MX2010011293A - Metodos para producir una proteina policlonal. - Google Patents
Metodos para producir una proteina policlonal.Info
- Publication number
- MX2010011293A MX2010011293A MX2010011293A MX2010011293A MX2010011293A MX 2010011293 A MX2010011293 A MX 2010011293A MX 2010011293 A MX2010011293 A MX 2010011293A MX 2010011293 A MX2010011293 A MX 2010011293A MX 2010011293 A MX2010011293 A MX 2010011293A
- Authority
- MX
- Mexico
- Prior art keywords
- cells
- protein
- polyclonal
- members
- different
- Prior art date
Links
- 108090000623 proteins and genes Proteins 0.000 title claims abstract description 330
- 102000004169 proteins and genes Human genes 0.000 title claims abstract description 305
- 238000000034 method Methods 0.000 title claims abstract description 124
- 238000004519 manufacturing process Methods 0.000 title claims abstract description 117
- 229940126534 drug product Drugs 0.000 claims abstract description 29
- 239000000825 pharmaceutical preparation Substances 0.000 claims abstract description 29
- 210000004027 cell Anatomy 0.000 claims description 322
- 239000000203 mixture Substances 0.000 claims description 73
- 230000014509 gene expression Effects 0.000 claims description 61
- 238000000746 purification Methods 0.000 claims description 44
- 239000002609 medium Substances 0.000 claims description 41
- 238000011081 inoculation Methods 0.000 claims description 32
- 239000013604 expression vector Substances 0.000 claims description 28
- 241000196324 Embryophyta Species 0.000 claims description 27
- 230000008569 process Effects 0.000 claims description 26
- 229940088679 drug related substance Drugs 0.000 claims description 24
- 238000010899 nucleation Methods 0.000 claims description 19
- 239000008186 active pharmaceutical agent Substances 0.000 claims description 18
- 238000004113 cell culture Methods 0.000 claims description 15
- 210000004962 mammalian cell Anatomy 0.000 claims description 13
- 239000001963 growth medium Substances 0.000 claims description 9
- 230000013595 glycosylation Effects 0.000 claims description 7
- 238000006206 glycosylation reaction Methods 0.000 claims description 7
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 6
- 241000233866 Fungi Species 0.000 claims description 5
- 238000003306 harvesting Methods 0.000 claims description 5
- 239000000126 substance Substances 0.000 claims description 5
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims description 4
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims description 4
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 4
- 239000004615 ingredient Substances 0.000 claims description 4
- 238000012258 culturing Methods 0.000 claims description 3
- 210000002950 fibroblast Anatomy 0.000 claims description 3
- 241000699802 Cricetulus griseus Species 0.000 claims description 2
- 206010035226 Plasma cell myeloma Diseases 0.000 claims description 2
- 241000251539 Vertebrata <Metazoa> Species 0.000 claims description 2
- 210000005260 human cell Anatomy 0.000 claims description 2
- 201000000050 myeloid neoplasm Diseases 0.000 claims description 2
- 210000001672 ovary Anatomy 0.000 claims description 2
- 210000001691 amnion Anatomy 0.000 claims 1
- 238000011143 downstream manufacturing Methods 0.000 abstract 1
- 238000011144 upstream manufacturing Methods 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 259
- 239000000047 product Substances 0.000 description 46
- 238000012545 processing Methods 0.000 description 24
- 238000002156 mixing Methods 0.000 description 21
- 239000006228 supernatant Substances 0.000 description 20
- 230000012010 growth Effects 0.000 description 18
- 108090000765 processed proteins & peptides Proteins 0.000 description 18
- 241001465754 Metazoa Species 0.000 description 17
- 108091008874 T cell receptors Proteins 0.000 description 16
- 238000004255 ion exchange chromatography Methods 0.000 description 16
- 239000003550 marker Substances 0.000 description 16
- 102000004196 processed proteins & peptides Human genes 0.000 description 16
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 15
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 15
- 150000001413 amino acids Chemical class 0.000 description 15
- 230000008901 benefit Effects 0.000 description 15
- 238000012512 characterization method Methods 0.000 description 14
- 229920001184 polypeptide Polymers 0.000 description 14
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 13
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 13
- 150000007523 nucleic acids Chemical group 0.000 description 13
- 235000002639 sodium chloride Nutrition 0.000 description 13
- 239000012634 fragment Substances 0.000 description 12
- 235000001014 amino acid Nutrition 0.000 description 11
- 239000000427 antigen Substances 0.000 description 11
- 108091007433 antigens Proteins 0.000 description 11
- 102000036639 antigens Human genes 0.000 description 11
- 238000002474 experimental method Methods 0.000 description 11
- 239000002054 inoculum Substances 0.000 description 11
- 230000010354 integration Effects 0.000 description 11
- 238000013411 master cell bank Methods 0.000 description 11
- 235000013336 milk Nutrition 0.000 description 11
- 239000008267 milk Substances 0.000 description 11
- 210000004080 milk Anatomy 0.000 description 11
- 108060003951 Immunoglobulin Proteins 0.000 description 10
- 102000018358 immunoglobulin Human genes 0.000 description 10
- 238000001890 transfection Methods 0.000 description 10
- 230000009261 transgenic effect Effects 0.000 description 10
- 108020004414 DNA Proteins 0.000 description 9
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 9
- 238000010257 thawing Methods 0.000 description 9
- 230000006978 adaptation Effects 0.000 description 8
- 238000005277 cation exchange chromatography Methods 0.000 description 8
- 230000010261 cell growth Effects 0.000 description 8
- 235000013601 eggs Nutrition 0.000 description 8
- 239000011780 sodium chloride Substances 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 108020004684 Internal Ribosome Entry Sites Proteins 0.000 description 7
- 238000001042 affinity chromatography Methods 0.000 description 7
- 238000004458 analytical method Methods 0.000 description 7
- 238000010923 batch production Methods 0.000 description 7
- 239000006285 cell suspension Substances 0.000 description 7
- 238000004587 chromatography analysis Methods 0.000 description 7
- 230000004048 modification Effects 0.000 description 7
- 238000012986 modification Methods 0.000 description 7
- 108020004707 nucleic acids Proteins 0.000 description 7
- 102000039446 nucleic acids Human genes 0.000 description 7
- 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 6
- 238000002835 absorbance Methods 0.000 description 6
- 230000027455 binding Effects 0.000 description 6
- 238000005352 clarification Methods 0.000 description 6
- 238000009826 distribution Methods 0.000 description 6
- 239000012467 final product Substances 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 238000011084 recovery Methods 0.000 description 6
- 210000002966 serum Anatomy 0.000 description 6
- 239000000725 suspension Substances 0.000 description 6
- 239000013598 vector Substances 0.000 description 6
- 108091026890 Coding region Proteins 0.000 description 5
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 5
- 238000002965 ELISA Methods 0.000 description 5
- 229930182816 L-glutamine Natural products 0.000 description 5
- 241000124008 Mammalia Species 0.000 description 5
- 210000000349 chromosome Anatomy 0.000 description 5
- 239000000356 contaminant Substances 0.000 description 5
- 238000001212 derivatisation Methods 0.000 description 5
- 239000013613 expression plasmid Substances 0.000 description 5
- 239000008103 glucose Substances 0.000 description 5
- 210000000056 organ Anatomy 0.000 description 5
- 150000003839 salts Chemical class 0.000 description 5
- 238000012360 testing method Methods 0.000 description 5
- 230000001225 therapeutic effect Effects 0.000 description 5
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 229910000831 Steel Inorganic materials 0.000 description 4
- 239000003242 anti bacterial agent Substances 0.000 description 4
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 4
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 239000003795 chemical substances by application Substances 0.000 description 4
- 238000011038 discontinuous diafiltration by volume reduction Methods 0.000 description 4
- 201000010099 disease Diseases 0.000 description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 4
- 239000003937 drug carrier Substances 0.000 description 4
- 238000001914 filtration Methods 0.000 description 4
- BRZYSWJRSDMWLG-CAXSIQPQSA-N geneticin Natural products O1C[C@@](O)(C)[C@H](NC)[C@@H](O)[C@H]1O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H]([C@@H](O)[C@H](O)[C@@H](C(C)O)O2)N)[C@@H](N)C[C@H]1N BRZYSWJRSDMWLG-CAXSIQPQSA-N 0.000 description 4
- -1 glucose or lactose) Chemical class 0.000 description 4
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 4
- 238000000338 in vitro Methods 0.000 description 4
- 239000012528 membrane Substances 0.000 description 4
- 239000001301 oxygen Substances 0.000 description 4
- 229910052760 oxygen Inorganic materials 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 230000001105 regulatory effect Effects 0.000 description 4
- 239000012679 serum free medium Substances 0.000 description 4
- 239000010959 steel Substances 0.000 description 4
- 238000012546 transfer Methods 0.000 description 4
- 241000271566 Aves Species 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 3
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 3
- 108010077544 Chromatin Proteins 0.000 description 3
- 102100024746 Dihydrofolate reductase Human genes 0.000 description 3
- 206010059866 Drug resistance Diseases 0.000 description 3
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 108091006027 G proteins Proteins 0.000 description 3
- 102000030782 GTP binding Human genes 0.000 description 3
- 108091000058 GTP-Binding Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 3
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 229910019142 PO4 Inorganic materials 0.000 description 3
- 102000004142 Trypsin Human genes 0.000 description 3
- 108090000631 Trypsin Proteins 0.000 description 3
- 229940088710 antibiotic agent Drugs 0.000 description 3
- 230000000890 antigenic effect Effects 0.000 description 3
- 238000013459 approach Methods 0.000 description 3
- 238000003556 assay Methods 0.000 description 3
- 239000002775 capsule Substances 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 3
- 210000003483 chromatin Anatomy 0.000 description 3
- 238000011210 chromatographic step Methods 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 230000002950 deficient Effects 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 239000012894 fetal calf serum Substances 0.000 description 3
- 102000005396 glutamine synthetase Human genes 0.000 description 3
- 108020002326 glutamine synthetase Proteins 0.000 description 3
- 239000003102 growth factor Substances 0.000 description 3
- 238000001727 in vivo Methods 0.000 description 3
- 239000007788 liquid Substances 0.000 description 3
- 239000012516 mab select resin Substances 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 125000003729 nucleotide group Chemical group 0.000 description 3
- 239000008188 pellet Substances 0.000 description 3
- 235000021317 phosphate Nutrition 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 239000004033 plastic Substances 0.000 description 3
- 230000008488 polyadenylation Effects 0.000 description 3
- 210000001236 prokaryotic cell Anatomy 0.000 description 3
- 238000003908 quality control method Methods 0.000 description 3
- 239000007974 sodium acetate buffer Substances 0.000 description 3
- 239000003826 tablet Substances 0.000 description 3
- 239000012588 trypsin Substances 0.000 description 3
- 238000000108 ultra-filtration Methods 0.000 description 3
- 239000011782 vitamin Substances 0.000 description 3
- 229930003231 vitamin Natural products 0.000 description 3
- 235000013343 vitamin Nutrition 0.000 description 3
- 229940088594 vitamin Drugs 0.000 description 3
- 238000012784 weak cation exchange Methods 0.000 description 3
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 108091008875 B cell receptors Proteins 0.000 description 2
- 101150074155 DHFR gene Proteins 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 2
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 2
- FBOZXECLQNJBKD-ZDUSSCGKSA-N L-methotrexate Chemical compound C=1N=C2N=C(N)N=C(N)C2=NC=1CN(C)C1=CC=C(C(=O)N[C@@H](CCC(O)=O)C(O)=O)C=C1 FBOZXECLQNJBKD-ZDUSSCGKSA-N 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- 241001529936 Murinae Species 0.000 description 2
- 102000007339 Nerve Growth Factor Receptors Human genes 0.000 description 2
- 108010032605 Nerve Growth Factor Receptors Proteins 0.000 description 2
- 241000725643 Respiratory syncytial virus Species 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 2
- 102000006601 Thymidine Kinase Human genes 0.000 description 2
- 108020004440 Thymidine kinase Proteins 0.000 description 2
- 108700019146 Transgenes Proteins 0.000 description 2
- 108010075344 Tryptophan synthase Proteins 0.000 description 2
- 241000700618 Vaccinia virus Species 0.000 description 2
- 108010084455 Zeocin Proteins 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 238000013019 agitation Methods 0.000 description 2
- 238000005571 anion exchange chromatography Methods 0.000 description 2
- 210000001106 artificial yeast chromosome Anatomy 0.000 description 2
- 230000008827 biological function Effects 0.000 description 2
- 239000012512 bulk drug substance Substances 0.000 description 2
- 230000001934 delay Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 230000000694 effects Effects 0.000 description 2
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 2
- 239000012527 feed solution Substances 0.000 description 2
- 239000000945 filler Substances 0.000 description 2
- 244000144992 flock Species 0.000 description 2
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 2
- 238000009472 formulation Methods 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 239000007789 gas Substances 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- KWIUHFFTVRNATP-UHFFFAOYSA-N glycine betaine Chemical compound C[N+](C)(C)CC([O-])=O KWIUHFFTVRNATP-UHFFFAOYSA-N 0.000 description 2
- 239000005090 green fluorescent protein Substances 0.000 description 2
- 244000144980 herd Species 0.000 description 2
- 238000013537 high throughput screening Methods 0.000 description 2
- 239000005556 hormone Substances 0.000 description 2
- 229940088597 hormone Drugs 0.000 description 2
- 238000012872 hydroxylapatite chromatography Methods 0.000 description 2
- FDGQSTZJBFJUBT-UHFFFAOYSA-N hypoxanthine Chemical compound O=C1NC=NC2=C1NC=N2 FDGQSTZJBFJUBT-UHFFFAOYSA-N 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection 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
- 239000002563 ionic surfactant Substances 0.000 description 2
- 239000000797 iron chelating agent Substances 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 238000011031 large-scale manufacturing process Methods 0.000 description 2
- 229960000485 methotrexate Drugs 0.000 description 2
- 239000002777 nucleoside Substances 0.000 description 2
- 125000003835 nucleoside group Chemical group 0.000 description 2
- 235000015097 nutrients Nutrition 0.000 description 2
- 239000008194 pharmaceutical composition Substances 0.000 description 2
- 239000000546 pharmaceutical excipient Substances 0.000 description 2
- CWCMIVBLVUHDHK-ZSNHEYEWSA-N phleomycin D1 Chemical compound N([C@H](C(=O)N[C@H](C)[C@@H](O)[C@H](C)C(=O)N[C@@H]([C@H](O)C)C(=O)NCCC=1SC[C@@H](N=1)C=1SC=C(N=1)C(=O)NCCCCNC(N)=N)[C@@H](O[C@H]1[C@H]([C@@H](O)[C@H](O)[C@H](CO)O1)O[C@@H]1[C@H]([C@@H](OC(N)=O)[C@H](O)[C@@H](CO)O1)O)C=1N=CNC=1)C(=O)C1=NC([C@H](CC(N)=O)NC[C@H](N)C(N)=O)=NC(N)=C1C CWCMIVBLVUHDHK-ZSNHEYEWSA-N 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- RXWNCPJZOCPEPQ-NVWDDTSBSA-N puromycin Chemical compound C1=CC(OC)=CC=C1C[C@H](N)C(=O)N[C@H]1[C@@H](O)[C@H](N2C3=NC=NC(=C3N=C2)N(C)C)O[C@@H]1CO RXWNCPJZOCPEPQ-NVWDDTSBSA-N 0.000 description 2
- 238000011002 quantification Methods 0.000 description 2
- 238000003259 recombinant expression Methods 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 238000010374 somatic cell nuclear transfer Methods 0.000 description 2
- 238000009331 sowing Methods 0.000 description 2
- 241000894007 species Species 0.000 description 2
- 238000003756 stirring Methods 0.000 description 2
- 239000000829 suppository Substances 0.000 description 2
- 238000004114 suspension culture Methods 0.000 description 2
- 239000003053 toxin Substances 0.000 description 2
- 231100000765 toxin Toxicity 0.000 description 2
- 239000011573 trace mineral Substances 0.000 description 2
- 235000013619 trace mineral Nutrition 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 238000003151 transfection method Methods 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 210000005253 yeast cell Anatomy 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- 108010024878 Adenovirus E1A Proteins Proteins 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical class [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- 101100005916 Arabidopsis thaliana CER3 gene Proteins 0.000 description 1
- 101100191603 Arabidopsis thaliana PRT6 gene Proteins 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 1
- 108010045123 Blasticidin-S deaminase Proteins 0.000 description 1
- 108010006654 Bleomycin Proteins 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 241000282836 Camelus dromedarius Species 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 208000024172 Cardiovascular disease Diseases 0.000 description 1
- 102000011632 Caseins Human genes 0.000 description 1
- 108010076119 Caseins Proteins 0.000 description 1
- 102000016289 Cell Adhesion Molecules Human genes 0.000 description 1
- 108010067225 Cell Adhesion Molecules Proteins 0.000 description 1
- 208000035473 Communicable disease Diseases 0.000 description 1
- 230000004544 DNA amplification Effects 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102400001368 Epidermal growth factor Human genes 0.000 description 1
- 101800003838 Epidermal growth factor Proteins 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 101001091269 Escherichia coli Hygromycin-B 4-O-kinase Proteins 0.000 description 1
- 241000287828 Gallus gallus Species 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101150003028 Hprt1 gene Proteins 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 108010091358 Hypoxanthine Phosphoribosyltransferase Proteins 0.000 description 1
- 102000018251 Hypoxanthine Phosphoribosyltransferase Human genes 0.000 description 1
- UGQMRVRMYYASKQ-UHFFFAOYSA-N Hypoxanthine nucleoside Natural products OC1C(O)C(CO)OC1N1C(NC=NC2=O)=C2N=C1 UGQMRVRMYYASKQ-UHFFFAOYSA-N 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 102000016844 Immunoglobulin-like domains Human genes 0.000 description 1
- 108050006430 Immunoglobulin-like domains Proteins 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 108010025815 Kanamycin Kinase Proteins 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- PWHULOQIROXLJO-UHFFFAOYSA-N Manganese Chemical compound [Mn] PWHULOQIROXLJO-UHFFFAOYSA-N 0.000 description 1
- 102000018697 Membrane Proteins Human genes 0.000 description 1
- 101100261636 Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) trpB2 gene Proteins 0.000 description 1
- 101000966481 Mus musculus Dihydrofolate reductase Proteins 0.000 description 1
- 101000969137 Mus musculus Metallothionein-1 Proteins 0.000 description 1
- 229930193140 Neomycin Natural products 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 102000007999 Nuclear Proteins Human genes 0.000 description 1
- 108010089610 Nuclear Proteins Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 238000010222 PCR analysis Methods 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000010292 Peptide Elongation Factor 1 Human genes 0.000 description 1
- 108010077524 Peptide Elongation Factor 1 Proteins 0.000 description 1
- 239000001888 Peptone Substances 0.000 description 1
- 108010080698 Peptones Proteins 0.000 description 1
- 101100124346 Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01) hisCD gene Proteins 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108010009736 Protein Hydrolysates Proteins 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- 101710197208 Regulatory protein cro Proteins 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- 244000061456 Solanum tuberosum Species 0.000 description 1
- 235000002595 Solanum tuberosum Nutrition 0.000 description 1
- 238000002105 Southern blotting Methods 0.000 description 1
- 101001091268 Streptomyces hygroscopicus Hygromycin-B 7''-O-kinase Proteins 0.000 description 1
- 108010022394 Threonine synthase Proteins 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 102000004338 Transferrin Human genes 0.000 description 1
- 108090000901 Transferrin Proteins 0.000 description 1
- 206010052779 Transplant rejections Diseases 0.000 description 1
- 206010046865 Vaccinia virus infection Diseases 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 108010027570 Xanthine phosphoribosyltransferase Proteins 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000004115 adherent culture Methods 0.000 description 1
- 239000000443 aerosol Substances 0.000 description 1
- 208000026935 allergic disease Diseases 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 239000003708 ampul Substances 0.000 description 1
- 235000021120 animal protein Nutrition 0.000 description 1
- 230000000340 anti-metabolite Effects 0.000 description 1
- 238000011091 antibody purification Methods 0.000 description 1
- 210000000628 antibody-producing cell Anatomy 0.000 description 1
- 229940100197 antimetabolite Drugs 0.000 description 1
- 239000002256 antimetabolite Substances 0.000 description 1
- 208000006673 asthma Diseases 0.000 description 1
- 238000013475 authorization Methods 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
- 229960003237 betaine Drugs 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 230000005540 biological transmission Effects 0.000 description 1
- 229930189065 blasticidin Natural products 0.000 description 1
- 229960001561 bleomycin Drugs 0.000 description 1
- OYVAGSVQBOHSSS-UAPAGMARSA-O bleomycin A2 Chemical compound N([C@H](C(=O)N[C@H](C)[C@@H](O)[C@H](C)C(=O)N[C@@H]([C@H](O)C)C(=O)NCCC=1SC=C(N=1)C=1SC=C(N=1)C(=O)NCCC[S+](C)C)[C@@H](O[C@H]1[C@H]([C@@H](O)[C@H](O)[C@H](CO)O1)O[C@@H]1[C@H]([C@@H](OC(N)=O)[C@H](O)[C@@H](CO)O1)O)C=1N=CNC=1)C(=O)C1=NC([C@H](CC(N)=O)NC[C@H](N)C(N)=O)=NC(N)=C1C OYVAGSVQBOHSSS-UAPAGMARSA-O 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 150000004649 carbonic acid derivatives Chemical class 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 210000003169 central nervous system Anatomy 0.000 description 1
- 239000013522 chelant Substances 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 235000013330 chicken meat Nutrition 0.000 description 1
- 238000011098 chromatofocusing Methods 0.000 description 1
- 238000010372 cloning stem cell Methods 0.000 description 1
- 238000003501 co-culture Methods 0.000 description 1
- 230000008045 co-localization Effects 0.000 description 1
- 238000012761 co-transfection Methods 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000010924 continuous production Methods 0.000 description 1
- 210000004246 corpus luteum Anatomy 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 238000009295 crossflow filtration Methods 0.000 description 1
- 108010057085 cytokine receptors Proteins 0.000 description 1
- 102000003675 cytokine receptors Human genes 0.000 description 1
- 239000007857 degradation product Substances 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 239000008121 dextrose Substances 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 102000004419 dihydrofolate reductase Human genes 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- AIUDWMLXCFRVDR-UHFFFAOYSA-N dimethyl 2-(3-ethyl-3-methylpentyl)propanedioate Chemical class CCC(C)(CC)CCC(C(=O)OC)C(=O)OC AIUDWMLXCFRVDR-UHFFFAOYSA-N 0.000 description 1
- 239000006185 dispersion Substances 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 239000003995 emulsifying agent Substances 0.000 description 1
- 230000002124 endocrine Effects 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 229940116977 epidermal growth factor Drugs 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 239000012526 feed medium Substances 0.000 description 1
- 230000001605 fetal effect Effects 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 238000000684 flow cytometry Methods 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 239000012737 fresh medium Substances 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 239000007903 gelatin capsule Substances 0.000 description 1
- 238000013340 harvest operation Methods 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 101150113423 hisD gene Proteins 0.000 description 1
- 230000003054 hormonal effect Effects 0.000 description 1
- 210000004408 hybridoma Anatomy 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 230000007233 immunological mechanism Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000007901 in situ hybridization Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 208000027866 inflammatory disease Diseases 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 230000006651 lactation Effects 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 239000008297 liquid dosage form Substances 0.000 description 1
- 239000011344 liquid material Substances 0.000 description 1
- 239000006193 liquid solution Substances 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 239000007937 lozenge Substances 0.000 description 1
- 239000011777 magnesium Substances 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 210000005075 mammary gland Anatomy 0.000 description 1
- 229910052748 manganese Inorganic materials 0.000 description 1
- 239000011572 manganese Substances 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 230000013011 mating Effects 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 239000012092 media component Substances 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- HPNSFSBZBAHARI-UHFFFAOYSA-N micophenolic acid Natural products OC1=C(CC=C(C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-UHFFFAOYSA-N 0.000 description 1
- 235000010755 mineral Nutrition 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 239000007758 minimum essential medium Substances 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 150000002772 monosaccharides Chemical class 0.000 description 1
- 229960000951 mycophenolic acid Drugs 0.000 description 1
- HPNSFSBZBAHARI-RUDMXATFSA-N mycophenolic acid Chemical compound OC1=C(C\C=C(/C)CCC(O)=O)C(OC)=C(C)C2=C1C(=O)OC2 HPNSFSBZBAHARI-RUDMXATFSA-N 0.000 description 1
- 238000001728 nano-filtration Methods 0.000 description 1
- 229960004927 neomycin Drugs 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 239000002674 ointment Substances 0.000 description 1
- 150000002482 oligosaccharides Polymers 0.000 description 1
- 210000000287 oocyte Anatomy 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 210000003463 organelle Anatomy 0.000 description 1
- 230000001033 osmoprotective effect Effects 0.000 description 1
- 230000008723 osmotic stress Effects 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 235000019319 peptone Nutrition 0.000 description 1
- 229940066779 peptones Drugs 0.000 description 1
- 230000010412 perfusion Effects 0.000 description 1
- 108010085336 phosphoribosyl-AMP cyclohydrolase Proteins 0.000 description 1
- 150000003013 phosphoric acid derivatives Chemical class 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000012910 preclinical development Methods 0.000 description 1
- 230000035935 pregnancy Effects 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 238000003672 processing method Methods 0.000 description 1
- 239000013587 production medium Substances 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 238000012514 protein characterization Methods 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 229950010131 puromycin Drugs 0.000 description 1
- 108010045647 puromycin N-acetyltransferase Proteins 0.000 description 1
- 230000002787 reinforcement Effects 0.000 description 1
- 208000023504 respiratory system disease Diseases 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 238000005070 sampling Methods 0.000 description 1
- 238000013341 scale-up Methods 0.000 description 1
- 239000012056 semi-solid material Substances 0.000 description 1
- 239000008299 semisolid dosage form Substances 0.000 description 1
- 239000000377 silicon dioxide Substances 0.000 description 1
- 238000007390 skin biopsy Methods 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000007909 solid dosage form Substances 0.000 description 1
- 239000011343 solid material Substances 0.000 description 1
- 238000003153 stable transfection Methods 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 210000000130 stem cell Anatomy 0.000 description 1
- 238000011146 sterile filtration Methods 0.000 description 1
- 239000012058 sterile packaged powder Substances 0.000 description 1
- 239000008223 sterile water Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 150000003467 sulfuric acid derivatives Chemical class 0.000 description 1
- 239000013595 supernatant sample Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 230000002459 sustained effect Effects 0.000 description 1
- AYEKOFBPNLCAJY-UHFFFAOYSA-O thiamine pyrophosphate Chemical compound CC1=C(CCOP(O)(=O)OP(O)(O)=O)SC=[N+]1CC1=CN=C(C)N=C1N AYEKOFBPNLCAJY-UHFFFAOYSA-O 0.000 description 1
- 125000003396 thiol group Chemical group [H]S* 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 230000009258 tissue cross reactivity Effects 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 239000012096 transfection reagent Substances 0.000 description 1
- 239000012581 transferrin Substances 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 238000003146 transient transfection Methods 0.000 description 1
- 230000014616 translation Effects 0.000 description 1
- 101150081616 trpB gene Proteins 0.000 description 1
- 101150111232 trpB-1 gene Proteins 0.000 description 1
- 230000034512 ubiquitination Effects 0.000 description 1
- 238000010798 ubiquitination 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
- 210000004291 uterus Anatomy 0.000 description 1
- 208000007089 vaccinia Diseases 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 238000009423 ventilation Methods 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- 108700026220 vif Genes Proteins 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 238000011179 visual inspection Methods 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 238000009736 wetting Methods 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- NWONKYPBYAMBJT-UHFFFAOYSA-L zinc sulfate Chemical compound [Zn+2].[O-]S([O-])(=O)=O NWONKYPBYAMBJT-UHFFFAOYSA-L 0.000 description 1
- 229960001763 zinc sulfate Drugs 0.000 description 1
- 229910000368 zinc sulfate Inorganic materials 0.000 description 1
- 235000021247 β-casein Nutrition 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- A61P11/06—Antiasthmatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/08—Antiallergic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P5/00—Drugs for disorders of the endocrine system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
- A61K2039/507—Comprising a combination of two or more separate antibodies
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- General Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Immunology (AREA)
- Pulmonology (AREA)
- Diabetes (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Cardiology (AREA)
- Obesity (AREA)
- Pain & Pain Management (AREA)
- Rheumatology (AREA)
- Biomedical Technology (AREA)
- Neurology (AREA)
- Neurosurgery (AREA)
- Hematology (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Heart & Thoracic Surgery (AREA)
- Endocrinology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US4738908P | 2008-04-23 | 2008-04-23 | |
| DKPA200800580 | 2008-04-23 | ||
| PCT/DK2009/050094 WO2009129814A1 (en) | 2008-04-23 | 2009-04-23 | Methods for manufacturing a polyclonal protein |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| MX2010011293A true MX2010011293A (es) | 2010-12-20 |
Family
ID=40091979
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MX2010011293A MX2010011293A (es) | 2008-04-23 | 2009-04-23 | Metodos para producir una proteina policlonal. |
Country Status (15)
| Country | Link |
|---|---|
| US (1) | US20110117605A1 (enExample) |
| EP (1) | EP2280998A1 (enExample) |
| JP (1) | JP2011518790A (enExample) |
| KR (1) | KR20110016899A (enExample) |
| CN (1) | CN102007146A (enExample) |
| AU (1) | AU2009240386A1 (enExample) |
| BR (1) | BRPI0910454A2 (enExample) |
| CA (1) | CA2722348A1 (enExample) |
| IL (1) | IL208163A0 (enExample) |
| MX (1) | MX2010011293A (enExample) |
| NZ (1) | NZ588651A (enExample) |
| RU (1) | RU2010147652A (enExample) |
| SG (1) | SG189793A1 (enExample) |
| WO (1) | WO2009129814A1 (enExample) |
| ZA (1) | ZA201006765B (enExample) |
Families Citing this family (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| MX2011001930A (es) * | 2008-08-29 | 2011-04-21 | Symphogen As | Metodo para clonar anticuerpos derivados de aves. |
| ES2692379T3 (es) | 2010-11-01 | 2018-12-03 | Symphogen A/S | Anticuerpos anti-HER3 y composiciones |
| CA2817751C (en) | 2010-11-16 | 2019-04-30 | Excelimmune, Inc. | Methods for producing recombinant proteins |
| WO2013164689A2 (en) | 2012-05-02 | 2013-11-07 | Lantto, Johan | Humanized pan-her antibody compositions |
| US20160289633A1 (en) * | 2013-12-20 | 2016-10-06 | Biogen Ma Inc. | Use of Perfusion Seed Cultures to Improve Biopharmaceutical Fed-Batch Production Capacity and Product Quality |
| WO2016042412A1 (en) | 2014-09-16 | 2016-03-24 | Symphogen A/S | Anti-met antibodies and compositions |
| DE102014220306B3 (de) * | 2014-10-07 | 2015-09-03 | Fraunhofer-Gesellschaft zur Förderung der angewandten Forschung e.V. | Automatisches Verfahren zur Beobachtung von Zellkulturwachstum |
| US11566082B2 (en) | 2014-11-17 | 2023-01-31 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| US10703774B2 (en) | 2016-09-30 | 2020-07-07 | Ge Healthcare Bioprocess R&D Ab | Separation method |
| US10654887B2 (en) | 2016-05-11 | 2020-05-19 | Ge Healthcare Bio-Process R&D Ab | Separation matrix |
| JP7031934B2 (ja) | 2016-05-11 | 2022-03-08 | サイティバ・バイオプロセス・アールアンドディ・アクチボラグ | 分離マトリックス |
| EP3455243B1 (en) | 2016-05-11 | 2021-03-24 | Cytiva BioProcess R&D AB | Separation matrix |
| US10730908B2 (en) | 2016-05-11 | 2020-08-04 | Ge Healthcare Bioprocess R&D Ab | Separation method |
| US10889615B2 (en) | 2016-05-11 | 2021-01-12 | Cytiva Bioprocess R&D Ab | Mutated immunoglobulin-binding polypeptides |
| ES2909833T3 (es) | 2016-05-11 | 2022-05-10 | Cytiva Bioprocess R & D Ab | Método de limpieza y/o desinfección de una matriz de separación |
| US11708390B2 (en) | 2016-05-11 | 2023-07-25 | Cytiva Bioprocess R&D Ab | Method of storing a separation matrix |
| US12448411B2 (en) | 2016-09-30 | 2025-10-21 | Cytiva Bioprocess R&D Ab | Separation method |
| CN110621698B (zh) | 2017-04-05 | 2024-04-12 | 法国施维雅药厂 | 靶向pd-1、tim-3及lag-3的组合疗法 |
| WO2019103976A1 (en) * | 2017-11-22 | 2019-05-31 | Culture Biosciences, Inc. | Fermentation automation workcell |
| US12071607B2 (en) * | 2018-06-01 | 2024-08-27 | Lonza Ltd. | Midscale model for organic growth and phasing |
| MA52945A (fr) | 2018-06-22 | 2021-04-28 | Genmab As | Procédé de production d'un mélange contrôlé d'au moins deux anticorps différents |
| WO2024240634A1 (en) | 2023-05-19 | 2024-11-28 | Les Laboratoires Servier | Anti-met antibodies, antibody-drug conjugates, compositions and uses thereof |
| US20250263653A1 (en) * | 2024-02-16 | 2025-08-21 | Lanzatech, Inc. | Methods and apparatus for the production of protein |
| KR102687341B1 (ko) * | 2024-04-09 | 2024-07-23 | 주식회사 휴온스랩 | 온전한 형태의 히알루로니다제의 생산방법 |
Family Cites Families (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DK1231268T3 (da) * | 1994-01-31 | 2005-11-21 | Univ Boston | Polyklonale antistofbiblioteker |
| EP1283720B1 (en) * | 2000-05-26 | 2007-04-18 | Symphogen A/S | Recombinant or purified polyclonal antibodies for treating allergy |
| US6849259B2 (en) * | 2000-06-16 | 2005-02-01 | Symphogen A/S | Polyclonal antibody composition for treating allergy |
| US6610472B1 (en) * | 2000-10-31 | 2003-08-26 | Genetastix Corporation | Assembly and screening of highly complex and fully human antibody repertoire in yeast |
| EP1337631A2 (en) * | 2000-11-28 | 2003-08-27 | Applied Molecular Evolution, Inc. | Eukaryotic expression libraries based on double lox recombination and methods of use |
| SI1523496T1 (sl) * | 2002-07-18 | 2011-11-30 | Merus B V | Rekombinantno proizvajanje zmesi protiteles |
| CA2512647C (en) * | 2003-01-07 | 2013-10-08 | Symphogen A/S | Method for manufacturing recombinant polyclonal proteins |
| US20060275766A1 (en) * | 2003-01-07 | 2006-12-07 | Haurum John S | Method for manufacturing recombinant polyclonal proteins |
| EP1706079B1 (en) * | 2003-08-14 | 2013-02-20 | ThromboGenics N.V. | Antibodies against factor viii with modified glycosylation in the variable region |
| RU2426795C2 (ru) * | 2004-07-20 | 2011-08-20 | Симфоген А/С | Способ структурной характеристики рекомбинантного поликлонального белка или поликлональной клеточной линии |
| BRPI0513706A (pt) * | 2004-07-20 | 2008-05-13 | Symphogen As | anticorpo policlonal recombinante anti-rhesus d e métodos de produção |
| US7612181B2 (en) * | 2005-08-19 | 2009-11-03 | Abbott Laboratories | Dual variable domain immunoglobulin and uses thereof |
| JP2009518320A (ja) * | 2005-12-05 | 2009-05-07 | シュムフォウエン アクティーゼルスカブ | 抗オルトポックスウイルス組換えポリクローナル抗体 |
| TW200846362A (en) * | 2007-02-09 | 2008-12-01 | Symphogen As | A polyclonal antibody product |
| NZ581316A (en) * | 2007-05-25 | 2012-02-24 | Symphogen As | Method for manufacturing a recombinant polyclonal protein |
-
2009
- 2009-04-23 BR BRPI0910454A patent/BRPI0910454A2/pt not_active IP Right Cessation
- 2009-04-23 KR KR1020107026241A patent/KR20110016899A/ko not_active Withdrawn
- 2009-04-23 US US12/989,340 patent/US20110117605A1/en not_active Abandoned
- 2009-04-23 CA CA2722348A patent/CA2722348A1/en not_active Abandoned
- 2009-04-23 WO PCT/DK2009/050094 patent/WO2009129814A1/en not_active Ceased
- 2009-04-23 SG SG2013028964A patent/SG189793A1/en unknown
- 2009-04-23 CN CN2009801131977A patent/CN102007146A/zh active Pending
- 2009-04-23 EP EP09734906A patent/EP2280998A1/en not_active Withdrawn
- 2009-04-23 NZ NZ588651A patent/NZ588651A/en not_active IP Right Cessation
- 2009-04-23 JP JP2011505362A patent/JP2011518790A/ja not_active Withdrawn
- 2009-04-23 RU RU2010147652/10A patent/RU2010147652A/ru not_active Application Discontinuation
- 2009-04-23 MX MX2010011293A patent/MX2010011293A/es active IP Right Grant
- 2009-04-23 AU AU2009240386A patent/AU2009240386A1/en not_active Abandoned
-
2010
- 2010-09-15 IL IL208163A patent/IL208163A0/en unknown
- 2010-09-21 ZA ZA2010/06765A patent/ZA201006765B/en unknown
Also Published As
| Publication number | Publication date |
|---|---|
| CN102007146A (zh) | 2011-04-06 |
| NZ588651A (en) | 2012-04-27 |
| IL208163A0 (en) | 2010-12-30 |
| WO2009129814A1 (en) | 2009-10-29 |
| RU2010147652A (ru) | 2012-05-27 |
| BRPI0910454A2 (pt) | 2018-03-27 |
| ZA201006765B (en) | 2012-03-28 |
| CA2722348A1 (en) | 2009-10-29 |
| EP2280998A1 (en) | 2011-02-09 |
| KR20110016899A (ko) | 2011-02-18 |
| SG189793A1 (en) | 2013-05-31 |
| JP2011518790A (ja) | 2011-06-30 |
| US20110117605A1 (en) | 2011-05-19 |
| AU2009240386A1 (en) | 2009-10-29 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| MX2010011293A (es) | Metodos para producir una proteina policlonal. | |
| KR101555658B1 (ko) | 재조합 폴리클로날 단백질의 제조 방법 | |
| JP4926054B2 (ja) | 抗−ＲｈＤ組換えポリクローナル抗体及び製造方法 | |
| AU734800B2 (en) | Production of a multimeric protein by cell fusion method | |
| MXPA05006724A (es) | Metodo para producir proteinas policlonales recombinantes. | |
| TWI821905B (zh) | 使用麩醯胺合成酶基因內互補載體直接選擇表現高水準異質蛋白的細胞 | |
| CA2609731A1 (en) | A method for the production of a monoclonal antibody to cd20 for the treatment of b-cell lymphoma | |
| TW200907059A (en) | Recombinant expression vector elements (rEVEs) for enhancing expression of recombinant proteins in host cells | |
| JP7267284B2 (ja) | ポリエーテルイオノフォアを使用するタンパク質マンノシル化プロファイルの調節方法 | |
| WO2004085474A2 (en) | Method of producing an antibody to epidermal growth factor receptor | |
| US20200299402A1 (en) | Methods of Controlling the Formation of Disulfide Bonds in Protein Solutions | |
| US20240239871A1 (en) | Hypersialylating cells | |
| US8529903B2 (en) | Anti-RhD monoclonal antibodies | |
| CN102498212B (zh) | Cho/cert细胞系 | |
| JP2019514411A (ja) | ペルアセチルガラクトースを使った組換えタンパク質のタンパク質ガラクトシル化プロファイルを改変する方法 | |
| US20060154334A1 (en) | Method of producing an antibody to epidermal growth factor receptor | |
| KR20250039513A (ko) | 래트 하이브리도마 세포에서 상업적 규모의 재조합 단백질 생산 | |
| CN111116749A (zh) | 重组的人源化gpc3抗体及其构建和应用 | |
| CN120322561A (zh) | 新型转座酶系统 | |
| HK40082650A (en) | Direct selection of cells expressing high levels of heteromeric proteins using glutamine synthetase intragenic complementation vectors | |
| EA043386B1 (ru) | Прямой отбор клеток, экспрессирующих высокие уровни гетеромерных белков, с использованием глутаминсинтетазных векторов внутригенной комплементации | |
| HK1134519B (en) | Method for manufacturing a recombinant polyclonal protein | |
| HK1167429A (en) | Cho/cert cell lines |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FG | Grant or registration |