JP4762904B2 - 免疫グロブリン不変領域の量産方法 - Google Patents
免疫グロブリン不変領域の量産方法 Download PDFInfo
- Publication number
- JP4762904B2 JP4762904B2 JP2006539397A JP2006539397A JP4762904B2 JP 4762904 B2 JP4762904 B2 JP 4762904B2 JP 2006539397 A JP2006539397 A JP 2006539397A JP 2006539397 A JP2006539397 A JP 2006539397A JP 4762904 B2 JP4762904 B2 JP 4762904B2
- Authority
- JP
- Japan
- Prior art keywords
- constant region
- immunoglobulin
- protein
- acid sequence
- region
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired - Lifetime
Links
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 title claims description 56
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 title claims description 56
- 238000004519 manufacturing process Methods 0.000 title claims description 20
- 238000000034 method Methods 0.000 claims abstract description 62
- 238000012258 culturing Methods 0.000 claims abstract description 6
- 241000588724 Escherichia coli Species 0.000 claims description 83
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 60
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 48
- 239000013604 expression vector Substances 0.000 claims description 48
- 108060003951 Immunoglobulin Proteins 0.000 claims description 45
- 102000018358 immunoglobulin Human genes 0.000 claims description 45
- 101710146739 Enterotoxin Proteins 0.000 claims description 32
- 231100000655 enterotoxin Toxicity 0.000 claims description 32
- 239000000147 enterotoxin Substances 0.000 claims description 32
- 150000007523 nucleic acids Chemical group 0.000 claims description 22
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 21
- 210000000805 cytoplasm Anatomy 0.000 claims description 14
- 238000003259 recombinant expression Methods 0.000 claims description 13
- 210000001236 prokaryotic cell Anatomy 0.000 claims description 10
- 229910052799 carbon Inorganic materials 0.000 claims description 5
- 230000001131 transforming effect Effects 0.000 claims description 4
- 239000013598 vector Substances 0.000 abstract description 27
- 239000003814 drug Substances 0.000 abstract description 14
- 229940079593 drug Drugs 0.000 abstract description 12
- 230000000694 effects Effects 0.000 abstract description 7
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 abstract description 5
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 abstract description 5
- 238000001727 in vivo Methods 0.000 abstract description 5
- 239000003937 drug carrier Substances 0.000 abstract description 3
- 230000009467 reduction Effects 0.000 abstract description 2
- 108090000623 proteins and genes Proteins 0.000 description 143
- 102000004169 proteins and genes Human genes 0.000 description 101
- 235000018102 proteins Nutrition 0.000 description 91
- 210000004027 cell Anatomy 0.000 description 30
- 230000014509 gene expression Effects 0.000 description 30
- 108090000765 processed proteins & peptides Proteins 0.000 description 28
- 239000013612 plasmid Substances 0.000 description 23
- 239000000539 dimer Substances 0.000 description 21
- 235000001014 amino acid Nutrition 0.000 description 20
- 210000004369 blood Anatomy 0.000 description 20
- 239000008280 blood Substances 0.000 description 20
- 229940024606 amino acid Drugs 0.000 description 19
- 150000001413 amino acids Chemical class 0.000 description 18
- 229920001223 polyethylene glycol Polymers 0.000 description 18
- 102000004196 processed proteins & peptides Human genes 0.000 description 18
- 239000000047 product Substances 0.000 description 18
- 108091008146 restriction endonucleases Proteins 0.000 description 18
- 239000000243 solution Substances 0.000 description 18
- 229920001184 polypeptide Polymers 0.000 description 17
- 102000003951 Erythropoietin Human genes 0.000 description 16
- 108090000394 Erythropoietin Proteins 0.000 description 16
- 238000009739 binding Methods 0.000 description 16
- 229940105423 erythropoietin Drugs 0.000 description 16
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 16
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 15
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 15
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 15
- 239000012634 fragment Substances 0.000 description 14
- 230000006870 function Effects 0.000 description 14
- 108020001507 fusion proteins Proteins 0.000 description 14
- 102000037865 fusion proteins Human genes 0.000 description 14
- 230000001965 increasing effect Effects 0.000 description 12
- 210000004102 animal cell Anatomy 0.000 description 11
- 239000000178 monomer Substances 0.000 description 11
- 238000006243 chemical reaction Methods 0.000 description 10
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 10
- 239000012636 effector Substances 0.000 description 10
- 239000000499 gel Substances 0.000 description 10
- 230000028993 immune response Effects 0.000 description 10
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 10
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 9
- 230000004927 fusion Effects 0.000 description 9
- 210000001322 periplasm Anatomy 0.000 description 9
- 230000001225 therapeutic effect Effects 0.000 description 9
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 8
- 102100029880 Glycodelin Human genes 0.000 description 8
- 101000585553 Homo sapiens Glycodelin Proteins 0.000 description 8
- 238000000855 fermentation Methods 0.000 description 8
- 230000004151 fermentation Effects 0.000 description 8
- 230000001939 inductive effect Effects 0.000 description 8
- 102000005962 receptors Human genes 0.000 description 8
- 108020003175 receptors Proteins 0.000 description 8
- 230000002829 reductive effect Effects 0.000 description 8
- 239000000126 substance Substances 0.000 description 8
- 235000000346 sugar Nutrition 0.000 description 8
- 102000004190 Enzymes Human genes 0.000 description 7
- 108090000790 Enzymes Proteins 0.000 description 7
- 241000282412 Homo Species 0.000 description 7
- 125000000539 amino acid group Chemical group 0.000 description 7
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 7
- 229940088598 enzyme Drugs 0.000 description 7
- 230000010437 erythropoiesis Effects 0.000 description 7
- 244000005700 microbiome Species 0.000 description 7
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- 125000003412 L-alanyl group Chemical group [H]N([H])[C@@](C([H])([H])[H])(C(=O)[*])[H] 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 229960000182 blood factors Drugs 0.000 description 6
- 238000010367 cloning Methods 0.000 description 6
- 238000003780 insertion Methods 0.000 description 6
- 230000037431 insertion Effects 0.000 description 6
- 239000012528 membrane Substances 0.000 description 6
- 230000008569 process Effects 0.000 description 6
- 230000006798 recombination Effects 0.000 description 6
- 238000006467 substitution reaction Methods 0.000 description 6
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 5
- 241001198387 Escherichia coli BL21(DE3) Species 0.000 description 5
- 102000009109 Fc receptors Human genes 0.000 description 5
- 108010087819 Fc receptors Proteins 0.000 description 5
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 5
- 239000000427 antigen Substances 0.000 description 5
- 102000036639 antigens Human genes 0.000 description 5
- 108091007433 antigens Proteins 0.000 description 5
- 230000000975 bioactive effect Effects 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- 230000003013 cytotoxicity Effects 0.000 description 5
- 231100000135 cytotoxicity Toxicity 0.000 description 5
- 238000012217 deletion Methods 0.000 description 5
- 230000037430 deletion Effects 0.000 description 5
- 229940072221 immunoglobulins Drugs 0.000 description 5
- 238000001556 precipitation Methods 0.000 description 5
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 5
- 238000003757 reverse transcription PCR Methods 0.000 description 5
- 239000000523 sample Substances 0.000 description 5
- 230000028327 secretion Effects 0.000 description 5
- -1 teat Chemical compound 0.000 description 5
- 102000014914 Carrier Proteins Human genes 0.000 description 4
- 108010019673 Darbepoetin alfa Proteins 0.000 description 4
- 101150002621 EPO gene Proteins 0.000 description 4
- 206010061218 Inflammation Diseases 0.000 description 4
- 102000015696 Interleukins Human genes 0.000 description 4
- 108010063738 Interleukins Proteins 0.000 description 4
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 4
- 108010025020 Nerve Growth Factor Proteins 0.000 description 4
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 4
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 4
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 4
- 229940115115 aranesp Drugs 0.000 description 4
- 108091008324 binding proteins Proteins 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 239000006227 byproduct Substances 0.000 description 4
- 239000013592 cell lysate Substances 0.000 description 4
- 238000004440 column chromatography Methods 0.000 description 4
- 230000000295 complement effect Effects 0.000 description 4
- 230000001419 dependent effect Effects 0.000 description 4
- 230000012010 growth Effects 0.000 description 4
- 230000004054 inflammatory process Effects 0.000 description 4
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 4
- 229910052757 nitrogen Inorganic materials 0.000 description 4
- CSCPPACGZOOCGX-UHFFFAOYSA-N Acetone Chemical compound CC(C)=O CSCPPACGZOOCGX-UHFFFAOYSA-N 0.000 description 3
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 3
- 102000004127 Cytokines Human genes 0.000 description 3
- 108090000695 Cytokines Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 102000006992 Interferon-alpha Human genes 0.000 description 3
- 108010047761 Interferon-alpha Proteins 0.000 description 3
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 3
- 125000000570 L-alpha-aspartyl group Chemical group [H]OC(=O)C([H])([H])[C@]([H])(N([H])[H])C(*)=O 0.000 description 3
- 102000007072 Nerve Growth Factors Human genes 0.000 description 3
- 239000002033 PVDF binder Substances 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 102000035195 Peptidases Human genes 0.000 description 3
- KWYUFKZDYYNOTN-UHFFFAOYSA-M Potassium hydroxide Chemical compound [OH-].[K+] KWYUFKZDYYNOTN-UHFFFAOYSA-M 0.000 description 3
- TUYWCHPXKQTISF-LPEHRKFASA-N Pro-Cys-Pro Chemical compound C1C[C@H](NC1)C(=O)N[C@@H](CS)C(=O)N2CCC[C@@H]2C(=O)O TUYWCHPXKQTISF-LPEHRKFASA-N 0.000 description 3
- 238000012300 Sequence Analysis Methods 0.000 description 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 3
- 108020005038 Terminator Codon Proteins 0.000 description 3
- 239000007983 Tris buffer Substances 0.000 description 3
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 230000000903 blocking effect Effects 0.000 description 3
- 210000000601 blood cell Anatomy 0.000 description 3
- 239000003638 chemical reducing agent Substances 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
- 238000012790 confirmation Methods 0.000 description 3
- 235000018417 cysteine Nutrition 0.000 description 3
- 239000003102 growth factor Substances 0.000 description 3
- 238000003018 immunoassay Methods 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 229940047122 interleukins Drugs 0.000 description 3
- 238000010369 molecular cloning Methods 0.000 description 3
- VLKZOEOYAKHREP-UHFFFAOYSA-N n-Hexane Chemical compound CCCCCC VLKZOEOYAKHREP-UHFFFAOYSA-N 0.000 description 3
- 108020004707 nucleic acids Proteins 0.000 description 3
- 102000039446 nucleic acids Human genes 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 229920002981 polyvinylidene fluoride Polymers 0.000 description 3
- 238000000746 purification Methods 0.000 description 3
- 238000005215 recombination Methods 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 238000002741 site-directed mutagenesis Methods 0.000 description 3
- 239000011734 sodium Substances 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 238000003756 stirring Methods 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 3
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 3
- 238000001262 western blot Methods 0.000 description 3
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonia chloride Chemical compound [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 description 2
- 108010053652 Butyrylcholinesterase Proteins 0.000 description 2
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 2
- 102100032404 Cholinesterase Human genes 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 102400001368 Epidermal growth factor Human genes 0.000 description 2
- 101800003838 Epidermal growth factor Proteins 0.000 description 2
- 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 2
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
- 108010000521 Human Growth Hormone Proteins 0.000 description 2
- 102100026120 IgG receptor FcRn large subunit p51 Human genes 0.000 description 2
- 101710177940 IgG receptor FcRn large subunit p51 Proteins 0.000 description 2
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 2
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 2
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 2
- 102000013463 Immunoglobulin Light Chains Human genes 0.000 description 2
- 108010065825 Immunoglobulin Light Chains Proteins 0.000 description 2
- 108020005350 Initiator Codon Proteins 0.000 description 2
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 2
- 108090000467 Interferon-beta Proteins 0.000 description 2
- 102000014150 Interferons Human genes 0.000 description 2
- 108010050904 Interferons Proteins 0.000 description 2
- 102000019223 Interleukin-1 receptor Human genes 0.000 description 2
- 108050006617 Interleukin-1 receptor Proteins 0.000 description 2
- 102000010787 Interleukin-4 Receptors Human genes 0.000 description 2
- 108010038486 Interleukin-4 Receptors Proteins 0.000 description 2
- 125000003440 L-leucyl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])C(C([H])([H])[H])([H])C([H])([H])[H] 0.000 description 2
- 125000002842 L-seryl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])O[H] 0.000 description 2
- 108010063045 Lactoferrin Proteins 0.000 description 2
- 102000010445 Lactoferrin Human genes 0.000 description 2
- 102000004882 Lipase Human genes 0.000 description 2
- 108090001060 Lipase Proteins 0.000 description 2
- 102100033342 Lysosomal acid glucosylceramidase Human genes 0.000 description 2
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
- 102100039364 Metalloproteinase inhibitor 1 Human genes 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
- 239000002202 Polyethylene glycol Substances 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 241000700159 Rattus Species 0.000 description 2
- 102000013275 Somatomedins Human genes 0.000 description 2
- 239000012505 Superdex™ Substances 0.000 description 2
- 230000002159 abnormal effect Effects 0.000 description 2
- 230000003213 activating effect Effects 0.000 description 2
- 239000012190 activator Substances 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- 102000005840 alpha-Galactosidase Human genes 0.000 description 2
- 108010030291 alpha-Galactosidase Proteins 0.000 description 2
- 238000003277 amino acid sequence analysis Methods 0.000 description 2
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 2
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 229940041514 candida albicans extract Drugs 0.000 description 2
- 239000004202 carbamide Substances 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 230000004540 complement-dependent cytotoxicity Effects 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 238000011033 desalting Methods 0.000 description 2
- 235000014113 dietary fatty acids Nutrition 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 238000010828 elution Methods 0.000 description 2
- 229940116977 epidermal growth factor Drugs 0.000 description 2
- 230000007717 exclusion Effects 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- 229930195729 fatty acid Natural products 0.000 description 2
- 239000000194 fatty acid Substances 0.000 description 2
- 150000004665 fatty acids Chemical class 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- 230000013595 glycosylation Effects 0.000 description 2
- 238000006206 glycosylation reaction Methods 0.000 description 2
- IPCSVZSSVZVIGE-UHFFFAOYSA-N hexadecanoic acid Chemical compound CCCCCCCCCCCCCCCC(O)=O IPCSVZSSVZVIGE-UHFFFAOYSA-N 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 230000036039 immunity Effects 0.000 description 2
- 230000001976 improved effect Effects 0.000 description 2
- 210000003000 inclusion body Anatomy 0.000 description 2
- 230000006698 induction 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
- 230000003993 interaction Effects 0.000 description 2
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 2
- CSSYQJWUGATIHM-IKGCZBKSSA-N l-phenylalanyl-l-lysyl-l-cysteinyl-l-arginyl-l-arginyl-l-tryptophyl-l-glutaminyl-l-tryptophyl-l-arginyl-l-methionyl-l-lysyl-l-lysyl-l-leucylglycyl-l-alanyl-l-prolyl-l-seryl-l-isoleucyl-l-threonyl-l-cysteinyl-l-valyl-l-arginyl-l-arginyl-l-alanyl-l-phenylal Chemical compound C([C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CS)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=CC=C1 CSSYQJWUGATIHM-IKGCZBKSSA-N 0.000 description 2
- 229940078795 lactoferrin Drugs 0.000 description 2
- 235000021242 lactoferrin Nutrition 0.000 description 2
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 2
- 239000003446 ligand Substances 0.000 description 2
- 210000002540 macrophage Anatomy 0.000 description 2
- 239000003550 marker Substances 0.000 description 2
- 239000003900 neurotrophic factor Substances 0.000 description 2
- 239000001301 oxygen Substances 0.000 description 2
- 229910052760 oxygen Inorganic materials 0.000 description 2
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 2
- COLNVLDHVKWLRT-QMMMGPOBSA-N phenylalanine group Chemical group N[C@@H](CC1=CC=CC=C1)C(=O)O COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- REQCZEXYDRLIBE-UHFFFAOYSA-N procainamide Chemical compound CCN(CC)CCNC(=O)C1=CC=C(N)C=C1 REQCZEXYDRLIBE-UHFFFAOYSA-N 0.000 description 2
- 235000019833 protease Nutrition 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 239000002464 receptor antagonist Substances 0.000 description 2
- 229940044551 receptor antagonist Drugs 0.000 description 2
- 238000010188 recombinant method Methods 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 210000002966 serum Anatomy 0.000 description 2
- 229910052708 sodium Inorganic materials 0.000 description 2
- 239000012086 standard solution Substances 0.000 description 2
- 150000008163 sugars Chemical class 0.000 description 2
- 238000001308 synthesis method Methods 0.000 description 2
- 238000012546 transfer Methods 0.000 description 2
- 230000032258 transport Effects 0.000 description 2
- 108010087967 type I signal peptidase Proteins 0.000 description 2
- 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 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 239000012138 yeast extract Substances 0.000 description 2
- COEXAQSTZUWMRI-STQMWFEESA-N (2s)-1-[2-[[(2s)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]acetyl]pyrrolidine-2-carboxylic acid Chemical compound C([C@H](N)C(=O)NCC(=O)N1[C@@H](CCC1)C(O)=O)C1=CC=C(O)C=C1 COEXAQSTZUWMRI-STQMWFEESA-N 0.000 description 1
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 description 1
- 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
- PAWQVTBBRAZDMG-UHFFFAOYSA-N 2-(3-bromo-2-fluorophenyl)acetic acid Chemical compound OC(=O)CC1=CC=CC(Br)=C1F PAWQVTBBRAZDMG-UHFFFAOYSA-N 0.000 description 1
- JVJUWEFOGFCHKR-UHFFFAOYSA-N 2-(diethylamino)ethyl 1-(3,4-dimethylphenyl)cyclopentane-1-carboxylate;hydrochloride Chemical compound Cl.C=1C=C(C)C(C)=CC=1C1(C(=O)OCCN(CC)CC)CCCC1 JVJUWEFOGFCHKR-UHFFFAOYSA-N 0.000 description 1
- 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 1
- HFDKKNHCYWNNNQ-YOGANYHLSA-N 75976-10-2 Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(N)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@@H](NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](C)N)C(C)C)[C@@H](C)O)C1=CC=C(O)C=C1 HFDKKNHCYWNNNQ-YOGANYHLSA-N 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- VHUUQVKOLVNVRT-UHFFFAOYSA-N Ammonium hydroxide Chemical compound [NH4+].[OH-] VHUUQVKOLVNVRT-UHFFFAOYSA-N 0.000 description 1
- 239000004254 Ammonium phosphate Substances 0.000 description 1
- 108010009906 Angiopoietins Proteins 0.000 description 1
- 102000009840 Angiopoietins Human genes 0.000 description 1
- 102400000068 Angiostatin Human genes 0.000 description 1
- 108010079709 Angiostatins Proteins 0.000 description 1
- 108010064733 Angiotensins Proteins 0.000 description 1
- 102000015427 Angiotensins Human genes 0.000 description 1
- 101710095339 Apolipoprotein E Proteins 0.000 description 1
- 102100029470 Apolipoprotein E Human genes 0.000 description 1
- 102100033367 Appetite-regulating hormone Human genes 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- 108010024976 Asparaginase Proteins 0.000 description 1
- 102000002723 Atrial Natriuretic Factor Human genes 0.000 description 1
- 101800001288 Atrial natriuretic factor Proteins 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 101000645291 Bos taurus Metalloproteinase inhibitor 2 Proteins 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 102400000667 Brain natriuretic peptide 32 Human genes 0.000 description 1
- 101800000407 Brain natriuretic peptide 32 Proteins 0.000 description 1
- 101800002247 Brain natriuretic peptide 45 Proteins 0.000 description 1
- 108010074051 C-Reactive Protein Proteins 0.000 description 1
- 102100032752 C-reactive protein Human genes 0.000 description 1
- 102000017420 CD3 protein, epsilon/gamma/delta subunit Human genes 0.000 description 1
- 108050005493 CD3 protein, epsilon/gamma/delta subunit Proteins 0.000 description 1
- 108060001064 Calcitonin Proteins 0.000 description 1
- 102000055006 Calcitonin Human genes 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 241000283707 Capra Species 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- 102000012286 Chitinases Human genes 0.000 description 1
- 108010022172 Chitinases Proteins 0.000 description 1
- 101800001982 Cholecystokinin Proteins 0.000 description 1
- 102100025841 Cholecystokinin Human genes 0.000 description 1
- 108010005939 Ciliary Neurotrophic Factor Proteins 0.000 description 1
- 102100031614 Ciliary neurotrophic factor Human genes 0.000 description 1
- 102100022641 Coagulation factor IX Human genes 0.000 description 1
- 102100023804 Coagulation factor VII Human genes 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 229940122097 Collagenase inhibitor Drugs 0.000 description 1
- 102000007644 Colony-Stimulating Factors Human genes 0.000 description 1
- 108010071942 Colony-Stimulating Factors Proteins 0.000 description 1
- 108010022152 Corticotropin-Releasing Hormone Proteins 0.000 description 1
- 239000000055 Corticotropin-Releasing Hormone Substances 0.000 description 1
- 102000012289 Corticotropin-Releasing Hormone Human genes 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- HNNGTYHNYDOSKV-FXQIFTODSA-N Cys-Cys-Val Chemical compound CC(C)[C@@H](C(=O)O)NC(=O)[C@H](CS)NC(=O)[C@H](CS)N HNNGTYHNYDOSKV-FXQIFTODSA-N 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 230000007018 DNA scission Effects 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 101100119167 Drosophila mojavensis Est-4 gene Proteins 0.000 description 1
- 108050004000 Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 Proteins 0.000 description 1
- 102100021977 Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 Human genes 0.000 description 1
- 108010092408 Eosinophil Peroxidase Proteins 0.000 description 1
- 241001131785 Escherichia coli HB101 Species 0.000 description 1
- 108010076282 Factor IX Proteins 0.000 description 1
- 108010023321 Factor VII Proteins 0.000 description 1
- 108010054218 Factor VIII Proteins 0.000 description 1
- 102000001690 Factor VIII Human genes 0.000 description 1
- 108010054265 Factor VIIa Proteins 0.000 description 1
- 108010071289 Factor XIII Proteins 0.000 description 1
- 108091006020 Fc-tagged proteins Proteins 0.000 description 1
- 108010073385 Fibrin Proteins 0.000 description 1
- 102000009123 Fibrin Human genes 0.000 description 1
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 1
- 108010079345 Follicle Stimulating Hormone Proteins 0.000 description 1
- 102000012673 Follicle Stimulating Hormone Human genes 0.000 description 1
- 229930091371 Fructose Natural products 0.000 description 1
- 239000005715 Fructose Substances 0.000 description 1
- RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 description 1
- 108700012941 GNRH1 Proteins 0.000 description 1
- 102000004862 Gastrin releasing peptide Human genes 0.000 description 1
- 108090001053 Gastrin releasing peptide Proteins 0.000 description 1
- 102000034615 Glial cell line-derived neurotrophic factor Human genes 0.000 description 1
- 108091010837 Glial cell line-derived neurotrophic factor Proteins 0.000 description 1
- OJGLIOXAKGFFDW-SRVKXCTJSA-N Glu-Arg-Lys Chemical compound C(CCN)C[C@@H](C(=O)O)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CCC(=O)O)N OJGLIOXAKGFFDW-SRVKXCTJSA-N 0.000 description 1
- OWVURWCRZZMAOZ-XHNCKOQMSA-N Glu-Cys-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CS)NC(=O)[C@H](CCC(=O)O)N)C(=O)O OWVURWCRZZMAOZ-XHNCKOQMSA-N 0.000 description 1
- BFEZQZKEPRKKHV-SRVKXCTJSA-N Glu-Pro-Lys Chemical compound C1C[C@H](N(C1)C(=O)[C@H](CCC(=O)O)N)C(=O)N[C@@H](CCCCN)C(=O)O BFEZQZKEPRKKHV-SRVKXCTJSA-N 0.000 description 1
- QOXDAWODGSIDDI-GUBZILKMSA-N Glu-Ser-Lys Chemical compound C(CCN)C[C@@H](C(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(=O)O)N QOXDAWODGSIDDI-GUBZILKMSA-N 0.000 description 1
- 102400000321 Glucagon Human genes 0.000 description 1
- 108060003199 Glucagon Proteins 0.000 description 1
- 108010017544 Glucosylceramidase Proteins 0.000 description 1
- 102000008214 Glutamate decarboxylase Human genes 0.000 description 1
- 108091022930 Glutamate decarboxylase Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 239000000579 Gonadotropin-Releasing Hormone Substances 0.000 description 1
- 108010054017 Granulocyte Colony-Stimulating Factor Receptors Proteins 0.000 description 1
- 102100039622 Granulocyte colony-stimulating factor receptor Human genes 0.000 description 1
- 239000000095 Growth Hormone-Releasing Hormone Substances 0.000 description 1
- 102100039939 Growth/differentiation factor 8 Human genes 0.000 description 1
- 101100508941 Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) ppa gene Proteins 0.000 description 1
- 101710121697 Heat-stable enterotoxin Proteins 0.000 description 1
- 102000001554 Hemoglobins Human genes 0.000 description 1
- 108010054147 Hemoglobins Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 102000007625 Hirudins Human genes 0.000 description 1
- 108010007267 Hirudins Proteins 0.000 description 1
- 101100333654 Homo sapiens EPO gene Proteins 0.000 description 1
- 101000987586 Homo sapiens Eosinophil peroxidase Proteins 0.000 description 1
- 101000920686 Homo sapiens Erythropoietin Proteins 0.000 description 1
- 101000746367 Homo sapiens Granulocyte colony-stimulating factor Proteins 0.000 description 1
- 101001054334 Homo sapiens Interferon beta Proteins 0.000 description 1
- 101000669513 Homo sapiens Metalloproteinase inhibitor 1 Proteins 0.000 description 1
- 101000611183 Homo sapiens Tumor necrosis factor Proteins 0.000 description 1
- 102000002265 Human Growth Hormone Human genes 0.000 description 1
- 239000000854 Human Growth Hormone Substances 0.000 description 1
- 102100029199 Iduronate 2-sulfatase Human genes 0.000 description 1
- 101710096421 Iduronate 2-sulfatase Proteins 0.000 description 1
- 102000004627 Iduronidase Human genes 0.000 description 1
- 108010003381 Iduronidase Proteins 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 102000001617 Interferon Receptors Human genes 0.000 description 1
- 108010054267 Interferon Receptors Proteins 0.000 description 1
- 102000007438 Interferon alpha-beta Receptor Human genes 0.000 description 1
- 108010086140 Interferon alpha-beta Receptor Proteins 0.000 description 1
- 102000003996 Interferon-beta Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 102000000589 Interleukin-1 Human genes 0.000 description 1
- 108010002352 Interleukin-1 Proteins 0.000 description 1
- 102000010782 Interleukin-7 Receptors Human genes 0.000 description 1
- 108010038498 Interleukin-7 Receptors Proteins 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- AEMOLEFTQBMNLQ-HNFCZKTMSA-N L-idopyranuronic acid Chemical compound OC1O[C@@H](C(O)=O)[C@@H](O)[C@H](O)[C@H]1O AEMOLEFTQBMNLQ-HNFCZKTMSA-N 0.000 description 1
- 125000001176 L-lysyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C([H])([H])C([H])([H])C([H])([H])C(N([H])[H])([H])[H] 0.000 description 1
- 125000000769 L-threonyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])[C@](O[H])(C([H])([H])[H])[H] 0.000 description 1
- 125000003580 L-valyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(C([H])([H])[H])(C([H])([H])[H])[H] 0.000 description 1
- 102000004407 Lactalbumin Human genes 0.000 description 1
- 108090000942 Lactalbumin Proteins 0.000 description 1
- 235000019687 Lamb Nutrition 0.000 description 1
- 102000016267 Leptin Human genes 0.000 description 1
- 108010092277 Leptin Proteins 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 108010073521 Luteinizing Hormone Proteins 0.000 description 1
- 102000009151 Luteinizing Hormone Human genes 0.000 description 1
- 102000004083 Lymphotoxin-alpha Human genes 0.000 description 1
- 108090000542 Lymphotoxin-alpha Proteins 0.000 description 1
- IEVXCWPVBYCJRZ-IXOXFDKPSA-N Lys-Thr-His Chemical compound NCCCC[C@H](N)C(=O)N[C@@H]([C@H](O)C)C(=O)N[C@H](C(O)=O)CC1=CN=CN1 IEVXCWPVBYCJRZ-IXOXFDKPSA-N 0.000 description 1
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 description 1
- 101710175625 Maltose/maltodextrin-binding periplasmic protein Proteins 0.000 description 1
- 241001465754 Metazoa Species 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 102400000569 Myeloperoxidase Human genes 0.000 description 1
- 108090000235 Myeloperoxidases Proteins 0.000 description 1
- 108010056852 Myostatin Proteins 0.000 description 1
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 206010028851 Necrosis Diseases 0.000 description 1
- 108090000028 Neprilysin Proteins 0.000 description 1
- 102000003729 Neprilysin Human genes 0.000 description 1
- 102000015336 Nerve Growth Factor Human genes 0.000 description 1
- 102000010803 Netrins Human genes 0.000 description 1
- 108010063605 Netrins Proteins 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 108010079246 OMPA outer membrane proteins Proteins 0.000 description 1
- 241000283973 Oryctolagus cuniculus Species 0.000 description 1
- 238000012408 PCR amplification Methods 0.000 description 1
- 235000021314 Palmitic acid Nutrition 0.000 description 1
- 102000018886 Pancreatic Polypeptide Human genes 0.000 description 1
- 108090000526 Papain Proteins 0.000 description 1
- 102000003982 Parathyroid hormone Human genes 0.000 description 1
- 108090000445 Parathyroid hormone Proteins 0.000 description 1
- 108010087702 Penicillinase Proteins 0.000 description 1
- 239000001888 Peptone Substances 0.000 description 1
- 108010080698 Peptones Proteins 0.000 description 1
- 102100031538 Phosphatidylcholine-sterol acyltransferase Human genes 0.000 description 1
- OAICVXFJPJFONN-UHFFFAOYSA-N Phosphorus Chemical compound [P] OAICVXFJPJFONN-UHFFFAOYSA-N 0.000 description 1
- 108010001014 Plasminogen Activators Proteins 0.000 description 1
- 102000001938 Plasminogen Activators Human genes 0.000 description 1
- 241001415846 Procellariidae Species 0.000 description 1
- 101800004937 Protein C Proteins 0.000 description 1
- 102000017975 Protein C Human genes 0.000 description 1
- 241000588770 Proteus mirabilis Species 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 102000003743 Relaxin Human genes 0.000 description 1
- 108090000103 Relaxin Proteins 0.000 description 1
- 229910003797 SPO1 Inorganic materials 0.000 description 1
- 229910003798 SPO2 Inorganic materials 0.000 description 1
- 101100150136 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) SPO1 gene Proteins 0.000 description 1
- 101800001700 Saposin-D Proteins 0.000 description 1
- 101100478210 Schizosaccharomyces pombe (strain 972 / ATCC 24843) spo2 gene Proteins 0.000 description 1
- 102100037505 Secretin Human genes 0.000 description 1
- 108010086019 Secretin Proteins 0.000 description 1
- KNCJWSPMTFFJII-ZLUOBGJFSA-N Ser-Cys-Asp Chemical compound [H]N[C@@H](CO)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(O)=O)C(O)=O KNCJWSPMTFFJII-ZLUOBGJFSA-N 0.000 description 1
- RFBKULCUBJAQFT-BIIVOSGPSA-N Ser-Cys-Pro Chemical compound C1C[C@@H](N(C1)C(=O)[C@H](CS)NC(=O)[C@H](CO)N)C(=O)O RFBKULCUBJAQFT-BIIVOSGPSA-N 0.000 description 1
- 101710142969 Somatoliberin Proteins 0.000 description 1
- 102100022831 Somatoliberin Human genes 0.000 description 1
- 241000191940 Staphylococcus Species 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 235000021355 Stearic acid Nutrition 0.000 description 1
- 108010023197 Streptokinase Proteins 0.000 description 1
- 241000187747 Streptomyces Species 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 235000019486 Sunflower oil Nutrition 0.000 description 1
- 102000019197 Superoxide Dismutase Human genes 0.000 description 1
- 108010012715 Superoxide dismutase Proteins 0.000 description 1
- 101000983124 Sus scrofa Pancreatic prohormone precursor Proteins 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 108010016283 TCF Transcription Factors Proteins 0.000 description 1
- 102000000479 TCF Transcription Factors Human genes 0.000 description 1
- 101150077103 TPO gene Proteins 0.000 description 1
- KWQBJOUOSNJDRR-XAVMHZPKSA-N Thr-Cys-Pro Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CS)C(=O)N1CCC[C@@H]1C(=O)O)N)O KWQBJOUOSNJDRR-XAVMHZPKSA-N 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 102000003790 Thrombin receptors Human genes 0.000 description 1
- 108090000166 Thrombin receptors Proteins 0.000 description 1
- 108010079274 Thrombomodulin Proteins 0.000 description 1
- 102100026966 Thrombomodulin Human genes 0.000 description 1
- 102000011923 Thyrotropin Human genes 0.000 description 1
- 108010061174 Thyrotropin Proteins 0.000 description 1
- 102100030951 Tissue factor pathway inhibitor Human genes 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 102000001742 Tumor Suppressor Proteins Human genes 0.000 description 1
- 108010040002 Tumor Suppressor Proteins Proteins 0.000 description 1
- 102100040247 Tumor necrosis factor Human genes 0.000 description 1
- 108010092464 Urate Oxidase Proteins 0.000 description 1
- 108090000435 Urokinase-type plasminogen activator Proteins 0.000 description 1
- 102000003990 Urokinase-type plasminogen activator Human genes 0.000 description 1
- 108091008605 VEGF receptors Proteins 0.000 description 1
- 102000009484 Vascular Endothelial Growth Factor Receptors Human genes 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 239000005862 Whey Substances 0.000 description 1
- 102000007544 Whey Proteins Human genes 0.000 description 1
- 108010046377 Whey Proteins Proteins 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- FJWGYAHXMCUOOM-QHOUIDNNSA-N [(2s,3r,4s,5r,6r)-2-[(2r,3r,4s,5r,6s)-4,5-dinitrooxy-2-(nitrooxymethyl)-6-[(2r,3r,4s,5r,6s)-4,5,6-trinitrooxy-2-(nitrooxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-3,5-dinitrooxy-6-(nitrooxymethyl)oxan-4-yl] nitrate Chemical compound O([C@@H]1O[C@@H]([C@H]([C@H](O[N+]([O-])=O)[C@H]1O[N+]([O-])=O)O[C@H]1[C@@H]([C@@H](O[N+]([O-])=O)[C@H](O[N+]([O-])=O)[C@@H](CO[N+]([O-])=O)O1)O[N+]([O-])=O)CO[N+](=O)[O-])[C@@H]1[C@@H](CO[N+]([O-])=O)O[C@@H](O[N+]([O-])=O)[C@H](O[N+]([O-])=O)[C@H]1O[N+]([O-])=O FJWGYAHXMCUOOM-QHOUIDNNSA-N 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 150000001298 alcohols Chemical class 0.000 description 1
- 150000001299 aldehydes Chemical group 0.000 description 1
- 230000000172 allergic effect Effects 0.000 description 1
- 102000015395 alpha 1-Antitrypsin Human genes 0.000 description 1
- 108010050122 alpha 1-Antitrypsin Proteins 0.000 description 1
- 229940024142 alpha 1-antitrypsin Drugs 0.000 description 1
- DTOSIQBPPRVQHS-PDBXOOCHSA-N alpha-linolenic acid Chemical compound CC\C=C/C\C=C/C\C=C/CCCCCCCC(O)=O DTOSIQBPPRVQHS-PDBXOOCHSA-N 0.000 description 1
- 235000020661 alpha-linolenic acid Nutrition 0.000 description 1
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 1
- 229910021529 ammonia Inorganic materials 0.000 description 1
- 235000019270 ammonium chloride Nutrition 0.000 description 1
- 239000000908 ammonium hydroxide Substances 0.000 description 1
- 229910000148 ammonium phosphate Inorganic materials 0.000 description 1
- 235000019289 ammonium phosphates 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
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 238000005349 anion exchange Methods 0.000 description 1
- 239000002518 antifoaming agent Substances 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- 108010092854 aspartyllysine Proteins 0.000 description 1
- FZCSTZYAHCUGEM-UHFFFAOYSA-N aspergillomarasmine B Natural products OC(=O)CNC(C(O)=O)CNC(C(O)=O)CC(O)=O FZCSTZYAHCUGEM-UHFFFAOYSA-N 0.000 description 1
- 208000010668 atopic eczema Diseases 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 description 1
- 230000008436 biogenesis Effects 0.000 description 1
- 238000010170 biological method Methods 0.000 description 1
- 230000036765 blood level Effects 0.000 description 1
- 238000006664 bond formation reaction Methods 0.000 description 1
- 210000000988 bone and bone Anatomy 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 229960004015 calcitonin Drugs 0.000 description 1
- BBBFJLBPOGFECG-VJVYQDLKSA-N calcitonin Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CSSC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 BBBFJLBPOGFECG-VJVYQDLKSA-N 0.000 description 1
- 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
- 235000013877 carbamide Nutrition 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 235000014633 carbohydrates Nutrition 0.000 description 1
- 229950008486 carperitide Drugs 0.000 description 1
- NSQLIUXCMFBZME-MPVJKSABSA-N carperitide Chemical compound C([C@H]1C(=O)NCC(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 NSQLIUXCMFBZME-MPVJKSABSA-N 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 239000004359 castor oil Substances 0.000 description 1
- 235000019438 castor oil Nutrition 0.000 description 1
- 235000019994 cava Nutrition 0.000 description 1
- 230000010261 cell growth Effects 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
- 230000008859 change Effects 0.000 description 1
- DDPFHDCZUJFNAT-PZPWKVFESA-N chembl2104402 Chemical compound N([C@H](C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1N=CNC=1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](C)C(=O)NCC(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(N)=O)C(C)C)C(=O)[C@@H]1CCCCCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1 DDPFHDCZUJFNAT-PZPWKVFESA-N 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 229940107137 cholecystokinin Drugs 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 239000003240 coconut oil Substances 0.000 description 1
- 235000019864 coconut oil Nutrition 0.000 description 1
- 239000002442 collagenase inhibitor Substances 0.000 description 1
- 238000004040 coloring Methods 0.000 description 1
- 230000004154 complement system Effects 0.000 description 1
- 210000002808 connective tissue Anatomy 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 239000003246 corticosteroid Substances 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 102000026898 cytokine binding proteins Human genes 0.000 description 1
- 108091008470 cytokine binding proteins Proteins 0.000 description 1
- 238000004042 decolorization Methods 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 229960000633 dextran sulfate Drugs 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- MNNHAPBLZZVQHP-UHFFFAOYSA-N diammonium hydrogen phosphate Chemical compound [NH4+].[NH4+].OP([O-])([O-])=O MNNHAPBLZZVQHP-UHFFFAOYSA-N 0.000 description 1
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
- ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 230000006334 disulfide bridging Effects 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 108700032313 elcatonin Proteins 0.000 description 1
- 229960000756 elcatonin Drugs 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 230000006126 farnesylation Effects 0.000 description 1
- 239000003925 fat Substances 0.000 description 1
- 235000019197 fats Nutrition 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 229950003499 fibrin Drugs 0.000 description 1
- 229940028334 follicle stimulating hormone Drugs 0.000 description 1
- 108010077689 gamma-aminobutyryl-2-methyltryptophyl-2-methyltryptophyl-2-methyltryptophyl-lysinamide Proteins 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- PUBCCFNQJQKCNC-XKNFJVFFSA-N gastrin-releasingpeptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(N)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC=1N=CNC=1)NC(=O)[C@H](CC(N)=O)NC(=O)CNC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)CNC(=O)CNC(=O)CNC(=O)[C@H](C)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CC(C)C)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)C(C)C)[C@@H](C)O)C(C)C)[C@@H](C)O)C(C)C)C1=CNC=N1 PUBCCFNQJQKCNC-XKNFJVFFSA-N 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 230000008571 general function Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 229960004666 glucagon Drugs 0.000 description 1
- MASNOZXLGMXCHN-ZLPAWPGGSA-N glucagon Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CO)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 MASNOZXLGMXCHN-ZLPAWPGGSA-N 0.000 description 1
- 230000036252 glycation Effects 0.000 description 1
- ZEMPKEQAKRGZGQ-XOQCFJPHSA-N glycerol triricinoleate Natural products CCCCCC[C@@H](O)CC=CCCCCCCCC(=O)OC[C@@H](COC(=O)CCCCCCCC=CC[C@@H](O)CCCCCC)OC(=O)CCCCCCCC=CC[C@H](O)CCCCCC ZEMPKEQAKRGZGQ-XOQCFJPHSA-N 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 229940006607 hirudin Drugs 0.000 description 1
- WQPDUTSPKFMPDP-OUMQNGNKSA-N hirudin Chemical compound C([C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC(OS(O)(=O)=O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H]1NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@@H]2CSSC[C@@H](C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@H](C(=O)N[C@H](C(NCC(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)N2)=O)CSSC1)C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]1NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@@H](NC(=O)[C@H](CC=2C=CC(O)=CC=2)NC(=O)[C@@H](NC(=O)[C@@H](N)C(C)C)C(C)C)[C@@H](C)O)CSSC1)C(C)C)[C@@H](C)O)[C@@H](C)O)C1=CC=CC=C1 WQPDUTSPKFMPDP-OUMQNGNKSA-N 0.000 description 1
- 102000044890 human EPO Human genes 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 108010039650 imiglucerase Proteins 0.000 description 1
- 229960002127 imiglucerase Drugs 0.000 description 1
- 210000002865 immune cell Anatomy 0.000 description 1
- 230000008105 immune reaction Effects 0.000 description 1
- 230000002637 immunotoxin Effects 0.000 description 1
- 231100000608 immunotoxin Toxicity 0.000 description 1
- 229940051026 immunotoxin Drugs 0.000 description 1
- 239000002596 immunotoxin Substances 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 102000002467 interleukin receptors Human genes 0.000 description 1
- 108010093036 interleukin receptors Proteins 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- 229910000358 iron sulfate Inorganic materials 0.000 description 1
- BAUYGSIQEAFULO-UHFFFAOYSA-L iron(2+) sulfate (anhydrous) Chemical compound [Fe+2].[O-]S([O-])(=O)=O BAUYGSIQEAFULO-UHFFFAOYSA-L 0.000 description 1
- 229940039781 leptin Drugs 0.000 description 1
- NRYBAZVQPHGZNS-ZSOCWYAHSA-N leptin Chemical compound O=C([C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC=1C2=CC=CC=C2NC=1)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](N)CC(C)C)CCSC)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CS)C(O)=O NRYBAZVQPHGZNS-ZSOCWYAHSA-N 0.000 description 1
- 229960004488 linolenic acid Drugs 0.000 description 1
- KQQKGWQCNNTQJW-UHFFFAOYSA-N linolenic acid Natural products CC=CCCC=CCC=CCCCCCCCC(O)=O KQQKGWQCNNTQJW-UHFFFAOYSA-N 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 108010013555 lipoprotein-associated coagulation inhibitor Proteins 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 229940040129 luteinizing hormone Drugs 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 230000006510 metastatic growth Effects 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
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 239000000203 mixture Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 229910000402 monopotassium phosphate Inorganic materials 0.000 description 1
- 235000019796 monopotassium phosphate Nutrition 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- WQEPLUUGTLDZJY-UHFFFAOYSA-N n-Pentadecanoic acid Natural products CCCCCCCCCCCCCCC(O)=O WQEPLUUGTLDZJY-UHFFFAOYSA-N 0.000 description 1
- 230000017074 necrotic cell death Effects 0.000 description 1
- 229940053128 nerve growth factor Drugs 0.000 description 1
- HPNRHPKXQZSDFX-OAQDCNSJSA-N nesiritide Chemical compound C([C@H]1C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)CNC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CCSC)NC(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CO)C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1N=CNC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 HPNRHPKXQZSDFX-OAQDCNSJSA-N 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 229940079938 nitrocellulose Drugs 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- QIQXTHQIDYTFRH-UHFFFAOYSA-N octadecanoic acid Chemical compound CCCCCCCCCCCCCCCCCC(O)=O QIQXTHQIDYTFRH-UHFFFAOYSA-N 0.000 description 1
- OQCDKBAXFALNLD-UHFFFAOYSA-N octadecanoic acid Natural products CCCCCCCC(C)CCCCCCCCC(O)=O OQCDKBAXFALNLD-UHFFFAOYSA-N 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
- 235000005985 organic acids Nutrition 0.000 description 1
- 125000001477 organic nitrogen group Chemical group 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 230000002188 osteogenic effect Effects 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 229940055729 papain Drugs 0.000 description 1
- 235000019834 papain Nutrition 0.000 description 1
- 239000000199 parathyroid hormone Substances 0.000 description 1
- 229960001319 parathyroid hormone Drugs 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 101150019841 penP gene Proteins 0.000 description 1
- 229950009506 penicillinase Drugs 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 235000019319 peptone Nutrition 0.000 description 1
- 150000002978 peroxides Chemical class 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 239000008055 phosphate buffer solution Substances 0.000 description 1
- PJNZPQUBCPKICU-UHFFFAOYSA-N phosphoric acid;potassium Chemical compound [K].OP(O)(O)=O PJNZPQUBCPKICU-UHFFFAOYSA-N 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 238000007745 plasma electrolytic oxidation reaction Methods 0.000 description 1
- 229940127126 plasminogen activator Drugs 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 229920001522 polyglycol ester Polymers 0.000 description 1
- 239000008057 potassium phosphate buffer Substances 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 230000009465 prokaryotic expression Effects 0.000 description 1
- 230000004952 protein activity Effects 0.000 description 1
- 229960000856 protein c Drugs 0.000 description 1
- 239000012474 protein marker Substances 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 230000030788 protein refolding Effects 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 101150079601 recA gene Proteins 0.000 description 1
- 239000002461 renin inhibitor Substances 0.000 description 1
- 229940086526 renin-inhibitors Drugs 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 239000012723 sample buffer Substances 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 229960002101 secretin Drugs 0.000 description 1
- OWMZNFCDEHGFEP-NFBCVYDUSA-N secretin human Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(N)=O)[C@@H](C)O)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)C1=CC=CC=C1 OWMZNFCDEHGFEP-NFBCVYDUSA-N 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- SQVRNKJHWKZAKO-OQPLDHBCSA-N sialic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)OC1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-OQPLDHBCSA-N 0.000 description 1
- HBMJWWWQQXIZIP-UHFFFAOYSA-N silicon carbide Chemical compound [Si+]#[C-] HBMJWWWQQXIZIP-UHFFFAOYSA-N 0.000 description 1
- 229910010271 silicon carbide Inorganic materials 0.000 description 1
- IZTQOLKUZKXIRV-YRVFCXMDSA-N sincalide Chemical compound C([C@@H](C(=O)N[C@@H](CCSC)C(=O)NCC(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(N)=O)NC(=O)[C@@H](N)CC(O)=O)C1=CC=C(OS(O)(=O)=O)C=C1 IZTQOLKUZKXIRV-YRVFCXMDSA-N 0.000 description 1
- BEOOHQFXGBMRKU-UHFFFAOYSA-N sodium cyanoborohydride Chemical compound [Na+].[B-]C#N BEOOHQFXGBMRKU-UHFFFAOYSA-N 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 239000007790 solid phase Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000003549 soybean oil Substances 0.000 description 1
- 235000012424 soybean oil Nutrition 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 239000008117 stearic acid Substances 0.000 description 1
- 239000012089 stop solution Substances 0.000 description 1
- 229960005202 streptokinase Drugs 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 230000019635 sulfation Effects 0.000 description 1
- 238000005670 sulfation reaction Methods 0.000 description 1
- 239000002600 sunflower oil Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 239000012085 test solution Substances 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 239000011573 trace mineral Substances 0.000 description 1
- 235000013619 trace mineral Nutrition 0.000 description 1
- 108091008023 transcriptional regulators Proteins 0.000 description 1
- 230000014616 translation 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
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 102000003390 tumor necrosis factor Human genes 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 238000002525 ultrasonication Methods 0.000 description 1
- 229960005356 urokinase Drugs 0.000 description 1
- 229960005486 vaccine Drugs 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
- 235000021241 α-lactalbumin Nutrition 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Images
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/30—Macromolecular organic or inorganic compounds, e.g. inorganic polyphosphates
- A61K47/42—Proteins; Polypeptides; Degradation products thereof; Derivatives thereof, e.g. albumin, gelatin or zein
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/68—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/68—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
- A61K47/6801—Drug-antibody or immunoglobulin conjugates defined by the pharmacologically or therapeutically active agent
- A61K47/6803—Drugs conjugated to an antibody or immunoglobulin, e.g. cisplatin-antibody conjugates
- A61K47/6811—Drugs conjugated to an antibody or immunoglobulin, e.g. cisplatin-antibody conjugates the drug being a protein or peptide, e.g. transferrin or bleomycin
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/68—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
- A61K47/6801—Drug-antibody or immunoglobulin conjugates defined by the pharmacologically or therapeutically active agent
- A61K47/6803—Drugs conjugated to an antibody or immunoglobulin, e.g. cisplatin-antibody conjugates
- A61K47/6811—Drugs conjugated to an antibody or immunoglobulin, e.g. cisplatin-antibody conjugates the drug being a protein or peptide, e.g. transferrin or bleomycin
- A61K47/6813—Drugs conjugated to an antibody or immunoglobulin, e.g. cisplatin-antibody conjugates the drug being a protein or peptide, e.g. transferrin or bleomycin the drug being a peptidic cytokine, e.g. an interleukin or interferon
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K47/00—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient
- A61K47/50—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates
- A61K47/51—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent
- A61K47/68—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment
- A61K47/6835—Medicinal preparations characterised by the non-active ingredients used, e.g. carriers or inert additives; Targeting or modifying agents chemically bound to the active ingredient the non-active ingredient being chemically bound to the active ingredient, e.g. polymer-drug conjugates the non-active ingredient being a modifying agent the modifying agent being an antibody, an immunoglobulin or a fragment thereof, e.g. an Fc-fragment the modifying agent being an antibody or an immunoglobulin bearing at least one antigen-binding site
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P15/00—Drugs for genital or sexual disorders; Contraceptives
-
- 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
- A61P3/04—Anorexiants; Antiobesity agents
-
- 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
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P5/00—Drugs for disorders of the endocrine system
- A61P5/06—Drugs for disorders of the endocrine system of the anterior pituitary hormones, e.g. TSH, ACTH, FSH, LH, PRL, GH
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P5/00—Drugs for disorders of the endocrine system
- A61P5/10—Drugs for disorders of the endocrine system of the posterior pituitary hormones, e.g. oxytocin, ADH
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/06—Antianaemics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- 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
- C07K14/475—Growth factors; Growth regulators
- C07K14/505—Erythropoietin [EPO]
-
- 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/53—Colony-stimulating factor [CSF]
- C07K14/535—Granulocyte CSF; Granulocyte-macrophage CSF
-
- 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
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/555—Interferons [IFN]
- C07K14/56—IFN-alpha
-
- 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
- C07K14/575—Hormones
- C07K14/61—Growth hormone [GH], i.e. somatotropin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/46—Hybrid immunoglobulins
-
- 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
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/52—Constant or Fc region; Isotype
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/732—Antibody-dependent cellular cytotoxicity [ADCC]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/734—Complement-dependent cytotoxicity [CDC]
-
- 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
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Molecular Biology (AREA)
- Immunology (AREA)
- Biochemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Epidemiology (AREA)
- Biophysics (AREA)
- Genetics & Genomics (AREA)
- Diabetes (AREA)
- Endocrinology (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Hematology (AREA)
- Obesity (AREA)
- Child & Adolescent Psychology (AREA)
- Emergency Medicine (AREA)
- Heart & Thoracic Surgery (AREA)
- Cardiology (AREA)
- Reproductive Health (AREA)
- Inorganic Chemistry (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Medicinal Preparation (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 |
|---|---|---|---|
| KR20030080299 | 2003-11-13 | ||
| KR10-2003-0080299 | 2003-11-13 | ||
| PCT/KR2004/002943 WO2005047335A1 (en) | 2003-11-13 | 2004-11-13 | Method for themass production of immunoglobulin constant region |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2007532098A JP2007532098A (ja) | 2007-11-15 |
| JP2007532098A5 JP2007532098A5 (enExample) | 2007-12-27 |
| JP4762904B2 true JP4762904B2 (ja) | 2011-08-31 |
Family
ID=36589418
Family Applications (7)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2006539398A Expired - Lifetime JP4870569B2 (ja) | 2003-11-13 | 2004-11-13 | 免疫グロブリン断片を用いた蛋白質結合体およびその製造方法 |
| JP2006539399A Expired - Lifetime JP5216216B2 (ja) | 2003-11-13 | 2004-11-13 | 免疫グロブリンFc領域をキャリアとして含む薬剤学的組成物 |
| JP2006539397A Expired - Lifetime JP4762904B2 (ja) | 2003-11-13 | 2004-11-13 | 免疫グロブリン不変領域の量産方法 |
| JP2006539396A Pending JP2007531513A (ja) | 2003-11-13 | 2004-11-13 | 薬物のキャリアとして有用なIgGFc断片およびその製造方法 |
| JP2011202199A Expired - Fee Related JP5425150B2 (ja) | 2003-11-13 | 2011-09-15 | 薬物のキャリアとして有用なIgGFc断片およびその製造方法 |
| JP2011209594A Abandoned JP2011256211A (ja) | 2003-11-13 | 2011-09-26 | 免疫グロブリン断片を用いた蛋白質結合体およびその製造方法 |
| JP2012166208A Withdrawn JP2012224635A (ja) | 2003-11-13 | 2012-07-26 | 免疫グロブリンFc領域をキャリアとして含む薬剤学的組成物 |
Family Applications Before (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2006539398A Expired - Lifetime JP4870569B2 (ja) | 2003-11-13 | 2004-11-13 | 免疫グロブリン断片を用いた蛋白質結合体およびその製造方法 |
| JP2006539399A Expired - Lifetime JP5216216B2 (ja) | 2003-11-13 | 2004-11-13 | 免疫グロブリンFc領域をキャリアとして含む薬剤学的組成物 |
Family Applications After (4)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2006539396A Pending JP2007531513A (ja) | 2003-11-13 | 2004-11-13 | 薬物のキャリアとして有用なIgGFc断片およびその製造方法 |
| JP2011202199A Expired - Fee Related JP5425150B2 (ja) | 2003-11-13 | 2011-09-15 | 薬物のキャリアとして有用なIgGFc断片およびその製造方法 |
| JP2011209594A Abandoned JP2011256211A (ja) | 2003-11-13 | 2011-09-26 | 免疫グロブリン断片を用いた蛋白質結合体およびその製造方法 |
| JP2012166208A Withdrawn JP2012224635A (ja) | 2003-11-13 | 2012-07-26 | 免疫グロブリンFc領域をキャリアとして含む薬剤学的組成物 |
Country Status (16)
| Country | Link |
|---|---|
| US (13) | US8846874B2 (enExample) |
| EP (6) | EP1682582B1 (enExample) |
| JP (7) | JP4870569B2 (enExample) |
| KR (5) | KR100725315B1 (enExample) |
| CN (4) | CN103212084B (enExample) |
| AT (3) | ATE522548T1 (enExample) |
| AU (2) | AU2004282985B8 (enExample) |
| BR (2) | BRPI0406606A (enExample) |
| CA (2) | CA2512933C (enExample) |
| DK (3) | DK1682583T3 (enExample) |
| ES (6) | ES2372495T3 (enExample) |
| MX (2) | MXPA05007211A (enExample) |
| PL (2) | PL2239273T3 (enExample) |
| PT (3) | PT2239273E (enExample) |
| RU (2) | RU2352583C2 (enExample) |
| WO (4) | WO2005047334A1 (enExample) |
Families Citing this family (272)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US7157555B1 (en) * | 1997-08-08 | 2007-01-02 | Amylin Pharmaceuticals, Inc. | Exendin agonist compounds |
| US7829084B2 (en) * | 2001-01-17 | 2010-11-09 | Trubion Pharmaceuticals, Inc. | Binding constructs and methods for use thereof |
| US7754208B2 (en) | 2001-01-17 | 2010-07-13 | Trubion Pharmaceuticals, Inc. | Binding domain-immunoglobulin fusion proteins |
| WO2004058988A2 (en) | 2002-12-20 | 2004-07-15 | Amgen, Inc. | Binding agents which inhibit myostatin |
| ATE497783T1 (de) | 2003-05-06 | 2011-02-15 | Syntonix Pharmaceuticals Inc | Gerinnungsfaktor vii-fc chimäre proteine zur behandlung von hämostatischen krankheiten |
| TWI353991B (en) | 2003-05-06 | 2011-12-11 | Syntonix Pharmaceuticals Inc | Immunoglobulin chimeric monomer-dimer hybrids |
| PL2520654T3 (pl) | 2003-08-26 | 2017-08-31 | The Regents Of The University Of Colorado, A Body Corporate | Inhibitory aktywności proteazy serynowej i ich zastosowanie w sposobach i kompozycjach do leczenia zakażeń bakteryjnych |
| US8263084B2 (en) * | 2003-11-13 | 2012-09-11 | Hanmi Science Co., Ltd | Pharmaceutical composition for treating obesity-related disease comprising insulinotropic peptide conjugate |
| KR101135244B1 (ko) * | 2007-11-29 | 2012-04-24 | 한미사이언스 주식회사 | 인슐린 분비 펩타이드 결합체를 포함하는 비만 관련질환 치료용 조성물 |
| US8110665B2 (en) | 2003-11-13 | 2012-02-07 | Hanmi Holdings Co., Ltd. | Pharmaceutical composition comprising an immunoglobulin FC region as a carrier |
| DK1682583T3 (da) * | 2003-11-13 | 2012-05-07 | Hanmi Holdings Co Ltd | Proteinkompleksdannelse under anvendelse af immunoglobulinfragment samt fremgangsmåde til fremstilling deraf |
| DE602005027461D1 (de) | 2004-04-21 | 2011-05-26 | Enobia Pharma Inc | Konjugate zur zuführung an knochen und verfahren zu deren verwendung beim hinführen von proteinen zum knochen |
| US20070081984A1 (en) | 2005-10-11 | 2007-04-12 | Shunji Tomatsu | Compositions and methods for treating hypophosphatasia |
| EP1773400A2 (en) * | 2004-07-08 | 2007-04-18 | Amgen Inc. | Therapeutic peptides |
| MX2007003320A (es) | 2004-09-24 | 2007-05-18 | Amgen Inc | Moleculas fc modificadas. |
| KR100594607B1 (ko) * | 2004-11-03 | 2006-06-30 | 재단법인서울대학교산학협력재단 | 신규한 경구투여용 재조합 인간 성장호르몬 분비미생물제제 및 그 제조방법 |
| US20090087478A1 (en) * | 2004-12-27 | 2009-04-02 | Progenics Pharmaceuticals (Nevada), Inc. | Orally Deliverable and Anti-Toxin Antibodies and Methods for Making and Using Them |
| EP1858923A4 (en) * | 2005-02-14 | 2008-10-15 | Apollo Life Sciences Ltd | MOLECULAR AND CHIMERAL MOLECULES FROM IT |
| KR100754667B1 (ko) * | 2005-04-08 | 2007-09-03 | 한미약품 주식회사 | 비펩타이드성 중합체로 개질된 면역글로불린 Fc 단편 및이를 포함하는 약제학적 조성물 |
| US7833979B2 (en) | 2005-04-22 | 2010-11-16 | Amgen Inc. | Toxin peptide therapeutic agents |
| SG10201403526YA (en) | 2005-07-25 | 2014-10-30 | Emergent Product Dev Seattle | B-cell reduction using cd37-specific and cd20-specific binding molecules |
| US8008453B2 (en) | 2005-08-12 | 2011-08-30 | Amgen Inc. | Modified Fc molecules |
| MY149128A (en) * | 2005-08-16 | 2013-07-15 | Hanmi Science Co Ltd | A method for the mass production of immunoglobulin fc region deleted initial methionine residues |
| KR100824505B1 (ko) * | 2005-08-16 | 2008-04-22 | 한미약품 주식회사 | 개시 메티오닌 잔기가 제거된 면역글로불린 Fc 영역의대량 생산방법 |
| CN101534865A (zh) * | 2005-10-19 | 2009-09-16 | Ibc药品公司 | 生物活性装配体的制备方法及其用途 |
| WO2007048127A2 (en) * | 2005-10-20 | 2007-04-26 | The Scripps Research Institute | Fc labeling for immunostaining and immunotargeting |
| TW200732350A (en) * | 2005-10-21 | 2007-09-01 | Amgen Inc | Methods for generating monovalent IgG |
| US8067562B2 (en) | 2005-11-01 | 2011-11-29 | Amgen Inc. | Isolated nucleic acid molecule comprising the amino acid sequence of SEQ ID NO:1 |
| KR101866623B1 (ko) * | 2005-11-28 | 2018-07-04 | 젠맵 에이/에스 | 재조합 1가 항체 및 그의 제조 방법 |
| US20070149458A1 (en) * | 2005-12-06 | 2007-06-28 | Amgen Inc. | Uses of myostatin antagonists |
| CN101002945B (zh) | 2006-01-20 | 2012-09-05 | 清华大学 | 一种用于肿瘤治疗的新型复合物 |
| CN100475270C (zh) | 2006-01-20 | 2009-04-08 | 清华大学 | 一种治疗肿瘤的药物及其应用 |
| AU2007257692B2 (en) * | 2006-06-12 | 2013-11-14 | Aptevo Research And Development Llc | Single-chain multivalent binding proteins with effector function |
| PL2061803T5 (pl) * | 2006-08-28 | 2023-03-27 | Ares Trading S.A. | Proces oczyszczania białek zawierających fc |
| US20140147441A1 (en) * | 2006-09-12 | 2014-05-29 | The General Hospital Corporation | Compositions containing alpha-1-antitrypsin and methods for use |
| US7910102B2 (en) | 2006-10-25 | 2011-03-22 | Amgen Inc. | Methods of using conjugated toxin peptide therapeutic agents |
| US20080181903A1 (en) * | 2006-12-21 | 2008-07-31 | Pdl Biopharma, Inc. | Conjugate of natriuretic peptide and antibody constant region |
| JP2008169195A (ja) * | 2007-01-05 | 2008-07-24 | Hanmi Pharmaceutical Co Ltd | キャリア物質を用いたインスリン分泌ペプチド薬物結合体 |
| CN101219219B (zh) | 2007-01-10 | 2013-02-13 | 北京普罗吉生物科技发展有限公司 | 包含血管抑素或其片段的复合物、其制备方法及应用 |
| WO2008127780A2 (en) * | 2007-02-21 | 2008-10-23 | Nantero, Inc. | Symmetric touch screen system with carbon nanotube-based transparent conductive electrode pairs |
| TWI454479B (zh) | 2007-03-06 | 2014-10-01 | Amgen Inc | 變異之活動素受體多肽及其用途 |
| US8501678B2 (en) | 2007-03-06 | 2013-08-06 | Atara Biotherapeutics, Inc. | Variant activin receptor polypeptides and uses thereof |
| JP5591691B2 (ja) | 2007-05-22 | 2014-09-17 | アムジエン・インコーポレーテツド | 生物活性を有する融合タンパク質を作製するための組成物及び方法 |
| EP3173484B1 (en) * | 2007-05-30 | 2018-09-26 | Postech Academy-Industry- Foundation | Immunoglobulin fusion proteins |
| AU2008255350B2 (en) | 2007-05-31 | 2014-07-10 | Genmab A/S | Transgenic animals producing monovalent human antibodies and antibodies obtainable from these animals |
| ES2565834T3 (es) | 2007-06-01 | 2016-04-07 | University Of Maryland, Baltimore | Agentes de unión a receptor de Fc de región constante de inmunoglobulina |
| EP2162464A1 (en) * | 2007-06-06 | 2010-03-17 | Boehringer Ingelheim International GmbH | Natriuretic fusion proteins |
| RU2010100638A (ru) * | 2007-06-12 | 2011-07-20 | УАЙТ ЭлЭлСи (US) | Композиции и способы лечения, направленные против cd20 |
| JP2010532764A (ja) * | 2007-07-06 | 2010-10-14 | トゥルビオン・ファーマシューティカルズ・インコーポレーテッド | C末端に配置された特異的結合性ドメインを有する結合性ペプチド |
| US8492347B2 (en) * | 2007-10-17 | 2013-07-23 | The Regents Of The University Of California | Peptide for induction of immune tolerance as treatment for systemic lupus erythematosus |
| EP2214700A4 (en) * | 2007-11-02 | 2012-08-22 | Janssen Biotech Inc | HALF-SYNTHETIC GLP-1 PEPTIDE FUSION CONSTRUCTS, METHOD AND USES |
| ES2368700T3 (es) * | 2008-04-11 | 2011-11-21 | Emergent Product Development Seattle, Llc | Agente inmunoterapéutico para cd37 y combinación con un agente quimioterapéutico bifuncional del mismo. |
| PE20110221A1 (es) | 2008-07-23 | 2011-04-06 | Hanmi Science Co Ltd | Un complejo polipeptidico que consiste en un polimero no-peptidil que posee tres terminaciones funcionales |
| RU2457856C2 (ru) * | 2008-08-05 | 2012-08-10 | Виктор Владимирович Чалов | Композиция, обладающая противовирусным и антимикробным действием, для перорального применения |
| EA020091B1 (ru) * | 2008-08-07 | 2014-08-29 | Ипсен Фарма С.А.С. | Аналоги глюкозозависимого инсулинотропного полипептида (gip), модифицированные по n-концу |
| EP2987805A3 (en) * | 2008-08-07 | 2016-04-13 | Ipsen Pharma S.A.S. | Analogues of glucose-dependent insulinotropic polypeptide |
| KR20110043688A (ko) | 2008-08-07 | 2011-04-27 | 입센 파마 에스.에이.에스 | 포도당 의존적인 인슐린 분비 자극성 폴리펩타이드 유사체 |
| US8449872B2 (en) * | 2008-09-19 | 2013-05-28 | Nektar Therapeutics | Polymer conjugates of nesiritide peptides |
| WO2010033240A2 (en) * | 2008-09-19 | 2010-03-25 | Nektar Therapeutics | Carbohydrate-based drug delivery polymers and conjugates thereof |
| WO2010051335A1 (en) * | 2008-10-31 | 2010-05-06 | Amgen Inc. | Materials and methods relating to stem cell mobilization by multi-pegylated granulocyte colony stimulating factor |
| JP5611222B2 (ja) | 2008-11-26 | 2014-10-22 | アムジエン・インコーポレーテツド | アクチビンiib受容体ポリペプチドの変異体及びその使用 |
| WO2010065578A2 (en) * | 2008-12-04 | 2010-06-10 | Leukosight Inc. | POLYPEPTIDES COMPRISING Fc FRAGMENTS OF IMMUNOGLOBULIN G (IgG) AND METHODS OF USING THE SAME |
| US20100158893A1 (en) * | 2008-12-19 | 2010-06-24 | Baxter International Inc. | Systems and methods for obtaining immunoglobulin from blood |
| TW201031752A (en) * | 2009-01-19 | 2010-09-01 | Hanmi Pharm Ind Co Ltd | Method for producing physiologically active protein or peptide using immunoglobulin fragment |
| WO2010096394A2 (en) | 2009-02-17 | 2010-08-26 | Redwood Biosciences, Inc. | Aldehyde-tagged protein-based drug carriers and methods of use |
| CA2751730A1 (en) | 2009-02-25 | 2010-09-02 | Merck Sharp & Dohme Corp. | Metabolic engineering of a galactose assimilation pathway in the glycoengineered yeast pichia pastoris |
| WO2010111414A1 (en) * | 2009-03-24 | 2010-09-30 | Bayer Healthcare Llc | Factor viii variants and methods of use |
| CN102439044B (zh) | 2009-04-22 | 2014-08-13 | 阿特根公司 | 通过体内持续释放维持的体内半衰期增加的融合蛋白质或融合肽以及使用所述融合蛋白质或融合肽增加体内半衰期的方法 |
| WO2011051916A2 (en) * | 2009-11-02 | 2011-05-05 | Universite De Geneve | Stabilized protein formulations and use thereof |
| WO2011075185A1 (en) | 2009-12-18 | 2011-06-23 | Oligasis | Targeted drug phosphorylcholine polymer conjugates |
| AU2010330750B2 (en) * | 2009-12-18 | 2015-10-01 | Exodos Life Sciences Limited Partnership | Methods and compositions for stable liquid drug formulations |
| BR112012017979B1 (pt) * | 2010-01-19 | 2021-10-13 | Hanmi Science Co., Ltd. | Formulações líquidas para conjugado de g-csf de ação prolongada |
| ES2700925T3 (es) * | 2010-01-19 | 2019-02-20 | Hanmi Science Co Ltd | Formulaciones líquidas para conjugado de eritropoyetina de acción prolongada |
| WO2011093470A1 (ja) * | 2010-01-28 | 2011-08-04 | 協和発酵キリン株式会社 | Bone morphogenetic protein receptor 1B(BMPR1B)細胞外ドメイン又はその変異体を含む蛋白質を含有する骨疾患治療用医薬組成物 |
| AU2011220878A1 (en) | 2010-02-24 | 2012-08-23 | Merck Sharp & Dohme Corp. | Method for increasing N-glycosylation site occupancy on therapeutic glycoproteins produced in Pichia pastoris |
| US9175067B2 (en) * | 2010-03-08 | 2015-11-03 | Ge Healthcare Bio-Sciences Ab | Immunoglobulin G Fc region binding polypeptide |
| AR081066A1 (es) * | 2010-04-02 | 2012-06-06 | Hanmi Holdings Co Ltd | Conjugado de insulina donde se usa un fragmento de inmunoglobulina |
| US9981017B2 (en) | 2010-04-02 | 2018-05-29 | Hanmi Science Co., Ltd. | Insulin conjugate using an immunoglobulin fragment |
| AR081755A1 (es) * | 2010-04-02 | 2012-10-17 | Hanmi Holdings Co Ltd | Formulacion de accion prolongada de la hormona estimuladora de los foliculos donde se usa un fragmento de inmunoglobulina, metodo de preparacion y metodo para tratar a un sujeto que sufre un trastorno reproductivo |
| AR080993A1 (es) * | 2010-04-02 | 2012-05-30 | Hanmi Holdings Co Ltd | Formulacion de accion prolongada de interferon beta donde se usa un fragmento de inmunoglobulina |
| SG185079A1 (en) | 2010-04-30 | 2012-12-28 | Alexion Pharma Internat Sarl | Methods, compositions, and kits for the treatment of matrix mineralization disorders |
| ES2674567T3 (es) * | 2010-05-21 | 2018-07-02 | Merrimack Pharmaceuticals, Inc. | Proteínas de fusión biespecíficas |
| KR101330868B1 (ko) * | 2010-06-08 | 2013-11-18 | 한미사이언스 주식회사 | 면역글로불린 단편을 이용한 인슐린 유도체 약물 결합체 |
| KR20120002129A (ko) * | 2010-06-30 | 2012-01-05 | 한미홀딩스 주식회사 | 면역글로불린 단편을 이용한 제7인자(Factor Ⅶa)약물 결합체 |
| KR101337797B1 (ko) * | 2010-07-14 | 2013-12-06 | 한미사이언스 주식회사 | 지속형 인간 성장 호르몬 결합체 액상 제제 |
| KR101382593B1 (ko) | 2010-07-21 | 2014-04-10 | 한미사이언스 주식회사 | 신규한 지속형 글루카곤 결합체 및 이를 포함하는 비만 예방 및 치료용 약학적 조성물 |
| KR102066996B1 (ko) | 2010-07-28 | 2020-01-17 | 글리크닉 인코포레이티드 | 순차적으로 다중화된 면역글로불린 fc 조성물을 제조하기 위한 천연 인간 단백질 단편들의 융합 단백질 |
| WO2012053828A2 (ko) * | 2010-10-20 | 2012-04-26 | 주식회사 한독약품 | 인간 인터루킨-1 수용체 길항제-하이브리드 Fc 융합단백질 |
| KR101333958B1 (ko) * | 2010-10-20 | 2013-11-27 | 주식회사 한독 | 인간 인터루킨-1 수용체 길항제-하이브리드 Fc 융합단백질 |
| KR101303388B1 (ko) | 2010-10-26 | 2013-09-03 | 한미사이언스 주식회사 | 지속형 인터페론 알파 결합체의 액상 제제 |
| EP2465536A1 (en) | 2010-12-14 | 2012-06-20 | CSL Behring AG | CD89 activation in therapy |
| WO2012085111A1 (en) | 2010-12-23 | 2012-06-28 | F. Hoffmann-La Roche Ag | Polypeptide-polynucleotide-complex and its use in targeted effector moiety delivery |
| CA2823066A1 (en) | 2010-12-27 | 2012-07-05 | Alexion Pharma International Sarl | Compositions comprising natriuretic peptides and methods of use thereof |
| EP2663647A4 (en) | 2011-01-14 | 2015-08-19 | Redwood Bioscience Inc | POLYPEPTIDE IMMUNOGLOBULINS WITH ALDEHYDIC MARKING AND THEIR USE METHOD |
| CN102309765B (zh) * | 2011-02-28 | 2013-10-16 | 北京韩美药品有限公司 | 包含免疫球蛋白Fc片段作为载体的长效抗凝多肽及其制备方法 |
| EP2694092B1 (en) | 2011-04-08 | 2017-01-04 | Amgen Inc. | Method of treating or ameliorating metabolic disorders using growth differentiation factor 15 (gdf-15) |
| UA113626C2 (xx) * | 2011-06-02 | 2017-02-27 | Композиція для лікування діабету, що містить кон'югат інсуліну тривалої дії та кон'югат інсулінотропного пептиду тривалої дії | |
| CN102807619B (zh) * | 2011-06-03 | 2016-08-03 | 北京韩美药品有限公司 | 含有免疫球蛋白Fc片段和粒细胞-巨噬细胞集落刺激因子的复合物及其药物组合物 |
| ES2692187T3 (es) | 2011-06-10 | 2018-11-30 | Hanmi Science Co., Ltd. | Nuevos derivados de oxintomodulina y composición farmacéutica para el tratamiento de obesidad que lo comprende |
| PH12013502517A1 (en) * | 2011-06-17 | 2014-01-20 | Hanmi Science Co Ltd | A conjugate comprising oxyntomodulin and an immunoglobulin fragment, and use thereof |
| US9938353B2 (en) * | 2011-06-24 | 2018-04-10 | The Regents Of The University Of Colorado, A Body Corporate | Compositions, methods and uses for alpha-1 antitrypsin fusion molecules |
| US10400029B2 (en) | 2011-06-28 | 2019-09-03 | Inhibrx, Lp | Serpin fusion polypeptides and methods of use thereof |
| AU2012275295B2 (en) * | 2011-06-28 | 2016-11-10 | Inhibrx, Lp | WAP domain fusion polypeptides and methods of use thereof |
| LT2726092T (lt) * | 2011-06-28 | 2019-10-10 | Inhibrx, Lp | Sulieti serpino polipeptidai ir jų panaudojimo būdai |
| BR112014005091A2 (pt) * | 2011-09-05 | 2017-06-13 | Beijing Hanmi Pharmaceutical Co Ltd | composição farmacêutica para o tratamento do câncer compreendendo conjugado de interferon alfa |
| UY34347A (es) * | 2011-09-26 | 2013-04-30 | Novartis Ag | Proteínas de función dual para tratar trastornos metabólicos |
| US9597378B2 (en) | 2011-10-06 | 2017-03-21 | Hanmi Science Co., Ltd. | Blood coagulation factor VII and VIIa derivatives, conjugates and complexes comprising the same, and use thereof |
| EP2784080B1 (en) * | 2011-10-31 | 2019-12-18 | Shimadzu Corporation | Peptide-hinge-free flexible antibody-like molecule |
| KR20130049671A (ko) * | 2011-11-04 | 2013-05-14 | 한미사이언스 주식회사 | 생리활성 폴리펩타이드 결합체 제조 방법 |
| AU2012364736A1 (en) | 2011-12-19 | 2014-07-24 | Amgen Inc. | Variant activin receptor polypeptides, alone or in combination with chemotherapy, and uses thereof |
| CN103172745A (zh) * | 2011-12-21 | 2013-06-26 | 北京韩美药品有限公司 | 包含免疫球蛋白Fc片段的长效人内皮抑素 |
| KR101895047B1 (ko) * | 2011-12-30 | 2018-09-06 | 한미사이언스 주식회사 | 면역글로불린 단편을 이용한 위치 특이적 글루카곤 유사 펩타이드-2 약물 결합체 |
| KR102041412B1 (ko) * | 2011-12-30 | 2019-11-11 | 한미사이언스 주식회사 | 면역글로불린 Fc 단편 유도체 |
| WO2013106485A2 (en) | 2012-01-09 | 2013-07-18 | The Scripps Research Institute | Ultralong complementarity determining regions and uses thereof |
| JP2015509091A (ja) | 2012-01-09 | 2015-03-26 | ザ スクリプス リサーチ インスティテュート | ヒト化抗体 |
| CA2896951A1 (en) | 2012-01-10 | 2013-07-18 | The Regents Of The University Of Colorado, A Body Corporate | Compositions, methods and uses for alpha-1 antitrypsin fusion molecules |
| BR112014018575A2 (pt) | 2012-01-26 | 2017-07-04 | Amgen Inc | polipetídeos de fator de diferenciação de crescimento 15 (gdf-15) |
| AR090281A1 (es) | 2012-03-08 | 2014-10-29 | Hanmi Science Co Ltd | Proceso mejorado para la preparacion de un complejo polipeptidico fisiologicamente activo |
| EP2636684A1 (en) | 2012-03-09 | 2013-09-11 | CSL Behring AG | Prevention of infection |
| EP2636681A1 (en) | 2012-03-09 | 2013-09-11 | CSL Behring AG | Process for enriching IgA |
| EP2822967B1 (en) | 2012-03-09 | 2019-08-07 | CSL Behring AG | Compositions comprising secretory-like immunoglobulins |
| US10064951B2 (en) * | 2012-03-30 | 2018-09-04 | Hanmi Science Co., Ltd. | Liquid formulation of highly concentrated long-acting human growth hormone conjugate |
| EP2842969B1 (en) * | 2012-04-23 | 2018-03-14 | NRL Pharma, Inc. | Lactoferrin fusion protein and method for preparation thereof |
| US10052366B2 (en) | 2012-05-21 | 2018-08-21 | Alexion Pharmaceuticsl, Inc. | Compositions comprising alkaline phosphatase and/or natriuretic peptide and methods of use thereof |
| DK2859017T3 (da) | 2012-06-08 | 2019-05-13 | Sutro Biopharma Inc | Antistoffer omfattrende stedsspecifikke ikke-naturlige aminosyrerester, fremgangsmåder til fremstilling heraf og fremgangsmåder til anvendelse heraf |
| ES2611788T3 (es) | 2012-06-26 | 2017-05-10 | Sutro Biopharma, Inc. | Proteínas de Fc modificadas que comprenden residuos de aminoácidos no naturales específicos del sitio, conjugados de las mismas, métodos para su preparación y métodos para su uso |
| EP2867253B1 (en) | 2012-06-27 | 2016-09-14 | F. Hoffmann-La Roche AG | Method for selection and production of tailor-made highly selective and multi-specific targeting entities containing at least two different binding entities and uses thereof |
| JP6309002B2 (ja) * | 2012-06-27 | 2018-04-11 | エフ.ホフマン−ラ ロシュ アーゲーF. Hoffmann−La Roche Aktiengesellschaft | 標的に特異的に結合する少なくとも1つの結合実体を含む抗体Fc領域結合体を作製するための方法およびその使用 |
| AR091902A1 (es) | 2012-07-25 | 2015-03-11 | Hanmi Pharm Ind Co Ltd | Formulacion liquida de un conjugado de insulina de accion prolongada |
| US10441665B2 (en) | 2012-07-25 | 2019-10-15 | Hanmi Pharm. Co., Ltd. | Liquid formulation of long acting insulinotropic peptide conjugate |
| AR092862A1 (es) | 2012-07-25 | 2015-05-06 | Hanmi Pharm Ind Co Ltd | Formulacion liquida de insulina de accion prolongada y un peptido insulinotropico y metodo de preparacion |
| KR101968344B1 (ko) | 2012-07-25 | 2019-04-12 | 한미약품 주식회사 | 옥신토모듈린 유도체를 포함하는 고지혈증 치료용 조성물 |
| AR094821A1 (es) * | 2012-07-25 | 2015-09-02 | Hanmi Pharm Ind Co Ltd | Formulación líquida de un conjugado de péptido insulinotrópico de acción prolongada |
| KR20150058236A (ko) | 2012-08-20 | 2015-05-28 | 글리크닉 인코포레이티드 | 항원 결합 및 다가 fc 감마 수용체 결합 활성을 가진 분자 |
| EP3584255B1 (en) | 2012-08-31 | 2022-02-16 | Sutro Biopharma, Inc. | Modified amino acids comprising an azido group |
| BR112015003938A2 (pt) | 2012-09-14 | 2018-09-04 | Hoffmann La Roche | métodos de produção de polipeptídeos, de produção de aglutinantes multiespecíficos, de seleção de aglutinantes multiespecíficos, de seleção de anticorpos biespecíficos e de determinação de combinação, anticorpo biespecífico, formulação farmcêutica e uso de anticorpo biespecífico |
| WO2014043523A1 (en) * | 2012-09-14 | 2014-03-20 | The Johns Hopkins University | Compositions and methods for rendering tumor cells susceptible to cd8+ t cell-mediated killing |
| KR101993393B1 (ko) * | 2012-11-06 | 2019-10-01 | 한미약품 주식회사 | 옥신토모듈린 유도체를 포함하는 당뇨병 또는 비만성 당뇨병 치료용 조성물 |
| ES2748158T3 (es) | 2012-11-06 | 2020-03-13 | Hanmi Pharm Ind Co Ltd | Formulación líquida de conjugado de proteínas que comprende la oxintomodulina y un fragmento de inmunoglobulina |
| CN105073781A (zh) | 2013-01-11 | 2015-11-18 | 加州生物医学研究所 | 牛融合抗体 |
| CN103217489B (zh) * | 2013-01-15 | 2016-03-09 | 珠海市丽珠单抗生物技术有限公司 | 一种测定蛋白纯化工艺过程中样品的糖基化和末端修饰情况的方法 |
| KR102073748B1 (ko) * | 2013-01-31 | 2020-02-05 | 한미약품 주식회사 | 재조합 효모 형질전환체 및 이를 이용하여 면역글로불린 단편을 생산하는 방법 |
| EA201591423A1 (ru) | 2013-02-01 | 2016-01-29 | Санта Мария Биотерапевтикс, Инк. | Введение антитела к активину-а пациентам |
| MX2015010927A (es) * | 2013-02-22 | 2015-10-29 | Zoetis Services Llc | Administracion in ovo de factores de crecimiento para mejorar el rendimiento de aves de corral. |
| PT2966083T (pt) * | 2013-03-05 | 2019-09-17 | Hanmi Pharm Ind Co Ltd | Método de preparação melhorado para produção de alto rendimento de conjugado de polipéptido fisiologicamente ativo |
| WO2014139994A1 (en) | 2013-03-11 | 2014-09-18 | Novo Nordisk Health Care Ag | Growth hormone compounds |
| US20140271641A1 (en) * | 2013-03-14 | 2014-09-18 | University Of Guelph | Thrombospondin-1 polypeptides and methods of using same |
| CA2907046C (en) | 2013-03-15 | 2021-04-20 | Atyr Pharma, Inc. | Histidyl-trna synthetase-fc conjugates |
| TWI745671B (zh) | 2013-03-15 | 2021-11-11 | 美商百歐維拉提夫治療公司 | 因子ix多肽調配物 |
| KR101895634B1 (ko) * | 2013-05-31 | 2018-09-05 | 한미약품 주식회사 | 변이된 힌지 영역을 포함하는 IgG4 Fc 단편 |
| ES2865473T3 (es) | 2013-07-10 | 2021-10-15 | Sutro Biopharma Inc | Anticuerpos que comprenden múltiples residuos de aminoácidos no naturales sitio-específicos, métodos para su preparación y métodos de uso |
| AR096891A1 (es) * | 2013-07-12 | 2016-02-03 | Hanmi Pharm Ind Co Ltd | Conjugado de monómero polipéptido biológicamente activo y conjugado de fragmento fc de inmunoglobulina, que muestra aclaramiento mediado por receptor reducido, y el método para la preparación del mismo |
| AR096890A1 (es) | 2013-07-12 | 2016-02-03 | Hanmi Pharm Ind Co Ltd | Conjugando fc de inmunoglobulina, que mantiene la afinidad de unión del fragmento fc de la inmunoglobulina a fcrn |
| US10640574B2 (en) | 2013-07-18 | 2020-05-05 | Taurus Biosciences, Llc | Humanized antibodies with ultralong complementary determining regions |
| WO2015017710A1 (en) | 2013-07-31 | 2015-02-05 | Amgen Inc. | Growth differentiation factor 15 (gdf-15) constructs |
| WO2015031673A2 (en) | 2013-08-28 | 2015-03-05 | Bioasis Technologies Inc. | Cns-targeted conjugates having modified fc regions and methods of use thereof |
| PL3041513T3 (pl) | 2013-09-08 | 2021-01-25 | Kodiak Sciences Inc. | Obojnaczojonowe polimerowe koniugaty czynnika viii |
| EP3043810B1 (en) | 2013-09-09 | 2019-10-23 | CanImGuide Therapeutics AB | Immune system modulators |
| HK1225976A1 (en) | 2013-09-27 | 2017-09-22 | Hanmi Pharm. Co., Ltd. | Sustained type human growth hormone preparation |
| EP3052697A1 (en) * | 2013-09-30 | 2016-08-10 | 3M Innovative Properties Company | Fibers and wipes with epoxidized fatty ester disposed thereon, and methods |
| US9975942B2 (en) | 2013-11-11 | 2018-05-22 | Wake Forest University Health Services | EPHA3 And multi-valent targeting of tumors |
| CN116987172A (zh) | 2014-01-20 | 2023-11-03 | 韩美药品株式会社 | 长效胰岛素及其用途 |
| WO2015112597A1 (en) * | 2014-01-21 | 2015-07-30 | Belmont Biosciences, Inc. | Variants of igg fc with limited amine groups that retain functional properties |
| CN117065044A (zh) | 2014-03-31 | 2023-11-17 | 韩美药品株式会社 | 通过使用免疫球蛋白Fc片段连接改善蛋白质和肽的溶解度的方法 |
| CN106459205B (zh) * | 2014-04-11 | 2021-04-09 | 免疫医疗有限责任公司 | 包含半胱氨酸工程化抗体的轭合化合物 |
| CN106536548A (zh) * | 2014-04-28 | 2017-03-22 | 国家生物技术研究所公司 | Dr3变体及其用途 |
| KR20150133576A (ko) * | 2014-05-20 | 2015-11-30 | 삼성전자주식회사 | 화학적 개질된 표적화 단백질 및 그의 이용 |
| AR100639A1 (es) | 2014-05-29 | 2016-10-19 | Hanmi Pharm Ind Co Ltd | Composición para tratar diabetes que comprende conjugados de análogos de insulina de acción prolongada y conjugados de péptidos insulinotrópicos de acción prolongada |
| TWI684458B (zh) | 2014-05-30 | 2020-02-11 | 南韓商韓美藥品股份有限公司 | 包含胰島素及glp-1/昇糖素雙重促效劑之治療糖尿病之組成物 |
| EP3161002A1 (en) | 2014-06-27 | 2017-05-03 | Innate Pharma | MULTISPECIFIC NKp46 BINDING PROTEINS |
| WO2015197598A2 (en) * | 2014-06-27 | 2015-12-30 | Innate Pharma | Multispecific antigen binding proteins |
| US9840553B2 (en) | 2014-06-28 | 2017-12-12 | Kodiak Sciences Inc. | Dual PDGF/VEGF antagonists |
| WO2016007873A1 (en) | 2014-07-11 | 2016-01-14 | The Regents Of The University Of Michigan | Compositions and methods for treating craniosynostosis |
| MX2017001022A (es) | 2014-07-24 | 2017-12-20 | Genentech Inc | Metodos para conjugar un agente a un resto tiol en una proteina que contiene al menos un enlace trisulfuro. |
| TWI772252B (zh) | 2014-09-16 | 2022-08-01 | 南韓商韓美藥品股份有限公司 | 長效glp-1/高血糖素受體雙促效劑治療非酒精性脂肝疾病之用途 |
| US9616114B1 (en) | 2014-09-18 | 2017-04-11 | David Gordon Bermudes | Modified bacteria having improved pharmacokinetics and tumor colonization enhancing antitumor activity |
| KR102210104B1 (ko) | 2014-10-17 | 2021-02-01 | 코디악 사이언시스 인코포레이티드 | 부티릴콜린에스테라제 양성이온성 중합체 컨쥬게이트 |
| RU2708068C2 (ru) | 2014-12-05 | 2019-12-04 | Алексион Фармасьютикалз, Инк. | Лечение судорог с использованием рекомбинантной щелочной фосфатазы |
| EP3575314B1 (en) | 2014-12-30 | 2024-02-14 | Hanmi Pharm. Co., Ltd. | Glucagon derivative |
| KR102418477B1 (ko) | 2014-12-30 | 2022-07-08 | 한미약품 주식회사 | 글루카곤 유도체 |
| AU2016211447B2 (en) | 2015-01-28 | 2021-09-23 | Alexion Pharmaceuticals, Inc. | Methods of treating a subject with an alkaline phosphatase deficiency |
| DK3265117T3 (da) | 2015-03-06 | 2021-02-08 | Canimguide Therapeutics Ab | Immunsystemmodulatorer og præparater |
| AU2016246602B2 (en) * | 2015-04-06 | 2020-11-19 | Acceleron Pharma Inc. | Single-arm type I and type II receptor fusion proteins and uses thereof |
| RS61881B1 (sr) * | 2015-04-22 | 2021-06-30 | Biogen Ma Inc | Novi hibridni actriib proteini zamke za ligand za lečenje bolesti gubljenja mišića |
| KR20170138569A (ko) * | 2015-04-29 | 2017-12-15 | 메디오라늄 파마세우티시 에스.피.에이. | 용해성 키메라 인터루킨-10 수용체 및 이의 치료학적 용도 |
| US10676723B2 (en) | 2015-05-11 | 2020-06-09 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| WO2016193380A1 (en) | 2015-06-02 | 2016-12-08 | Novo Nordisk A/S | Insulins with polar recombinant extensions |
| US11820807B2 (en) * | 2015-06-12 | 2023-11-21 | Ubi Pharma Inc | Immunoglobulin fusion proteins and uses thereof |
| KR102721401B1 (ko) * | 2015-06-12 | 2024-11-04 | 유비아이 파마 인크. | 이뮤노글로불린 융합 단백질 및 그의 용도 |
| WO2016207278A1 (en) | 2015-06-23 | 2016-12-29 | Innate Pharma | Multispecific nk engager proteins |
| EP3322437B1 (en) | 2015-06-30 | 2024-01-17 | Hanmi Pharm. Co., Ltd. | Glucagon derivative and a composition comprising a long acting conjugate of the same |
| MX394116B (es) | 2015-07-24 | 2025-03-19 | Gliknik Inc | Proteinas de fusion de fragmentos de proteina humana para crear composiciones de fc de inmunoglobulina multimerizada de forma ordenada con union al complemento aumentada. |
| WO2017018742A1 (en) | 2015-07-24 | 2017-02-02 | Hanmi Pharm. Co., Ltd. | Method of preparing physiologically active polypeptide conjugate |
| RU2745528C2 (ru) | 2015-08-17 | 2021-03-26 | Алексион Фармасьютикалз, Инк. | Производство щелочных фосфатаз |
| UY36870A (es) | 2015-08-28 | 2017-03-31 | Hanmi Pharm Ind Co Ltd | Análogos de insulina novedosos |
| WO2017053469A2 (en) | 2015-09-21 | 2017-03-30 | Aptevo Research And Development Llc | Cd3 binding polypeptides |
| EP4534107A3 (en) * | 2015-09-24 | 2025-12-10 | Hanmi Pharm. Co., Ltd. | Protein complex by use of a specific site of an immunoglobulin fragment for linkage |
| TW201718629A (zh) * | 2015-09-25 | 2017-06-01 | 韓美藥品股份有限公司 | 包含多個生理多肽及免疫球蛋白Fc區之蛋白質接合物 |
| EP3355904A4 (en) | 2015-09-28 | 2019-06-12 | Alexion Pharmaceuticals, Inc. | IDENTIFICATION OF EFFECTIVE DOSE SHEETS FOR TISSUE-SPECIFIC ALKALINE PHOSPHATASE ENZYMERSAT THERAPY OF HYPOPHOSPHATASIA |
| IL316210A (en) | 2015-10-01 | 2024-12-01 | Heat Biologics Inc | Compounds and methods for connecting type 1 and 2 extracellular complexes as heterologous chimeric proteins |
| MA43348A (fr) | 2015-10-01 | 2018-08-08 | Novo Nordisk As | Conjugués de protéines |
| JP7005019B2 (ja) | 2015-10-02 | 2022-02-04 | シルバー・クリーク・ファーマシューティカルズ・インコーポレイテッド | 組織修復のための二重特異性治療用タンパク質 |
| US20170095577A1 (en) * | 2015-10-06 | 2017-04-06 | Washington University | Noninvasive imaging of focal atherosclerotic lesions using fluorescence molecular tomography |
| US11400140B2 (en) | 2015-10-30 | 2022-08-02 | Alexion Pharmaceuticals, Inc. | Methods for treating craniosynostosis in a patient |
| WO2017107914A1 (zh) * | 2015-12-21 | 2017-06-29 | 合肥立方制药股份有限公司 | 一种药物设计方法和获得的药物及其应用 |
| CA3010056A1 (en) | 2015-12-30 | 2017-07-06 | Kodiak Sciences Inc. | Antibodies and conjugates thereof |
| KR20170079409A (ko) * | 2015-12-30 | 2017-07-10 | 한미약품 주식회사 | 지속형 인간 성장 호르몬 결합체의 신규 액상 제제 |
| CN116059389A (zh) | 2015-12-31 | 2023-05-05 | 韩美药品株式会社 | 胰高血糖素/glp-1/gip受体三重激动剂的长效缀合物 |
| CN109069664B (zh) | 2016-01-27 | 2022-05-13 | 苏特罗生物制药公司 | 抗cd74抗体偶联物,包含抗cd74抗体偶联物的组合物以及抗cd74抗体偶联物的使用方法 |
| AR107483A1 (es) | 2016-01-29 | 2018-05-02 | Hanmi Pharm Ind Co Ltd | Conjugado de enzimas terapéuticas |
| WO2017155569A1 (en) | 2016-03-08 | 2017-09-14 | Alexion Pharmaceuticals, Inc. | Methods for treating hypophosphatasia in children |
| US10898549B2 (en) | 2016-04-01 | 2021-01-26 | Alexion Pharmaceuticals, Inc. | Methods for treating hypophosphatasia in adolescents and adults |
| EP3436052A4 (en) | 2016-04-01 | 2019-10-09 | Alexion Pharmaceuticals, Inc. | TREATMENT OF MUSCLE WEAKNESS WITH ALKALINE PHOSPHATASES |
| US11208632B2 (en) | 2016-04-26 | 2021-12-28 | R.P. Scherer Technologies, Llc | Antibody conjugates and methods of making and using the same |
| WO2017191817A1 (ja) | 2016-05-02 | 2017-11-09 | 味の素株式会社 | アジド基含有Fcタンパク質 |
| CN106008722B (zh) * | 2016-05-13 | 2019-10-15 | 未名生物医药有限公司 | 一种重组β-hNGF-Fc融合蛋白、制备方法及用途 |
| US10988744B2 (en) | 2016-06-06 | 2021-04-27 | Alexion Pharmaceuticals, Inc. | Method of producing alkaline phosphatase |
| AU2017279538A1 (en) | 2016-06-07 | 2019-01-03 | Gliknik Inc. | Cysteine-optimized stradomers |
| BR112018077457A2 (pt) | 2016-06-29 | 2019-04-02 | Hanmi Pharm. Co., Ltd. | composição farmacêutica para evitar ou tratar hiperinsulinismo congênito e seu método, hipoglicemia e seu método, síndrome metabólica e seu método e peptídeo isolado |
| EP3500289B1 (en) | 2016-08-18 | 2024-10-09 | Alexion Pharmaceuticals, Inc. | Asfotase alfa for use in treating tracheobronchomalacia |
| JOP20190019A1 (ar) * | 2016-08-30 | 2019-02-12 | Genexine Inc | تركيبة صيدلانية لعلاج نقص في هرمون نمو يحتوي على بروتين اندماجي لهرمون نمو بشري (hGH) |
| CN110546161B (zh) | 2016-09-23 | 2024-01-26 | 韩美药品股份有限公司 | 对胰岛素受体具有降低的结合力的胰岛素类似物及其用途 |
| JOP20190085A1 (ar) | 2016-10-20 | 2019-04-17 | Biogen Ma Inc | طرق علاج الضمور العضلي ومرض العظام باستخدام بروتينات احتجاز مركب ترابطي actriib هجين حديثة |
| JP2019536823A (ja) * | 2016-12-05 | 2019-12-19 | ハンミ ファーマシューティカル カンパニー リミテッド | 免疫反応が弱化された結合体 |
| US11129906B1 (en) | 2016-12-07 | 2021-09-28 | David Gordon Bermudes | Chimeric protein toxins for expression by therapeutic bacteria |
| US11180535B1 (en) | 2016-12-07 | 2021-11-23 | David Gordon Bermudes | Saccharide binding, tumor penetration, and cytotoxic antitumor chimeric peptides from therapeutic bacteria |
| IL317014A (en) | 2016-12-09 | 2025-01-01 | Gliknik Inc | Production optimization of GL-2045, a multimerization sterol. |
| CN110022898B (zh) | 2016-12-09 | 2023-07-04 | 格利克尼克股份有限公司 | 用多价Fc化合物治疗炎性疾病的方法 |
| WO2018143729A1 (ko) * | 2017-02-03 | 2018-08-09 | 한미약품 주식회사 | 지속성이 증가된 생리활성 물질의 결합체 및 이의 용도 |
| JP7128195B2 (ja) | 2017-02-27 | 2022-08-30 | シャタック ラボ,インコーポレイテッド | 細胞外ドメインベースのキメラタンパク質の製造方法及び使用方法 |
| EP3585409A4 (en) | 2017-02-27 | 2020-12-02 | Shattuck Labs, Inc. | CHEMERICAL PROTEINS BASED ON CSF1R |
| EP3604328A4 (en) | 2017-03-23 | 2021-01-06 | Hanmi Pharm. Co., Ltd. | INSULIN ANALOGUE COMPLEX WITH REDUCED AFFINITY FOR THE INSULIN RECEPTOR AND USE OF IT |
| BR112019020506A2 (pt) | 2017-03-31 | 2020-08-04 | Alexion Pharmaceuticals, Inc. | métodos para o tratamento de hipofosfatasia (hpp) em adultos e adolescentes |
| EP3606560A2 (en) | 2017-04-05 | 2020-02-12 | Novo Nordisk A/S | Oligomer extended insulin-fc conjugates |
| WO2018195338A1 (en) | 2017-04-20 | 2018-10-25 | Atyr Pharma, Inc. | Compositions and methods for treating lung inflammation |
| JP2020517657A (ja) * | 2017-04-20 | 2020-06-18 | ノヴォ ノルディスク アー/エス | アルブミン融合タンパク質の精製方法 |
| CN109206522B (zh) * | 2017-07-07 | 2021-11-09 | 北京三有利和泽生物科技有限公司 | 一种长效抗凝血融合蛋白及其应用 |
| JP6566324B2 (ja) * | 2017-09-29 | 2019-08-28 | サイデン化学株式会社 | 粘着シート |
| WO2019066603A1 (ko) | 2017-09-29 | 2019-04-04 | 한미약품 주식회사 | 효력이 향상된 지속성 단백질 결합체 |
| WO2019070577A1 (en) | 2017-10-02 | 2019-04-11 | Denali Therapeutics Inc. | FUSION PROTEINS COMPRISING SUBSTITUTE ENZYM THERAPY ENZYMES |
| KR20190045081A (ko) * | 2017-10-23 | 2019-05-02 | 주식회사 프로젠 | 변형된 egf 단백질 및 이를 유효성분으로 포함하는 피부 상태 개선용 화장료 조성물 |
| KR102167827B1 (ko) * | 2017-12-20 | 2020-10-20 | 주식회사 알테오젠 | 신규한 성장 호르몬 수용체 길항제 및 이의 융합 단백질 |
| CN108218998A (zh) * | 2017-12-31 | 2018-06-29 | 武汉班科生物技术股份有限公司 | 一种突变型人源IgG的Fc片段及其制备方法与应用 |
| KR101974305B1 (ko) * | 2018-02-14 | 2019-04-30 | 한미사이언스 주식회사 | 생리활성 폴리펩타이드 결합체 제조 방법 |
| CN112203679A (zh) | 2018-03-02 | 2021-01-08 | 科达制药股份有限公司 | Il-6抗体及其融合构建体和缀合物 |
| CN116420679B (zh) * | 2018-03-26 | 2025-10-03 | 瑞泽恩制药公司 | 用于测试治疗剂的人源化啮齿动物 |
| KR102209108B1 (ko) | 2018-03-27 | 2021-01-28 | 국립암센터 | Oct4 기능 저해용 펩티드를 포함하는 줄기세포성 억제용 조성물 |
| EP3773684A1 (en) | 2018-03-30 | 2021-02-17 | Alexion Pharmaceuticals, Inc. | Manufacturing of glycoproteins |
| AU2019253462B2 (en) | 2018-04-09 | 2025-04-24 | Amgen Inc. | Growth differentiation factor 15 fusion proteins |
| WO2020033867A2 (en) | 2018-08-10 | 2020-02-13 | Alexion Pharmaceuticals, Inc. | Methods of treating neurofibromatosis type 1 and related conditions with alkaline phosphatase |
| US10780121B2 (en) | 2018-08-29 | 2020-09-22 | Shattuck Labs, Inc. | FLT3L-based chimeric proteins |
| CA3136969A1 (en) * | 2019-04-23 | 2020-10-29 | Lg Chem, Ltd. | Fusion polypeptide comprising fc region of immunoglobulin and gdf15 |
| US11267858B2 (en) * | 2019-05-31 | 2022-03-08 | Spectrum Pharmaceuticals, Inc. | Methods of treatment using G-CSF protein complex |
| CN112142850A (zh) * | 2019-06-27 | 2020-12-29 | 深圳市卫光生物制品股份有限公司 | 人神经生长因子-乳铁蛋白重组蛋白及用途 |
| CN114786731A (zh) | 2019-10-10 | 2022-07-22 | 科达制药股份有限公司 | 治疗眼部病症的方法 |
| CN110669134A (zh) * | 2019-10-15 | 2020-01-10 | 广东菲鹏生物有限公司 | IgM-FC片段、IgM-FC抗体及制备方法和应用 |
| KR20220111693A (ko) | 2019-12-09 | 2022-08-09 | 알렉시온 파마슈티칼스, 인코포레이티드 | 알칼리성 포스파타제 폴리펩티드 및 이의 이용 방법 |
| EP4071166A4 (en) * | 2019-12-11 | 2023-07-26 | Lg Chem, Ltd. | Fusion polypeptide comprising gdf15 and polypeptide region capable of o-glycosylation |
| CN111153996B (zh) * | 2020-01-10 | 2021-12-14 | 苏州睿瀛生物技术有限公司 | G蛋白偶联受体的抗体及其制备方法和g蛋白偶联受体试剂盒 |
| CN111505291B (zh) * | 2020-04-14 | 2023-04-25 | 山东省千佛山医院 | 一种排除巨酶分子对血清酶浓度检测带来干扰的方法 |
| MX2022014670A (es) | 2020-05-22 | 2023-02-13 | Hanmi Pharm Ind Co Ltd | Formulacion liquida. |
| CN112098639B (zh) * | 2020-09-21 | 2024-01-02 | 天津医科大学 | 以氧化石墨烯为载体的二抗的合成及应用 |
| JP2023548496A (ja) * | 2020-11-03 | 2023-11-17 | プロタリクス リミテッド | 修飾ウリカーゼ及びその使用 |
| KR20230145120A (ko) | 2021-02-12 | 2023-10-17 | 알렉시온 파마슈티칼스, 인코포레이티드 | 알칼리성 포스파타제 폴리펩타이드 및 이의 사용 방법 |
| WO2023034809A1 (en) | 2021-08-30 | 2023-03-09 | Lassen Therapeutics 1, Inc. | Anti-il-11rα antibodies |
| MX2024008933A (es) * | 2022-01-28 | 2024-09-30 | argenx BV | Anticuerpos anti-musk para uso en el tratamiento de trastornos neuromusculares. |
| JP2025508988A (ja) * | 2022-03-03 | 2025-04-10 | ザ・トラステイーズ・オブ・ザ・ユニバーシテイ・オブ・ペンシルベニア | 副甲状腺ホルモン融合物をコードするウイルスベクター及び副甲状腺機能低下症の治療におけるその使用 |
| CN114588315A (zh) * | 2022-03-14 | 2022-06-07 | 东莞市人民医院 | 抗炎蛋白涂层的制备方法、生物工程功能材料及其应用 |
| JP2025540182A (ja) * | 2022-12-05 | 2025-12-11 | アレクシオン ファーマシューティカルズ, インコーポレイテッド | Baff、april、及び新生児fc受容体の多機能阻害のためのtaci-fc融合タンパク質 |
| EP4646441A1 (en) | 2023-01-06 | 2025-11-12 | Lassen Therapeutics, Inc. | Anti-il-11r alpha antibodies for treating thyroid eye disease |
| WO2024148241A1 (en) | 2023-01-06 | 2024-07-11 | Lassen Therapeutics 1, Inc. | Anti-il-18bp antibodies |
| IL321948A (en) | 2023-01-06 | 2025-09-01 | Lassen Therapeutics Inc | Anti-IL-18 BP antibodies |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2003521925A (ja) * | 2000-01-19 | 2003-07-22 | ハンミ ファーム. シーオー., エルティーディー. | ヒトインターフェロンアルファの発現分泌ベクターおよびそれを用いたヒトインターフェロンアルファの生産方法 |
| JP2004537262A (ja) * | 2000-12-14 | 2004-12-16 | ジェネンテック・インコーポレーテッド | 細菌性宿主株 |
| JP2005501052A (ja) * | 2001-07-31 | 2005-01-13 | イムノメディクス, インコーポレイテッド | ポリマー送達系 |
Family Cites Families (118)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| 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 |
| GB8504099D0 (en) | 1985-02-18 | 1985-03-20 | Wellcome Found | Physiologically active substances |
| JPS62153300A (ja) * | 1985-12-26 | 1987-07-08 | Teijin Ltd | ヒト免疫グロブリンGFc領域蛋白質およびその製造方法 |
| JPH0728746B2 (ja) | 1986-02-28 | 1995-04-05 | 理化学研究所 | 新規プラスミド、微生物細胞及びヒト免疫グロブリンG Fc領域蛋白質の製造法 |
| US5643758A (en) * | 1987-03-10 | 1997-07-01 | New England Biolabs, Inc. | Production and purification of a protein fused to a binding protein |
| JPS63245691A (ja) | 1987-03-31 | 1988-10-12 | Teijin Ltd | ヒト免疫グロブリンGFc領域蛋白質およびその製造方法 |
| JPS63290899A (ja) | 1987-05-22 | 1988-11-28 | Takeda Chem Ind Ltd | ヒトIgEFc蛋白質のフラグメントおよびその製造法 |
| US6710169B2 (en) * | 1987-10-02 | 2004-03-23 | Genentech, Inc. | Adheson variants |
| US5169770A (en) | 1987-12-21 | 1992-12-08 | The University Of Toledo | Agrobacterium mediated transformation of germinating plant seeds |
| US6004781A (en) | 1988-01-22 | 1999-12-21 | The General Hospital Corporation | Nucleic acid encoding Ig-CD4 fusion proteins |
| US6018026A (en) | 1988-01-22 | 2000-01-25 | Zymogenetics, Inc. | Biologically active dimerized and multimerized polypeptide fusions |
| US5567584A (en) | 1988-01-22 | 1996-10-22 | Zymogenetics, Inc. | Methods of using biologically active dimerized polypeptide fusions to detect PDGF |
| GB8824869D0 (en) | 1988-10-24 | 1988-11-30 | Stevenson G T | Synthetic antibody |
| US5116964A (en) | 1989-02-23 | 1992-05-26 | Genentech, Inc. | Hybrid immunoglobulins |
| US5225538A (en) | 1989-02-23 | 1993-07-06 | Genentech, Inc. | Lymphocyte homing receptor/immunoglobulin fusion proteins |
| US6406697B1 (en) | 1989-02-23 | 2002-06-18 | Genentech, Inc. | Hybrid immunoglobulins |
| US6307025B1 (en) | 1989-04-28 | 2001-10-23 | Biogen, Inc. | VCAM fusion proteins and DNA coding therefor |
| FR2650598B1 (fr) | 1989-08-03 | 1994-06-03 | Rhone Poulenc Sante | Derives de l'albumine a fonction therapeutique |
| US5605690A (en) | 1989-09-05 | 1997-02-25 | Immunex Corporation | Methods of lowering active TNF-α levels in mammals using tumor necrosis factor receptor |
| US6541610B1 (en) | 1989-09-05 | 2003-04-01 | Immunex Corporation | Fusion proteins comprising tumor necrosis factor receptor |
| GB9009106D0 (en) | 1990-04-23 | 1990-06-20 | 3I Res Expl Ltd | Processes and intermediates for synthetic antibody derivatives |
| US5349053A (en) | 1990-06-01 | 1994-09-20 | Protein Design Labs, Inc. | Chimeric ligand/immunoglobulin molecules and their uses |
| US7253264B1 (en) | 1990-06-28 | 2007-08-07 | Sanofi-Arentideutschland GmbH | Immunoglobulin fusion proteins, their production and use |
| ES2120949T4 (es) | 1990-06-28 | 2011-12-29 | Sanofi-Aventis Deutschland Gmbh 50% | Proteinas de fusión con porciones de inmunoglobulinas, su preparación y empleo. |
| US5650150A (en) | 1990-11-09 | 1997-07-22 | Gillies; Stephen D. | Recombinant antibody cytokine fusion proteins |
| US5191066A (en) | 1990-12-07 | 1993-03-02 | Abbott Laboratories | Site-specific conjugation of immunoglobulins and detectable labels |
| ES2237727T3 (es) | 1991-02-08 | 2005-08-01 | Progenics Pharmaceuticals, Inc. | Quimeras de gamma2-cd4 y igg2-cd4. |
| ATE240740T1 (de) | 1991-03-15 | 2003-06-15 | Amgen Inc | Pegylation von polypeptiden |
| KR0172969B1 (ko) * | 1991-04-17 | 1999-02-01 | 삐에르 까스뗄 | 인터페론 알파 및 베타에 대해 높은 친화력을 갖는 수용성 폴리펩티드 |
| EP0533006A1 (en) | 1991-09-18 | 1993-03-24 | F.Hoffmann-La Roche & Co. Aktiengesellschaft | Chimaeric interleukin 5-receptor/immunoglobulin polypeptides |
| US20020037558A1 (en) | 1991-10-23 | 2002-03-28 | Kin-Ming Lo | E.coli produced immunoglobulin constructs |
| FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| FR2686901A1 (fr) | 1992-01-31 | 1993-08-06 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides antithrombotiques, leur preparation et compositions pharmaceutiques les contenant. |
| GB9206422D0 (en) * | 1992-03-24 | 1992-05-06 | Bolt Sarah L | Antibody preparation |
| US5447851B1 (en) | 1992-04-02 | 1999-07-06 | Univ Texas System Board Of | Dna encoding a chimeric polypeptide comprising the extracellular domain of tnf receptor fused to igg vectors and host cells |
| JPH0640945A (ja) | 1992-07-23 | 1994-02-15 | Kureha Chem Ind Co Ltd | Fcフラグメント結合抗腫瘍剤 |
| CA2141673A1 (en) * | 1992-08-07 | 1994-02-17 | Graham P. Allaway | Non-peptidyl moiety-conjugated cd4-gamma2 and cd4-igg2 immunoconjugates, and uses thereof |
| IT1263831B (it) | 1993-01-29 | 1996-09-04 | Paolo Chiesi | Complessi di inclusione multicomponente ad elevata solubilita' costituiti da un farmaco di tipo basico, un acido ed una ciclodestrina |
| US6482919B2 (en) | 1993-02-01 | 2002-11-19 | Bristol-Myers Squibb Company | Expression vectors encoding bispecific fusion proteins and methods of producing biologically active bispecific fusion proteins in a mammalian cell |
| US5470952A (en) | 1993-10-20 | 1995-11-28 | Regeneron Pharmaceuticals, Inc. | CNTF and IL-6 antagonists |
| US5738846A (en) | 1994-11-10 | 1998-04-14 | Enzon, Inc. | Interferon polymer conjugates and process for preparing the same |
| US6410008B1 (en) | 1994-12-12 | 2002-06-25 | Beth Israel Hospital Association | Chimeric IL-10 proteins and uses thereof |
| US6030613A (en) * | 1995-01-17 | 2000-02-29 | The Brigham And Women's Hospital, Inc. | Receptor specific transepithelial transport of therapeutics |
| EP0816381B1 (en) | 1995-03-10 | 2004-01-14 | NAKAMURA, Toshikazu | Polyethylene glycol modified hepatocyte growth factor (hgf) |
| US6096871A (en) | 1995-04-14 | 2000-08-01 | Genentech, Inc. | Polypeptides altered to contain an epitope from the Fc region of an IgG molecule for increased half-life |
| GB9511935D0 (en) | 1995-06-13 | 1995-08-09 | Smithkline Beecham Plc | Novel compound |
| NZ318472A (en) * | 1995-09-21 | 1999-10-28 | Quadrant Healthcare Uk Ltd | Composition or conjugate containing a gp60 receptor and a transcytosis enhancer (typically albumin) |
| US6936439B2 (en) | 1995-11-22 | 2005-08-30 | Amgen Inc. | OB fusion protein compositions and methods |
| US6620413B1 (en) * | 1995-12-27 | 2003-09-16 | Genentech, Inc. | OB protein-polymer chimeras |
| WO1997024440A1 (en) * | 1995-12-27 | 1997-07-10 | Genentech, Inc. | Ob protein derivatives having prolonged half-life |
| US5723125A (en) | 1995-12-28 | 1998-03-03 | Tanox Biosystems, Inc. | Hybrid with interferon-alpha and an immunoglobulin Fc linked through a non-immunogenic peptide |
| US6750334B1 (en) * | 1996-02-02 | 2004-06-15 | Repligen Corporation | CTLA4-immunoglobulin fusion proteins having modified effector functions and uses therefor |
| AU728657B2 (en) | 1996-03-18 | 2001-01-18 | Board Of Regents, The University Of Texas System | Immunoglobulin-like domains with increased half-lives |
| KR19980038061A (ko) | 1996-11-23 | 1998-08-05 | 유우준 | 음식물 쓰레기 수분분리 처리장치 |
| US7122636B1 (en) * | 1997-02-21 | 2006-10-17 | Genentech, Inc. | Antibody fragment-polymer conjugates and uses of same |
| US6277375B1 (en) | 1997-03-03 | 2001-08-21 | Board Of Regents, The University Of Texas System | Immunoglobulin-like domains with increased half-lives |
| AR012448A1 (es) * | 1997-04-18 | 2000-10-18 | Ipsen Pharma Biotech | Composicion en forma de microcapsulas o de implantes que comprende un excipiente biodegradable, polimero o co-polimero, o una mezcla de talesexcipientes, y una sustancia activa o una mezcla de sustancias activas, procedimiento para la preparacion de una sustancia soluble en agua de elevada |
| US5990237A (en) * | 1997-05-21 | 1999-11-23 | Shearwater Polymers, Inc. | Poly(ethylene glycol) aldehyde hydrates and related polymers and applications in modifying amines |
| US6165476A (en) | 1997-07-10 | 2000-12-26 | Beth Israel Deaconess Medical Center | Fusion proteins with an immunoglobulin hinge region linker |
| WO1999002709A1 (en) | 1997-07-10 | 1999-01-21 | Beth Israel Deaconess Medical Center | Recombinant erythropoietin / immunoglobulin fusion proteins |
| US6451986B1 (en) * | 1998-06-22 | 2002-09-17 | Immunex Corporation | Site specific protein modification |
| US6703381B1 (en) * | 1998-08-14 | 2004-03-09 | Nobex Corporation | Methods for delivery therapeutic compounds across the blood-brain barrier |
| KR100316347B1 (ko) * | 1998-09-15 | 2002-08-27 | 한미약품(주) | 대장균엔테로톡신ⅱ신호펩티드의변형체와인체성장호르몬의융합단백질을발현하는재조합미생물및그를이용한인체성장호르몬의제조방법 |
| MXPA01003790A (es) * | 1998-10-16 | 2002-09-18 | Biogen Inc | Proteinas de fusion beta - interferon y sus usos. |
| US6660843B1 (en) * | 1998-10-23 | 2003-12-09 | Amgen Inc. | Modified peptides as therapeutic agents |
| EP1141013A2 (en) | 1999-01-07 | 2001-10-10 | Lexigen Pharmaceuticals Corp. | EXPRESSION AND EXPORT OF ANTI-OBESITY PROTEINS AS Fc FUSION PROTEINS |
| US6737056B1 (en) * | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| US6656728B1 (en) | 1999-02-08 | 2003-12-02 | Chiron Corporation | Fibroblast growth factor receptor-immunoglobulin fusion |
| US20040266673A1 (en) * | 2002-07-31 | 2004-12-30 | Peter Bakis | Long lasting natriuretic peptide derivatives |
| CN1361793A (zh) * | 1999-05-19 | 2002-07-31 | 利思进药品公司 | 干扰素-α蛋白作为Fc融合蛋白的表达和运输 |
| US6833349B2 (en) * | 1999-06-08 | 2004-12-21 | Regeneron Pharmaceuticals, Inc. | Methods of treating inflammatory skin diseases |
| PE20010288A1 (es) * | 1999-07-02 | 2001-03-07 | Hoffmann La Roche | Derivados de eritropoyetina |
| IL147270A0 (en) * | 1999-07-02 | 2002-08-14 | Genentech Inc | Fusion peptides comprising a peptide ligand domain and a multimerization domain |
| JP4944324B2 (ja) * | 1999-07-13 | 2012-05-30 | ボルダー バイオテクノロジー, インコーポレイテッド | 免疫グロブリン融合タンパク質 |
| AU2001257173B2 (en) * | 2000-04-21 | 2005-09-22 | Amgen Inc. | Apo-ai/aii peptide derivatives |
| US6756480B2 (en) * | 2000-04-27 | 2004-06-29 | Amgen Inc. | Modulators of receptors for parathyroid hormone and parathyroid hormone-related protein |
| US20020168367A1 (en) * | 2000-04-28 | 2002-11-14 | Planet Biotechnology Incorporated | Novel immunoadhesins for treating and preventing viral and bacterial diseases |
| US6677136B2 (en) * | 2000-05-03 | 2004-01-13 | Amgen Inc. | Glucagon antagonists |
| DE10021731B4 (de) | 2000-05-04 | 2005-12-08 | Aventis Pharma Deutschland Gmbh | Cyclipostine, Verfahren zu ihrer Herstellung und pharmazeutische Zubereitung derselben |
| US6417237B1 (en) | 2000-06-08 | 2002-07-09 | The Board Of Trustees Of The University Of Illinois | Macromolecular drug complexes and compositions containing the same |
| WO2002046227A2 (en) * | 2000-12-07 | 2002-06-13 | Eli Lilly And Company | Glp-1 fusion proteins |
| US6979556B2 (en) | 2000-12-14 | 2005-12-27 | Genentech, Inc. | Separate-cistron contructs for secretion of aglycosylated antibodies from prokaryotes |
| US7829084B2 (en) | 2001-01-17 | 2010-11-09 | Trubion Pharmaceuticals, Inc. | Binding constructs and methods for use thereof |
| US7754208B2 (en) | 2001-01-17 | 2010-07-13 | Trubion Pharmaceuticals, Inc. | Binding domain-immunoglobulin fusion proteins |
| CN1630720A (zh) | 2001-01-18 | 2005-06-22 | 默克专利有限公司 | 具有葡糖脑苷脂酶活性的双功能融合蛋白 |
| CA2438628A1 (en) * | 2001-02-19 | 2002-08-29 | Merck Patent Gesellschaft Mit Beschraenkter Haftung | Artificial proteins with reduced immunogenicity |
| KR100566911B1 (ko) | 2001-06-25 | 2006-04-03 | 주식회사 삼양사 | 약물 전달체용 음이온기-함유 양친성 블록 공중합체 및 그의 양이온성 약물과의 복합체 |
| EP1411983A4 (en) * | 2001-06-26 | 2006-06-21 | Imclone Systems Inc | BISPECIFIC ANTIBODIES BINDING TO VEGF RECEPTORS |
| US6900292B2 (en) | 2001-08-17 | 2005-05-31 | Lee-Hwei K. Sun | Fc fusion proteins of human erythropoietin with increased biological activities |
| US6797493B2 (en) * | 2001-10-01 | 2004-09-28 | Lee-Hwei K. Sun | Fc fusion proteins of human granulocyte colony-stimulating factor with increased biological activities |
| US7125843B2 (en) * | 2001-10-19 | 2006-10-24 | Neose Technologies, Inc. | Glycoconjugates including more than one peptide |
| US7138370B2 (en) | 2001-10-11 | 2006-11-21 | Amgen Inc. | Specific binding agents of human angiopoietin-2 |
| KR100811138B1 (ko) | 2001-11-13 | 2008-03-07 | 오리온피디피주식회사 | 저온소성세라믹기판을 이용한 다층회로기판의 제조방법과 이에 의해 제조된 다층회로기판 |
| WO2003049684A2 (en) * | 2001-12-07 | 2003-06-19 | Centocor, Inc. | Pseudo-antibody constructs |
| AU2003217912A1 (en) * | 2002-03-01 | 2003-09-16 | Xencor | Antibody optimization |
| EP1572936A2 (en) | 2002-03-05 | 2005-09-14 | Eli Lilly And Company | Heterologous g-csf fusion proteins |
| CN101143221A (zh) | 2002-03-15 | 2008-03-19 | 布赖汉姆妇女医院 | 适合治疗剂全身性递送的中央气道给药 |
| US20030191056A1 (en) * | 2002-04-04 | 2003-10-09 | Kenneth Walker | Use of transthyretin peptide/protein fusions to increase the serum half-life of pharmacologically active peptides/proteins |
| EP1539811A4 (en) * | 2002-09-16 | 2006-05-24 | Elusys Therapeutics Inc | PREPARATION OF BISPEQIFIC MOLECULES WITH POLYETHYLENE GLYCOL LINKER |
| US7608429B2 (en) * | 2002-10-31 | 2009-10-27 | Genentech, Inc. | Methods and compositions for increasing antibody production |
| WO2004058988A2 (en) | 2002-12-20 | 2004-07-15 | Amgen, Inc. | Binding agents which inhibit myostatin |
| WO2004064731A2 (en) | 2003-01-14 | 2004-08-05 | University Of Washington | Lipid-drug formulations and methods for targeted delivery of lipid-drug complexes to lymlplhoid tissues |
| US20050176108A1 (en) | 2003-03-13 | 2005-08-11 | Young-Min Kim | Physiologically active polypeptide conjugate having prolonged in vivo half-life |
| KR20040083268A (ko) | 2003-03-21 | 2004-10-01 | 한미약품 주식회사 | 안정성이 증가된 인간 과립구 콜로니 자극인자 융합체 및이의 제조방법 |
| ATE497783T1 (de) | 2003-05-06 | 2011-02-15 | Syntonix Pharmaceuticals Inc | Gerinnungsfaktor vii-fc chimäre proteine zur behandlung von hämostatischen krankheiten |
| US20050281829A1 (en) | 2003-05-06 | 2005-12-22 | Hehir Cristina A T | Fc chimeric proteins with anti-HIV drugs |
| TWI353991B (en) | 2003-05-06 | 2011-12-11 | Syntonix Pharmaceuticals Inc | Immunoglobulin chimeric monomer-dimer hybrids |
| US20070041972A1 (en) * | 2003-05-30 | 2007-02-22 | Alexion Pharmaceuticals, Inc. | Antibodies and fusion proteins that include engineered constant regions |
| DK1682583T3 (da) * | 2003-11-13 | 2012-05-07 | Hanmi Holdings Co Ltd | Proteinkompleksdannelse under anvendelse af immunoglobulinfragment samt fremgangsmåde til fremstilling deraf |
| CN1926237A (zh) | 2004-01-28 | 2007-03-07 | 森托尼克斯制药有限公司 | 用于治疗不育症的异二聚体促卵泡激素-Fc(FSH-Fc)融合蛋白 |
| US20060084145A1 (en) | 2004-09-27 | 2006-04-20 | Anderson Glenn M | sRAGE mimetibody, compositions, methods and uses |
| KR100594607B1 (ko) | 2004-11-03 | 2006-06-30 | 재단법인서울대학교산학협력재단 | 신규한 경구투여용 재조합 인간 성장호르몬 분비미생물제제 및 그 제조방법 |
| KR100754667B1 (ko) * | 2005-04-08 | 2007-09-03 | 한미약품 주식회사 | 비펩타이드성 중합체로 개질된 면역글로불린 Fc 단편 및이를 포함하는 약제학적 조성물 |
| KR20100038061A (ko) | 2008-10-02 | 2010-04-12 | 도쿠리츠다이가쿠호징 가나자와다이가쿠 | 리마프로스트를 함유하는, 암화학 요법에 기인하는 말초신경장애 예방, 치료 및/또는 증상 경감제 |
| AR081066A1 (es) * | 2010-04-02 | 2012-06-06 | Hanmi Holdings Co Ltd | Conjugado de insulina donde se usa un fragmento de inmunoglobulina |
| AR081755A1 (es) * | 2010-04-02 | 2012-10-17 | Hanmi Holdings Co Ltd | Formulacion de accion prolongada de la hormona estimuladora de los foliculos donde se usa un fragmento de inmunoglobulina, metodo de preparacion y metodo para tratar a un sujeto que sufre un trastorno reproductivo |
| AR080993A1 (es) * | 2010-04-02 | 2012-05-30 | Hanmi Holdings Co Ltd | Formulacion de accion prolongada de interferon beta donde se usa un fragmento de inmunoglobulina |
| KR20120002129A (ko) * | 2010-06-30 | 2012-01-05 | 한미홀딩스 주식회사 | 면역글로불린 단편을 이용한 제7인자(Factor Ⅶa)약물 결합체 |
-
2004
- 2004-11-13 DK DK04800091.3T patent/DK1682583T3/da active
- 2004-11-13 BR BR0406606-5A patent/BRPI0406606A/pt not_active Application Discontinuation
- 2004-11-13 EP EP04800090A patent/EP1682582B1/en not_active Expired - Lifetime
- 2004-11-13 EP EP04800091A patent/EP1682583B1/en not_active Expired - Lifetime
- 2004-11-13 JP JP2006539398A patent/JP4870569B2/ja not_active Expired - Lifetime
- 2004-11-13 PL PL10006326T patent/PL2239273T3/pl unknown
- 2004-11-13 CN CN201210190634.9A patent/CN103212084B/zh not_active Expired - Lifetime
- 2004-11-13 EP EP04800092.1A patent/EP1682584B1/en not_active Expired - Lifetime
- 2004-11-13 RU RU2005120239/13A patent/RU2352583C2/ru active
- 2004-11-13 PT PT100063262T patent/PT2239273E/pt unknown
- 2004-11-13 US US10/535,341 patent/US8846874B2/en not_active Expired - Lifetime
- 2004-11-13 MX MXPA05007211A patent/MXPA05007211A/es active IP Right Grant
- 2004-11-13 ES ES04800090T patent/ES2372495T3/es not_active Expired - Lifetime
- 2004-11-13 ES ES10006326.2T patent/ES2438098T3/es not_active Expired - Lifetime
- 2004-11-13 ES ES04800092T patent/ES2426169T3/es not_active Expired - Lifetime
- 2004-11-13 PL PL10009129T patent/PL2256134T3/pl unknown
- 2004-11-13 KR KR1020040092782A patent/KR100725315B1/ko not_active Expired - Lifetime
- 2004-11-13 CN CN2004800017702A patent/CN1723219B/zh not_active Expired - Lifetime
- 2004-11-13 JP JP2006539399A patent/JP5216216B2/ja not_active Expired - Lifetime
- 2004-11-13 EP EP10006326.2A patent/EP2239273B1/en not_active Expired - Lifetime
- 2004-11-13 CN CNA2004800017755A patent/CN1723220A/zh active Pending
- 2004-11-13 JP JP2006539397A patent/JP4762904B2/ja not_active Expired - Lifetime
- 2004-11-13 AT AT04800090T patent/ATE522548T1/de not_active IP Right Cessation
- 2004-11-13 US US10/535,312 patent/US8029789B2/en not_active Expired - Lifetime
- 2004-11-13 EP EP10009129.7A patent/EP2256134B1/en not_active Expired - Lifetime
- 2004-11-13 WO PCT/KR2004/002942 patent/WO2005047334A1/en not_active Ceased
- 2004-11-13 CA CA2512933A patent/CA2512933C/en not_active Expired - Fee Related
- 2004-11-13 MX MXPA05007210A patent/MXPA05007210A/es active IP Right Grant
- 2004-11-13 ES ES04800089T patent/ES2383300T3/es not_active Expired - Lifetime
- 2004-11-13 JP JP2006539396A patent/JP2007531513A/ja active Pending
- 2004-11-13 CA CA2512657A patent/CA2512657C/en not_active Expired - Lifetime
- 2004-11-13 WO PCT/KR2004/002943 patent/WO2005047335A1/en not_active Ceased
- 2004-11-13 PT PT04800091T patent/PT1682583E/pt unknown
- 2004-11-13 EP EP04800089A patent/EP1682581B1/en not_active Expired - Lifetime
- 2004-11-13 KR KR1020040092781A patent/KR100775343B1/ko not_active Expired - Lifetime
- 2004-11-13 AU AU2004282985A patent/AU2004282985B8/en not_active Expired
- 2004-11-13 CN CN201810616347.7A patent/CN108743967B/zh not_active Expired - Lifetime
- 2004-11-13 AT AT04800091T patent/ATE540980T1/de active
- 2004-11-13 US US10/535,232 patent/US7737260B2/en not_active Expired - Lifetime
- 2004-11-13 DK DK10009129.7T patent/DK2256134T3/en active
- 2004-11-13 AT AT04800089T patent/ATE555133T1/de active
- 2004-11-13 AU AU2004282984A patent/AU2004282984B2/en not_active Expired
- 2004-11-13 BR BRPI0406605A patent/BRPI0406605B8/pt active IP Right Grant
- 2004-11-13 ES ES04800091T patent/ES2378167T3/es not_active Expired - Lifetime
- 2004-11-13 WO PCT/KR2004/002944 patent/WO2005047336A1/en not_active Ceased
- 2004-11-13 ES ES10009129.7T patent/ES2454666T3/es not_active Expired - Lifetime
- 2004-11-13 DK DK10006326.2T patent/DK2239273T3/da active
- 2004-11-13 KR KR1020040092783A patent/KR100725314B1/ko not_active Expired - Lifetime
- 2004-11-13 PT PT100091297T patent/PT2256134E/pt unknown
- 2004-11-13 RU RU2005120240/13A patent/RU2356909C2/ru active
- 2004-11-13 KR KR1020040092780A patent/KR20050047030A/ko not_active Withdrawn
- 2004-11-13 WO PCT/KR2004/002945 patent/WO2005047337A1/en not_active Ceased
- 2004-11-13 US US10/535,231 patent/US7736653B2/en not_active Expired - Lifetime
-
2006
- 2006-04-24 KR KR1020060036697A patent/KR20060054252A/ko not_active Ceased
-
2007
- 2007-05-03 US US11/744,162 patent/US20080085862A1/en not_active Abandoned
- 2007-05-10 US US11/747,153 patent/US20080124347A1/en not_active Abandoned
-
2010
- 2010-04-09 US US12/757,635 patent/US20100255014A1/en not_active Abandoned
-
2011
- 2011-04-15 US US13/087,593 patent/US8822650B2/en not_active Expired - Lifetime
- 2011-09-15 JP JP2011202199A patent/JP5425150B2/ja not_active Expired - Fee Related
- 2011-09-26 JP JP2011209594A patent/JP2011256211A/ja not_active Abandoned
-
2012
- 2012-07-26 JP JP2012166208A patent/JP2012224635A/ja not_active Withdrawn
-
2013
- 2013-03-12 US US13/796,135 patent/US10071166B2/en not_active Expired - Lifetime
-
2014
- 2014-07-09 US US14/327,064 patent/US10272159B2/en not_active Expired - Lifetime
- 2014-07-09 US US14/327,120 patent/US9750820B2/en not_active Expired - Lifetime
-
2018
- 2018-07-20 US US16/041,263 patent/US20180326083A1/en not_active Abandoned
-
2019
- 2019-03-12 US US16/351,338 patent/US11058776B2/en not_active Expired - Fee Related
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2003521925A (ja) * | 2000-01-19 | 2003-07-22 | ハンミ ファーム. シーオー., エルティーディー. | ヒトインターフェロンアルファの発現分泌ベクターおよびそれを用いたヒトインターフェロンアルファの生産方法 |
| JP2004537262A (ja) * | 2000-12-14 | 2004-12-16 | ジェネンテック・インコーポレーテッド | 細菌性宿主株 |
| JP2005501052A (ja) * | 2001-07-31 | 2005-01-13 | イムノメディクス, インコーポレイテッド | ポリマー送達系 |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP4762904B2 (ja) | 免疫グロブリン不変領域の量産方法 | |
| JP5846712B2 (ja) | 開始メチオニン残基が除去された免疫グロブリンFc領域の大量生産方法 | |
| US11147857B2 (en) | IgG4 Fc fragment comprising modified hinge region | |
| KR102231217B1 (ko) | 면역글로불린 단편의 특정 위치를 연결 부위로 이용한 단백질 결합체 | |
| KR100824505B1 (ko) | 개시 메티오닌 잔기가 제거된 면역글로불린 Fc 영역의대량 생산방법 | |
| HK1220464B (en) | Igg4 fc fragment comprising modified hinge region | |
| HK1121768B (en) | A method for the mass production of immunoglobulin fc region deleted initial methionine residues |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20071112 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20071112 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20100921 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20101220 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20110121 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20101228 |
|
| TRDD | Decision of grant or rejection written | ||
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20110524 |
|
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20110608 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20140617 Year of fee payment: 3 |
|
| R150 | Certificate of patent or registration of utility model |
Ref document number: 4762904 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
| S111 | Request for change of ownership or part of ownership |
Free format text: JAPANESE INTERMEDIATE CODE: R313113 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20140617 Year of fee payment: 3 |
|
| R350 | Written notification of registration of transfer |
Free format text: JAPANESE INTERMEDIATE CODE: R350 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| EXPY | Cancellation because of completion of term |