ES2651483T3 - Método para preparar la forma activa de la proteína de fusión TNRF-Fc - Google Patents
Método para preparar la forma activa de la proteína de fusión TNRF-Fc Download PDFInfo
- Publication number
- ES2651483T3 ES2651483T3 ES12823797.1T ES12823797T ES2651483T3 ES 2651483 T3 ES2651483 T3 ES 2651483T3 ES 12823797 T ES12823797 T ES 12823797T ES 2651483 T3 ES2651483 T3 ES 2651483T3
- Authority
- ES
- Spain
- Prior art keywords
- tnfr
- buffer
- fusion protein
- column
- protein
- 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
- 238000000034 method Methods 0.000 title claims abstract description 58
- 102000037865 fusion proteins Human genes 0.000 title claims abstract description 40
- 108020001507 fusion proteins Proteins 0.000 title claims abstract description 40
- 108010008165 Etanercept Proteins 0.000 claims abstract description 87
- 238000004191 hydrophobic interaction chromatography Methods 0.000 claims abstract description 53
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 claims abstract description 39
- 102000003298 tumor necrosis factor receptor Human genes 0.000 claims abstract description 39
- PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 claims abstract description 34
- 229910052938 sodium sulfate Inorganic materials 0.000 claims abstract description 34
- 235000011152 sodium sulphate Nutrition 0.000 claims abstract description 34
- 239000001509 sodium citrate Substances 0.000 claims abstract description 32
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 claims abstract description 32
- 239000001488 sodium phosphate Substances 0.000 claims abstract description 30
- 229910000162 sodium phosphate Inorganic materials 0.000 claims abstract description 30
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 claims abstract description 30
- 239000000203 mixture Substances 0.000 claims abstract description 29
- 239000006167 equilibration buffer Substances 0.000 claims abstract description 26
- 150000003839 salts Chemical class 0.000 claims abstract description 26
- 239000012149 elution buffer Substances 0.000 claims abstract description 20
- 238000011068 loading method Methods 0.000 claims abstract description 16
- 239000011534 wash buffer Substances 0.000 claims abstract description 9
- 239000012539 chromatography resin Substances 0.000 claims abstract description 6
- 108090000623 proteins and genes Proteins 0.000 claims description 96
- 239000000872 buffer Substances 0.000 claims description 38
- 239000013598 vector Substances 0.000 claims description 22
- 239000003446 ligand Substances 0.000 claims description 7
- 125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 6
- 238000004255 ion exchange chromatography Methods 0.000 claims description 4
- 238000001042 affinity chromatography Methods 0.000 claims description 3
- 125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 claims description 3
- 125000000217 alkyl group Chemical group 0.000 claims description 2
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 claims description 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 claims description 2
- 235000011130 ammonium sulphate Nutrition 0.000 claims description 2
- 238000010612 desalination reaction Methods 0.000 claims description 2
- 125000002347 octyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 claims description 2
- 235000011083 sodium citrates Nutrition 0.000 claims description 2
- 241001125831 Istiophoridae Species 0.000 claims 1
- 229910019142 PO4 Inorganic materials 0.000 claims 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims 1
- 239000010452 phosphate Substances 0.000 claims 1
- 210000004962 mammalian cell Anatomy 0.000 abstract description 2
- 238000005406 washing Methods 0.000 abstract description 2
- 102000004169 proteins and genes Human genes 0.000 description 80
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 31
- 210000004027 cell Anatomy 0.000 description 14
- 239000013604 expression vector Substances 0.000 description 14
- 108060003951 Immunoglobulin Proteins 0.000 description 13
- 125000003275 alpha amino acid group Chemical group 0.000 description 13
- 102000018358 immunoglobulin Human genes 0.000 description 13
- 102000005396 glutamine synthetase Human genes 0.000 description 12
- 108020002326 glutamine synthetase Proteins 0.000 description 12
- 102100040247 Tumor necrosis factor Human genes 0.000 description 11
- 230000000694 effects Effects 0.000 description 11
- 230000004071 biological effect Effects 0.000 description 10
- 238000000926 separation method Methods 0.000 description 10
- 239000011780 sodium chloride Substances 0.000 description 10
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 9
- 102100033733 Tumor necrosis factor receptor superfamily member 1B Human genes 0.000 description 9
- 230000027455 binding Effects 0.000 description 9
- 230000014509 gene expression Effects 0.000 description 9
- 108091033319 polynucleotide Proteins 0.000 description 9
- 239000002157 polynucleotide Substances 0.000 description 9
- 102000040430 polynucleotide Human genes 0.000 description 9
- 239000000243 solution Substances 0.000 description 9
- 101710187830 Tumor necrosis factor receptor superfamily member 1B Proteins 0.000 description 8
- 150000001413 amino acids Chemical class 0.000 description 8
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 8
- 230000002209 hydrophobic effect Effects 0.000 description 8
- 239000007853 buffer solution Substances 0.000 description 7
- 238000006073 displacement reaction Methods 0.000 description 7
- 230000003993 interaction Effects 0.000 description 7
- 238000000746 purification Methods 0.000 description 7
- 241000699800 Cricetinae Species 0.000 description 6
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 6
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 6
- 239000000539 dimer Substances 0.000 description 6
- 229940027941 immunoglobulin g Drugs 0.000 description 6
- 238000006467 substitution reaction Methods 0.000 description 6
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 5
- 239000012617 Butyl Sepharose™ 4 Fast Flow Substances 0.000 description 5
- 101150074155 DHFR gene Proteins 0.000 description 5
- 108090000765 processed proteins & peptides Proteins 0.000 description 5
- 101150074355 GS gene Proteins 0.000 description 4
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 4
- 238000007792 addition Methods 0.000 description 4
- 239000012491 analyte Substances 0.000 description 4
- 210000004102 animal cell Anatomy 0.000 description 4
- 238000004587 chromatography analysis Methods 0.000 description 4
- 238000007796 conventional method Methods 0.000 description 4
- 238000012217 deletion Methods 0.000 description 4
- 230000037430 deletion Effects 0.000 description 4
- 229920001184 polypeptide Polymers 0.000 description 4
- 238000002360 preparation method Methods 0.000 description 4
- 230000008569 process Effects 0.000 description 4
- 102000004196 processed proteins & peptides Human genes 0.000 description 4
- 239000000047 product Substances 0.000 description 4
- 238000001542 size-exclusion chromatography Methods 0.000 description 4
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 108020004511 Recombinant DNA Proteins 0.000 description 3
- 238000004113 cell culture Methods 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 238000004140 cleaning Methods 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 239000012228 culture supernatant Substances 0.000 description 3
- 238000004925 denaturation Methods 0.000 description 3
- 230000036425 denaturation Effects 0.000 description 3
- 238000010586 diagram Methods 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 239000003814 drug Substances 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 238000011067 equilibration Methods 0.000 description 3
- 239000000284 extract Substances 0.000 description 3
- 239000012634 fragment Substances 0.000 description 3
- 230000004927 fusion Effects 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 238000002955 isolation Methods 0.000 description 3
- 239000002609 medium Substances 0.000 description 3
- 239000002773 nucleotide Substances 0.000 description 3
- 125000003729 nucleotide group Chemical group 0.000 description 3
- 239000012460 protein solution Substances 0.000 description 3
- 230000002829 reductive effect Effects 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 239000006228 supernatant Substances 0.000 description 3
- MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 2
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- 239000004475 Arginine Substances 0.000 description 2
- 208000023275 Autoimmune disease Diseases 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- 102100024746 Dihydrofolate reductase Human genes 0.000 description 2
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 239000004471 Glycine Substances 0.000 description 2
- 101100288095 Klebsiella pneumoniae neo gene Proteins 0.000 description 2
- 241001045988 Neogene Species 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 150000001483 arginine derivatives Chemical class 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 108020001096 dihydrofolate reductase Proteins 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 239000012091 fetal bovine serum Substances 0.000 description 2
- 238000004128 high performance liquid chromatography Methods 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 229930027917 kanamycin Natural products 0.000 description 2
- 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 2
- 229960000318 kanamycin Drugs 0.000 description 2
- 229930182823 kanamycin A Natural products 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 101150091879 neo gene Proteins 0.000 description 2
- 230000002018 overexpression Effects 0.000 description 2
- 230000036961 partial effect Effects 0.000 description 2
- 239000011347 resin Substances 0.000 description 2
- 229920005989 resin Polymers 0.000 description 2
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 2
- 239000012266 salt solution Substances 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- 238000000108 ultra-filtration Methods 0.000 description 2
- VZSRBBMJRBPUNF-UHFFFAOYSA-N 2-(2,3-dihydro-1H-inden-2-ylamino)-N-[3-oxo-3-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)propyl]pyrimidine-5-carboxamide Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C(=O)NCCC(N1CC2=C(CC1)NN=N2)=O VZSRBBMJRBPUNF-UHFFFAOYSA-N 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 102000014914 Carrier Proteins Human genes 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101000801232 Homo sapiens Tumor necrosis factor receptor superfamily member 1B Proteins 0.000 description 1
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 1
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 1
- 108020004684 Internal Ribosome Entry Sites Proteins 0.000 description 1
- 239000012097 Lipofectamine 2000 Substances 0.000 description 1
- NIPNSKYNPDTRPC-UHFFFAOYSA-N N-[2-oxo-2-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)ethyl]-2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidine-5-carboxamide Chemical compound O=C(CNC(=O)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F)N1CC2=C(CC1)NN=N2 NIPNSKYNPDTRPC-UHFFFAOYSA-N 0.000 description 1
- AFCARXCZXQIEQB-UHFFFAOYSA-N N-[3-oxo-3-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)propyl]-2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidine-5-carboxamide Chemical compound O=C(CCNC(=O)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F)N1CC2=C(CC1)NN=N2 AFCARXCZXQIEQB-UHFFFAOYSA-N 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 108010022394 Threonine synthase Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- 239000003463 adsorbent Substances 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 125000000539 amino acid group Chemical group 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 108091008324 binding proteins Proteins 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 238000012832 cell culture technique Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000009792 diffusion process Methods 0.000 description 1
- 102000004419 dihydrofolate reductase Human genes 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 239000003344 environmental pollutant Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 125000004185 ester group Chemical group 0.000 description 1
- 229960000403 etanercept Drugs 0.000 description 1
- RTZKZFJDLAIYFH-UHFFFAOYSA-N ether Substances CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 239000013020 final formulation Substances 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229940098197 human immunoglobulin g Drugs 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 238000004811 liquid chromatography Methods 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 239000011159 matrix material Substances 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 238000001471 micro-filtration Methods 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 230000009871 nonspecific binding Effects 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 231100000719 pollutant Toxicity 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 230000011218 segmentation Effects 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 230000005026 transcription initiation Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70578—NGF-receptor/TNF-receptor superfamily, e.g. CD27, CD30, CD40, CD95
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K19/00—Hybrid peptides, i.e. peptides covalently bound to nucleic acids, or non-covalently bound protein-protein complexes
-
- 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
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/715—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons
- C07K14/7151—Receptors; Cell surface antigens; Cell surface determinants for cytokines; for lymphokines; for interferons for tumor necrosis factor [TNF], for lymphotoxin [LT]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Cell Biology (AREA)
- Immunology (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Analytical Chemistry (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| KR20110081854 | 2011-08-17 | ||
| KR20110081854 | 2011-08-17 | ||
| PCT/KR2012/006564 WO2013025079A1 (en) | 2011-08-17 | 2012-08-17 | Method for preparing active form of tnfr-fc fusion protein |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| ES2651483T3 true ES2651483T3 (es) | 2018-01-26 |
Family
ID=47715279
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| ES12823797.1T Active ES2651483T3 (es) | 2011-08-17 | 2012-08-17 | Método para preparar la forma activa de la proteína de fusión TNRF-Fc |
Country Status (6)
| Country | Link |
|---|---|
| US (1) | US9279014B2 (enExample) |
| EP (1) | EP2753634B1 (enExample) |
| JP (2) | JP6223338B2 (enExample) |
| KR (1) | KR101454316B1 (enExample) |
| ES (1) | ES2651483T3 (enExample) |
| WO (1) | WO2013025079A1 (enExample) |
Families Citing this family (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SG11201401562RA (en) | 2011-10-18 | 2014-09-26 | Coherus Biosciences Inc | Etanercept formulations stabilized with sodium chloride |
| EP2825641A4 (en) * | 2012-03-12 | 2015-09-30 | Hanwha Chemical Corp | EXPRESSION VECTOR WITH A POLYNUCLEOTIDE CODING FOR A MODIFIED GLUTAMINE SYNTHETASE AND METHOD FOR PRODUCING A TARGET PROTEIN THEREFOR |
| AU2013315750B9 (en) | 2012-09-11 | 2018-11-15 | Coherus Biosciences, Inc. | Correctly folded etanercept in high purity and excellent yield |
| AU2014217561B2 (en) | 2013-02-13 | 2018-11-15 | Laboratoire Francais Du Fractionnement Et Des Biotechnologies | Highly galactosylated anti-TNF-alpha antibodies and uses thereof |
| WO2015189832A1 (en) * | 2014-06-13 | 2015-12-17 | Lupin Limited | Process for the purification of tnfr:fc fusion protein |
| ES2733298T3 (es) | 2014-07-18 | 2019-11-28 | Sandoz Ag | Cuantificación de TNFR2:Fc plegado erróneamente |
| US10988527B2 (en) | 2014-12-31 | 2021-04-27 | Lg Chem, Ltd. | Method for preparing TNFR-Fc fusion protein containing target content of impurities |
| WO2016149139A1 (en) * | 2015-03-13 | 2016-09-22 | Samsung Bioepis Co., Ltd. | Anti-tnf-alpha polypeptide composition and use thereof |
| US11952399B2 (en) * | 2018-12-18 | 2024-04-09 | Amgen Inc. | Methods for purifying proteins |
| US12411064B2 (en) | 2020-05-08 | 2025-09-09 | Waters Technologies Corporation | Methods for heat-assisted enzyme digestion |
| CN115552215A (zh) | 2020-05-08 | 2022-12-30 | 沃特世科技公司 | 用于热辅助酶消化的方法 |
Family Cites Families (8)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| TR200504220T2 (tr) | 1998-12-17 | 2007-04-24 | Biogen Idec Ma Inc. | Aktif limfotoksin-beta reseptör imunoglobülin şimeAktif limfotoksin-beta reseptör imunoglobülin şimerik proteinlerinin yüksek düzey ifadesi ve saflaştrik proteinlerinin yüksek düzey ifadesi ve saflaştırılması için bir yöntem.ırılması için bir yöntem. |
| US7294481B1 (en) | 1999-01-05 | 2007-11-13 | Immunex Corporation | Method for producing recombinant proteins |
| SI1478394T1 (sl) * | 2002-02-27 | 2008-12-31 | Immunex Corp | STABILIZIRAN TNFR-Fc SESTAVEK Z ARGININOM |
| DE602004026343D1 (de) * | 2003-10-24 | 2010-05-12 | Amgen Inc | Verfahren zur aufreinigung von proteinen in einer durchflussfraktion aus der chromatographie mit hydrophoben wechselwirkungen |
| US7781395B2 (en) | 2004-01-30 | 2010-08-24 | Immunex Corporation | Process for purifying proteins |
| JP2011514895A (ja) * | 2008-02-29 | 2011-05-12 | バイオジェン・アイデック・エムエイ・インコーポレイテッド | 精製免疫グロブリン融合タンパク質およびその精製方法 |
| CN102675465A (zh) * | 2011-03-09 | 2012-09-19 | 上海赛金生物医药有限公司 | 重组人ⅱ型肿瘤坏死因子受体-抗体融合蛋白的纯化方法 |
| EP2723759A4 (en) * | 2011-06-24 | 2015-01-28 | Reddys Lab Ltd Dr | PURIFICATION OF CHIMERIC PROTEIN |
-
2012
- 2012-08-17 KR KR1020120090341A patent/KR101454316B1/ko not_active Expired - Fee Related
- 2012-08-17 WO PCT/KR2012/006564 patent/WO2013025079A1/en not_active Ceased
- 2012-08-17 US US14/239,216 patent/US9279014B2/en active Active
- 2012-08-17 EP EP12823797.1A patent/EP2753634B1/en active Active
- 2012-08-17 JP JP2014525943A patent/JP6223338B2/ja not_active Expired - Fee Related
- 2012-08-17 ES ES12823797.1T patent/ES2651483T3/es active Active
-
2016
- 2016-05-26 JP JP2016105574A patent/JP2016168049A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| US9279014B2 (en) | 2016-03-08 |
| WO2013025079A1 (en) | 2013-02-21 |
| EP2753634B1 (en) | 2017-11-01 |
| JP2016168049A (ja) | 2016-09-23 |
| EP2753634A1 (en) | 2014-07-16 |
| JP2014521364A (ja) | 2014-08-28 |
| US20140316114A1 (en) | 2014-10-23 |
| JP6223338B2 (ja) | 2017-11-01 |
| KR20130020644A (ko) | 2013-02-27 |
| EP2753634A4 (en) | 2015-05-20 |
| KR101454316B1 (ko) | 2014-10-27 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US9279014B2 (en) | Methods for preparing an active TNFR-Fc fusion protein | |
| ES2322945T5 (es) | Métodos para purficación de proteína | |
| ES2732907T3 (es) | Procedimiento de expresión | |
| JP7201599B2 (ja) | プロテインｌを用いたタンパク質精製 | |
| ES2554482T3 (es) | Un método para la expresión a alto nivel de proteínas de fusión del miembro lg de la familia del receptor de TNF activas y su purificación | |
| ES2839211T3 (es) | Método para purificar proteínas de fusión a albúmina | |
| CN113227134A (zh) | 抗体的Fc区变体 | |
| ES2656167T5 (es) | Cromatografía de intercambio iónico con selectividad mejorada para la separación de monómeros, agregados y fragmentos polipeptídicos mediante la modulación de la fase móvil | |
| BR112021006737A2 (pt) | engenharia de enzimas dnase para fabricação e terapia | |
| ES2813501T3 (es) | Métodos de replegado de proteínas basados en filtración de flujo tangencial | |
| ES2942024T3 (es) | Métodos para caracterizar enlaces disulfuro | |
| JP2016519144A (ja) | 最小限の単量体の分離を伴う組換えポリクローナル多量体の分離 | |
| ES2733298T3 (es) | Cuantificación de TNFR2:Fc plegado erróneamente | |
| Minchiotti et al. | Structural characterization, stability and fatty acid-binding properties of two French genetic variants of human serum albumin | |
| AU2005259269A1 (en) | Process for the purification of IL-18 binding protein | |
| CA3133740A1 (en) | Recombinant ccn domain proteins and fusion proteins | |
| ES2612427T3 (es) | Método para purificar teriparatida (PTH1-34) | |
| CN104379598B (zh) | 高度糖基化的长效人生长激素蛋白及其生产方法 | |
| ES3040791T3 (en) | Methods for the purification of refolded fc-peptide fusion protein | |
| RU2670166C1 (ru) | Способ получения слитого белка tnfr-fc с заданным содержанием примесей | |
| CN116745309A (zh) | 用于纯化抗-4-1bb/抗-her2双特异性抗体的方法 | |
| ES2841648T3 (es) | Procedimiento para purificar eritropoyetina PEGilada | |
| JP2013545440A (ja) | マカカ・ファシキュラリス（Ｍａｃａｃａｆａｓｃｉｃｕｌａｒｉｓ）ＣＣＬ１７ | |
| JP2026082949A (ja) | 製造及び治療のためのｄｎａｓｅ酵素の操作 | |
| NZ733388B (en) | Method for preparing tnfr-fc fusion protein containing target content of impurities |