CA2381173A1 (https=) |
| CY (1) | CY1106111T1 (https=) |
| DE (1) | DE59913565D1 (https=) |
| DK (1) | DK1200561T3 (https=) |
| ES (1) | ES2267280T3 (https=) |
| PT (1) | PT1200561E (https=) |
| WO (1) | WO2001011021A1 (https=) |
Families Citing this family (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP1482031B1 (en) | 1996-08-30 | 2015-10-28 | Life Technologies Corporation | Serum-free mammalian cell culture medium, and uses thereof |
| US6475725B1 (en) | 1997-06-20 | 2002-11-05 | Baxter Aktiengesellschaft | Recombinant cell clones having increased stability and methods of making and using the same |
| AT409379B (de) | 1999-06-02 | 2002-07-25 | Baxter Ag | Medium zur protein- und serumfreien kultivierung von zellen |
| EP1325127B1 (en) * | 2000-10-02 | 2009-03-11 | Novo Nordisk Health Care AG | Method for the production of vitamin k-dependent proteins |
| EP1434857B1 (en) | 2001-10-02 | 2007-08-01 | Novo Nordisk Health Care AG | Method for production of recombinant proteins in eukaryote cells |
| HUP0402226A2 (hu) * | 2001-11-28 | 2005-02-28 | Sandoz Ag. | Eljárás sejttenyésztésre |
| WO2003048357A1 (fr) * | 2001-12-04 | 2003-06-12 | Mitsubishi Pharma Corporation | Procede d'activation de proteine |
| PT2287288E (pt) | 2002-07-09 | 2012-12-10 | Baxter Int | Meio isento de proteína animal para cultura de células |
| DE10338531A1 (de) * | 2003-08-19 | 2005-04-07 | Boehringer Ingelheim Pharma Gmbh & Co. Kg | Verfahren zur Reklonierung von Produktionszellen |
| US8669109B2 (en) | 2003-08-19 | 2014-03-11 | Boehringer Ingelheim Pharma Gmbh & Co. Kg | Methods of producing proteins in Chinese hamster ovary (CHO) cells |
| JP2008504008A (ja) * | 2003-12-31 | 2008-02-14 | メルク パテント ゲゼルシャフト ミット ベシュレンクテル ハフトング | 改良された薬物動態を有するFc−エリスロポエチン融合タンパク質 |
| US20060094104A1 (en) * | 2004-10-29 | 2006-05-04 | Leopold Grillberger | Animal protein-free media for cultivation of cells |
| AU2011221414B2 (en) * | 2004-10-29 | 2012-09-20 | Takeda Pharmaceutical Company Limited | Animal Protein-Free Media for Cultivation of Cells |
| ATE541919T1 (de) | 2005-02-11 | 2012-02-15 | Novo Nordisk Healthcare Ag | Herstellung eines proteins in serumfreier zellkultur, die ein proteinhydrolysat aus pflanzen enthält |
| EP3653699A1 (en) | 2006-01-04 | 2020-05-20 | Baxalta Incorporated | Oligopeptide-free cell culture media |
| CA2742107A1 (en) | 2008-11-12 | 2010-05-20 | Baxter International Inc. | Method of producing serum-free insulin-free factor vii |
| WO2024024671A1 (ja) * | 2022-07-27 | 2024-02-01 | 不二製油グループ本社株式会社 | 動物細胞増殖促進剤 |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5851800A (en) * | 1996-05-14 | 1998-12-22 | Pharmacia & Upjohn Ab | Process for producing a protein |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9022545D0 (en) * | 1990-10-17 | 1990-11-28 | Wellcome Found | Culture medium |
| DE4313620A1 (de) * | 1993-04-26 | 1994-10-27 | Biotechnolog Forschung Gmbh | Hamsterzellinien und Verfahren zur Glykoproteingewinnung |
| EP0666312A1 (en) * | 1994-02-08 | 1995-08-09 | Wolfgang A. Renner | Process for the improvement of mammalian cell growth |
| ES2378409T3 (es) * | 1994-11-10 | 2012-04-12 | Baxter Healthcare S.A. | Método para producir sustancias biológicas en cultivo sin proteínas |
| EP0799310A1 (en) * | 1994-12-16 | 1997-10-08 | Novartis AG | Production of recombinant secretory component |
| AUPN442295A0 (en) * | 1995-07-26 | 1995-08-17 | Commonwealth Scientific And Industrial Research Organisation | Regulated autocrine growth of mammalian cells |
-
1999
- 1999-08-05 AT AT99939251T patent/ATE330003T1/de active
- 1999-08-05 DE DE59913565T patent/DE59913565D1/de not_active Expired - Lifetime
- 1999-08-05 CA CA 2381173 patent/CA2381173A1/en not_active Abandoned
- 1999-08-05 AU AU53636/99A patent/AU780810B2/en not_active Expired
- 1999-08-05 EP EP99939251A patent/EP1200561B1/de not_active Revoked
- 1999-08-05 WO PCT/AT1999/000197 patent/WO2001011021A1/de not_active Ceased
- 1999-08-05 PT PT99939251T patent/PT1200561E/pt unknown
- 1999-08-05 DK DK99939251T patent/DK1200561T3/da active
- 1999-08-05 ES ES99939251T patent/ES2267280T3/es not_active Expired - Lifetime
- 1999-08-05 JP JP2001515808A patent/JP2003506077A/ja not_active Withdrawn
-
2006
- 2006-07-03 CY CY20061100911T patent/CY1106111T1/el unknown
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5851800A (en) * | 1996-05-14 | 1998-12-22 | Pharmacia & Upjohn Ab | Process for producing a protein |
Non-Patent Citations (2)
| Title |
|---|
| KAUFMAN R J ET AL (1989) MOL. & CELL. BIOLOGY 9:1233-1242 * |
| ZANG M ET AL (1995) BIOTECHNOLOGY 13:389-392 * |
Also Published As
| Publication number | Publication date |
|---|---|
| DE59913565D1 (de) | 2006-07-27 |
| CY1106111T1 (el) | 2011-06-08 |
| WO2001011021A1 (de) | 2001-02-15 |
| ES2267280T3 (es) | 2007-03-01 |
| DK1200561T3 (da) | 2006-10-16 |
| AU5363699A (en) | 2001-03-05 |
| CA2381173A1 (en) | 2001-02-15 |
| ATE330003T1 (de) | 2006-07-15 |
| PT1200561E (pt) | 2006-09-29 |
| EP1200561B1 (de) | 2006-06-14 |
| JP2003506077A (ja) | 2003-02-18 |
| EP1200561A1 (de) | 2002-05-02 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| USRE46897E1 (en) | Recombinant cell clones having increased stability and methods of making and using the same | |
| US6100061A (en) | Recombinant cell clone having increased stability in serum- and protein-free medium and a method of recovering the stable cell clone and the production of recombinant proteins by using a stable cell clone | |
| AU780810B2 (en) | Recombinant stable cell clone, its production and use thereof | |
| US9441203B2 (en) | Medium for the protein-free and serum-free cultivation of cells | |
| JP6245299B2 (ja) | 組換え安定細胞クローン、その産生およびその使用 | |
| JP2011004754A (ja) | 組換え安定細胞クローン、その産生およびその使用 | |
| JP6097725B2 (ja) | 組換え安定細胞クローン、その産生およびその使用 | |
| JP2010099093A (ja) | 組換え安定細胞クローン、その産生およびその使用 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MK14 | Patent ceased section 143(a) (annual fees not paid) or expired |