DK2726600T3 - Pattedyrcellekultur - Google Patents
Pattedyrcellekultur Download PDFInfo
- Publication number
- DK2726600T3 DK2726600T3 DK12738674.6T DK12738674T DK2726600T3 DK 2726600 T3 DK2726600 T3 DK 2726600T3 DK 12738674 T DK12738674 T DK 12738674T DK 2726600 T3 DK2726600 T3 DK 2726600T3
- Authority
- DK
- Denmark
- Prior art keywords
- perfusion
- cell
- culture
- cells
- day
- Prior art date
Links
- 238000004113 cell culture Methods 0.000 title claims description 74
- 210000004962 mammalian cell Anatomy 0.000 title claims description 35
- 210000004027 cell Anatomy 0.000 claims description 266
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 claims description 198
- 230000010412 perfusion Effects 0.000 claims description 143
- 229960001230 asparagine Drugs 0.000 claims description 113
- 238000004519 manufacturing process Methods 0.000 claims description 84
- 238000000034 method Methods 0.000 claims description 79
- 239000002609 medium Substances 0.000 claims description 48
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 claims description 32
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 claims description 32
- 230000003698 anagen phase Effects 0.000 claims description 21
- 230000001965 increasing effect Effects 0.000 claims description 17
- 239000006143 cell culture medium Substances 0.000 claims description 15
- 239000001963 growth medium Substances 0.000 claims description 14
- 235000003642 hunger Nutrition 0.000 claims description 12
- 230000037351 starvation Effects 0.000 claims description 12
- 230000010261 cell growth Effects 0.000 claims description 11
- 239000004017 serum-free culture medium Substances 0.000 claims description 11
- 238000009472 formulation Methods 0.000 claims description 10
- 238000003306 harvesting Methods 0.000 claims description 10
- 239000000203 mixture Substances 0.000 claims description 10
- 102000004127 Cytokines Human genes 0.000 claims description 9
- 108090000695 Cytokines Proteins 0.000 claims description 9
- 235000015097 nutrients Nutrition 0.000 claims description 7
- 230000001939 inductive effect Effects 0.000 claims description 6
- 230000007704 transition Effects 0.000 claims description 6
- 230000000977 initiatory effect Effects 0.000 claims description 5
- 238000012258 culturing Methods 0.000 claims description 4
- 241000699802 Cricetulus griseus Species 0.000 claims description 3
- 210000001672 ovary Anatomy 0.000 claims description 3
- 230000001502 supplementing effect Effects 0.000 claims description 3
- 239000012679 serum free medium Substances 0.000 claims 1
- 108090000623 proteins and genes Proteins 0.000 description 41
- 102000004169 proteins and genes Human genes 0.000 description 38
- 235000018102 proteins Nutrition 0.000 description 37
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 26
- 235000009582 asparagine Nutrition 0.000 description 26
- 230000035899 viability Effects 0.000 description 22
- 230000012010 growth Effects 0.000 description 19
- 239000012526 feed medium Substances 0.000 description 17
- 108090000765 processed proteins & peptides Proteins 0.000 description 17
- 239000000047 product Substances 0.000 description 16
- 102000004196 processed proteins & peptides Human genes 0.000 description 15
- 239000000427 antigen Substances 0.000 description 14
- 102000036639 antigens Human genes 0.000 description 14
- 108091007433 antigens Proteins 0.000 description 14
- 230000035611 feeding Effects 0.000 description 14
- 239000007787 solid Substances 0.000 description 14
- 229920001184 polypeptide Polymers 0.000 description 13
- 239000003446 ligand Substances 0.000 description 11
- 230000008569 process Effects 0.000 description 11
- 102000005962 receptors Human genes 0.000 description 11
- 108020003175 receptors Proteins 0.000 description 11
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 10
- 238000011020 pilot scale process Methods 0.000 description 9
- 229930182816 L-glutamine Natural products 0.000 description 8
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 8
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 8
- 238000013019 agitation Methods 0.000 description 8
- 238000011021 bench scale process Methods 0.000 description 8
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 7
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 7
- 230000002354 daily effect Effects 0.000 description 7
- 239000008103 glucose Substances 0.000 description 7
- 230000014616 translation Effects 0.000 description 7
- 206010028980 Neoplasm Diseases 0.000 description 6
- 150000001413 amino acids Chemical class 0.000 description 6
- 210000004102 animal cell Anatomy 0.000 description 6
- 239000010432 diamond Substances 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- 238000001914 filtration Methods 0.000 description 6
- 230000000670 limiting effect Effects 0.000 description 6
- 239000005557 antagonist Substances 0.000 description 5
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 5
- 230000007423 decrease Effects 0.000 description 5
- 239000003102 growth factor Substances 0.000 description 5
- 239000012510 hollow fiber Substances 0.000 description 5
- 229910052760 oxygen Inorganic materials 0.000 description 5
- 239000001301 oxygen Substances 0.000 description 5
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 4
- 239000002028 Biomass Substances 0.000 description 4
- 238000010923 batch production Methods 0.000 description 4
- 230000027455 binding Effects 0.000 description 4
- 230000003833 cell viability Effects 0.000 description 4
- 238000009295 crossflow filtration Methods 0.000 description 4
- 238000012136 culture method Methods 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 238000004128 high performance liquid chromatography Methods 0.000 description 4
- 230000006872 improvement Effects 0.000 description 4
- 238000011081 inoculation Methods 0.000 description 4
- 230000002503 metabolic effect Effects 0.000 description 4
- 238000010369 molecular cloning Methods 0.000 description 4
- 101001031613 Homo sapiens Fibroleukin Proteins 0.000 description 3
- 108060003951 Immunoglobulin Proteins 0.000 description 3
- 108010002350 Interleukin-2 Proteins 0.000 description 3
- 102000000588 Interleukin-2 Human genes 0.000 description 3
- 102000014128 RANK Ligand Human genes 0.000 description 3
- 108010025832 RANK Ligand Proteins 0.000 description 3
- 108010022394 Threonine synthase Proteins 0.000 description 3
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 3
- 102100036922 Tumor necrosis factor ligand superfamily member 13B Human genes 0.000 description 3
- 238000009825 accumulation Methods 0.000 description 3
- 229940024606 amino acid Drugs 0.000 description 3
- 235000001014 amino acid Nutrition 0.000 description 3
- 239000000872 buffer Substances 0.000 description 3
- 239000006227 byproduct Substances 0.000 description 3
- 230000001276 controlling effect Effects 0.000 description 3
- 229910003460 diamond Inorganic materials 0.000 description 3
- 102000004419 dihydrofolate reductase Human genes 0.000 description 3
- 238000011143 downstream manufacturing Methods 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 239000012634 fragment Substances 0.000 description 3
- 230000014509 gene expression Effects 0.000 description 3
- 102000018358 immunoglobulin Human genes 0.000 description 3
- 239000000411 inducer Substances 0.000 description 3
- 229940047124 interferons Drugs 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 3
- 108010028006 B-Cell Activating Factor Proteins 0.000 description 2
- 102100038080 B-cell receptor CD22 Human genes 0.000 description 2
- 101150013553 CD40 gene Proteins 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- 108010022366 Carcinoembryonic Antigen Proteins 0.000 description 2
- 102100025475 Carcinoembryonic antigen-related cell adhesion molecule 5 Human genes 0.000 description 2
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 2
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 102000018651 Epithelial Cell Adhesion Molecule Human genes 0.000 description 2
- 108010066687 Epithelial Cell Adhesion Molecule Proteins 0.000 description 2
- 102100038647 Fibroleukin Human genes 0.000 description 2
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 2
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 2
- 102000006354 HLA-DR Antigens Human genes 0.000 description 2
- 108010058597 HLA-DR Antigens Proteins 0.000 description 2
- 101000884305 Homo sapiens B-cell receptor CD22 Proteins 0.000 description 2
- 101001133056 Homo sapiens Mucin-1 Proteins 0.000 description 2
- 101000914484 Homo sapiens T-lymphocyte activation antigen CD80 Proteins 0.000 description 2
- 241000725303 Human immunodeficiency virus Species 0.000 description 2
- 108010064600 Intercellular Adhesion Molecule-3 Proteins 0.000 description 2
- 102100037871 Intercellular adhesion molecule 3 Human genes 0.000 description 2
- 102000014150 Interferons Human genes 0.000 description 2
- 108010050904 Interferons Proteins 0.000 description 2
- 102000000589 Interleukin-1 Human genes 0.000 description 2
- 108010002352 Interleukin-1 Proteins 0.000 description 2
- 102000004557 Interleukin-18 Receptors Human genes 0.000 description 2
- 108010017537 Interleukin-18 Receptors Proteins 0.000 description 2
- 102000010789 Interleukin-2 Receptors Human genes 0.000 description 2
- 108010038453 Interleukin-2 Receptors Proteins 0.000 description 2
- 102100026878 Interleukin-2 receptor subunit alpha Human genes 0.000 description 2
- 108010002386 Interleukin-3 Proteins 0.000 description 2
- 102100039064 Interleukin-3 Human genes 0.000 description 2
- 102000010787 Interleukin-4 Receptors Human genes 0.000 description 2
- 108010038486 Interleukin-4 Receptors Proteins 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- 102000004058 Leukemia inhibitory factor Human genes 0.000 description 2
- 108090000581 Leukemia inhibitory factor Proteins 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 102100034256 Mucin-1 Human genes 0.000 description 2
- 102000004140 Oncostatin M Human genes 0.000 description 2
- 108090000630 Oncostatin M Proteins 0.000 description 2
- 102000003982 Parathyroid hormone Human genes 0.000 description 2
- 108090000445 Parathyroid hormone Proteins 0.000 description 2
- 108010038036 Receptor Activator of Nuclear Factor-kappa B Proteins 0.000 description 2
- 102000010498 Receptor Activator of Nuclear Factor-kappa B Human genes 0.000 description 2
- 102100027222 T-lymphocyte activation antigen CD80 Human genes 0.000 description 2
- 108010000449 TNF-Related Apoptosis-Inducing Ligand Receptors Proteins 0.000 description 2
- 102000002259 TNF-Related Apoptosis-Inducing Ligand Receptors Human genes 0.000 description 2
- 102100040245 Tumor necrosis factor receptor superfamily member 5 Human genes 0.000 description 2
- -1 WO 01/36637) Proteins 0.000 description 2
- 102000013529 alpha-Fetoproteins Human genes 0.000 description 2
- 108010026331 alpha-Fetoproteins Proteins 0.000 description 2
- 229910021529 ammonia Inorganic materials 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- RYYVLZVUVIJVGH-UHFFFAOYSA-N caffeine Chemical compound CN1C(=O)N(C)C(=O)C2=C1N=CN2C RYYVLZVUVIJVGH-UHFFFAOYSA-N 0.000 description 2
- 230000022131 cell cycle Effects 0.000 description 2
- 230000004663 cell proliferation Effects 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 210000001072 colon Anatomy 0.000 description 2
- 238000010960 commercial process Methods 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 230000001976 improved effect Effects 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 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 2
- 238000012007 large scale cell culture Methods 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 239000012092 media component Substances 0.000 description 2
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 2
- 238000005457 optimization Methods 0.000 description 2
- 229960001319 parathyroid hormone Drugs 0.000 description 2
- 239000000199 parathyroid hormone Substances 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 238000004062 sedimentation Methods 0.000 description 2
- 235000002639 sodium chloride Nutrition 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 230000000153 supplemental effect Effects 0.000 description 2
- 230000002459 sustained effect Effects 0.000 description 2
- 235000013343 vitamin Nutrition 0.000 description 2
- 229940088594 vitamin Drugs 0.000 description 2
- 239000011782 vitamin Substances 0.000 description 2
- 229930003231 vitamin Natural products 0.000 description 2
- MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 1
- RTQWWZBSTRGEAV-PKHIMPSTSA-N 2-[[(2s)-2-[bis(carboxymethyl)amino]-3-[4-(methylcarbamoylamino)phenyl]propyl]-[2-[bis(carboxymethyl)amino]propyl]amino]acetic acid Chemical compound CNC(=O)NC1=CC=C(C[C@@H](CN(CC(C)N(CC(O)=O)CC(O)=O)CC(O)=O)N(CC(O)=O)CC(O)=O)C=C1 RTQWWZBSTRGEAV-PKHIMPSTSA-N 0.000 description 1
- MJZJYWCQPMNPRM-UHFFFAOYSA-N 6,6-dimethyl-1-[3-(2,4,5-trichlorophenoxy)propoxy]-1,6-dihydro-1,3,5-triazine-2,4-diamine Chemical compound CC1(C)N=C(N)N=C(N)N1OCCCOC1=CC(Cl)=C(Cl)C=C1Cl MJZJYWCQPMNPRM-UHFFFAOYSA-N 0.000 description 1
- 108091007505 ADAM17 Proteins 0.000 description 1
- 230000005730 ADP ribosylation Effects 0.000 description 1
- 108010054404 Adenylyl-sulfate kinase Proteins 0.000 description 1
- 102100034608 Angiopoietin-2 Human genes 0.000 description 1
- 108010048036 Angiopoietin-2 Proteins 0.000 description 1
- 102100029470 Apolipoprotein E Human genes 0.000 description 1
- 101710095339 Apolipoprotein E Proteins 0.000 description 1
- 102000007592 Apolipoproteins Human genes 0.000 description 1
- 108010071619 Apolipoproteins Proteins 0.000 description 1
- 108010070255 Aspartate-ammonia ligase Proteins 0.000 description 1
- 102100022005 B-lymphocyte antigen CD20 Human genes 0.000 description 1
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 1
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 102000004219 Brain-derived neurotrophic factor Human genes 0.000 description 1
- 108090000715 Brain-derived neurotrophic factor 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
- 101710167766 C-type lectin domain family 11 member A Proteins 0.000 description 1
- 102100032528 C-type lectin domain family 11 member A Human genes 0.000 description 1
- 108010008629 CA-125 Antigen Proteins 0.000 description 1
- 102000007269 CA-125 Antigen Human genes 0.000 description 1
- 102100024217 CAMPATH-1 antigen Human genes 0.000 description 1
- 108010046080 CD27 Ligand Proteins 0.000 description 1
- 102100027207 CD27 antigen Human genes 0.000 description 1
- 108010017987 CD30 Ligand Proteins 0.000 description 1
- 102100032912 CD44 antigen Human genes 0.000 description 1
- 108010065524 CD52 Antigen Proteins 0.000 description 1
- 102100025221 CD70 antigen Human genes 0.000 description 1
- 102000055006 Calcitonin Human genes 0.000 description 1
- 108060001064 Calcitonin Proteins 0.000 description 1
- 102000013602 Cardiac Myosins Human genes 0.000 description 1
- 108010051609 Cardiac Myosins Proteins 0.000 description 1
- 108010055166 Chemokine CCL5 Proteins 0.000 description 1
- 102000001327 Chemokine CCL5 Human genes 0.000 description 1
- 102100022641 Coagulation factor IX Human genes 0.000 description 1
- 206010009944 Colon cancer Diseases 0.000 description 1
- 108010071942 Colony-Stimulating Factors Proteins 0.000 description 1
- 102000007644 Colony-Stimulating Factors Human genes 0.000 description 1
- 108010028773 Complement C5 Proteins 0.000 description 1
- 102100039498 Cytotoxic T-lymphocyte protein 4 Human genes 0.000 description 1
- 102000010170 Death domains Human genes 0.000 description 1
- 108050001718 Death domains Proteins 0.000 description 1
- 101800001224 Disintegrin Proteins 0.000 description 1
- 102100031111 Disintegrin and metalloproteinase domain-containing protein 17 Human genes 0.000 description 1
- 102000001301 EGF receptor Human genes 0.000 description 1
- 108060006698 EGF receptor Proteins 0.000 description 1
- 102100029722 Ectonucleoside triphosphate diphosphohydrolase 1 Human genes 0.000 description 1
- 101800003838 Epidermal growth factor Proteins 0.000 description 1
- 108010008165 Etanercept Proteins 0.000 description 1
- 108010076282 Factor IX Proteins 0.000 description 1
- 108010054218 Factor VIII Proteins 0.000 description 1
- 102000001690 Factor VIII Human genes 0.000 description 1
- 102000009109 Fc receptors Human genes 0.000 description 1
- 108010087819 Fc receptors Proteins 0.000 description 1
- 102000003972 Fibroblast growth factor 7 Human genes 0.000 description 1
- 108090000385 Fibroblast growth factor 7 Proteins 0.000 description 1
- 230000005526 G1 to G0 transition Effects 0.000 description 1
- 208000032612 Glial tumor Diseases 0.000 description 1
- 206010018338 Glioma Diseases 0.000 description 1
- 102400000321 Glucagon Human genes 0.000 description 1
- 108060003199 Glucagon Proteins 0.000 description 1
- 108010017544 Glucosylceramidase Proteins 0.000 description 1
- 102000004547 Glucosylceramidase Human genes 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 description 1
- 102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 description 1
- 108010054017 Granulocyte Colony-Stimulating Factor Receptors Proteins 0.000 description 1
- 102100039622 Granulocyte colony-stimulating factor receptor Human genes 0.000 description 1
- 102000016355 Granulocyte-Macrophage Colony-Stimulating Factor Receptors Human genes 0.000 description 1
- 108010092372 Granulocyte-Macrophage Colony-Stimulating Factor Receptors Proteins 0.000 description 1
- 108010051696 Growth Hormone Proteins 0.000 description 1
- 241000700721 Hepatitis B virus Species 0.000 description 1
- 108090000100 Hepatocyte Growth Factor Proteins 0.000 description 1
- 102100021866 Hepatocyte growth factor Human genes 0.000 description 1
- 101000897405 Homo sapiens B-lymphocyte antigen CD20 Proteins 0.000 description 1
- 101000914511 Homo sapiens CD27 antigen Proteins 0.000 description 1
- 101000868273 Homo sapiens CD44 antigen Proteins 0.000 description 1
- 101000889276 Homo sapiens Cytotoxic T-lymphocyte protein 4 Proteins 0.000 description 1
- 101001012447 Homo sapiens Ectonucleoside triphosphate diphosphohydrolase 1 Proteins 0.000 description 1
- 101000935040 Homo sapiens Integrin beta-2 Proteins 0.000 description 1
- 101001057504 Homo sapiens Interferon-stimulated gene 20 kDa protein Proteins 0.000 description 1
- 101001055144 Homo sapiens Interleukin-2 receptor subunit alpha Proteins 0.000 description 1
- 101000878605 Homo sapiens Low affinity immunoglobulin epsilon Fc receptor Proteins 0.000 description 1
- 101000934338 Homo sapiens Myeloid cell surface antigen CD33 Proteins 0.000 description 1
- 101001012157 Homo sapiens Receptor tyrosine-protein kinase erbB-2 Proteins 0.000 description 1
- 101000851376 Homo sapiens Tumor necrosis factor receptor superfamily member 8 Proteins 0.000 description 1
- 102100023915 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 1
- 108010008212 Integrin alpha4beta1 Proteins 0.000 description 1
- 102100025390 Integrin beta-2 Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 102000019223 Interleukin-1 receptor Human genes 0.000 description 1
- 108050006617 Interleukin-1 receptor Proteins 0.000 description 1
- 102000003814 Interleukin-10 Human genes 0.000 description 1
- 108090000174 Interleukin-10 Proteins 0.000 description 1
- 102000004556 Interleukin-15 Receptors Human genes 0.000 description 1
- 108010017535 Interleukin-15 Receptors Proteins 0.000 description 1
- 102000004554 Interleukin-17 Receptors Human genes 0.000 description 1
- 108010017525 Interleukin-17 Receptors Proteins 0.000 description 1
- 102000004388 Interleukin-4 Human genes 0.000 description 1
- 108090000978 Interleukin-4 Proteins 0.000 description 1
- 108010002616 Interleukin-5 Proteins 0.000 description 1
- 102000000743 Interleukin-5 Human genes 0.000 description 1
- 102000010781 Interleukin-6 Receptors Human genes 0.000 description 1
- 108010038501 Interleukin-6 Receptors Proteins 0.000 description 1
- 108010002586 Interleukin-7 Proteins 0.000 description 1
- 102000000704 Interleukin-7 Human genes 0.000 description 1
- 108090001007 Interleukin-8 Proteins 0.000 description 1
- 102000004890 Interleukin-8 Human genes 0.000 description 1
- 102000015696 Interleukins Human genes 0.000 description 1
- 108010063738 Interleukins Proteins 0.000 description 1
- 239000007760 Iscove's Modified Dulbecco's Medium Substances 0.000 description 1
- LPHGQDQBBGAPDZ-UHFFFAOYSA-N Isocaffeine Natural products CN1C(=O)N(C)C(=O)C2=C1N(C)C=N2 LPHGQDQBBGAPDZ-UHFFFAOYSA-N 0.000 description 1
- 208000008839 Kidney Neoplasms Diseases 0.000 description 1
- 108010092694 L-Selectin Proteins 0.000 description 1
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 1
- 102100033467 L-selectin Human genes 0.000 description 1
- JVTAAEKCZFNVCJ-UHFFFAOYSA-M Lactate Chemical compound CC(O)C([O-])=O JVTAAEKCZFNVCJ-UHFFFAOYSA-M 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 102100038007 Low affinity immunoglobulin epsilon Fc receptor Human genes 0.000 description 1
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 1
- 102000003959 Lymphotoxin-beta Human genes 0.000 description 1
- 108090000362 Lymphotoxin-beta Proteins 0.000 description 1
- 101710132836 Membrane primary amine oxidase Proteins 0.000 description 1
- 102000005741 Metalloproteases Human genes 0.000 description 1
- 108010006035 Metalloproteases Proteins 0.000 description 1
- 101000845218 Mus musculus Thymic stromal lymphopoietin Proteins 0.000 description 1
- 102100025243 Myeloid cell surface antigen CD33 Human genes 0.000 description 1
- BNQSTAOJRULKNX-UHFFFAOYSA-N N-(6-acetamidohexyl)acetamide Chemical compound CC(=O)NCCCCCCNC(C)=O BNQSTAOJRULKNX-UHFFFAOYSA-N 0.000 description 1
- 108010025020 Nerve Growth Factor Proteins 0.000 description 1
- 102000015336 Nerve Growth Factor Human genes 0.000 description 1
- 206010029260 Neuroblastoma Diseases 0.000 description 1
- 108090000742 Neurotrophin 3 Proteins 0.000 description 1
- 102100029268 Neurotrophin-3 Human genes 0.000 description 1
- 108010035042 Osteoprotegerin Proteins 0.000 description 1
- 206010061902 Pancreatic neoplasm Diseases 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 102000015795 Platelet Membrane Glycoproteins Human genes 0.000 description 1
- 108010010336 Platelet Membrane Glycoproteins Proteins 0.000 description 1
- 102100033237 Pro-epidermal growth factor Human genes 0.000 description 1
- 102000001253 Protein Kinase Human genes 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- 102100030086 Receptor tyrosine-protein kinase erbB-2 Human genes 0.000 description 1
- 206010038389 Renal cancer Diseases 0.000 description 1
- 108050006698 Sclerostin Proteins 0.000 description 1
- 102100034201 Sclerostin Human genes 0.000 description 1
- 102000013275 Somatomedins Human genes 0.000 description 1
- 102100038803 Somatotropin Human genes 0.000 description 1
- 102100039024 Sphingosine kinase 1 Human genes 0.000 description 1
- 108010039445 Stem Cell Factor Proteins 0.000 description 1
- 241000194019 Streptococcus mutans Species 0.000 description 1
- 102000019197 Superoxide Dismutase Human genes 0.000 description 1
- 108010012715 Superoxide dismutase Proteins 0.000 description 1
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 description 1
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 1
- 102100032100 Tumor necrosis factor ligand superfamily member 8 Human genes 0.000 description 1
- 102100032236 Tumor necrosis factor receptor superfamily member 11B Human genes 0.000 description 1
- 102100036857 Tumor necrosis factor receptor superfamily member 8 Human genes 0.000 description 1
- 108091008605 VEGF receptors Proteins 0.000 description 1
- 102000009484 Vascular Endothelial Growth Factor Receptors Human genes 0.000 description 1
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 1
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 229960000446 abciximab Drugs 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 229960002964 adalimumab Drugs 0.000 description 1
- 238000004115 adherent culture Methods 0.000 description 1
- 230000001464 adherent effect Effects 0.000 description 1
- 229960000548 alemtuzumab Drugs 0.000 description 1
- 102000015395 alpha 1-Antitrypsin Human genes 0.000 description 1
- 108010050122 alpha 1-Antitrypsin Proteins 0.000 description 1
- 229940024142 alpha 1-antitrypsin Drugs 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000002518 antifoaming agent Substances 0.000 description 1
- 230000006907 apoptotic process Effects 0.000 description 1
- 229950001863 bapineuzumab Drugs 0.000 description 1
- 229960004669 basiliximab Drugs 0.000 description 1
- 229960005347 belatacept Drugs 0.000 description 1
- 229960003270 belimumab Drugs 0.000 description 1
- 229960000397 bevacizumab Drugs 0.000 description 1
- 230000002051 biphasic effect Effects 0.000 description 1
- 239000003114 blood coagulation factor Substances 0.000 description 1
- 229940077737 brain-derived neurotrophic factor Drugs 0.000 description 1
- 210000000481 breast Anatomy 0.000 description 1
- 229960002874 briakinumab Drugs 0.000 description 1
- 229960001948 caffeine Drugs 0.000 description 1
- VJEONQKOZGKCAK-UHFFFAOYSA-N caffeine Natural products CN1C(=O)N(C)C(=O)C2=C1C=CN2C VJEONQKOZGKCAK-UHFFFAOYSA-N 0.000 description 1
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 1
- 229960004015 calcitonin Drugs 0.000 description 1
- 229960001838 canakinumab Drugs 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 229940077731 carbohydrate nutrients Drugs 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 229910002092 carbon dioxide Inorganic materials 0.000 description 1
- 239000001569 carbon dioxide Substances 0.000 description 1
- 230000025084 cell cycle arrest Effects 0.000 description 1
- 230000011712 cell development Effects 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 229960003115 certolizumab pegol Drugs 0.000 description 1
- 229960005395 cetuximab Drugs 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 208000029742 colonic neoplasm Diseases 0.000 description 1
- 229940047120 colony stimulating factors Drugs 0.000 description 1
- 238000012777 commercial manufacturing Methods 0.000 description 1
- 229950007276 conatumumab Drugs 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 229960001251 denosumab Drugs 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 229960002224 eculizumab Drugs 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 229940116977 epidermal growth factor Drugs 0.000 description 1
- 229960000403 etanercept Drugs 0.000 description 1
- 230000003203 everyday effect Effects 0.000 description 1
- 229960004222 factor ix Drugs 0.000 description 1
- 229960000301 factor viii Drugs 0.000 description 1
- 239000012091 fetal bovine serum Substances 0.000 description 1
- 108700014844 flt3 ligand Proteins 0.000 description 1
- 238000005187 foaming Methods 0.000 description 1
- 239000012737 fresh medium Substances 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 230000006251 gamma-carboxylation Effects 0.000 description 1
- 229960003297 gemtuzumab ozogamicin Drugs 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 102000018146 globin Human genes 0.000 description 1
- 108060003196 globin Proteins 0.000 description 1
- 229960004666 glucagon Drugs 0.000 description 1
- MASNOZXLGMXCHN-ZLPAWPGGSA-N glucagon Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 MASNOZXLGMXCHN-ZLPAWPGGSA-N 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 229960001743 golimumab Drugs 0.000 description 1
- 239000000122 growth hormone Substances 0.000 description 1
- 238000012787 harvest procedure Methods 0.000 description 1
- 108010037896 heparin-binding hemagglutinin Proteins 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 102000056133 human AOC3 Human genes 0.000 description 1
- 102000051284 human FGL2 Human genes 0.000 description 1
- 230000033444 hydroxylation Effects 0.000 description 1
- 238000005805 hydroxylation reaction Methods 0.000 description 1
- 229960001001 ibritumomab tiuxetan Drugs 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 238000012606 in vitro cell culture Methods 0.000 description 1
- 229960000598 infliximab Drugs 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 108010043603 integrin alpha4beta7 Proteins 0.000 description 1
- 108010044426 integrins Proteins 0.000 description 1
- 102000006495 integrins Human genes 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 229960003130 interferon gamma Drugs 0.000 description 1
- 229940047122 interleukins Drugs 0.000 description 1
- 201000010982 kidney cancer Diseases 0.000 description 1
- 229950000518 labetuzumab Drugs 0.000 description 1
- 150000002605 large molecules Chemical class 0.000 description 1
- 238000011031 large-scale manufacturing process Methods 0.000 description 1
- 230000002045 lasting effect Effects 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 201000005202 lung cancer Diseases 0.000 description 1
- 208000020816 lung neoplasm Diseases 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 208000015486 malignant pancreatic neoplasm Diseases 0.000 description 1
- 229950001869 mapatumumab Drugs 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 229950008001 matuzumab Drugs 0.000 description 1
- 238000011177 media preparation Methods 0.000 description 1
- 201000001441 melanoma Diseases 0.000 description 1
- 229960005108 mepolizumab Drugs 0.000 description 1
- 239000007758 minimum essential medium Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 229960001521 motavizumab Drugs 0.000 description 1
- 229960003816 muromonab-cd3 Drugs 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 229960005027 natalizumab Drugs 0.000 description 1
- 230000001338 necrotic effect Effects 0.000 description 1
- 229940053128 nerve growth factor Drugs 0.000 description 1
- 229940032018 neurotrophin 3 Drugs 0.000 description 1
- 229950010203 nimotuzumab Drugs 0.000 description 1
- 238000010899 nucleation Methods 0.000 description 1
- 235000021232 nutrient availability Nutrition 0.000 description 1
- XXUPLYBCNPLTIW-UHFFFAOYSA-N octadec-7-ynoic acid Chemical compound CCCCCCCCCCC#CCCCCCC(O)=O XXUPLYBCNPLTIW-UHFFFAOYSA-N 0.000 description 1
- 229960002450 ofatumumab Drugs 0.000 description 1
- 229960000470 omalizumab Drugs 0.000 description 1
- 229950007283 oregovomab Drugs 0.000 description 1
- 229960000402 palivizumab Drugs 0.000 description 1
- 201000002528 pancreatic cancer Diseases 0.000 description 1
- 208000008443 pancreatic carcinoma Diseases 0.000 description 1
- 229960001972 panitumumab Drugs 0.000 description 1
- 229960005570 pemtumomab Drugs 0.000 description 1
- 229960002087 pertuzumab Drugs 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- GCYXWQUSHADNBF-AAEALURTSA-N preproglucagon 78-108 Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC=1N=CNC=1)[C@@H](C)O)[C@@H](C)O)C(C)C)C1=CC=CC=C1 GCYXWQUSHADNBF-AAEALURTSA-N 0.000 description 1
- 238000004886 process control Methods 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 108060006633 protein kinase Proteins 0.000 description 1
- 238000005086 pumping Methods 0.000 description 1
- 229960003876 ranibizumab Drugs 0.000 description 1
- 239000002464 receptor antagonist Substances 0.000 description 1
- 229940044551 receptor antagonist Drugs 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000000241 respiratory effect Effects 0.000 description 1
- 229960004641 rituximab Drugs 0.000 description 1
- 238000005096 rolling process Methods 0.000 description 1
- 229950009092 rovelizumab Drugs 0.000 description 1
- 238000011218 seed culture Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000011343 solid material Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 230000019635 sulfation Effects 0.000 description 1
- 238000005670 sulfation reaction Methods 0.000 description 1
- 230000003319 supportive effect Effects 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000004114 suspension culture Methods 0.000 description 1
- 101150047061 tag-72 gene Proteins 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 239000003104 tissue culture media Substances 0.000 description 1
- 229960000187 tissue plasminogen activator Drugs 0.000 description 1
- 229960003989 tocilizumab Drugs 0.000 description 1
- 229960005267 tositumomab Drugs 0.000 description 1
- 239000011573 trace mineral Substances 0.000 description 1
- 235000013619 trace mineral Nutrition 0.000 description 1
- 230000002463 transducing effect Effects 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 229960000575 trastuzumab Drugs 0.000 description 1
- 238000003211 trypan blue cell staining Methods 0.000 description 1
- VBEQCZHXXJYVRD-GACYYNSASA-N uroanthelone Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)NCC(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(C)C)[C@@H](C)O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CS)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CS)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC(N)=O)C(C)C)[C@@H](C)CC)C1=CC=C(O)C=C1 VBEQCZHXXJYVRD-GACYYNSASA-N 0.000 description 1
- 229960003824 ustekinumab Drugs 0.000 description 1
- 239000013598 vector Substances 0.000 description 1
- 231100000747 viability assay Toxicity 0.000 description 1
- 238000003026 viability measurement method Methods 0.000 description 1
- 239000002699 waste material Substances 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
- 229950008250 zalutumumab Drugs 0.000 description 1
- 229950009002 zanolimumab Drugs 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
-
- 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
- C12N5/0037—Serum-free medium, which may still contain naturally-sourced components
-
- 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
- C12N5/06—Animal cells or tissues; Human cells or tissues
- C12N5/0602—Vertebrate cells
- C12N5/0603—Embryonic cells ; Embryoid bodies
- C12N5/0604—Whole embryos; Culture medium therefor
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/02—Preparation of peptides or proteins having a known sequence of two or more amino acids, e.g. glutathione
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/10—Immunoglobulins specific features characterized by their source of isolation or production
- C07K2317/14—Specific host cells or culture conditions, e.g. components, pH or temperature
-
- 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
- C12N2500/02—Atmosphere, e.g. low oxygen conditions
-
- 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
- C12N2500/30—Organic components
- C12N2500/32—Amino acids
-
- 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
- C12N2500/99—Serum-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
- C12N2510/00—Genetically modified cells
- C12N2510/02—Cells for production
-
- 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
- C12N2523/00—Culture process characterised by temperature
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Biotechnology (AREA)
- Biomedical Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Cell Biology (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Immunology (AREA)
- Gynecology & Obstetrics (AREA)
- Developmental Biology & Embryology (AREA)
- Reproductive Health (AREA)
- Analytical Chemistry (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Peptides Or Proteins (AREA)
Claims (22)
- PAT E NT K RAV1. Fremgangsmåde til dyrkning af pattedyrceller, der eksprimerer et rekombi-nant protein, omfattende: at etablere en pattedyrcellekultur i et serumfrit dyrkningsmedium i en bioreaktor ved at pode bioreaktoren med mindst 0,5 x 106 til 3,0 x 106celler/ml_ i et serumfrit dyrkningsmedium; at dyrke pattedyrcellerne under en vækstfase og at supplere dyrkningsmediet med bolusforsyninger af et serumfrit næringsmedium, at starte perfusion på eller omkring dag 5 til på eller omkring dag 9 af cellekulturen, og at bevare pattedyrcellerne under en produktionsfase ved perfusion med et serumfrit perfusionsmedium, hvor det pakkede cellevolumen under produktionsfasen er mindre end eller lig med 35%.
- 2. Fremgangsmåde ifølge krav 1, hvor perfusionen begynder på eller omkring dag 5 til på eller omkring dag 7 af cellekulturen.
- 3. Fremgangsmåde ifølge krav 1, hvor perfusionen begynder, når cellerne har nået en produktionsfase.
- 4. Fremgangsmåde ifølge krav 1, der endvidere omfatter (a) at inducere cellevækstarrest med L-asparaginudsultning efterfulgt af perfusion med et serumfrit perfusionsmedium med en L-asparagi nkoncentration på 5 mM eller mindre eller (b) at inducere cellevækstarrest ved perfusion med et serumfrit perfusionsmedium med en L-asparagi nkoncentration på 5 mM eller mindre.
- 5. Fremgangsmåde ifølge krav 4, hvor koncentrationen af L-asparagin i det serumfri perfusionsmedium er mindre end eller lig med 5 mM, mindre end eller lig med 4,0 mM, mindre end eller lig med 3,0 mM, mindre end eller lig med 2,0 mM, mindre end eller lig med 1,0 mM eller er 0 mM.
- 6. Fremgangsmåde ifølge krav 4(a), hvor L-asparaginkoncentrationen af cellekulturmediet overvåges forud for og under L-asparaginudsultningen.
- 7. Fremgangsmåde ifølge krav 1, hvor det pakkede cellevolumen er mindre end eller lig med 30%.
- 8. Fremgangsmåde ifølge krav 1, hvor den levende celletæthed af pattedyrcellekulturen ved et pakket cellevolumen mindre end eller lig med 35% er 10x106 levende celler/ml til 80x106 levende celler/ml, hvor den levende celletæthed af pattedyrcellekulturen fortrinsvis er 20x106 levende celler/ml til 30x106 levende celler/ml.
- 9. Fremgangsmåde ifølge krav 1, hvor perfusionen omfatter kontinuerlig perfusion.
- 10. Fremgangsmåde ifølge krav 1, hvor perfusionshastigheden er konstant.
- 11. Fremgangsmåde ifølge krav 1, hvor perfusion udføres (a) ved en hastighed på mindre end eller lig med 1,0 arbejdsvoluminer per dag eller (b) ved en hastighed, der stiger under produktionsfasen fra 0,25 arbejdsvolumen per dag til 1,0 arbejdsvolumen per dag under celledyrkningen.
- 12. Fremgangsmåde ifølge krav 1, hvor perfusion udføres ved en hastighed, der når 1,0 arbejdsvolumen per dag på dag 9 til dag 11 af cellekulturen, fortrinsvis på dag 10 af cellekulturen.
- 13. Fremgangsmåde ifølge krav 1, hvor bolusforsyningerne af serumfrit medium begynder på dag 3 eller dag 4 af cellekulturen.
- 14. Fremgangsmåde ifølge krav 1, hvor pattedyrcellekulturen etableres ved podning af bioreaktoren med mindst 0,5 x 106 til 1,5 x 106 celler/mL i et serumfrit dyrkningsmedium.
- 15. Fremgangsmåde ifølge krav 1, der endvidere omfatter et temperaturskifte fra 36°C til 31 °C eller fra 36°C til 33°C.
- 16. Fremgangsmåde ifølge krav 15, hvor temperaturskiftet sker ved overgangen mellem vækstfasen og produktionsfasen eller under produktionsfasen.
- 17. Fremgangsmåde ifølge krav 1, hvor perfusionen gennemføres ved vekslende tangentiel strøm.
- 18. Fremgangsmåde ifølge krav 1, hvor bioreaktoren har en kapacitet på mindst 500L, fortrinsvis mindst 500L til 2000L eller mindst 1000L til 2000L.
- 19. Fremgangsmåde ifølge krav 1, hvor pattedyrcellerne er kinesiske hamster-ovarieceller (CHO).
- 20. Fremgangsmåde ifølge krav 1, hvor det rekombinante protein er valgt blandt gruppen bestående af et humant antistof, et humaniseret antistof, et kimært antistof, et rekombinant fusionsprotein eller et cytokin.
- 21. Fremgangsmåde ifølge krav 1, der endvidere omfatter et trin med at høste det rekombinante protein, der er produceret af cellekulturen.
- 22. Fremgangsmåde ifølge krav 1, hvor det rekombinante protein, der er produceret af cellekulturen, renses og formuleres til en farmaceutisk acceptabel formulering.
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201161503737P | 2011-07-01 | 2011-07-01 | |
| PCT/US2012/045070 WO2013006479A2 (en) | 2011-07-01 | 2012-06-29 | Mammalian cell culture |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| DK2726600T3 true DK2726600T3 (da) | 2017-05-15 |
Family
ID=46579326
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK14187232.5T DK2837680T3 (da) | 2011-07-01 | 2012-06-29 | Mammaliacellekultur |
| DK12738674.6T DK2726600T3 (da) | 2011-07-01 | 2012-06-29 | Pattedyrcellekultur |
Family Applications Before (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DK14187232.5T DK2837680T3 (da) | 2011-07-01 | 2012-06-29 | Mammaliacellekultur |
Country Status (24)
| Country | Link |
|---|---|
| US (7) | US11292829B2 (da) |
| EP (2) | EP2726600B1 (da) |
| JP (1) | JP5897708B2 (da) |
| KR (7) | KR102358951B1 (da) |
| CN (2) | CN103827292B (da) |
| AU (5) | AU2012279230B2 (da) |
| BR (2) | BR112013033730B1 (da) |
| CA (2) | CA2838695C (da) |
| CL (2) | CL2013003792A1 (da) |
| CY (2) | CY1118863T1 (da) |
| DK (2) | DK2837680T3 (da) |
| EA (1) | EA039023B1 (da) |
| ES (2) | ES2625045T3 (da) |
| HK (2) | HK1206057A1 (da) |
| HU (2) | HUE033279T2 (da) |
| IL (5) | IL288509B2 (da) |
| LT (2) | LT2726600T (da) |
| MX (1) | MX351974B (da) |
| PL (2) | PL2726600T3 (da) |
| PT (2) | PT2837680T (da) |
| SG (1) | SG10201702537RA (da) |
| SI (2) | SI2837680T1 (da) |
| WO (1) | WO2013006479A2 (da) |
| ZA (1) | ZA201309372B (da) |
Families Citing this family (62)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SG10201510384UA (en) | 2006-09-13 | 2016-01-28 | Abbvie Inc | Cell culture improvements |
| US8911964B2 (en) | 2006-09-13 | 2014-12-16 | Abbvie Inc. | Fed-batch method of making human anti-TNF-alpha antibody |
| CA2738499A1 (en) | 2008-10-20 | 2010-04-29 | Abbott Laboratories | Viral inactivation during purification of antibodies |
| AU2009347206C1 (en) | 2008-10-20 | 2016-12-08 | Abbvie Inc. | Isolation and purification of antibodies using Protein A affinity chromatography |
| EP2702077A2 (en) | 2011-04-27 | 2014-03-05 | AbbVie Inc. | Methods for controlling the galactosylation profile of recombinantly-expressed proteins |
| CN103827292B (zh) * | 2011-07-01 | 2018-01-26 | 安姆根有限公司 | 哺乳动物细胞培养 |
| US10493151B2 (en) | 2011-10-18 | 2019-12-03 | Coherus Biosciences, Inc. | Etanercept formulations stabilized with sodium chloride |
| KR20140079491A (ko) | 2011-10-18 | 2014-06-26 | 코히러스 바이오사이언시즈, 인코포레이티드 | 당과 폴리올과의 배합물로 안정화된 에타너셉트 제형 |
| US9067990B2 (en) | 2013-03-14 | 2015-06-30 | Abbvie, Inc. | Protein purification using displacement chromatography |
| WO2013158273A1 (en) | 2012-04-20 | 2013-10-24 | Abbvie Inc. | Methods to modulate c-terminal lysine variant distribution |
| US9150645B2 (en) | 2012-04-20 | 2015-10-06 | Abbvie, Inc. | Cell culture methods to reduce acidic species |
| US9249182B2 (en) | 2012-05-24 | 2016-02-02 | Abbvie, Inc. | Purification of antibodies using hydrophobic interaction chromatography |
| AU2013290289B2 (en) | 2012-07-09 | 2018-03-29 | Coherus Biosciences, Inc. | Etanercept formulations exhibiting marked reduction in sub-visible particles |
| US9206390B2 (en) | 2012-09-02 | 2015-12-08 | Abbvie, Inc. | Methods to control protein heterogeneity |
| US9512214B2 (en) | 2012-09-02 | 2016-12-06 | Abbvie, Inc. | Methods to control protein heterogeneity |
| EP2895188B1 (en) | 2012-09-11 | 2017-11-15 | Coherus Biosciences, Inc. | Correctly folded etanercept in high purity and excellent yield |
| WO2014109858A1 (en) * | 2013-01-14 | 2014-07-17 | Amgen Inc. | Methods of using cell-cycle inhibitors to modulate one or more properties of a cell culture |
| CA2905010A1 (en) | 2013-03-12 | 2014-09-18 | Abbvie Inc. | Human antibodies that bind human tnf-alpha and methods of preparing the same |
| US9017687B1 (en) | 2013-10-18 | 2015-04-28 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same using displacement chromatography |
| WO2014151878A2 (en) | 2013-03-14 | 2014-09-25 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosacharides |
| WO2014159579A1 (en) | 2013-03-14 | 2014-10-02 | Abbvie Inc. | MUTATED ANTI-TNFα ANTIBODIES AND METHODS OF THEIR USE |
| TWI832345B (zh) | 2013-03-14 | 2024-02-11 | 美商安美基公司 | 用於增加重組蛋白質之甘露糖含量之方法 |
| CA2907771C (en) * | 2013-03-26 | 2023-01-10 | Coherus Biosciences, Inc. | Perfusion method for manufacturing etanercept |
| US9481901B2 (en) | 2013-05-30 | 2016-11-01 | Amgen Inc. | Methods for increasing mannose content of recombinant proteins |
| EP3052640A2 (en) | 2013-10-04 | 2016-08-10 | AbbVie Inc. | Use of metal ions for modulation of protein glycosylation profiles of recombinant proteins |
| US11390663B2 (en) | 2013-10-11 | 2022-07-19 | Regeneron Pharmaceuticals, Inc. | Metabolically optimized cell culture |
| US9085618B2 (en) | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
| US9181337B2 (en) | 2013-10-18 | 2015-11-10 | Abbvie, Inc. | Modulated lysine variant species compositions and methods for producing and using the same |
| US8946395B1 (en) | 2013-10-18 | 2015-02-03 | Abbvie Inc. | Purification of proteins using hydrophobic interaction chromatography |
| EP3063287A1 (en) * | 2013-10-31 | 2016-09-07 | Amgen Inc. | Use of monensin to regulate glycosylation of recombinant proteins |
| WO2015073884A2 (en) | 2013-11-15 | 2015-05-21 | Abbvie, Inc. | Glycoengineered binding protein compositions |
| EP3083933A1 (en) | 2013-12-20 | 2016-10-26 | Biogen MA Inc. | Use of perfusion seed cultures to improve biopharmaceutical fed-batch production capacity and product quality |
| EP3094735A1 (en) | 2014-01-13 | 2016-11-23 | Amgen Inc. | Regulating ornithine metabolism to manipulate the high mannose glycoform content of recombinant proteins |
| EA202092845A1 (ru) | 2014-01-30 | 2021-06-30 | Кохерус Байосайенсис, Инк. | Перфузионная среда |
| PL3152317T3 (pl) * | 2014-06-04 | 2019-08-30 | Amgen Inc. | Sposoby zbierania hodowli ssaczych komórek |
| TWI743024B (zh) | 2014-06-06 | 2021-10-21 | 美商健臻公司 | 灌注培養方法及其用途 |
| TWI707949B (zh) * | 2014-06-09 | 2020-10-21 | 美商健臻公司 | 種子罐培養法（ｓｅｅｄ ｔｒａｉｎ ｐｒｏｃｅｓｓｅｓ）及其用途 |
| JP6530171B2 (ja) * | 2014-09-09 | 2019-06-12 | 旭化成メディカル株式会社 | 培養産生物の回収方法 |
| CA2969225C (en) | 2014-12-01 | 2023-08-22 | Amgen Inc. | Process for manipulating the level of glycan content of a glycoprotein |
| KR102007930B1 (ko) | 2014-12-31 | 2019-08-06 | 주식회사 엘지화학 | 재조합 당단백질의 글리코실화 조절 방법 |
| CN105385731B (zh) * | 2015-12-25 | 2018-10-30 | 上海莱士血液制品股份有限公司 | 一种表达重组八因子的灌注培养方法 |
| MX2018008448A (es) * | 2016-01-06 | 2019-05-30 | Oncobiologics Inc | Reducción de especies de alto peso molecular, especies con carga ácida, y fragmentos en una composición de anticuerpo monoclonal. |
| AU2017213775A1 (en) | 2016-02-03 | 2018-08-16 | Outlook Therapeutics, Inc. | Buffer formulations for enhanced antibody stability |
| IL261411B2 (en) * | 2016-03-02 | 2024-03-01 | Lonza Ag | Improved fermentation process |
| EP3601584A1 (en) * | 2017-03-31 | 2020-02-05 | Boehringer Ingelheim International GmbH | Perfusion medium |
| US11702628B2 (en) | 2017-03-31 | 2023-07-18 | Boehringer Ingelheim International Gmbh | Perfusion medium for culturing mammalian cells and reducing cell bleed in a perfusion cell culture |
| AU2018313950A1 (en) | 2017-08-09 | 2020-02-13 | Juno Therapeutics, Inc. | Methods for producing genetically engineered cell compositions and related compositions |
| KR20200068697A (ko) | 2017-10-06 | 2020-06-15 | 론자 리미티드 | 라만 분광법을 사용하는 세포 배양의 자동 제어 |
| CN118580926A (zh) | 2017-10-16 | 2024-09-03 | 里珍纳龙药品有限公司 | 灌注生物反应器及相关使用方法 |
| CN112004824B (zh) * | 2017-12-08 | 2024-09-13 | 朱诺治疗学股份有限公司 | 生产工程化t细胞组合物的过程 |
| CA3099163A1 (en) | 2018-05-01 | 2019-11-07 | Amgen Inc. | Antibodies with modulated glycan profiles |
| RS65472B1 (sr) * | 2018-07-03 | 2024-05-31 | Bristol Myers Squibb Co | Postupak proizvodnje rekombinantnih proteina |
| AU2019419406B2 (en) | 2018-12-31 | 2023-05-18 | Repligen Corporation | Filter for mammalian cell culture perfusion and clarification with hydrophobic hollow fiber |
| KR20220066970A (ko) * | 2019-09-27 | 2022-05-24 | 베링거 인겔하임 인터내셔날 게엠베하 | 농축 관류식 배지 |
| WO2022036275A2 (en) * | 2020-08-14 | 2022-02-17 | Bristol-Myers Squibb Company | Manufacturing process for protein |
| MX2023002417A (es) * | 2020-08-31 | 2023-03-22 | Regeneron Pharma | Estrategias de suministro de asparagina para mejorar el rendimiento del cultivo celular y mitigar las variantes de secuencia de asparagina. |
| JP2023542924A (ja) | 2020-09-22 | 2023-10-12 | ブリストル－マイヤーズ スクイブ カンパニー | 治療タンパク質を生産するための方法 |
| CN114574430A (zh) * | 2022-03-22 | 2022-06-03 | 成都博宠生物科技有限公司 | 一种Expi293F细胞培养方法 |
| CN115287251A (zh) * | 2022-08-25 | 2022-11-04 | 无锡药明生物技术股份有限公司 | 间歇性灌流联合分批流加培养 |
| US20240076709A1 (en) | 2022-09-06 | 2024-03-07 | Amgen Inc. | Lean perfusion cell culture methods |
| WO2024059235A2 (en) | 2022-09-16 | 2024-03-21 | Amgen Inc. | A method for harvesting products from perfusion cultures |
| CN116790483B (zh) * | 2023-08-22 | 2023-10-20 | 苏州依科赛生物科技股份有限公司 | 一种cho细胞无血清培养基及其应用 |
Family Cites Families (64)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6936694B1 (en) | 1982-05-06 | 2005-08-30 | Intermune, Inc. | Manufacture and expression of large structural genes |
| US4499064A (en) | 1982-06-03 | 1985-02-12 | Clayton Foundation For Research | Assessment of nutritional status of individuals |
| AU588819B2 (en) | 1984-10-29 | 1989-09-28 | Immunex Corporation | Cloning of human granulocyte-macrophage colony stimulating factor gene |
| US5672502A (en) | 1985-06-28 | 1997-09-30 | Celltech Therapeutics Limited | Animal cell culture |
| US4816401A (en) * | 1985-09-09 | 1989-03-28 | University Of Rochester | Serum free cell culture medium |
| US5045468A (en) | 1986-12-12 | 1991-09-03 | Cell Enterprises, Inc. | Protein-free culture medium which promotes hybridoma growth |
| US4968607A (en) | 1987-11-25 | 1990-11-06 | Immunex Corporation | Interleukin-1 receptors |
| US5075222A (en) | 1988-05-27 | 1991-12-24 | Synergen, Inc. | Interleukin-1 inhibitors |
| AU643427B2 (en) | 1988-10-31 | 1993-11-18 | Immunex Corporation | Interleukin-4 receptors |
| US5143842A (en) * | 1988-11-01 | 1992-09-01 | The University Of Colorado Foundation, Inc. | Media for normal human muscle satellite cells |
| US5395760A (en) | 1989-09-05 | 1995-03-07 | Immunex Corporation | DNA encoding tumor necrosis factor-α and -β receptors |
| EP0939121B2 (de) | 1989-09-12 | 2007-12-26 | AHP Manufacturing B.V. | TFN-bindende Proteine |
| US6204363B1 (en) | 1989-10-16 | 2001-03-20 | Amgen Inc. | Stem cell factor |
| US5272064A (en) | 1989-12-19 | 1993-12-21 | Amgen Inc. | DNA molecules encoding platelet-derived growth factor B chain analogs and method for expression thereof |
| US5149792A (en) | 1989-12-19 | 1992-09-22 | Amgen Inc. | Platelet-derived growth factor B chain analogs |
| US5292655A (en) * | 1990-01-29 | 1994-03-08 | Wille Jr John J | Method for the formation of a histologically-complete skin substitute |
| US7037721B1 (en) * | 1990-01-29 | 2006-05-02 | Hy-Gene Biomedical, Inc. | Protein-free defined media for the growth of normal human keratinocytes |
| WO1991018982A1 (en) | 1990-06-05 | 1991-12-12 | Immunex Corporation | Type ii interleukin-1 receptors |
| US5350683A (en) | 1990-06-05 | 1994-09-27 | Immunex Corporation | DNA encoding type II interleukin-1 receptors |
| GB9118664D0 (en) | 1991-08-30 | 1991-10-16 | Celltech Ltd | Cell culture |
| CA2146559A1 (en) | 1992-10-23 | 1994-05-11 | Melanie K. Spriggs | Methods of preparing soluble, oligomeric proteins |
| US5554512A (en) | 1993-05-24 | 1996-09-10 | Immunex Corporation | Ligands for flt3 receptors |
| US6310185B1 (en) | 1994-03-08 | 2001-10-30 | Memorial Sloan Kettering Cancer Center | Recombinant human anti-Lewis Y antibodies |
| US5856179A (en) | 1994-03-10 | 1999-01-05 | Genentech, Inc. | Polypeptide production in animal cell culture |
| US5981713A (en) | 1994-10-13 | 1999-11-09 | Applied Research Systems Ars Holding N.V. | Antibodies to intereleukin-1 antagonists |
| CA2225378C (en) | 1995-06-29 | 2012-04-17 | Immunex Corporation | Cytokine that induces apoptosis |
| US6613544B1 (en) | 1995-12-22 | 2003-09-02 | Amgen Inc. | Osteoprotegerin |
| US6096728A (en) | 1996-02-09 | 2000-08-01 | Amgen Inc. | Composition and method for treating inflammatory diseases |
| EP2221361A3 (en) | 1996-08-30 | 2011-02-09 | Life Technologies Corporation | Method for producing a polypeptide in vitro in mammalian cells in a protein-free and serum-free culture medium |
| US6271349B1 (en) | 1996-12-23 | 2001-08-07 | Immunex Corporation | Receptor activator of NF-κB |
| US20020012991A1 (en) | 1997-04-07 | 2002-01-31 | Florence Chua Nee Ho Kit Fong | Cell culture media for enhanced protein production |
| US6235883B1 (en) | 1997-05-05 | 2001-05-22 | Abgenix, Inc. | Human monoclonal antibodies to epidermal growth factor receptor |
| US6337072B1 (en) | 1998-04-03 | 2002-01-08 | Hyseq, Inc. | Interleukin-1 receptor antagonist and recombinant production thereof |
| AU1920301A (en) | 1999-11-17 | 2001-05-30 | Immunex Corporation | Receptor activator of nf-kappa b |
| US6544424B1 (en) | 1999-12-03 | 2003-04-08 | Refined Technology Company | Fluid filtration system |
| US20030036505A1 (en) | 2000-09-25 | 2003-02-20 | Human Genome Sciences, Inc. | Signal transduction pathway component polynucleotides, polypeptides, antibodies and methods based thereon |
| WO2002101019A2 (en) | 2001-06-13 | 2002-12-19 | Genentech, Inc. | Methods of culturing animal cells and polypeptide production in animal cells |
| US7320789B2 (en) | 2001-09-26 | 2008-01-22 | Wyeth | Antibody inhibitors of GDF-8 and uses thereof |
| AU2003220529B2 (en) | 2002-03-27 | 2006-09-07 | Immunex Corporation | Methods for increasing polypeptide production |
| JP2007525984A (ja) * | 2004-03-05 | 2007-09-13 | ディーエスエム アイピー アセッツ ビー．ブイ． | 連続的灌流および交互接線流による細胞培養の方法 |
| CN1332024C (zh) * | 2004-06-09 | 2007-08-15 | 中国科学院大连化学物理研究所 | 一种海绵细胞的微载体三维培养方法 |
| EP2246075A1 (en) | 2004-07-07 | 2010-11-03 | Coloplast A/S | Preparation of hydrophilic coatings utilizing a 1,3-dioxolane compound |
| TWI374935B (en) * | 2004-08-27 | 2012-10-21 | Pfizer Ireland Pharmaceuticals | Production of α-abeta |
| TWI384069B (zh) * | 2004-08-27 | 2013-02-01 | Pfizer Ireland Pharmaceuticals | 多胜肽之製法 |
| AU2005302516A1 (en) * | 2004-10-29 | 2006-05-11 | Centocor, Inc. | Chemically defined media compositions |
| DK1885753T3 (da) * | 2005-06-03 | 2011-10-03 | Ares Trading Sa | Fremstilling af rekombinant II-18-proteiner |
| SI2041259T1 (sl) | 2006-07-14 | 2016-04-29 | Dpx Holdings B.V. | Izboljšan postopek kultiviranja celic |
| WO2008024769A2 (en) * | 2006-08-21 | 2008-02-28 | Raven Biotechnologies, Inc. | Intensified perfusion production method |
| KR101523782B1 (ko) | 2006-11-08 | 2015-05-28 | 와이어쓰 엘엘씨 | 세포 배양을 위한 합리적으로 설계된 배지 |
| WO2008154014A2 (en) | 2007-06-11 | 2008-12-18 | Amgen Inc. | A method for culturing mammalian cells to improve recombinant protein production |
| EP2188371B1 (en) | 2007-08-09 | 2017-12-20 | Wyeth LLC | Use of perfusion to enhance production of fed-batch cell culture in bioreactors |
| MX2011002638A (es) | 2008-09-15 | 2011-04-05 | Genentech Inc | Composiciones y metodos para regular osmolaridad celular. |
| CN101603026B (zh) * | 2009-06-19 | 2011-01-19 | 华东理工大学 | 适于动物细胞产品生产的无动物来源低蛋白培养基 |
| US8580554B2 (en) | 2009-07-31 | 2013-11-12 | Baxter International Inc. | Method of producing a polypeptide or virus of interest in a continuous cell culture |
| PT2459702T (pt) | 2009-07-31 | 2016-08-02 | Baxalta Inc | Meio de cultura de células para a expressão da proteína adamts |
| KR20180114966A (ko) | 2009-08-11 | 2018-10-19 | 제넨테크, 인크. | 글루타민-비함유 세포 배양 배지에서의 단백질의 생성 |
| DK2501822T3 (da) | 2009-11-17 | 2017-11-27 | Squibb & Sons Llc | Fremgangsmåder til forbedret proteinproduktion |
| WO2011065940A1 (en) | 2009-11-24 | 2011-06-03 | Biogen Idec Ma Inc. | Method of supplementing culture media to prevent undesirable amino acid substitutions |
| ES2692379T3 (es) * | 2010-11-01 | 2018-12-03 | Symphogen A/S | Anticuerpos anti-HER3 y composiciones |
| WO2012145682A1 (en) * | 2011-04-21 | 2012-10-26 | Amgen Inc. | A method for culturing mammalian cells to improve recombinant protein production |
| CN103827292B (zh) * | 2011-07-01 | 2018-01-26 | 安姆根有限公司 | 哺乳动物细胞培养 |
| TWI832345B (zh) | 2013-03-14 | 2024-02-11 | 美商安美基公司 | 用於增加重組蛋白質之甘露糖含量之方法 |
| EP3063287A1 (en) | 2013-10-31 | 2016-09-07 | Amgen Inc. | Use of monensin to regulate glycosylation of recombinant proteins |
| WO2017085602A1 (en) * | 2015-11-17 | 2017-05-26 | Pfizer Inc. | Media and fermentation methods for producing polysaccharides in bacterial cell culture |
-
2012
- 2012-06-29 CN CN201280032874.4A patent/CN103827292B/zh active Active
- 2012-06-29 KR KR1020207012533A patent/KR102358951B1/ko active IP Right Grant
- 2012-06-29 PT PT141872325T patent/PT2837680T/pt unknown
- 2012-06-29 SI SI201231761T patent/SI2837680T1/sl unknown
- 2012-06-29 SG SG10201702537RA patent/SG10201702537RA/en unknown
- 2012-06-29 KR KR1020237024499A patent/KR20230114317A/ko active IP Right Grant
- 2012-06-29 US US14/127,050 patent/US11292829B2/en active Active
- 2012-06-29 ES ES12738674.6T patent/ES2625045T3/es active Active
- 2012-06-29 EA EA201391826A patent/EA039023B1/ru unknown
- 2012-06-29 KR KR1020227003428A patent/KR102558247B1/ko active IP Right Grant
- 2012-06-29 WO PCT/US2012/045070 patent/WO2013006479A2/en active Application Filing
- 2012-06-29 IL IL288509A patent/IL288509B2/en unknown
- 2012-06-29 AU AU2012279230A patent/AU2012279230B2/en active Active
- 2012-06-29 CA CA2838695A patent/CA2838695C/en not_active Expired - Fee Related
- 2012-06-29 HU HUE12738674A patent/HUE033279T2/en unknown
- 2012-06-29 DK DK14187232.5T patent/DK2837680T3/da active
- 2012-06-29 KR KR1020167015700A patent/KR101857380B1/ko active IP Right Grant
- 2012-06-29 IL IL297998A patent/IL297998B2/en unknown
- 2012-06-29 PT PT127386746T patent/PT2726600T/pt unknown
- 2012-06-29 KR KR1020147001985A patent/KR101662412B1/ko active IP Right Grant
- 2012-06-29 SI SI201230945A patent/SI2726600T1/sl unknown
- 2012-06-29 LT LTEP12738674.6T patent/LT2726600T/lt unknown
- 2012-06-29 ES ES14187232T patent/ES2788132T3/es active Active
- 2012-06-29 LT LTEP14187232.5T patent/LT2837680T/lt unknown
- 2012-06-29 PL PL12738674T patent/PL2726600T3/pl unknown
- 2012-06-29 BR BR112013033730-3A patent/BR112013033730B1/pt active IP Right Grant
- 2012-06-29 BR BR122021007265-5A patent/BR122021007265B1/pt active IP Right Grant
- 2012-06-29 EP EP12738674.6A patent/EP2726600B1/en not_active Revoked
- 2012-06-29 PL PL14187232T patent/PL2837680T3/pl unknown
- 2012-06-29 KR KR1020187012639A patent/KR102108663B1/ko active IP Right Grant
- 2012-06-29 HU HUE14187232A patent/HUE049119T2/hu unknown
- 2012-06-29 KR KR1020237043604A patent/KR20240005106A/ko not_active Application Discontinuation
- 2012-06-29 IL IL310968A patent/IL310968A/en unknown
- 2012-06-29 JP JP2014519184A patent/JP5897708B2/ja active Active
- 2012-06-29 CA CA2952347A patent/CA2952347A1/en not_active Abandoned
- 2012-06-29 MX MX2013014937A patent/MX351974B/es active IP Right Grant
- 2012-06-29 EP EP14187232.5A patent/EP2837680B1/en active Active
- 2012-06-29 CN CN201711406697.2A patent/CN107988166B/zh active Active
- 2012-06-29 DK DK12738674.6T patent/DK2726600T3/da active
-
2013
- 2013-12-05 IL IL229803A patent/IL229803B/en active IP Right Grant
- 2013-12-10 ZA ZA2013/09372A patent/ZA201309372B/en unknown
- 2013-12-30 CL CL2013003792A patent/CL2013003792A1/es unknown
-
2014
- 2014-10-20 HK HK15106530.7A patent/HK1206057A1/xx unknown
- 2014-10-20 HK HK14110449A patent/HK1197081A1/xx unknown
-
2016
- 2016-05-18 CL CL2016001190A patent/CL2016001190A1/es unknown
- 2016-10-12 AU AU2016244255A patent/AU2016244255A1/en not_active Abandoned
-
2017
- 2017-03-22 CY CY20171100366T patent/CY1118863T1/el unknown
-
2018
- 2018-06-05 AU AU2018203972A patent/AU2018203972B2/en active Active
-
2020
- 2020-05-25 CY CY20201100473T patent/CY1123146T1/el unknown
- 2020-09-11 US US17/018,564 patent/US11673941B2/en active Active
- 2020-09-11 US US17/018,557 patent/US11634476B2/en active Active
- 2020-11-02 IL IL278430A patent/IL278430B/en unknown
- 2020-12-03 AU AU2020281075A patent/AU2020281075B2/en active Active
-
2022
- 2022-03-04 US US17/686,766 patent/US20220185869A1/en active Pending
- 2022-12-14 US US18/066,251 patent/US11685772B2/en active Active
- 2022-12-20 US US18/068,922 patent/US20230129523A1/en active Pending
-
2023
- 2023-02-24 AU AU2023201127A patent/AU2023201127A1/en active Pending
- 2023-03-08 US US18/180,828 patent/US11827692B2/en active Active
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US11685772B2 (en) | Mammalian cell culture | |
| EA045739B1 (ru) | Культивирование клеток млекопитающих |