ES2535734T3 - Aislamiento y purificación de anticuerpos mediante cromatografía de afinidad con la proteína A - Google Patents
Aislamiento y purificación de anticuerpos mediante cromatografía de afinidad con la proteína A Download PDFInfo
- Publication number
- ES2535734T3 ES2535734T3 ES09744006.9T ES09744006T ES2535734T3 ES 2535734 T3 ES2535734 T3 ES 2535734T3 ES 09744006 T ES09744006 T ES 09744006T ES 2535734 T3 ES2535734 T3 ES 2535734T3
- Authority
- ES
- Spain
- Prior art keywords
- sample
- antibody
- protein
- buffer
- antibodies
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 108090000623 proteins and genes Proteins 0.000 title abstract description 37
- 102000004169 proteins and genes Human genes 0.000 title abstract description 34
- 238000001042 affinity chromatography Methods 0.000 title abstract description 5
- 238000000746 purification Methods 0.000 title description 7
- 238000002955 isolation Methods 0.000 title 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 abstract description 31
- 239000000427 antigen Substances 0.000 abstract description 20
- 102000036639 antigens Human genes 0.000 abstract description 20
- 108091007433 antigens Proteins 0.000 abstract description 20
- 238000011084 recovery Methods 0.000 abstract description 19
- 238000000034 method Methods 0.000 abstract description 18
- 238000002360 preparation method Methods 0.000 abstract description 18
- 239000011780 sodium chloride Substances 0.000 abstract description 17
- 238000004191 hydrophobic interaction chromatography Methods 0.000 abstract description 16
- 239000000203 mixture Substances 0.000 abstract description 16
- 239000000872 buffer Substances 0.000 abstract description 15
- 239000011347 resin Substances 0.000 abstract description 9
- 229920005989 resin Polymers 0.000 abstract description 9
- 230000002829 reductive effect Effects 0.000 abstract description 7
- 238000005406 washing Methods 0.000 abstract description 7
- VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 abstract description 3
- 238000005342 ion exchange Methods 0.000 abstract description 3
- 238000004519 manufacturing process Methods 0.000 abstract description 3
- 230000020477 pH reduction Effects 0.000 abstract description 3
- 239000001632 sodium acetate Substances 0.000 abstract description 3
- 235000017281 sodium acetate Nutrition 0.000 abstract description 3
- NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 abstract 1
- 229940069078 citric acid / sodium citrate Drugs 0.000 abstract 1
- 239000003456 ion exchange resin Substances 0.000 abstract 1
- 229920003303 ion-exchange polymer Polymers 0.000 abstract 1
- 210000004027 cell Anatomy 0.000 description 39
- 239000000523 sample Substances 0.000 description 39
- 235000018102 proteins Nutrition 0.000 description 31
- 102000003810 Interleukin-18 Human genes 0.000 description 27
- 108090000171 Interleukin-18 Proteins 0.000 description 27
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 26
- 230000000694 effects Effects 0.000 description 23
- 239000000654 additive Substances 0.000 description 22
- 239000000243 solution Substances 0.000 description 20
- 230000000996 additive effect Effects 0.000 description 19
- 208000035475 disorder Diseases 0.000 description 18
- 238000004458 analytical method Methods 0.000 description 16
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 14
- 239000005018 casein Substances 0.000 description 13
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 13
- 235000021240 caseins Nutrition 0.000 description 13
- 239000000463 material Substances 0.000 description 13
- -1 for example Substances 0.000 description 12
- 238000011068 loading method Methods 0.000 description 12
- 108020004414 DNA Proteins 0.000 description 11
- 238000004364 calculation method Methods 0.000 description 10
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 9
- 229920002684 Sepharose Polymers 0.000 description 9
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 9
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 9
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 description 9
- 239000012086 standard solution Substances 0.000 description 9
- 239000011248 coating agent Substances 0.000 description 8
- 238000000576 coating method Methods 0.000 description 8
- 238000010790 dilution Methods 0.000 description 8
- 239000012895 dilution Substances 0.000 description 8
- 201000010099 disease Diseases 0.000 description 8
- 238000004128 high performance liquid chromatography Methods 0.000 description 8
- 239000012516 mab select resin Substances 0.000 description 8
- 108020004707 nucleic acids Proteins 0.000 description 8
- 102000039446 nucleic acids Human genes 0.000 description 8
- 150000007523 nucleic acids Chemical class 0.000 description 8
- 230000008569 process Effects 0.000 description 8
- 238000012546 transfer Methods 0.000 description 8
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 7
- 230000002209 hydrophobic effect Effects 0.000 description 7
- 230000003993 interaction Effects 0.000 description 7
- 239000012901 Milli-Q water Substances 0.000 description 6
- 229920004890 Triton X-100 Polymers 0.000 description 6
- 238000002835 absorbance Methods 0.000 description 6
- 239000007900 aqueous suspension Substances 0.000 description 6
- 239000013024 dilution buffer Substances 0.000 description 6
- 230000003287 optical effect Effects 0.000 description 6
- 238000003259 recombinant expression Methods 0.000 description 6
- 238000007789 sealing Methods 0.000 description 6
- 239000011534 wash buffer Substances 0.000 description 6
- 239000004743 Polypropylene Substances 0.000 description 5
- 238000004113 cell culture Methods 0.000 description 5
- 238000004587 chromatography analysis Methods 0.000 description 5
- 239000012470 diluted sample Substances 0.000 description 5
- 239000013604 expression vector Substances 0.000 description 5
- 230000003472 neutralizing effect Effects 0.000 description 5
- 108010087904 neutravidin Proteins 0.000 description 5
- 229920001155 polypropylene Polymers 0.000 description 5
- 150000003839 salts Chemical class 0.000 description 5
- 238000003756 stirring Methods 0.000 description 5
- 102000013462 Interleukin-12 Human genes 0.000 description 4
- 108010065805 Interleukin-12 Proteins 0.000 description 4
- 239000013504 Triton X-100 Substances 0.000 description 4
- 229960002964 adalimumab Drugs 0.000 description 4
- 230000008859 change Effects 0.000 description 4
- 238000005352 clarification Methods 0.000 description 4
- KNHUKKLJHYUCFP-UHFFFAOYSA-N clofibrate Chemical compound CCOC(=O)C(C)(C)OC1=CC=C(Cl)C=C1 KNHUKKLJHYUCFP-UHFFFAOYSA-N 0.000 description 4
- 238000001914 filtration Methods 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- 238000001556 precipitation Methods 0.000 description 4
- 239000011734 sodium Substances 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- 239000000758 substrate Substances 0.000 description 4
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 238000012855 HCP-ELISA Methods 0.000 description 3
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 3
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 3
- 230000004071 biological effect Effects 0.000 description 3
- 230000003196 chaotropic effect Effects 0.000 description 3
- 229940061607 dibasic sodium phosphate Drugs 0.000 description 3
- BNIILDVGGAEEIG-UHFFFAOYSA-L disodium hydrogen phosphate Chemical compound [Na+].[Na+].OP([O-])([O-])=O BNIILDVGGAEEIG-UHFFFAOYSA-L 0.000 description 3
- 238000010494 dissociation reaction Methods 0.000 description 3
- 230000005593 dissociations Effects 0.000 description 3
- 239000012535 impurity Substances 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 230000005764 inhibitory process Effects 0.000 description 3
- 230000000302 ischemic effect Effects 0.000 description 3
- 239000013627 low molecular weight specie Substances 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 239000012898 sample dilution Substances 0.000 description 3
- 238000001542 size-exclusion chromatography Methods 0.000 description 3
- 239000011550 stock solution Substances 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- 239000013598 vector Substances 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
- HNSDLXPSAYFUHK-UHFFFAOYSA-N 1,4-bis(2-ethylhexyl) sulfosuccinate Chemical compound CCCCC(CC)COC(=O)CC(S(O)(=O)=O)C(=O)OCC(CC)CCCC HNSDLXPSAYFUHK-UHFFFAOYSA-N 0.000 description 2
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- 208000023275 Autoimmune disease Diseases 0.000 description 2
- 101100028791 Caenorhabditis elegans pbs-5 gene Proteins 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 206010008909 Chronic Hepatitis Diseases 0.000 description 2
- 208000000668 Chronic Pancreatitis Diseases 0.000 description 2
- RTZKZFJDLAIYFH-UHFFFAOYSA-N Diethyl ether Chemical compound CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 2
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 241000287828 Gallus gallus Species 0.000 description 2
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
- 101000960954 Homo sapiens Interleukin-18 Proteins 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- 206010033645 Pancreatitis Diseases 0.000 description 2
- 206010033647 Pancreatitis acute Diseases 0.000 description 2
- 206010033649 Pancreatitis chronic Diseases 0.000 description 2
- 241001504519 Papio ursinus Species 0.000 description 2
- 241000288906 Primates Species 0.000 description 2
- 201000004681 Psoriasis Diseases 0.000 description 2
- 206010040047 Sepsis Diseases 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 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
- 206010052779 Transplant rejections Diseases 0.000 description 2
- 206010067584 Type 1 diabetes mellitus Diseases 0.000 description 2
- 239000002253 acid Substances 0.000 description 2
- 230000002378 acidificating effect Effects 0.000 description 2
- 201000003229 acute pancreatitis Diseases 0.000 description 2
- OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 2
- 150000001413 amino acids Chemical class 0.000 description 2
- 208000029028 brain injury Diseases 0.000 description 2
- 239000011575 calcium Substances 0.000 description 2
- 229920002301 cellulose acetate Polymers 0.000 description 2
- 239000003638 chemical reducing agent Substances 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 238000000855 fermentation Methods 0.000 description 2
- 230000004151 fermentation Effects 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 208000006454 hepatitis Diseases 0.000 description 2
- 210000003494 hepatocyte Anatomy 0.000 description 2
- 102000043959 human IL18 Human genes 0.000 description 2
- 125000001165 hydrophobic group Chemical group 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 230000002779 inactivation Effects 0.000 description 2
- 230000002757 inflammatory effect Effects 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
- 210000003292 kidney cell Anatomy 0.000 description 2
- 239000003446 ligand Substances 0.000 description 2
- 239000011777 magnesium Substances 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 201000006417 multiple sclerosis Diseases 0.000 description 2
- 208000010125 myocardial infarction Diseases 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 238000011002 quantification Methods 0.000 description 2
- 206010039073 rheumatoid arthritis Diseases 0.000 description 2
- 208000013223 septicemia Diseases 0.000 description 2
- JHJLBTNAGRQEKS-UHFFFAOYSA-M sodium bromide Chemical compound [Na+].[Br-] JHJLBTNAGRQEKS-UHFFFAOYSA-M 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 230000003612 virological effect Effects 0.000 description 2
- 238000012784 weak cation exchange Methods 0.000 description 2
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
- AXAVXPMQTGXXJZ-UHFFFAOYSA-N 2-aminoacetic acid;2-amino-2-(hydroxymethyl)propane-1,3-diol Chemical compound NCC(O)=O.OCC(N)(CO)CO AXAVXPMQTGXXJZ-UHFFFAOYSA-N 0.000 description 1
- GUPXYSSGJWIURR-UHFFFAOYSA-N 3-octoxypropane-1,2-diol Chemical compound CCCCCCCCOCC(O)CO GUPXYSSGJWIURR-UHFFFAOYSA-N 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonia chloride Chemical compound [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 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
- 206010006187 Breast cancer Diseases 0.000 description 1
- 239000002126 C01EB10 - Adenosine Substances 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 241000282465 Canis Species 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 241000282552 Chlorocebus aethiops Species 0.000 description 1
- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 101150074155 DHFR gene Proteins 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 102000009024 Epidermal Growth Factor Human genes 0.000 description 1
- 101800003838 Epidermal growth factor Proteins 0.000 description 1
- CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 0.000 description 1
- 229930182566 Gentamicin Natural products 0.000 description 1
- 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 1
- 239000007995 HEPES buffer Substances 0.000 description 1
- 108060003951 Immunoglobulin Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 208000022559 Inflammatory bowel disease Diseases 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 102000004560 Interleukin-12 Receptors Human genes 0.000 description 1
- 108010017515 Interleukin-12 Receptors Proteins 0.000 description 1
- 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 1
- FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 101000960949 Mus musculus Interleukin-18 Proteins 0.000 description 1
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
- 239000007832 Na2SO4 Substances 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241000282577 Pan troglodytes Species 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- 241000700157 Rattus norvegicus Species 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 239000012722 SDS sample buffer Substances 0.000 description 1
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 1
- UIIMBOGNXHQVGW-DEQYMQKBSA-M Sodium bicarbonate-14C Chemical compound [Na+].O[14C]([O-])=O UIIMBOGNXHQVGW-DEQYMQKBSA-M 0.000 description 1
- 102000004338 Transferrin Human genes 0.000 description 1
- 108090000901 Transferrin Proteins 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 244000000188 Vaccinium ovalifolium Species 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 230000001594 aberrant effect Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 229960005305 adenosine Drugs 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 125000000217 alkyl group Chemical group 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 235000019270 ammonium chloride Nutrition 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 230000009830 antibody antigen interaction Effects 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 230000009286 beneficial effect Effects 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
- 230000001588 bifunctional effect Effects 0.000 description 1
- 230000008033 biological extinction Effects 0.000 description 1
- 239000013060 biological fluid Substances 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 208000019065 cervical carcinoma Diseases 0.000 description 1
- 238000010382 chemical cross-linking Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 238000002967 competitive immunoassay Methods 0.000 description 1
- 229920001577 copolymer Polymers 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 238000007405 data analysis Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
- 238000004090 dissolution Methods 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 229940116977 epidermal growth factor Drugs 0.000 description 1
- 239000006167 equilibration buffer Substances 0.000 description 1
- 239000000706 filtrate Substances 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 229960002518 gentamicin Drugs 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 208000019622 heart disease Diseases 0.000 description 1
- 206010073071 hepatocellular carcinoma Diseases 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 239000013315 hypercross-linked polymer Substances 0.000 description 1
- 102000018358 immunoglobulin Human genes 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 150000002484 inorganic compounds Chemical class 0.000 description 1
- 229910010272 inorganic material Inorganic materials 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 239000012633 leachable Substances 0.000 description 1
- 230000003902 lesion Effects 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- 239000012160 loading buffer Substances 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 210000005265 lung cell Anatomy 0.000 description 1
- 229910052749 magnesium Inorganic materials 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 241001515942 marmosets Species 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 229960000485 methotrexate Drugs 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 239000004005 microsphere Substances 0.000 description 1
- 239000003607 modifier Substances 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 208000031225 myocardial ischemia Diseases 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 239000002773 nucleotide Substances 0.000 description 1
- 125000003729 nucleotide group Chemical group 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 238000012856 packing Methods 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 230000007310 pathophysiology Effects 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 210000002381 plasma Anatomy 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 230000035755 proliferation Effects 0.000 description 1
- 125000001436 propyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 239000012857 radioactive material Substances 0.000 description 1
- 230000001869 rapid Effects 0.000 description 1
- 238000001525 receptor binding assay Methods 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000005185 salting out Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 210000000717 sertoli cell Anatomy 0.000 description 1
- 210000002966 serum Anatomy 0.000 description 1
- 238000003998 size exclusion chromatography high performance liquid chromatography Methods 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 229910052938 sodium sulfate Inorganic materials 0.000 description 1
- 235000011152 sodium sulphate Nutrition 0.000 description 1
- VGTPCRGMBIAPIM-UHFFFAOYSA-M sodium thiocyanate Chemical compound [Na+].[S-]C#N VGTPCRGMBIAPIM-UHFFFAOYSA-M 0.000 description 1
- 238000001179 sorption measurement Methods 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 210000000130 stem cell Anatomy 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 210000001179 synovial fluid Anatomy 0.000 description 1
- 125000000999 tert-butyl group Chemical group [H]C([H])([H])C(*)(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 235000013619 trace mineral Nutrition 0.000 description 1
- 239000011573 trace mineral Substances 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 239000012581 transferrin Substances 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 229960004418 trolamine Drugs 0.000 description 1
- 238000000870 ultraviolet spectroscopy Methods 0.000 description 1
- 238000002211 ultraviolet spectrum 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
- 230000003313 weakening effect Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/241—Tumor Necrosis Factors
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/06—Antipsoriatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- 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
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- 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
- A61P37/02—Immunomodulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- 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
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/165—Extraction; Separation; Purification by chromatography mixed-mode chromatography
-
- 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
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/18—Ion-exchange chromatography
-
- 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
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/20—Partition-, reverse-phase or hydrophobic interaction chromatography
-
- 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
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/22—Affinity chromatography or related techniques based upon selective absorption processes
-
- 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
- C07K1/36—Extraction; Separation; Purification by a combination of two or more processes of different types
-
- 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
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/244—Interleukins [IL]
-
- 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
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/22—Immunoglobulins specific features characterized by taxonomic origin from camelids, e.g. camel, llama or dromedary
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S436/00—Chemistry: analytical and immunological testing
- Y10S436/824—Immunological separation techniques
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Immunology (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Analytical Chemistry (AREA)
- Diabetes (AREA)
- Rheumatology (AREA)
- Obesity (AREA)
- Emergency Medicine (AREA)
- Endocrinology (AREA)
- Hematology (AREA)
- Pain & Pain Management (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Physical Education & Sports Medicine (AREA)
- Dermatology (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US19675308P | 2008-10-20 | 2008-10-20 | |
| US196753P | 2008-10-20 | ||
| PCT/US2009/061329 WO2010141039A1 (en) | 2008-10-20 | 2009-10-20 | Isolation and purification of antibodies using protein a affinity chromatography |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2535734T3 true ES2535734T3 (es) | 2015-05-14 |
Family
ID=41835469
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES09744006.9T Active ES2535734T3 (es) | 2008-10-20 | 2009-10-20 | Aislamiento y purificación de anticuerpos mediante cromatografía de afinidad con la proteína A |
Country Status (18)
| Country | Link |
|---|---|
| US (5) | US8895709B2 (enExample) |
| EP (2) | EP2350127B1 (enExample) |
| JP (2) | JP5808249B2 (enExample) |
| KR (1) | KR20110091678A (enExample) |
| CN (2) | CN105111309A (enExample) |
| AU (4) | AU2009347206C1 (enExample) |
| BR (1) | BRPI0920027A2 (enExample) |
| CA (3) | CA2911256A1 (enExample) |
| ES (1) | ES2535734T3 (enExample) |
| HK (1) | HK1209428A1 (enExample) |
| IL (3) | IL211918A (enExample) |
| MX (3) | MX2011004200A (enExample) |
| NZ (1) | NZ592095A (enExample) |
| RU (1) | RU2520838C2 (enExample) |
| SG (1) | SG10201702922VA (enExample) |
| TW (2) | TW201024318A (enExample) |
| WO (1) | WO2010141039A1 (enExample) |
| ZA (1) | ZA201102523B (enExample) |
Families Citing this family (102)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2742268T3 (es) | 2007-12-26 | 2020-02-13 | Xencor Inc | Variantes de Fc con unión alterada a FcRn |
| KR20110091678A (ko) * | 2008-10-20 | 2011-08-12 | 아보트 러보러터리즈 | 단백질 a 친화성 크로마토그래피를 이용한 항체의 분리 및 정제 |
| NZ592097A (en) | 2008-10-20 | 2013-01-25 | Abbott Lab | Viral inactivation during purification of il-12 and il-18 antibodies |
| US9056265B2 (en) | 2009-06-05 | 2015-06-16 | Tenfold Technologies, LLC | Isolated bioactive compounds and method of use |
| US8262912B1 (en) * | 2009-06-05 | 2012-09-11 | Tenfold Technologies, LLC | Isolated bioactive compounds and method of use |
| CA2772653C (en) * | 2009-09-01 | 2019-06-25 | Genentech, Inc. | Enhanced protein purification through a modified protein a elution |
| SG10201508401TA (en) * | 2010-10-11 | 2015-11-27 | Abbvie Bahamas Ltd | Processes for purification of proteins |
| JP2013544524A (ja) | 2010-12-06 | 2013-12-19 | ターポン バイオシステムズ,インコーポレイテッド | 生物学的生成物の連続プロセス法 |
| US20120238730A1 (en) * | 2011-03-15 | 2012-09-20 | Abbott Laboratories | Integrated approach to the isolation and purification of antibodies |
| EP2702077A2 (en) | 2011-04-27 | 2014-03-05 | AbbVie Inc. | Methods for controlling the galactosylation profile of recombinantly-expressed proteins |
| JP6024025B2 (ja) * | 2011-05-02 | 2016-11-09 | イミューノメディクス、インコーポレイテッドImmunomedics, Inc. | 少容量投与用のアロタイプ選択抗体の限外濾過濃縮 |
| WO2012160536A1 (en) * | 2011-05-26 | 2012-11-29 | Dr Reddy's Laboratories Limited | Antibody purification |
| EP3210662A1 (en) * | 2011-06-08 | 2017-08-30 | Agency For Science, Technology And Research | Purification of biological products by constrained cohydration chromatography |
| EP2773439A4 (en) * | 2011-10-31 | 2015-07-01 | Merck Sharp & Dohme | CHROMATOGRAPHY METHOD FOR RESOLVING HETEROGENIC ANTIBODY AGGREGATES |
| AU2012340826A1 (en) * | 2011-11-21 | 2014-05-29 | Genentech, Inc. | Purification of anti-c-met antibodies |
| WO2013158273A1 (en) | 2012-04-20 | 2013-10-24 | Abbvie Inc. | Methods to modulate c-terminal lysine variant distribution |
| US9067990B2 (en) | 2013-03-14 | 2015-06-30 | Abbvie, Inc. | Protein purification using displacement chromatography |
| WO2013158279A1 (en) | 2012-04-20 | 2013-10-24 | Abbvie Inc. | Protein purification methods to reduce acidic species |
| BR112014028129A2 (pt) | 2012-05-14 | 2017-06-27 | Novo Nordisk As | soluções de proteína estabilizadas |
| US20130336957A1 (en) * | 2012-05-21 | 2013-12-19 | Abbvie, Inc. | Novel purification of human, humanized, or chimeric antibodies using protein a affinity chromatography |
| US20140154270A1 (en) * | 2012-05-21 | 2014-06-05 | Chen Wang | Purification of non-human antibodies using kosmotropic salt enhanced protein a affinity chromatography |
| WO2013176754A1 (en) | 2012-05-24 | 2013-11-28 | Abbvie Inc. | Novel purification of antibodies using hydrophobic interaction chromatography |
| JP2015520026A (ja) * | 2012-06-06 | 2015-07-16 | イー・エム・デイー・ミリポア・コーポレイシヨン | 溶媒抽出法で処理される低有機抽出物デプスフィルター媒体 |
| CN104411820B (zh) * | 2012-06-29 | 2017-05-03 | Emd密理博公司 | 在蛋白纯化过程中灭活病毒的方法 |
| BR112015004467A2 (pt) | 2012-09-02 | 2017-03-21 | Abbvie Inc | método para controlar a heterogeneidade de proteínas |
| US9512214B2 (en) | 2012-09-02 | 2016-12-06 | Abbvie, Inc. | Methods to control protein heterogeneity |
| WO2014034457A1 (ja) | 2012-09-03 | 2014-03-06 | 株式会社カネカ | ミックスモード抗体アフィニティー分離マトリックスとそれを用いた精製方法および標的分子 |
| MX2015003007A (es) | 2012-09-07 | 2015-06-05 | Coherus Biosciences Inc | Formulaciones acuosas estables de adalimumab. |
| WO2014102814A1 (en) * | 2012-12-31 | 2014-07-03 | Intas Biopharmaceuticals Limited | Process for the purification of fc fusion proteins |
| HK1219964A1 (zh) | 2013-03-08 | 2017-04-21 | Genzyme Corporation | 治疗性蛋白药物物质的整合连续制造 |
| CA2905010A1 (en) | 2013-03-12 | 2014-09-18 | Abbvie Inc. | Human antibodies that bind human tnf-alpha and methods of preparing the same |
| US10023608B1 (en) | 2013-03-13 | 2018-07-17 | Amgen Inc. | Protein purification methods to remove impurities |
| WO2014151878A2 (en) | 2013-03-14 | 2014-09-25 | Abbvie Inc. | Methods for modulating protein glycosylation profiles of recombinant protein therapeutics using monosaccharides and oligosacharides |
| US8921526B2 (en) | 2013-03-14 | 2014-12-30 | Abbvie, Inc. | Mutated anti-TNFα antibodies and methods of their use |
| 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 |
| EP2970375A1 (en) * | 2013-03-14 | 2016-01-20 | AbbVie Inc. | Low acidic species compositions and methods for producing the same using displacement chromatography |
| WO2014142882A1 (en) * | 2013-03-14 | 2014-09-18 | Abbvie Inc. | Protein purification using displacement chromatography |
| EP3395423B1 (en) * | 2013-03-14 | 2023-09-20 | Amgen Inc. | Removal of leaked affinity purification ligand |
| EP2997036B1 (en) | 2013-05-15 | 2021-03-03 | Medimmune Limited | Purification of recombinantly produced polypeptides |
| KR101569783B1 (ko) * | 2013-06-05 | 2015-11-19 | 한화케미칼 주식회사 | 항체의 정제 방법 |
| AR096713A1 (es) * | 2013-06-25 | 2016-01-27 | Cadila Healthcare Ltd | Proceso de purificación para anticuerpos monoclonales |
| CA2910770C (en) | 2013-07-12 | 2018-02-27 | Merck Patent Gmbh | Removal of fragments from a sample containing a target protein using activated carbon |
| BR112016004437A2 (pt) | 2013-09-13 | 2017-10-17 | Genentech Inc | métodos de imunoteste e de seleção de linhagem de células, anticorpos e kit |
| CN105722532A (zh) | 2013-09-13 | 2016-06-29 | 豪夫迈·罗氏有限公司 | 包含纯化的重组多肽的方法和组合物 |
| EP3048109A4 (en) * | 2013-09-17 | 2017-04-19 | Kaneka Corporation | Novel antibody purification method and antibody obtained therefrom, and novel antibody purification method using cation exchanger and antibody obtained therefrom |
| US9598667B2 (en) | 2013-10-04 | 2017-03-21 | Abbvie Inc. | Use of metal ions for modulation of protein glycosylation profiles of recombinant proteins |
| US10376582B2 (en) | 2013-10-16 | 2019-08-13 | Outlook Therapeutics, Inc. | Buffer formulations for enhanced antibody stability |
| 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 |
| US20150139988A1 (en) | 2013-11-15 | 2015-05-21 | Abbvie, Inc. | Glycoengineered binding protein compositions |
| CN106029682B (zh) * | 2013-12-27 | 2021-04-13 | 中外制药株式会社 | 等电点低的抗体的纯化方法 |
| TWI671312B (zh) | 2014-01-17 | 2019-09-11 | 美商健臻公司 | 無菌層析法及製法 |
| TWI709569B (zh) | 2014-01-17 | 2020-11-11 | 美商健臻公司 | 無菌層析樹脂及其用於製造方法的用途 |
| PT3116891T (pt) | 2014-03-10 | 2020-05-18 | Richter Gedeon Nyrt | Purificação de imunoglobulina utilizando passos de pré-limpeza |
| US10478498B2 (en) | 2014-06-20 | 2019-11-19 | Reform Biologics, Llc | Excipient compounds for biopolymer formulations |
| US20160074515A1 (en) | 2014-06-20 | 2016-03-17 | Reform Biologics, Llc | Viscosity-reducing excipient compounds for protein formulations |
| US11357857B2 (en) | 2014-06-20 | 2022-06-14 | Comera Life Sciences, Inc. | Excipient compounds for protein processing |
| US20170183376A1 (en) | 2014-06-24 | 2017-06-29 | Insight Biopharmaceuticals Ltd. | Methods of purifying antibodies |
| US10329323B2 (en) | 2014-07-25 | 2019-06-25 | The United States Of America, As Represented By The Secretary, Department Of Health & Human Services | Method for purifying antibodies using PBS |
| JP6630036B2 (ja) * | 2014-09-30 | 2020-01-15 | Jsr株式会社 | 標的物の精製方法、及び、ミックスモード用担体 |
| TW201628649A (zh) | 2014-10-09 | 2016-08-16 | 再生元醫藥公司 | 減少醫藥調配物中微可見顆粒之方法 |
| CN105566442A (zh) * | 2014-10-11 | 2016-05-11 | 江苏泰康生物医药有限公司 | 一种降低单克隆抗体生产中宿主细胞蛋白含量的亲和纯化工艺 |
| WO2016118707A1 (en) | 2015-01-21 | 2016-07-28 | Oncobiologics, Inc. | Modulation of charge variants in a monoclonal antibody composition |
| KR102490956B1 (ko) * | 2015-03-13 | 2023-01-19 | 브리스톨-마이어스 스큅 컴퍼니 | 불순물을 제거하기 위한 크로마토그래피 동안의 알칼리성 세척의 용도 |
| EP3334747B1 (en) | 2015-08-13 | 2023-09-27 | Amgen Inc. | Charged depth filtration of antigen-binding proteins |
| KR20180048731A (ko) * | 2015-08-20 | 2018-05-10 | 제넨테크, 인크. | 재조합 폴리펩티드를 제조하기 위한 fkpa의 정제 및 그의 용도 |
| US11229702B1 (en) | 2015-10-28 | 2022-01-25 | Coherus Biosciences, Inc. | High concentration formulations of adalimumab |
| AU2017213775A1 (en) | 2016-02-03 | 2018-08-16 | Outlook Therapeutics, Inc. | Buffer formulations for enhanced antibody stability |
| US11186858B1 (en) | 2016-03-15 | 2021-11-30 | Fresenius Kabi Deutschland Gmbh | Methods for increasing biosimilarity |
| BR112018068803A2 (pt) * | 2016-04-01 | 2019-01-22 | Ucb Biopharma Sprl | método para purificação de proteína |
| ES2994760T3 (en) | 2016-04-14 | 2025-01-30 | Lonza Ag | Methods for the detection of host cell proteins |
| WO2017184880A1 (en) | 2016-04-20 | 2017-10-26 | Coherus Biosciences, Inc. | A method of filling a container with no headspace |
| KR102369014B1 (ko) | 2016-08-16 | 2022-03-02 | 리제너론 파아마슈티컬스, 인크. | 혼합물로부터 개별 항체들을 정량하는 방법 |
| ES3032778T3 (en) | 2016-10-25 | 2025-07-24 | Regeneron Pharma | Methods for chromatography data analysis |
| AU2017371179B2 (en) | 2016-12-09 | 2022-07-14 | Gliknik Inc. | Manufacturing optimization of GL-2045, a multimerizing stradomer |
| AU2017371182B2 (en) | 2016-12-09 | 2024-03-28 | Gliknik Inc. | Methods of treating inflammatory disorders with multivalent Fc compounds |
| EP3824906A1 (en) | 2016-12-21 | 2021-05-26 | Amgen Inc. | Anti-tnf alpha antibody formulations |
| CR20190291A (es) | 2016-12-23 | 2019-11-05 | Serum Institute Of India Pvt Ltd | Métodos mejorados para estimular la productividad de anticuerpos en el cultivo de células de mamiferos y reducir la agregación durante los procesos de formulación post-tratamiento (downstream) y formulaciones de anticuerpos estables obtenidas a partir de los mismos |
| CA3067735A1 (en) | 2017-08-17 | 2019-02-21 | Just Biotherapeutics, Inc. | Method of purifying glycosylated protein from host cell galectins and other contaminants |
| US12161993B2 (en) * | 2017-08-23 | 2024-12-10 | Jsr Corporation | Chromatography carrier, ligand-immobilizing carrier, chromatography column, target substance purification method, and chromatography carrier production method |
| MY203415A (en) | 2017-09-19 | 2024-06-27 | Regeneron Pharma | Methods of reducing particle formation and compositions formed thereby |
| CA3080656A1 (en) | 2017-10-30 | 2019-05-09 | Baxalta GmbH | Environmentally compatible detergents for inactivation of lipid-enveloped viruses |
| AU2018392697B2 (en) * | 2017-12-21 | 2025-08-14 | Genzyme Corporation | Methods for enhanced removal of impurities during protein a chromatography |
| CN119881293A (zh) | 2018-03-21 | 2025-04-25 | 沃特世科技公司 | 基于非抗体高亲和力的样品制备、吸附剂、装置和方法 |
| CN108239146A (zh) * | 2018-03-26 | 2018-07-03 | 江苏中新医药有限公司 | 一种高纯度rhNGF的制备方法 |
| US12018075B2 (en) | 2018-04-20 | 2024-06-25 | Janssen Biotech, Inc. | Chromatography column qualification in manufacturing methods for producing anti-TNF antibody compositions |
| TW202448568A (zh) | 2018-07-02 | 2024-12-16 | 美商里珍納龍藥品有限公司 | 自混合物製備多肽之系統及方法 |
| AU2019332764B2 (en) * | 2018-08-31 | 2025-05-29 | Genzyme Corporation | Sterile chromatography resin and use thereof in manufacturing processes |
| KR102337683B1 (ko) * | 2018-09-21 | 2021-12-13 | 주식회사 녹십자 | 고효율 항-tfpi 항체 조성물 |
| CN111072773A (zh) * | 2018-10-19 | 2020-04-28 | 菲鹏生物股份有限公司 | 抗体的纯化方法、抗体和应用 |
| CN111153993B (zh) * | 2018-11-07 | 2024-06-28 | 正大天晴药业集团南京顺欣制药有限公司 | 抗TNF-α单克隆抗体的制备方法 |
| EP3886909A4 (en) * | 2018-11-29 | 2023-03-29 | Comera Life Sciences, Inc. | ADDITOR COMPOUNDS FOR PROTEIN PROCESSING |
| GB201904741D0 (en) * | 2019-04-04 | 2019-05-22 | Glaxosmithkline Ip Dev Ltd | Novel process |
| US20220306727A1 (en) * | 2019-06-05 | 2022-09-29 | Seagen Inc. | Methods of Purifying Masked Antibodies |
| AU2021355518A1 (en) * | 2020-10-02 | 2023-06-08 | Eli Lilly And Company | Methods for reducing host cell protein content in protein purification processes |
| WO2023284073A1 (zh) * | 2021-07-13 | 2023-01-19 | 江苏荃信生物医药股份有限公司 | 降低单克隆抗体生产中宿主细胞蛋白含量的亲和纯化方法、抗人ifnar1单克隆抗体浓缩溶液的制备方法以及液体制剂 |
| CN113501857A (zh) * | 2021-08-17 | 2021-10-15 | 沈阳百发科技有限公司 | 一种高活性重组蛋白的制备方法 |
| CN114292328B (zh) * | 2021-12-30 | 2025-07-25 | 武汉原谷生物科技有限责任公司 | 一种来源于美洲羊驼中天然抗体的纯化方法及其应用 |
| JP2025502949A (ja) * | 2022-01-24 | 2025-01-30 | ユニバーシティ オブ フロリダ リサーチ ファウンデーション,インコーポレイティド | 抗トロンビンiiiのポイントオブケア試験システム |
| CN115073590A (zh) * | 2022-07-08 | 2022-09-20 | 杭州艾策生物技术有限公司 | 一种减少单克隆抗体氧化杂质的深层过滤方法 |
| WO2025059162A1 (en) | 2023-09-11 | 2025-03-20 | Dana-Farber Cancer Institute, Inc. | Car-engager containing il-2 variants to enhance the functionality of car t cells |
Family Cites Families (208)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| USRE30985E (en) | 1978-01-01 | 1982-06-29 | Serum-free cell culture media | |
| US4399216A (en) | 1980-02-25 | 1983-08-16 | The Trustees Of Columbia University | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| US5179017A (en) | 1980-02-25 | 1993-01-12 | The Trustees Of Columbia University In The City Of New York | Processes for inserting DNA into eucaryotic cells and for producing proteinaceous materials |
| US4510245A (en) | 1982-11-18 | 1985-04-09 | Chiron Corporation | Adenovirus promoter system |
| US4560655A (en) | 1982-12-16 | 1985-12-24 | Immunex Corporation | Serum-free cell culture medium and process for making same |
| US4657866A (en) | 1982-12-21 | 1987-04-14 | Sudhir Kumar | Serum-free, synthetic, completely chemically defined tissue culture media |
| JPS59156299A (ja) | 1983-02-28 | 1984-09-05 | Noda Sangyo Kagaku Kenkyusho | N−アセチルヘキソサミンの定量法及びその定量用試薬 |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4534972A (en) | 1983-03-29 | 1985-08-13 | Miles Laboratories, Inc. | Protein compositions substantially free from infectious agents |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| DD266710A3 (de) | 1983-06-06 | 1989-04-12 | Ve Forschungszentrum Biotechnologie | Verfahren zur biotechnischen Herstellung van alkalischer Phosphatase |
| US4767704A (en) | 1983-10-07 | 1988-08-30 | Columbia University In The City Of New York | Protein-free culture medium |
| EP0154316B1 (en) | 1984-03-06 | 1989-09-13 | Takeda Chemical Industries, Ltd. | Chemically modified lymphokine and production thereof |
| US4879231A (en) | 1984-10-30 | 1989-11-07 | Phillips Petroleum Company | Transformation of yeasts of the genus pichia |
| US5168062A (en) | 1985-01-30 | 1992-12-01 | University Of Iowa Research Foundation | Transfer vectors and microorganisms containing human cytomegalovirus immediate-early promoter-regulatory DNA sequence |
| GB8516415D0 (en) | 1985-06-28 | 1985-07-31 | Celltech Ltd | Culture of animal cells |
| US4968615A (en) | 1985-12-18 | 1990-11-06 | Ciba-Geigy Corporation | Deoxyribonucleic acid segment from a virus |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| US4927762A (en) | 1986-04-01 | 1990-05-22 | Cell Enterprises, Inc. | Cell culture medium with antioxidant |
| GB8610600D0 (en) | 1986-04-30 | 1986-06-04 | Novo Industri As | Transformation of trichoderma |
| US5045468A (en) * | 1986-12-12 | 1991-09-03 | Cell Enterprises, Inc. | Protein-free culture medium which promotes hybridoma growth |
| US5476996A (en) | 1988-06-14 | 1995-12-19 | Lidak Pharmaceuticals | Human immune system in non-human animal |
| US5223409A (en) | 1988-09-02 | 1993-06-29 | Protein Engineering Corp. | Directed evolution of novel binding proteins |
| US6048728A (en) * | 1988-09-23 | 2000-04-11 | Chiron Corporation | Cell culture medium for enhanced cell growth, culture longevity, and product expression |
| EP0435911B1 (en) | 1988-09-23 | 1996-03-13 | Cetus Oncology Corporation | Cell culture medium for enhanced cell growth, culture longevity and product expression |
| EP0401384B1 (en) | 1988-12-22 | 1996-03-13 | Kirin-Amgen, Inc. | Chemically modified granulocyte colony stimulating factor |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| EP0402226A1 (en) | 1989-06-06 | 1990-12-12 | Institut National De La Recherche Agronomique | Transformation vectors for yeast yarrowia |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| US5110913A (en) * | 1990-05-25 | 1992-05-05 | Miles Inc. | Antibody purification method |
| US5096816A (en) * | 1990-06-05 | 1992-03-17 | Cetus Corporation | In vitro management of ammonia's effect on glycosylation of cell products through pH control |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| AU665190B2 (en) | 1990-07-10 | 1995-12-21 | Cambridge Antibody Technology Limited | Methods for producing members of specific binding pairs |
| US5122469A (en) | 1990-10-03 | 1992-06-16 | Genentech, Inc. | Method for culturing Chinese hamster ovary cells to improve production of recombinant proteins |
| WO1992009690A2 (en) | 1990-12-03 | 1992-06-11 | Genentech, Inc. | Enrichment method for variant proteins with altered binding properties |
| ATE439435T1 (de) | 1991-03-01 | 2009-08-15 | Dyax Corp | Chimäres protein mit mikroprotein mit zwei oder mehr disulfidbindungen und ausgestaltungen davon |
| DE69233750D1 (de) | 1991-04-10 | 2009-01-02 | Scripps Research Inst | Bibliotheken heterodimerer Rezeptoren mittels Phagemiden |
| DE4122599C2 (de) | 1991-07-08 | 1993-11-11 | Deutsches Krebsforsch | Phagemid zum Screenen von Antikörpern |
| EP0666312A1 (en) * | 1994-02-08 | 1995-08-09 | Wolfgang A. Renner | Process for the improvement of mammalian cell growth |
| US5429746A (en) * | 1994-02-22 | 1995-07-04 | Smith Kline Beecham Corporation | Antibody purification |
| US5853714A (en) * | 1995-03-27 | 1998-12-29 | Genetics Institute, Inc. | Method for purification of IL-12 |
| US5641870A (en) * | 1995-04-20 | 1997-06-24 | Genentech, Inc. | Low pH hydrophobic interaction chromatography for antibody purification |
| US5705364A (en) * | 1995-06-06 | 1998-01-06 | Genentech, Inc. | Mammalian cell culture process |
| US5721121A (en) * | 1995-06-06 | 1998-02-24 | Genentech, Inc. | Mammalian cell culture process for producing a tumor necrosis factor receptor immunoglobulin chimeric protein |
| US6656466B1 (en) * | 1995-06-06 | 2003-12-02 | Genetech, Inc. | Human tumor necrosis factor—immunoglobulin(TNFR1-IgG1) chimera composition |
| JP4306813B2 (ja) * | 1995-09-19 | 2009-08-05 | アスビオファーマ株式会社 | 動物細胞の新規培養方法 |
| DE69623109T2 (de) * | 1996-04-19 | 2002-12-12 | Societe Des Produits Nestle S.A., Vevey | Menschliche immortalisierte Colon-Epithelialzellen |
| AU5082698A (en) | 1996-10-23 | 1998-05-15 | Oravax, Inc | Heat inactivation of viruses in antibody preparations |
| EP0936923B1 (en) * | 1996-11-15 | 2003-12-17 | Kennedy Institute Of Rheumatology | SUPPRESSION OF TNFalpha AND IL-12 IN THERAPY |
| JP4031049B2 (ja) * | 1996-11-27 | 2008-01-09 | ジェネンテック,インコーポレーテッド | タンパク質精製 |
| US6955917B2 (en) * | 1997-06-20 | 2005-10-18 | Bayer Healthcare Llc | Chromatographic method for high yield purification and viral inactivation of antibodies |
| IL121900A (en) | 1997-10-07 | 2001-12-23 | Omrix Biopharmaceuticals Ltd | A method for the purification of immunoglobulins |
| US20020045207A1 (en) * | 1997-10-31 | 2002-04-18 | Lynne A. Krummen | Glycoprotein production process |
| WO1999032605A1 (en) | 1997-12-19 | 1999-07-01 | Novo Nordisk A/S | Method for producing heterologous proteins in eukaryotic cells on an industrial scale using nucleotide-manipulating agents |
| ATE321066T1 (de) * | 1998-05-06 | 2006-04-15 | Genentech Inc | Anti-her2 antikörperzusammensetzung |
| US6528286B1 (en) * | 1998-05-29 | 2003-03-04 | Genentech, Inc. | Mammalian cell culture process for producing glycoproteins |
| US6914128B1 (en) | 1999-03-25 | 2005-07-05 | Abbott Gmbh & Co. Kg | Human antibodies that bind human IL-12 and methods for producing |
| AU7614600A (en) * | 1999-09-27 | 2001-04-30 | Genentech Inc. | Methods for making recombinant proteins using apoptosis inhibitors |
| ES2266159T3 (es) * | 2000-02-08 | 2007-03-01 | Genentech, Inc. | Mejora de la galactosilacion de glicoproteinas recombinantes. |
| CA2399148A1 (en) | 2000-02-10 | 2001-08-16 | Abbott Laboratories | Antibodies that bind human interleukin-18 and methods of making and using |
| US7598055B2 (en) | 2000-06-28 | 2009-10-06 | Glycofi, Inc. | N-acetylglucosaminyltransferase III expression in lower eukaryotes |
| EP1175931A1 (en) * | 2000-07-25 | 2002-01-30 | Computer Cell Culture Center S.A. | Integration of high cell density bioreactor operation with ultra fast on-line downstream processing |
| AU2001294520A1 (en) * | 2000-08-21 | 2002-03-04 | Clonex Development, Inc. | Methods and compositions for increasing protein yield from a cell culture |
| US6693173B2 (en) * | 2000-12-26 | 2004-02-17 | Alpha Therapeutic Corporation | Method to remove citrate and aluminum from proteins |
| US20030096414A1 (en) * | 2001-03-27 | 2003-05-22 | Invitrogen Corporation | Culture medium for cell growth and transfection |
| DE60227067D1 (de) | 2001-05-11 | 2008-07-24 | Kirin Pharma Kk | Künstliches menschliches chromosom mit dem gen für die lambda-leichte kette menschlicher antikörper |
| DK1714982T3 (da) * | 2001-06-05 | 2009-05-04 | Genetics Inst Llc | Fremgangsmåde til rensning af stærkt anioniske proteiner |
| CA2455365C (en) * | 2001-08-03 | 2014-07-29 | Glycart Biotechnology Ag | Antibody glycosylation variants having increased antibody-dependent cellular cytotoxicity |
| ES2291534T3 (es) * | 2001-10-02 | 2008-03-01 | Novo Nordisk Health Care Ag | Metodo para la produccion de proteinas recombinantes en celulas eucariotas. |
| ATE430580T1 (de) * | 2001-10-25 | 2009-05-15 | Genentech Inc | Glycoprotein-zusammensetzungen |
| IL161858A0 (en) | 2001-11-28 | 2005-11-20 | Sandoz Ag | Cell culture process |
| WO2003059935A2 (en) * | 2001-12-21 | 2003-07-24 | Immunex Corporation | Methods for purifying protein |
| US20030201229A1 (en) * | 2002-02-04 | 2003-10-30 | Martin Siwak | Process for prefiltration of a protein solution |
| JP4460302B2 (ja) * | 2002-02-05 | 2010-05-12 | ジェネンテック インコーポレイテッド | タンパク質精製法 |
| CA2417689C (en) * | 2002-03-05 | 2006-05-09 | F. Hoffmann-La Roche Ag | Improved methods for growing mammalian cells in vitro |
| US20030190710A1 (en) * | 2002-03-28 | 2003-10-09 | Devries Ruth L. | Control of glycoforms in IgG |
| JPWO2003085118A1 (ja) * | 2002-04-09 | 2005-08-11 | 協和醗酵工業株式会社 | 抗体組成物の製造方法 |
| RU2304587C2 (ru) * | 2002-06-10 | 2007-08-20 | Гуд Байотек Копэрейшн | СПОСОБ СЕЛЕКТИВНОГО ВЫДЕЛЕНИЯ АНТИТЕЛ IgY ИЗ ЯИЧНОГО ЖЕЛТКА ПТИЦ ОТРЯДА ГУСЕОБРАЗНЫХ (ВАРИАНТЫ) |
| PL376381A1 (en) * | 2002-07-15 | 2005-12-27 | Immunex Corporation | Methods and media for controlling sialylation of proteins produced by mammalian cells |
| CN101745112A (zh) * | 2002-07-19 | 2010-06-23 | 艾博特生物技术有限公司 | TNFα相关疾病的治疗 |
| US6974681B1 (en) * | 2002-08-23 | 2005-12-13 | Immunex Corporation | Cell culture performance with vanadate |
| US7067279B1 (en) * | 2002-08-23 | 2006-06-27 | Immunex Corporation | Cell culture performance with betaine |
| WO2004026427A2 (en) | 2002-09-17 | 2004-04-01 | Gtc Biotherapeutics, Inc. | Isolation of immunoglobulin molecules that lack inter-heavy chain disulfide bonds |
| US7208585B2 (en) * | 2002-09-18 | 2007-04-24 | Genencor International, Inc. | Protein purification |
| US20040162414A1 (en) | 2002-11-22 | 2004-08-19 | Santora Ling C. | Method for reducing or preventing modification of a polypeptide in solution |
| BR0317723A (pt) | 2002-12-23 | 2005-11-22 | Bristol Myers Squibb Co | Processo de cultura de células de mamìfero para a produção de proteìna |
| KR101088223B1 (ko) * | 2002-12-23 | 2011-11-30 | 브리스톨-마이어스 스큅 컴퍼니 | 단백질 생산을 위한 포유류 세포 배양 방법에서의 생산물품질 향상 |
| SI1623019T1 (sl) * | 2003-05-15 | 2010-10-29 | Wyeth Llc | Omejeno glukozno dovajanje za živalsko celično kulturo |
| PL3095793T3 (pl) * | 2003-07-28 | 2020-09-07 | Genentech, Inc. | Redukcja wycieku białka A w trakcie chromatografii powinowactwa z białkiem A |
| GB2404665B (en) * | 2003-08-08 | 2005-07-06 | Cambridge Antibody Tech | Cell culture |
| EP1673452B1 (en) * | 2003-10-10 | 2015-12-23 | Novo Nordisk Health Care AG | Method for large-scale production of a polypeptide in eukaryote cells |
| AU2004286938B2 (en) * | 2003-10-27 | 2011-06-30 | Wyeth | Removal of high molecular weight aggregates using hydroxyapatite chromatography |
| US8084032B2 (en) | 2004-01-21 | 2011-12-27 | Ajinomoto Co., Inc. | Purification method which prevents denaturation of an antibody |
| SE0400886D0 (sv) * | 2004-04-02 | 2004-04-02 | Amersham Biosciences Ab | Process of purification |
| US20060127950A1 (en) * | 2004-04-15 | 2006-06-15 | Massachusetts Institute Of Technology | Methods and products related to the improved analysis of carbohydrates |
| ES2339953T5 (es) | 2004-05-04 | 2020-05-06 | Novo Nordisk Healthcare Ag | Glicoformas de factor VII ligadas a O y método de fabricación |
| US7294484B2 (en) | 2004-08-27 | 2007-11-13 | Wyeth Research Ireland Limited | Production of polypeptides |
| KR101238798B1 (ko) * | 2004-09-30 | 2013-03-04 | 바이엘 헬스케어, 엘엘씨 | 생물학적 분자의 통합된 연속 제조를 위한 장치 및 방법 |
| US20060094104A1 (en) | 2004-10-29 | 2006-05-04 | Leopold Grillberger | Animal protein-free media for cultivation of cells |
| JP2006143601A (ja) * | 2004-11-16 | 2006-06-08 | Yamato Yakuhin Kk | 血液粘度低下剤 |
| US8728828B2 (en) * | 2004-12-22 | 2014-05-20 | Ge Healthcare Bio-Sciences Ab | Purification of immunoglobulins |
| JP5523674B2 (ja) | 2005-02-11 | 2014-06-18 | ノボ ノルディスク ヘルス ケア アクチェンゲゼルシャフト | 植物タンパク質加水分解産物を含有する血清フリーの細胞培養液におけるポリペプチドの生産 |
| KR101482791B1 (ko) * | 2005-03-11 | 2015-01-21 | 와이어쓰 엘엘씨 | 약한 분배성 크로마토그래피법 |
| JP2008535913A (ja) | 2005-04-11 | 2008-09-04 | メダレックス インコーポレーティッド | タンパク質精製方法 |
| WO2006113743A2 (en) * | 2005-04-18 | 2006-10-26 | Massachusetts Institute Of Technology | Compositions and methods for rna interference with sialidase expression and uses thereof |
| US7247457B2 (en) * | 2005-04-26 | 2007-07-24 | United States Of America As Represented By The Secretary Of The Department Of Health And Human Services, Centers For Disease Control And Prevention | Detection and identification of enteroviruses by semi-nested amplification of the enterovirus VP1 protein |
| KR20080032065A (ko) * | 2005-06-03 | 2008-04-14 | 제넨테크, 인크. | 푸코실화 수준이 조절된 항체의 생성 방법 |
| EP1909831A4 (en) * | 2005-06-14 | 2013-02-20 | Amgen Inc | SELF-BUFFING PROTEIN FORMULATIONS |
| EA201100177A1 (ru) * | 2005-06-17 | 2011-06-30 | Элан Фарма Интернэшнл Лимитед | СПОСОБЫ ОЧИСТКИ АНТИТЕЛ К β-АМИЛОИДУ |
| HUE038947T2 (hu) * | 2005-08-26 | 2018-12-28 | Ares Trading Sa | Eljárás glikozilált béta-interferon elõállítására |
| PE20070796A1 (es) * | 2005-10-24 | 2007-08-15 | Wyeth Corp | Metodo de produccion proteica utilizando compuestos anti-senescencia |
| EP2495308A1 (en) * | 2005-12-08 | 2012-09-05 | Amgen Inc. | Improved production of glycoproteins using manganese |
| US20070190057A1 (en) * | 2006-01-23 | 2007-08-16 | Jian Wu | Methods for modulating mannose content of recombinant proteins |
| EP2738178A1 (en) * | 2006-04-05 | 2014-06-04 | AbbVie Biotechnology Ltd | Antibody purification |
| US7851438B2 (en) * | 2006-05-19 | 2010-12-14 | GlycoFi, Incorporated | Erythropoietin compositions |
| US20100234577A1 (en) * | 2006-06-14 | 2010-09-16 | Smithkline Beecham Corporation | Methods for purifying antibodies using ceramic hydroxyapatite |
| WO2008007280A2 (en) | 2006-06-28 | 2008-01-17 | Koninklijke Philips Electronics N.V. | Assay system and method |
| DK2041270T3 (da) | 2006-07-13 | 2014-01-27 | Wyeth Llc | Fremstilling af glycoproteiner |
| ES2755386T5 (es) * | 2006-08-28 | 2023-04-05 | Ares Trading Sa | Proceso para la purificación de proteínas que contienen fragmentos Fc |
| CL2007002615A1 (es) * | 2006-09-08 | 2008-04-18 | Wyeth Corp | Metodos para aislar o purificar un producto que comprende poner el producto enlazado en contacto con al menos una solucion de lavado que comprende arginina y luego eluir el producto; y dicho producto. |
| US8911964B2 (en) * | 2006-09-13 | 2014-12-16 | Abbvie Inc. | Fed-batch method of making human anti-TNF-alpha antibody |
| EP2500413A1 (en) * | 2006-09-13 | 2012-09-19 | Abbott Laboratories | Cell culture improvements |
| US10982250B2 (en) * | 2006-09-18 | 2021-04-20 | Genentech, Inc. | Methods of protein production |
| WO2008036899A2 (en) | 2006-09-22 | 2008-03-27 | Amgen Inc. | Methods for removing viral contaminants during protein purification |
| CA2666317C (en) * | 2006-11-03 | 2013-08-06 | Wyeth | Glycolysis-inhibiting substances in cell culture |
| WO2008068879A1 (en) | 2006-12-06 | 2008-06-12 | Jcr Pharmaceuticals Co., Ltd. | Method for production of human erythropoietin |
| US8163886B2 (en) | 2006-12-21 | 2012-04-24 | Emd Millipore Corporation | Purification of proteins |
| KR20090127326A (ko) * | 2007-03-02 | 2009-12-10 | 와이어쓰 | 폴리펩티드의 생산을 위한 세포 배양물 중에서 구리 및 글루타메이트의 용도 |
| AU2008232903B9 (en) | 2007-03-30 | 2013-09-05 | Medimmune Llc | Antibodies with decreased deamidation profiles |
| TW200907059A (en) * | 2007-03-30 | 2009-02-16 | Abbott Lab | Recombinant expression vector elements (rEVEs) for enhancing expression of recombinant proteins in host cells |
| EP2508613A3 (en) * | 2007-04-03 | 2012-11-28 | Oxyrane UK Limited | Glycosylation of molecules |
| US20100113294A1 (en) | 2007-04-16 | 2010-05-06 | Momenta Pharmaceuticals, Inc. | Defined glycoprotein products and related methods |
| TW200902708A (en) * | 2007-04-23 | 2009-01-16 | Wyeth Corp | Methods of protein production using anti-senescence compounds |
| EP1988101A1 (en) | 2007-05-04 | 2008-11-05 | Novo Nordisk A/S | Improvement of factor VIII polypeptide titers in cell cultures |
| WO2008135498A2 (en) | 2007-05-04 | 2008-11-13 | Novo Nordisk A/S | Prevention of protein degradation in mammalian cell cultures |
| CA2687082C (en) | 2007-05-11 | 2014-01-14 | Amgen Inc. | Improved feed media |
| WO2008154014A2 (en) * | 2007-06-11 | 2008-12-18 | Amgen Inc. | A method for culturing mammalian cells to improve recombinant protein production |
| WO2009009523A2 (en) * | 2007-07-09 | 2009-01-15 | Genentech, Inc. | Prevention of disulfide bond reduction during recombinant production of polypeptides |
| EP3327132A3 (en) | 2007-08-09 | 2018-07-18 | Wyeth LLC | Use of perfusion to enhance production of fed-batch cell culture in bioreactors |
| WO2009058769A1 (en) | 2007-10-30 | 2009-05-07 | Schering Corporation | Purification of antibodies containing hydrophobic variants |
| CL2008003218A1 (es) | 2007-10-30 | 2009-03-06 | Genentech Inc | Método para la purificación de un anticuerpo a partir de una composición que comprende el anticuerpo y al menos un contaminante. |
| TWM332870U (en) * | 2007-11-22 | 2008-05-21 | Delta Electronics Inc | Side-edge type backlight module |
| TWI661833B (zh) * | 2007-11-30 | 2019-06-11 | 百慕達商艾伯維生物技術有限責任公司 | 蛋白質調配物及製造其之方法 |
| PL2235197T3 (pl) | 2007-12-27 | 2018-01-31 | Baxalta GmbH | Sposoby hodowli komórek |
| EP2287174B8 (en) * | 2008-01-18 | 2016-12-07 | Bio-Rad Laboratories, Inc. | Enhanced purification of antibody fragments by apatite chromatography |
| WO2009114641A1 (en) * | 2008-03-11 | 2009-09-17 | Genentech, Inc. | Antibodies with enhanced adcc function |
| WO2009129226A1 (en) * | 2008-04-15 | 2009-10-22 | Talecris Biotherapeutics, Inc. | Two-stage ultrafiltration/diafiltration |
| CN102076865B (zh) * | 2008-05-02 | 2016-03-16 | 西雅图基因公司 | 用于制造核心岩藻糖基化降低的抗体和抗体衍生物的方法和组合物 |
| EP2331700A2 (en) | 2008-08-08 | 2011-06-15 | Biogen Idec MA Inc. | Nutrient monitoring and feedback control for increased bioproduct production |
| KR101843915B1 (ko) * | 2008-08-14 | 2018-04-02 | 제넨테크, 인크. | 고유 단백질 대체 이온 교환 막 크로마토그래피를 이용한 오염물의 제거 방법 |
| US8080415B2 (en) | 2008-09-26 | 2011-12-20 | Eureka Therapeutics, Inc. | Modified host cells and uses thereof |
| NZ592097A (en) * | 2008-10-20 | 2013-01-25 | Abbott Lab | Viral inactivation during purification of il-12 and il-18 antibodies |
| KR20110091678A (ko) * | 2008-10-20 | 2011-08-12 | 아보트 러보러터리즈 | 단백질 a 친화성 크로마토그래피를 이용한 항체의 분리 및 정제 |
| NZ592096A (en) | 2008-10-20 | 2013-01-25 | Abbott Lab | Antibodies that bind to il-12 and methods of purifying the same |
| EP2346901A1 (en) | 2008-10-20 | 2011-07-27 | Abbott Laboratories | Antibodies that bind to il-18 and methods of purifying the same |
| EP2350130B1 (en) * | 2008-10-31 | 2018-10-03 | Wyeth LLC | Purification of acidic proteins using ceramic hydroxyapatite chromatography |
| US20110236391A1 (en) * | 2008-12-09 | 2011-09-29 | Hanns-Christian Mahler | Method for obtaining an excipient-free antibody solution |
| CA2745707A1 (en) | 2008-12-22 | 2010-07-01 | F. Hoffmann-La Roche Ag | Immunoglobulin purification |
| EP2373676B1 (en) | 2009-01-08 | 2017-04-19 | GE Healthcare BioProcess R&D AB | Separation method using single polymer phase systems |
| JP5728392B2 (ja) | 2009-03-05 | 2015-06-03 | バイオジェン アイデック エムエー インコーポレイティドBiogen Idec Inc. | 免疫グロブリンの精製 |
| US9056896B2 (en) * | 2009-03-27 | 2015-06-16 | Asahi Kasei Medical Co., Ltd. | Method for removing viruses from high concentration monoclonal antibody solution |
| WO2010120739A1 (en) | 2009-04-13 | 2010-10-21 | Bristol-Myers Squibb Company | Protein purification by citrate precipitation |
| EP2421892A1 (en) | 2009-04-20 | 2012-02-29 | Pfizer Inc. | Control of protein glycosylation and compositions and methods relating thereto |
| WO2010136515A1 (en) * | 2009-05-28 | 2010-12-02 | Boehringer Ingelheim International Gmbh | Method for a rational cell culturing process |
| WO2010141855A1 (en) * | 2009-06-05 | 2010-12-09 | Momenta Pharmaceuticals, Inc. | Methods of modulating fucosylation of glycoproteins |
| PL2451936T3 (pl) | 2009-07-06 | 2020-02-28 | F. Hoffmann-La Roche Ag | Sposób hodowli komórek eukariotycznych |
| WO2011009623A1 (en) | 2009-07-24 | 2011-01-27 | F. Hoffmann-La Roche Ag | Optimizing the production of antibodies |
| WO2011015926A1 (en) | 2009-08-03 | 2011-02-10 | Avesthagen Limited | A process of fermentation, purification and production of recombinant soluble tumour necrosis factor alfa receptor (tnfr) - human igg fc fusion protein |
| KR101844859B1 (ko) | 2009-08-06 | 2018-05-18 | 제넨테크, 인크. | 단백질 정제 시의 바이러스 제거의 개선방법 |
| WO2011019622A1 (en) * | 2009-08-14 | 2011-02-17 | Genentech, Inc. | Cell culture methods to make antibodies with enhanced adcc function |
| WO2011024025A1 (en) | 2009-08-28 | 2011-03-03 | Avesthagen Limited | An erythropoietin analogue and a method thereof |
| CA2772653C (en) | 2009-09-01 | 2019-06-25 | Genentech, Inc. | Enhanced protein purification through a modified protein a elution |
| US9540426B2 (en) | 2009-10-06 | 2017-01-10 | Bristol-Myers Squibb Company | Mammalian cell culture processes for protein production |
| EP2490780A4 (en) * | 2009-10-20 | 2014-04-09 | Merck Sharp & Dohme | USE OF A MIXED MODE CHROMATOGRAPHY FOR THE DETECTION AND PURIFICATION OF BASIC ANTIBODY PRODUCTS |
| PL3037104T3 (pl) * | 2009-10-20 | 2020-11-16 | Abbvie Inc. | Izolacja i oczyszczanie przeciwciał anty-il-13 z zastosowaniem chromatografii powinowactwa z białkiem a |
| US9096879B2 (en) | 2009-11-24 | 2015-08-04 | Biogen Ma Inc. | Method of supplementing culture media to prevent undesirable amino acid substitutions |
| WO2011069056A2 (en) | 2009-12-04 | 2011-06-09 | Momenta Pharmaceuticals, Inc. | Antennary fucosylation in glycoproteins from cho cells |
| US8277649B2 (en) | 2009-12-14 | 2012-10-02 | General Electric Company | Membranes and associated methods for purification of antibodies |
| JP5909450B2 (ja) * | 2009-12-18 | 2016-04-26 | ノバルティス アーゲー | 洗浄溶液及びアフィニティークロマトグラフィーの方法 |
| WO2011087301A2 (ko) * | 2010-01-15 | 2011-07-21 | 성균관대학교산학협력단 | 기체 및 수분 차단용 그래핀 보호막, 이의 형성 방법 및 그의 용도 |
| KR20130048218A (ko) * | 2010-04-06 | 2013-05-09 | 헬리아에 디벨롭먼트, 엘엘씨 | 조류의 탈수 및 그것으로부터의 물을 재사용하기 위한 방법 및 시스템 |
| CA2794697A1 (en) | 2010-04-07 | 2011-10-13 | Momenta Pharmaceuticals, Inc. | High mannose glycans |
| ES2533074T3 (es) | 2010-04-26 | 2015-04-07 | Novartis Ag | Medio de cultivo celular mejorado |
| EP3862423A1 (en) | 2010-04-26 | 2021-08-11 | Novartis AG | Improved cell cultivation process |
| RU2614125C2 (ru) | 2010-05-28 | 2017-03-22 | Дженентек, Инк. | Снижение уровня лактата и увеличение продукции полипептида путем ингибирования экспрессии лактатдегидрогеназы и киназы пируватдегидрогеназы |
| SG187198A1 (en) | 2010-08-05 | 2013-03-28 | Amgen Inc | Dipeptides to enhance yield and viability from cell cultures |
| WO2012030512A1 (en) | 2010-09-03 | 2012-03-08 | Percivia Llc. | Flow-through protein purification process |
| BR112013006403A2 (pt) * | 2010-09-20 | 2015-09-29 | Abbvie Inc | purificação de anticorpos usando cromatografia de leito móvel simulado |
| SG10201508401TA (en) * | 2010-10-11 | 2015-11-27 | Abbvie Bahamas Ltd | Processes for purification of proteins |
| KR101898302B1 (ko) | 2010-10-15 | 2018-09-13 | 제이씨알 파마 가부시키가이샤 | 당사슬의 비환원 말단이 만노오스 잔기인 당 단백질의 제조 방법 |
| EP2450375A1 (en) | 2010-11-09 | 2012-05-09 | Sandoz Gmbh | Cell culture medium and process for protein expression, said medium and process comprising a PAM inhibitor |
| EP2649087A1 (en) * | 2010-12-08 | 2013-10-16 | Amgen Inc. | Ion exchange chromatography in the presence of an amino acid |
| MX357821B (es) | 2010-12-21 | 2018-07-25 | Hoffmann La Roche | Preparación de anticuerpo enriquecida con isoforma y método para obtenerla. |
| AU2012226398B9 (en) | 2011-03-06 | 2017-04-13 | Merck Serono S.A. | Low fucose cell lines and uses thereof |
| MX2013010737A (es) | 2011-03-25 | 2014-03-12 | Genentech Inc | Novedosos metodos de purificacion de proteinas. |
| EP2511293A1 (en) | 2011-04-13 | 2012-10-17 | LEK Pharmaceuticals d.d. | A method for controlling the main complex N-glycan structures and the acidic variants and variability in bioprocesses producing recombinant proteins |
| WO2012145682A1 (en) | 2011-04-21 | 2012-10-26 | Amgen Inc. | A method for culturing mammalian cells to improve recombinant protein production |
| MY166973A (en) | 2011-04-29 | 2018-07-27 | Biocon Res Limited | Methods for reducing accumulation of lactate during culturing and method for producing polypeptide |
| US20120283419A1 (en) | 2011-05-03 | 2012-11-08 | Avantor Performance Materials, Inc. | Separation of protein monomers from aggregates by solid weak anion exchange support functionalized with amine moieties |
| EP3388443A1 (en) | 2011-05-13 | 2018-10-17 | Biogen MA Inc. | Methods of preventing and removing trisulfide bonds |
| WO2013006461A1 (en) | 2011-07-01 | 2013-01-10 | Biogen Idec Ma Inc. | Cholesterol-based media supplementals for cell culture |
| HUE033279T2 (en) | 2011-07-01 | 2017-11-28 | Amgen Inc | Mammalian cell culture |
| US9475858B2 (en) | 2011-07-08 | 2016-10-25 | Momenta Pharmaceuticals, Inc. | Cell culture process |
| WO2013013013A2 (en) | 2011-07-21 | 2013-01-24 | Alnylam Pharmaceuticals, Inc. | Compositions and methods for producing modified glycoproteins |
| WO2013057078A1 (en) | 2011-10-19 | 2013-04-25 | Roche Glycart Ag | Separation method for fucosylated antibodies |
| WO2013158279A1 (en) * | 2012-04-20 | 2013-10-24 | Abbvie Inc. | Protein purification methods to reduce acidic species |
| WO2013176754A1 (en) * | 2012-05-24 | 2013-11-28 | Abbvie Inc. | Novel purification of antibodies using hydrophobic interaction chromatography |
| US9085618B2 (en) * | 2013-10-18 | 2015-07-21 | Abbvie, Inc. | Low acidic species compositions and methods for producing and using the same |
-
2009
- 2009-10-20 KR KR1020117011176A patent/KR20110091678A/ko not_active Ceased
- 2009-10-20 EP EP09744006.9A patent/EP2350127B1/en not_active Revoked
- 2009-10-20 WO PCT/US2009/061329 patent/WO2010141039A1/en not_active Ceased
- 2009-10-20 RU RU2011120191/10A patent/RU2520838C2/ru active
- 2009-10-20 JP JP2011532332A patent/JP5808249B2/ja active Active
- 2009-10-20 US US12/582,506 patent/US8895709B2/en active Active
- 2009-10-20 BR BRPI0920027A patent/BRPI0920027A2/pt active Search and Examination
- 2009-10-20 CN CN201510422235.4A patent/CN105111309A/zh active Pending
- 2009-10-20 CA CA2911256A patent/CA2911256A1/en not_active Abandoned
- 2009-10-20 AU AU2009347206A patent/AU2009347206C1/en active Active
- 2009-10-20 TW TW098135624A patent/TW201024318A/zh unknown
- 2009-10-20 NZ NZ592095A patent/NZ592095A/xx unknown
- 2009-10-20 EP EP15152668.8A patent/EP2921501A1/en not_active Withdrawn
- 2009-10-20 TW TW104138280A patent/TWI610936B/zh active
- 2009-10-20 CN CN2009801514052A patent/CN102257006A/zh active Pending
- 2009-10-20 MX MX2011004200A patent/MX2011004200A/es active IP Right Grant
- 2009-10-20 SG SG10201702922VA patent/SG10201702922VA/en unknown
- 2009-10-20 CA CA2738498A patent/CA2738498A1/en active Pending
- 2009-10-20 CA CA2932207A patent/CA2932207A1/en not_active Abandoned
- 2009-10-20 ES ES09744006.9T patent/ES2535734T3/es active Active
-
2011
- 2011-03-24 IL IL211918A patent/IL211918A/en active IP Right Grant
- 2011-04-05 ZA ZA2011/02523A patent/ZA201102523B/en unknown
- 2011-04-19 MX MX2015001391A patent/MX343087B/es unknown
- 2011-04-19 MX MX2018014395A patent/MX2018014395A/es unknown
-
2014
- 2014-03-26 US US14/226,636 patent/US9018361B2/en active Active
- 2014-05-13 IL IL232601A patent/IL232601A0/en unknown
- 2014-09-25 JP JP2014195268A patent/JP2015042645A/ja not_active Ceased
-
2015
- 2015-04-13 US US14/685,130 patent/US20150210735A1/en not_active Abandoned
- 2015-04-27 US US14/697,063 patent/US20160083452A1/en not_active Abandoned
- 2015-07-30 AU AU2015207915A patent/AU2015207915C1/en active Active
- 2015-10-12 HK HK15109937.0A patent/HK1209428A1/en unknown
-
2016
- 2016-02-16 IL IL244157A patent/IL244157A0/en unknown
- 2016-08-29 AU AU2016222301A patent/AU2016222301A1/en not_active Abandoned
-
2017
- 2017-02-03 US US15/424,295 patent/US20170158760A1/en not_active Abandoned
-
2018
- 2018-05-30 AU AU2018203810A patent/AU2018203810A1/en not_active Abandoned
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| ES2535734T3 (es) | Aislamiento y purificación de anticuerpos mediante cromatografía de afinidad con la proteína A | |
| RU2558367C2 (ru) | Способ очистки полипептидных растворов | |
| US8017740B2 (en) | Enhanced capacity and purification of antibodies by mixed mode chromatography in the presence of aqueous-soluble nonionic organic polymers | |
| US9957318B2 (en) | Protein purification methods to reduce acidic species | |
| ES2797480T3 (es) | Un procedimiento de cromatografía de reparto débil | |
| ES2539232T3 (es) | Métodos para reducir el nivel de una o más impurezas en una muestra durante la purificación de proteínas | |
| RU2553214C2 (ru) | Способы очистки однодоменных антигенсвязывающих молекул | |
| CA3031028C (en) | Affinity chromatography wash buffer | |
| US11426706B2 (en) | Cation exchange chromatography wash buffer | |
| TWI669314B (zh) | 針對tau之抗體及其用途 | |
| US9193787B2 (en) | Human antibodies that bind human TNF-alpha and methods of preparing the same | |
| JP2022536486A (ja) | 抗α4β7抗体の産生方法 | |
| CA3031390A1 (en) | Anti- immunoglobulin g aptamers and uses thereof | |
| US20090264630A1 (en) | Method of separating monomeric protein(s) | |
| JP2011041475A (ja) | 抗体製造方法 | |
| de Rham | Specificity and Other Biophysical Properties to Guide Developability of Agonistic Bispecific Antibodies | |
| JP2025509572A (ja) | 二重特異性抗体を精製する方法 | |
| JP2025183228A (ja) | 安定性及び生産力価を向上させるためのモノクローナル抗体操作 | |
| Rosa | A phenylboronate chromatography based approach as an effective alternative for the downstream processing of biomolecules | |
| dos Santos | An alternative capture step for monoclonal antibodies: phenylboronate as a new multi-modal ligand |