JP2013534426A - 第ix因子ポリペプチドおよびその使用方法 - Google Patents
第ix因子ポリペプチドおよびその使用方法 Download PDFInfo
- Publication number
- JP2013534426A JP2013534426A JP2013518876A JP2013518876A JP2013534426A JP 2013534426 A JP2013534426 A JP 2013534426A JP 2013518876 A JP2013518876 A JP 2013518876A JP 2013518876 A JP2013518876 A JP 2013518876A JP 2013534426 A JP2013534426 A JP 2013534426A
- Authority
- JP
- Japan
- Prior art keywords
- dose
- factor
- activity
- polypeptide
- bleeding
- 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.)
- Pending
Links
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 225
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 211
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 209
- 108010076282 Factor IX Proteins 0.000 title claims abstract description 152
- 102100022641 Coagulation factor IX Human genes 0.000 title claims abstract description 150
- 229960004222 factor ix Drugs 0.000 title claims abstract description 149
- 238000000034 method Methods 0.000 title claims abstract description 128
- 102100026120 IgG receptor FcRn large subunit p51 Human genes 0.000 claims abstract description 75
- 101710177940 IgG receptor FcRn large subunit p51 Proteins 0.000 claims abstract description 74
- 108091033319 polynucleotide Proteins 0.000 claims abstract description 31
- 102000040430 polynucleotide Human genes 0.000 claims abstract description 31
- 239000002157 polynucleotide Substances 0.000 claims abstract description 31
- 230000027455 binding Effects 0.000 claims abstract description 26
- 230000000694 effects Effects 0.000 claims description 183
- 208000032843 Hemorrhage Diseases 0.000 claims description 102
- 208000034158 bleeding Diseases 0.000 claims description 99
- 230000000740 bleeding effect Effects 0.000 claims description 99
- 238000011282 treatment Methods 0.000 claims description 66
- 150000001413 amino acids Chemical class 0.000 claims description 38
- 238000011084 recovery Methods 0.000 claims description 38
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 37
- 238000001356 surgical procedure Methods 0.000 claims description 37
- 108090000623 proteins and genes Proteins 0.000 claims description 33
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 32
- 102000004169 proteins and genes Human genes 0.000 claims description 30
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 19
- 208000014674 injury Diseases 0.000 claims description 19
- 230000002829 reductive effect Effects 0.000 claims description 18
- 230000002265 prevention Effects 0.000 claims description 17
- 210000004027 cell Anatomy 0.000 claims description 16
- 230000036470 plasma concentration Effects 0.000 claims description 14
- 230000000069 prophylactic effect Effects 0.000 claims description 14
- 238000011321 prophylaxis Methods 0.000 claims description 12
- 208000024891 symptom Diseases 0.000 claims description 12
- 230000008733 trauma Effects 0.000 claims description 10
- 230000026731 phosphorylation Effects 0.000 claims description 9
- 238000006366 phosphorylation reaction Methods 0.000 claims description 9
- 238000002360 preparation method Methods 0.000 claims description 8
- 230000019635 sulfation Effects 0.000 claims description 8
- 238000005670 sulfation reaction Methods 0.000 claims description 8
- 102000009027 Albumins Human genes 0.000 claims description 7
- 108010088751 Albumins Proteins 0.000 claims description 7
- 241000282412 Homo Species 0.000 claims description 7
- 238000007917 intracranial administration Methods 0.000 claims description 7
- 210000001503 joint Anatomy 0.000 claims description 7
- 210000003205 muscle Anatomy 0.000 claims description 7
- 208000034656 Contusions Diseases 0.000 claims description 6
- 206010051297 Soft tissue haemorrhage Diseases 0.000 claims description 6
- 238000000605 extraction Methods 0.000 claims description 6
- 238000007912 intraperitoneal administration Methods 0.000 claims description 6
- 206010028024 Mouth haemorrhage Diseases 0.000 claims description 5
- 238000004519 manufacturing process Methods 0.000 claims description 5
- 208000012310 mouth bleeding Diseases 0.000 claims description 5
- 206010072043 Central nervous system haemorrhage Diseases 0.000 claims description 4
- 238000007918 intramuscular administration Methods 0.000 claims description 4
- 101150050927 Fcgrt gene Proteins 0.000 claims description 3
- 206010018276 Gingival bleeding Diseases 0.000 claims description 3
- 206010061298 Mucosal haemorrhage Diseases 0.000 claims description 3
- 206010028309 Muscle haemorrhage Diseases 0.000 claims description 3
- 206010034827 Pharyngeal haemorrhage Diseases 0.000 claims description 3
- 210000004556 brain Anatomy 0.000 claims description 3
- 208000001780 epistaxis Diseases 0.000 claims description 3
- 208000011759 gum bleeding Diseases 0.000 claims description 3
- 208000002085 hemarthrosis Diseases 0.000 claims description 3
- 208000006750 hematuria Diseases 0.000 claims description 3
- 230000000399 orthopedic effect Effects 0.000 claims description 3
- 239000008194 pharmaceutical composition Substances 0.000 claims description 3
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 3
- 210000001835 viscera Anatomy 0.000 claims description 3
- 208000012671 Gastrointestinal haemorrhages Diseases 0.000 claims description 2
- 206010019909 Hernia Diseases 0.000 claims description 2
- 208000029836 Inguinal Hernia Diseases 0.000 claims description 2
- 241000700605 Viruses Species 0.000 claims description 2
- 238000007428 craniotomy Methods 0.000 claims description 2
- 210000004748 cultured cell Anatomy 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims description 2
- 208000030304 gastrointestinal bleeding Diseases 0.000 claims description 2
- 210000003127 knee Anatomy 0.000 claims description 2
- 238000013150 knee replacement Methods 0.000 claims description 2
- 239000013612 plasmid Substances 0.000 claims description 2
- 238000002271 resection Methods 0.000 claims description 2
- 238000007483 tonsillectomy Methods 0.000 claims description 2
- 206010061249 Intra-abdominal haemorrhage Diseases 0.000 claims 1
- 229960000027 human factor ix Drugs 0.000 claims 1
- 238000011866 long-term treatment Methods 0.000 claims 1
- 230000003387 muscular Effects 0.000 claims 1
- 210000000653 nervous system Anatomy 0.000 claims 1
- 125000002924 primary amino group Chemical class [H]N([H])* 0.000 claims 1
- 210000000574 retroperitoneal space Anatomy 0.000 claims 1
- 229940031422 benefix Drugs 0.000 description 72
- 208000031220 Hemophilia Diseases 0.000 description 66
- 208000009292 Hemophilia A Diseases 0.000 description 66
- 241000699670 Mus sp. Species 0.000 description 59
- 239000000427 antigen Substances 0.000 description 50
- 102000036639 antigens Human genes 0.000 description 50
- 108091007433 antigens Proteins 0.000 description 50
- 239000008280 blood Substances 0.000 description 41
- 210000004369 blood Anatomy 0.000 description 41
- 238000004458 analytical method Methods 0.000 description 33
- 230000035602 clotting Effects 0.000 description 25
- 238000001802 infusion Methods 0.000 description 25
- 238000001990 intravenous administration Methods 0.000 description 23
- 235000018102 proteins Nutrition 0.000 description 22
- 235000001014 amino acid Nutrition 0.000 description 20
- 125000003729 nucleotide group Chemical group 0.000 description 20
- 239000002773 nucleotide Substances 0.000 description 18
- 238000009826 distribution Methods 0.000 description 17
- 238000002266 amputation Methods 0.000 description 16
- 238000003556 assay Methods 0.000 description 16
- 238000002965 ELISA Methods 0.000 description 15
- 230000002950 deficient Effects 0.000 description 15
- 238000012217 deletion Methods 0.000 description 15
- 230000037430 deletion Effects 0.000 description 15
- 230000035772 mutation Effects 0.000 description 14
- 238000013169 thromboelastometry Methods 0.000 description 14
- 210000003462 vein Anatomy 0.000 description 14
- 239000012634 fragment Substances 0.000 description 13
- 238000005070 sampling Methods 0.000 description 13
- 206010053567 Coagulopathies Diseases 0.000 description 12
- 239000003814 drug Substances 0.000 description 12
- 230000008030 elimination Effects 0.000 description 12
- 238000003379 elimination reaction Methods 0.000 description 12
- 230000037396 body weight Effects 0.000 description 11
- 229940079593 drug Drugs 0.000 description 11
- 238000001727 in vivo Methods 0.000 description 11
- 230000006378 damage Effects 0.000 description 10
- 230000007423 decrease Effects 0.000 description 10
- 231100000673 dose–response relationship Toxicity 0.000 description 10
- 238000011287 therapeutic dose Methods 0.000 description 10
- 238000005571 anion exchange chromatography Methods 0.000 description 9
- 238000004364 calculation method Methods 0.000 description 9
- 241001465754 Metazoa Species 0.000 description 8
- 208000027418 Wounds and injury Diseases 0.000 description 8
- 125000000539 amino acid group Chemical group 0.000 description 8
- 230000023555 blood coagulation Effects 0.000 description 8
- 238000000338 in vitro Methods 0.000 description 8
- 230000004083 survival effect Effects 0.000 description 8
- 238000002347 injection Methods 0.000 description 7
- 239000007924 injection Substances 0.000 description 7
- 230000007774 longterm Effects 0.000 description 7
- 102000039446 nucleic acids Human genes 0.000 description 7
- 108020004707 nucleic acids Proteins 0.000 description 7
- 150000007523 nucleic acids Chemical class 0.000 description 7
- 239000000523 sample Substances 0.000 description 7
- 241000894007 species Species 0.000 description 7
- 238000007920 subcutaneous administration Methods 0.000 description 7
- 238000012360 testing method Methods 0.000 description 7
- 102100028516 Receptor-type tyrosine-protein phosphatase U Human genes 0.000 description 6
- 208000007536 Thrombosis Diseases 0.000 description 6
- 230000015572 biosynthetic process Effects 0.000 description 6
- 238000011156 evaluation Methods 0.000 description 6
- 230000006251 gamma-carboxylation Effects 0.000 description 6
- 208000009429 hemophilia B Diseases 0.000 description 6
- 230000006872 improvement Effects 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 230000003285 pharmacodynamic effect Effects 0.000 description 6
- 229920001469 poly(aryloxy)thionylphosphazene Polymers 0.000 description 6
- 241000282472 Canis lupus familiaris Species 0.000 description 5
- 241000282693 Cercopithecidae Species 0.000 description 5
- 108091028043 Nucleic acid sequence Proteins 0.000 description 5
- 230000004071 biological effect Effects 0.000 description 5
- 230000001419 dependent effect Effects 0.000 description 5
- 230000008034 disappearance Effects 0.000 description 5
- 230000005847 immunogenicity Effects 0.000 description 5
- 150000003839 salts Chemical class 0.000 description 5
- 108060003951 Immunoglobulin Proteins 0.000 description 4
- 241000282567 Macaca fascicularis Species 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 108010000499 Thromboplastin Proteins 0.000 description 4
- 102000002262 Thromboplastin Human genes 0.000 description 4
- 238000007792 addition Methods 0.000 description 4
- 238000001042 affinity chromatography Methods 0.000 description 4
- 230000008901 benefit Effects 0.000 description 4
- 230000015271 coagulation Effects 0.000 description 4
- 238000005345 coagulation Methods 0.000 description 4
- 238000004590 computer program Methods 0.000 description 4
- 238000010828 elution Methods 0.000 description 4
- 108020001507 fusion proteins Proteins 0.000 description 4
- 102000037865 fusion proteins Human genes 0.000 description 4
- 238000002873 global sequence alignment Methods 0.000 description 4
- 102000018358 immunoglobulin Human genes 0.000 description 4
- 238000005342 ion exchange Methods 0.000 description 4
- 238000007726 management method Methods 0.000 description 4
- 239000000203 mixture Substances 0.000 description 4
- 230000036961 partial effect Effects 0.000 description 4
- 238000002203 pretreatment Methods 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 238000000746 purification Methods 0.000 description 4
- 102000005962 receptors Human genes 0.000 description 4
- 108020003175 receptors Proteins 0.000 description 4
- 230000009467 reduction Effects 0.000 description 4
- 230000004044 response Effects 0.000 description 4
- 238000012216 screening Methods 0.000 description 4
- 238000002864 sequence alignment Methods 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 230000003442 weekly effect Effects 0.000 description 4
- PGOHTUIFYSHAQG-LJSDBVFPSA-N (2S)-6-amino-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-4-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-1-[(2S,3R)-2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-4-methylsulfanylbutanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-5-carbamimidamidopentanoyl]amino]propanoyl]pyrrolidine-2-carbonyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]-4-methylpentanoyl]amino]acetyl]amino]-3-hydroxypropanoyl]amino]-4-methylpentanoyl]amino]-3-sulfanylpropanoyl]amino]-4-methylsulfanylbutanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-hydroxybutanoyl]pyrrolidine-2-carbonyl]amino]-5-oxopentanoyl]amino]-3-hydroxypropanoyl]amino]-3-hydroxypropanoyl]amino]-3-(1H-imidazol-5-yl)propanoyl]amino]-4-methylpentanoyl]amino]-3-hydroxybutanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-5-carbamimidamidopentanoyl]amino]-5-oxopentanoyl]amino]-3-hydroxybutanoyl]amino]-3-hydroxypropanoyl]amino]-3-carboxypropanoyl]amino]-3-hydroxypropanoyl]amino]-5-oxopentanoyl]amino]-5-oxopentanoyl]amino]-3-phenylpropanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-methylbutanoyl]amino]-4-methylpentanoyl]amino]-4-oxobutanoyl]amino]-5-carbamimidamidopentanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-carboxybutanoyl]amino]-5-oxopentanoyl]amino]hexanoic acid Chemical compound CSCC[C@H](N)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](Cc1cnc[nH]1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(O)=O PGOHTUIFYSHAQG-LJSDBVFPSA-N 0.000 description 3
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 3
- 108020004705 Codon Proteins 0.000 description 3
- 206010016077 Factor IX deficiency Diseases 0.000 description 3
- 241000282326 Felis catus Species 0.000 description 3
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 3
- 238000000342 Monte Carlo simulation Methods 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- 230000004988 N-glycosylation Effects 0.000 description 3
- 108700026244 Open Reading Frames Proteins 0.000 description 3
- 102000001708 Protein Isoforms Human genes 0.000 description 3
- 108010029485 Protein Isoforms Proteins 0.000 description 3
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 3
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 3
- 239000003114 blood coagulation factor Substances 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 230000000295 complement effect Effects 0.000 description 3
- 239000012141 concentrate Substances 0.000 description 3
- 238000012937 correction Methods 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 230000018109 developmental process Effects 0.000 description 3
- HRLIOXLXPOHXTA-NSHDSACASA-N dexmedetomidine Chemical compound C1([C@@H](C)C=2C(=C(C)C=CC=2)C)=CN=C[N]1 HRLIOXLXPOHXTA-NSHDSACASA-N 0.000 description 3
- 229960004253 dexmedetomidine Drugs 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 230000006870 function Effects 0.000 description 3
- 235000013922 glutamic acid Nutrition 0.000 description 3
- 239000004220 glutamic acid Substances 0.000 description 3
- 230000013595 glycosylation Effects 0.000 description 3
- 238000006206 glycosylation reaction Methods 0.000 description 3
- 238000005805 hydroxylation reaction Methods 0.000 description 3
- 239000003112 inhibitor Substances 0.000 description 3
- 239000000178 monomer Substances 0.000 description 3
- 108010068617 neonatal Fc receptor Proteins 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 238000006467 substitution reaction Methods 0.000 description 3
- 230000002459 sustained effect Effects 0.000 description 3
- 230000001225 therapeutic effect Effects 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 2
- 102000015081 Blood Coagulation Factors Human genes 0.000 description 2
- 108010039209 Blood Coagulation Factors Proteins 0.000 description 2
- 102000013831 Coagulation factor IX Human genes 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 241000283086 Equidae Species 0.000 description 2
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 2
- 101000823435 Homo sapiens Coagulation factor IX Proteins 0.000 description 2
- 108010091135 Immunoglobulin Fc Fragments Proteins 0.000 description 2
- 102000018071 Immunoglobulin Fc Fragments Human genes 0.000 description 2
- 241000581650 Ivesia Species 0.000 description 2
- YQEZLKZALYSWHR-UHFFFAOYSA-N Ketamine Chemical compound C=1C=CC=C(Cl)C=1C1(NC)CCCCC1=O YQEZLKZALYSWHR-UHFFFAOYSA-N 0.000 description 2
- 101001018085 Lysobacter enzymogenes Lysyl endopeptidase Proteins 0.000 description 2
- 241000124008 Mammalia Species 0.000 description 2
- 108010056902 Mononine Proteins 0.000 description 2
- 230000004989 O-glycosylation Effects 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 241000288906 Primates Species 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 108010094028 Prothrombin Proteins 0.000 description 2
- 206010038980 Retroperitoneal haemorrhage Diseases 0.000 description 2
- 241000282887 Suidae Species 0.000 description 2
- DRTQHJPVMGBUCF-XVFCMESISA-N Uridine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C(=O)NC(=O)C=C1 DRTQHJPVMGBUCF-XVFCMESISA-N 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 238000006664 bond formation reaction Methods 0.000 description 2
- 229940105774 coagulation factor ix Drugs 0.000 description 2
- 238000003066 decision tree Methods 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 229940088598 enzyme Drugs 0.000 description 2
- 238000013213 extrapolation Methods 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 230000023597 hemostasis Effects 0.000 description 2
- 229960002897 heparin Drugs 0.000 description 2
- 229920000669 heparin Polymers 0.000 description 2
- 229940052349 human coagulation factor ix Drugs 0.000 description 2
- 230000033444 hydroxylation Effects 0.000 description 2
- 230000000977 initiatory effect Effects 0.000 description 2
- 229960003299 ketamine Drugs 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 244000144972 livestock Species 0.000 description 2
- 238000012423 maintenance Methods 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 238000005259 measurement Methods 0.000 description 2
- 238000012544 monitoring process Methods 0.000 description 2
- 229940090053 mononine Drugs 0.000 description 2
- 210000003800 pharynx Anatomy 0.000 description 2
- 230000004481 post-translational protein modification Effects 0.000 description 2
- 230000003449 preventive effect Effects 0.000 description 2
- 230000002947 procoagulating effect Effects 0.000 description 2
- 230000002035 prolonged effect Effects 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000009450 sialylation Effects 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 238000007619 statistical method Methods 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 230000009885 systemic effect Effects 0.000 description 2
- 238000002560 therapeutic procedure Methods 0.000 description 2
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 2
- 238000002054 transplantation Methods 0.000 description 2
- 238000005303 weighing Methods 0.000 description 2
- AWFYPPSBLUWMFQ-UHFFFAOYSA-N 2-[5-[2-(2,3-dihydro-1H-inden-2-ylamino)pyrimidin-5-yl]-1,3,4-oxadiazol-2-yl]-1-(1,4,6,7-tetrahydropyrazolo[4,3-c]pyridin-5-yl)ethanone Chemical compound C1C(CC2=CC=CC=C12)NC1=NC=C(C=N1)C1=NN=C(O1)CC(=O)N1CC2=C(CC1)NN=C2 AWFYPPSBLUWMFQ-UHFFFAOYSA-N 0.000 description 1
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 description 1
- ODHCTXKNWHHXJC-VKHMYHEASA-N 5-oxo-L-proline Chemical compound OC(=O)[C@@H]1CCC(=O)N1 ODHCTXKNWHHXJC-VKHMYHEASA-N 0.000 description 1
- 230000005730 ADP ribosylation Effects 0.000 description 1
- 208000012260 Accidental injury Diseases 0.000 description 1
- 206010002198 Anaphylactic reaction Diseases 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 208000010392 Bone Fractures Diseases 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 241000282465 Canis Species 0.000 description 1
- 102100023804 Coagulation factor VII Human genes 0.000 description 1
- 102100026735 Coagulation factor VIII Human genes 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 229940117942 Factor IX inhibitor Drugs 0.000 description 1
- 108010014172 Factor V 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
- 108010014173 Factor X Proteins 0.000 description 1
- 108010074864 Factor XI Proteins 0.000 description 1
- 108010080865 Factor XII Proteins 0.000 description 1
- 102000000429 Factor XII Human genes 0.000 description 1
- 108010071289 Factor XIII Proteins 0.000 description 1
- 108010049003 Fibrinogen Proteins 0.000 description 1
- 102000008946 Fibrinogen Human genes 0.000 description 1
- 102100028071 Fibroblast growth factor 7 Human genes 0.000 description 1
- 206010017076 Fracture Diseases 0.000 description 1
- 229920001503 Glucan Polymers 0.000 description 1
- 208000024659 Hemostatic disease Diseases 0.000 description 1
- 108010000487 High-Molecular-Weight Kininogen Proteins 0.000 description 1
- 101000911390 Homo sapiens Coagulation factor VIII Proteins 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 108010073807 IgG Receptors Proteins 0.000 description 1
- 102000009490 IgG Receptors Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 206010022095 Injection Site reaction Diseases 0.000 description 1
- 102000008070 Interferon-gamma Human genes 0.000 description 1
- 108010074328 Interferon-gamma Proteins 0.000 description 1
- 108010068093 K1K2 peptide Proteins 0.000 description 1
- 108060005987 Kallikrein Proteins 0.000 description 1
- 102000001399 Kallikrein Human genes 0.000 description 1
- 102100035792 Kininogen-1 Human genes 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
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- 206010027476 Metastases Diseases 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 125000000729 N-terminal amino-acid group Chemical group 0.000 description 1
- 108091092724 Noncoding DNA Proteins 0.000 description 1
- 108020004485 Nonsense Codon Proteins 0.000 description 1
- 206010033372 Pain and discomfort Diseases 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 102100027378 Prothrombin Human genes 0.000 description 1
- 101000913100 Rattus norvegicus IgG receptor FcRn large subunit p51 Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 206010038460 Renal haemorrhage Diseases 0.000 description 1
- 206010062237 Renal impairment Diseases 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- AUNGANRZJHBGPY-SCRDCRAPSA-N Riboflavin Chemical compound OC[C@@H](O)[C@@H](O)[C@@H](O)CN1C=2C=C(C)C(C)=CC=2N=C2C1=NC(=O)NC2=O AUNGANRZJHBGPY-SCRDCRAPSA-N 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- 102000012479 Serine Proteases Human genes 0.000 description 1
- 210000001744 T-lymphocyte Anatomy 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 108020004566 Transfer RNA Proteins 0.000 description 1
- 108060008539 Transglutaminase Proteins 0.000 description 1
- 206010065441 Venous haemorrhage Diseases 0.000 description 1
- 229930003448 Vitamin K Natural products 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 230000010933 acylation Effects 0.000 description 1
- 238000005917 acylation reaction Methods 0.000 description 1
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 1
- XAGFODPZIPBFFR-UHFFFAOYSA-N aluminium Chemical compound [Al] XAGFODPZIPBFFR-UHFFFAOYSA-N 0.000 description 1
- 229910052782 aluminium Inorganic materials 0.000 description 1
- 230000009435 amidation Effects 0.000 description 1
- 238000007112 amidation reaction Methods 0.000 description 1
- 230000036783 anaphylactic response Effects 0.000 description 1
- 208000003455 anaphylaxis Diseases 0.000 description 1
- 230000003466 anti-cipated effect Effects 0.000 description 1
- 238000011225 antiretroviral therapy Methods 0.000 description 1
- HSWPZIDYAHLZDD-UHFFFAOYSA-N atipamezole Chemical compound C1C2=CC=CC=C2CC1(CC)C1=CN=CN1 HSWPZIDYAHLZDD-UHFFFAOYSA-N 0.000 description 1
- 229960003002 atipamezole Drugs 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- DRTQHJPVMGBUCF-PSQAKQOGSA-N beta-L-uridine Natural products O[C@H]1[C@@H](O)[C@H](CO)O[C@@H]1N1C(=O)NC(=O)C=C1 DRTQHJPVMGBUCF-PSQAKQOGSA-N 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 208000015294 blood coagulation disease Diseases 0.000 description 1
- 230000036772 blood pressure Effects 0.000 description 1
- 238000010241 blood sampling Methods 0.000 description 1
- 210000004204 blood vessel Anatomy 0.000 description 1
- 230000036760 body temperature Effects 0.000 description 1
- -1 bromobutyl Chemical group 0.000 description 1
- 229920005557 bromobutyl Polymers 0.000 description 1
- 229940087828 buprenex Drugs 0.000 description 1
- UAIXRPCCYXNJMQ-RZIPZOSSSA-N buprenorphine hydrochlorie Chemical compound [Cl-].C([C@]12[C@H]3OC=4C(O)=CC=C(C2=4)C[C@@H]2[C@]11CC[C@]3([C@H](C1)[C@](C)(O)C(C)(C)C)OC)C[NH+]2CC1CC1 UAIXRPCCYXNJMQ-RZIPZOSSSA-N 0.000 description 1
- 210000001217 buttock Anatomy 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 238000004422 calculation algorithm Methods 0.000 description 1
- 238000011088 calibration curve Methods 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 238000012754 cardiac puncture Methods 0.000 description 1
- 230000032823 cell division Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 230000009852 coagulant defect Effects 0.000 description 1
- AGVAZMGAQJOSFJ-WZHZPDAFSA-M cobalt(2+);[(2r,3s,4r,5s)-5-(5,6-dimethylbenzimidazol-1-yl)-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl] [(2r)-1-[3-[(1r,2r,3r,4z,7s,9z,12s,13s,14z,17s,18s,19r)-2,13,18-tris(2-amino-2-oxoethyl)-7,12,17-tris(3-amino-3-oxopropyl)-3,5,8,8,13,15,18,19-octamethyl-2 Chemical compound [Co+2].N#[C-].[N-]([C@@H]1[C@H](CC(N)=O)[C@@]2(C)CCC(=O)NC[C@@H](C)OP(O)(=O)O[C@H]3[C@H]([C@H](O[C@@H]3CO)N3C4=CC(C)=C(C)C=C4N=C3)O)\C2=C(C)/C([C@H](C\2(C)C)CCC(N)=O)=N/C/2=C\C([C@H]([C@@]/2(CC(N)=O)C)CCC(N)=O)=N\C\2=C(C)/C2=N[C@]1(C)[C@@](C)(CC(N)=O)[C@@H]2CCC(N)=O AGVAZMGAQJOSFJ-WZHZPDAFSA-M 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 239000003246 corticosteroid Substances 0.000 description 1
- 229960001334 corticosteroids Drugs 0.000 description 1
- 238000004132 cross linking Methods 0.000 description 1
- 238000011461 current therapy Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 238000002716 delivery method Methods 0.000 description 1
- 230000017858 demethylation Effects 0.000 description 1
- 238000010520 demethylation reaction Methods 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 230000000916 dilatatory effect Effects 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 229920001971 elastomer Polymers 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 210000003722 extracellular fluid Anatomy 0.000 description 1
- 108700007283 factor IX Fc fusion Proteins 0.000 description 1
- 229940012413 factor vii Drugs 0.000 description 1
- 229960000301 factor viii Drugs 0.000 description 1
- 229940012444 factor xiii Drugs 0.000 description 1
- 229940012952 fibrinogen Drugs 0.000 description 1
- 230000037406 food intake Effects 0.000 description 1
- 238000005755 formation reaction Methods 0.000 description 1
- 239000012537 formulation buffer Substances 0.000 description 1
- 230000022244 formylation Effects 0.000 description 1
- 238000006170 formylation reaction Methods 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 150000003278 haem Chemical group 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 208000031169 hemorrhagic disease Diseases 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000001900 immune effect Effects 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 239000012678 infectious agent Substances 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 229960003130 interferon gamma Drugs 0.000 description 1
- 210000002977 intracellular fluid Anatomy 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 230000026045 iodination Effects 0.000 description 1
- 238000006192 iodination reaction Methods 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 210000003292 kidney cell Anatomy 0.000 description 1
- 230000005977 kidney dysfunction Effects 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 208000019423 liver disease Diseases 0.000 description 1
- 230000005976 liver dysfunction Effects 0.000 description 1
- 238000001325 log-rank test Methods 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 210000001161 mammalian embryo Anatomy 0.000 description 1
- 238000004949 mass spectrometry Methods 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 230000009401 metastasis Effects 0.000 description 1
- 230000011987 methylation Effects 0.000 description 1
- 238000007069 methylation reaction Methods 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 230000000869 mutational effect Effects 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 230000037434 nonsense mutation Effects 0.000 description 1
- 238000001543 one-way ANOVA Methods 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 230000003647 oxidation Effects 0.000 description 1
- 238000007254 oxidation reaction Methods 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000006320 pegylation Effects 0.000 description 1
- 150000003905 phosphatidylinositols Chemical class 0.000 description 1
- 150000003904 phospholipids Chemical class 0.000 description 1
- SHUZOJHMOBOZST-UHFFFAOYSA-N phylloquinone Natural products CC(C)CCCCC(C)CCC(C)CCCC(=CCC1=C(C)C(=O)c2ccccc2C1=O)C SHUZOJHMOBOZST-UHFFFAOYSA-N 0.000 description 1
- 230000037081 physical activity Effects 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 229940068977 polysorbate 20 Drugs 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000013823 prenylation Effects 0.000 description 1
- 238000002331 protein detection Methods 0.000 description 1
- 230000004853 protein function Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 230000004850 protein–protein interaction Effects 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 229940039716 prothrombin Drugs 0.000 description 1
- 230000005180 public health Effects 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 229940043131 pyroglutamate Drugs 0.000 description 1
- 230000006340 racemization Effects 0.000 description 1
- 238000002708 random mutagenesis Methods 0.000 description 1
- 238000009256 replacement therapy Methods 0.000 description 1
- 230000036387 respiratory rate Effects 0.000 description 1
- 238000007363 ring formation reaction Methods 0.000 description 1
- 231100000279 safety data Toxicity 0.000 description 1
- 238000003118 sandwich ELISA Methods 0.000 description 1
- 238000007789 sealing Methods 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 238000011410 subtraction method Methods 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 229940113082 thymine Drugs 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 102000003601 transglutaminase Human genes 0.000 description 1
- 102000035160 transmembrane proteins Human genes 0.000 description 1
- 108091005703 transmembrane proteins Proteins 0.000 description 1
- 230000006107 tyrosine sulfation Effects 0.000 description 1
- 230000034512 ubiquitination Effects 0.000 description 1
- 238000010798 ubiquitination Methods 0.000 description 1
- 238000011870 unpaired t-test Methods 0.000 description 1
- DRTQHJPVMGBUCF-UHFFFAOYSA-N uracil arabinoside Natural products OC1C(O)C(CO)OC1N1C(=O)NC(=O)C=C1 DRTQHJPVMGBUCF-UHFFFAOYSA-N 0.000 description 1
- 229940045145 uridine Drugs 0.000 description 1
- 235000019168 vitamin K Nutrition 0.000 description 1
- 239000011712 vitamin K Substances 0.000 description 1
- 150000003721 vitamin K derivatives Chemical class 0.000 description 1
- 229940046010 vitamin k Drugs 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000002424 x-ray crystallography Methods 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/43—Enzymes; Proenzymes; Derivatives thereof
- A61K38/46—Hydrolases (3)
- A61K38/48—Hydrolases (3) acting on peptide bonds (3.4)
- A61K38/482—Serine endopeptidases (3.4.21)
- A61K38/4846—Factor VII (3.4.21.21); Factor IX (3.4.21.22); Factor Xa (3.4.21.6); Factor XI (3.4.21.27); Factor XII (3.4.21.38)
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/36—Blood coagulation or fibrinolysis factors
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/38—Albumins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
- A61K39/3955—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals against proteinaceous materials, e.g. enzymes, hormones, lymphokines
-
- 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
- A61K47/62—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 a protein, peptide or polyamino acid
- A61K47/64—Drug-peptide, drug-protein or drug-polyamino acid conjugates, i.e. the modifying agent being a peptide, protein or polyamino acid which is covalently bonded or complexed to a therapeutically active agent
- A61K47/643—Albumins, e.g. HSA, BSA, ovalbumin or a Keyhole Limpet Hemocyanin [KHL]
-
- 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
- A61K9/00—Medicinal preparations characterised by special physical form
- A61K9/0012—Galenical forms characterised by the site of application
- A61K9/0019—Injectable compositions; Intramuscular, intravenous, arterial, subcutaneous administration; Compositions to be administered through the skin in an invasive manner
-
- 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
- A61P7/04—Antihaemorrhagics; Procoagulants; Haemostatic agents; Antifibrinolytic agents
-
- 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
- C07K14/76—Albumins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/644—Coagulation factor IXa (3.4.21.22)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21022—Coagulation factor IXa (3.4.21.22)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/90—Immunoglobulins specific features characterized by (pharmaco)kinetic aspects or by stability of the immunoglobulin
- C07K2317/94—Stability, e.g. half-life, pH, temperature or enzyme-resistance
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/31—Fusion polypeptide fusions, other than Fc, for prolonged plasma life, e.g. albumin
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/33—Fusion polypeptide fusions for targeting to specific cell types, e.g. tissue specific targeting, targeting of a bacterial subspecies
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Epidemiology (AREA)
- Zoology (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Microbiology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Hematology (AREA)
- Mycology (AREA)
- Biotechnology (AREA)
- Diabetes (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Biophysics (AREA)
- Endocrinology (AREA)
- Dermatology (AREA)
- Toxicology (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
Applications Claiming Priority (13)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US36306410P | 2010-07-09 | 2010-07-09 | |
| US61/363,064 | 2010-07-09 | ||
| US201061424555P | 2010-12-17 | 2010-12-17 | |
| US61/424,555 | 2010-12-17 | ||
| US201161430819P | 2011-01-07 | 2011-01-07 | |
| US61/430,819 | 2011-01-07 | ||
| US201161438572P | 2011-02-01 | 2011-02-01 | |
| US61/438,572 | 2011-02-01 | ||
| US201161442079P | 2011-02-11 | 2011-02-11 | |
| US61/442,079 | 2011-02-11 | ||
| US201161470951P | 2011-04-01 | 2011-04-01 | |
| US61/470,951 | 2011-04-01 | ||
| PCT/US2011/043569 WO2012006624A2 (en) | 2010-07-09 | 2011-07-11 | Factor ix polypeptides and methods of use thereof |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2015224436A Division JP2016034973A (ja) | 2010-07-09 | 2015-11-17 | 第ix因子ポリペプチドおよびその使用方法 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| JP2013534426A true JP2013534426A (ja) | 2013-09-05 |
| JP2013534426A5 JP2013534426A5 (enExample) | 2014-08-28 |
Family
ID=45441870
Family Applications (5)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2013518876A Pending JP2013534426A (ja) | 2010-07-09 | 2011-07-11 | 第ix因子ポリペプチドおよびその使用方法 |
| JP2015224436A Pending JP2016034973A (ja) | 2010-07-09 | 2015-11-17 | 第ix因子ポリペプチドおよびその使用方法 |
| JP2016218597A Withdrawn JP2017036328A (ja) | 2010-07-09 | 2016-11-09 | 第ix因子ポリペプチドおよびその使用方法 |
| JP2018218122A Withdrawn JP2019023242A (ja) | 2010-07-09 | 2018-11-21 | 第ix因子ポリペプチドおよびその使用方法 |
| JP2022012817A Pending JP2022044828A (ja) | 2010-07-09 | 2022-01-31 | 第ix因子ポリペプチドおよびその使用方法 |
Family Applications After (4)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2015224436A Pending JP2016034973A (ja) | 2010-07-09 | 2015-11-17 | 第ix因子ポリペプチドおよびその使用方法 |
| JP2016218597A Withdrawn JP2017036328A (ja) | 2010-07-09 | 2016-11-09 | 第ix因子ポリペプチドおよびその使用方法 |
| JP2018218122A Withdrawn JP2019023242A (ja) | 2010-07-09 | 2018-11-21 | 第ix因子ポリペプチドおよびその使用方法 |
| JP2022012817A Pending JP2022044828A (ja) | 2010-07-09 | 2022-01-31 | 第ix因子ポリペプチドおよびその使用方法 |
Country Status (23)
| Country | Link |
|---|---|
| US (13) | US9670475B2 (enExample) |
| EP (3) | EP2590668A4 (enExample) |
| JP (5) | JP2013534426A (enExample) |
| KR (5) | KR20230156435A (enExample) |
| CN (1) | CN103140237A (enExample) |
| AU (5) | AU2011274414B2 (enExample) |
| BR (1) | BR112013000650A8 (enExample) |
| CA (1) | CA2804274A1 (enExample) |
| CL (1) | CL2013000058A1 (enExample) |
| DK (1) | DK3552619T3 (enExample) |
| EA (2) | EA028067B1 (enExample) |
| FI (1) | FI3552619T3 (enExample) |
| IL (3) | IL223990B (enExample) |
| LT (1) | LT3552619T (enExample) |
| MX (3) | MX375112B (enExample) |
| MY (2) | MY166954A (enExample) |
| NZ (1) | NZ605348A (enExample) |
| PL (1) | PL3552619T3 (enExample) |
| PT (1) | PT3552619T (enExample) |
| RS (1) | RS67366B1 (enExample) |
| SG (3) | SG186856A1 (enExample) |
| UA (2) | UA126265C2 (enExample) |
| WO (1) | WO2012006624A2 (enExample) |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| KR20160137577A (ko) * | 2014-03-24 | 2016-11-30 | 바이오젠 엠에이 인코포레이티드 | 동결건조된 ix 인자 제형 |
| JP2017502036A (ja) * | 2013-12-23 | 2017-01-19 | シーエスエル、リミテッド | 血友病の予防的処置のための第ix因子を含む融合タンパク質およびその方法 |
| JP2018522563A (ja) * | 2015-08-03 | 2018-08-16 | バイオベラティブ セラピューティクス インコーポレイテッド | 第ix因子融合タンパク質及びそれらの製造方法及び使用方法 |
| US11642398B2 (en) | 2013-03-15 | 2023-05-09 | Bioverativ Therapeutics Inc. | Factor IX polypeptide formulations |
Families Citing this family (76)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| TWI353991B (en) | 2003-05-06 | 2011-12-11 | Syntonix Pharmaceuticals Inc | Immunoglobulin chimeric monomer-dimer hybrids |
| US7855279B2 (en) | 2005-09-27 | 2010-12-21 | Amunix Operating, Inc. | Unstructured recombinant polymers and uses thereof |
| WO2010091122A1 (en) | 2009-02-03 | 2010-08-12 | Amunix, Inc. | Extended recombinant polypeptides and compositions comprising same |
| BR112012004094A2 (pt) | 2009-08-24 | 2016-03-08 | Amunix Operating Inc | composições de fator vii de coagulação e métodos para fazer e usar as mesmas |
| WO2012006635A1 (en) | 2010-07-09 | 2012-01-12 | Biogen Idec Hemophilia Inc. | Processable single chain molecules and polypeptides made using same |
| CN103140237A (zh) | 2010-07-09 | 2013-06-05 | 比奥根艾迪克依蒙菲利亚公司 | 因子ix多肽及其使用方法 |
| CA2807552A1 (en) | 2010-08-06 | 2012-02-09 | Moderna Therapeutics, Inc. | Engineered nucleic acids and methods of use thereof |
| EP3431485B2 (en) | 2010-10-01 | 2024-09-04 | ModernaTX, Inc. | Engineered nucleic acids and methods of use thereof |
| WO2012135805A2 (en) | 2011-03-31 | 2012-10-04 | modeRNA Therapeutics | Delivery and formulation of engineered nucleic acids |
| US10656167B2 (en) | 2011-07-25 | 2020-05-19 | Bioverativ Therapeutics Inc. | Assays to monitor bleeding disorders |
| US9464124B2 (en) | 2011-09-12 | 2016-10-11 | Moderna Therapeutics, Inc. | Engineered nucleic acids and methods of use thereof |
| EP2763701B1 (en) | 2011-10-03 | 2018-12-19 | Moderna Therapeutics, Inc. | Modified nucleosides, nucleotides, and nucleic acids, and uses thereof |
| KR20140102759A (ko) | 2011-12-16 | 2014-08-22 | 모더나 세라퓨틱스, 인코포레이티드 | 변형된 뉴클레오사이드, 뉴클레오타이드 및 핵산 조성물 |
| PL3453402T3 (pl) | 2012-01-12 | 2022-03-21 | Bioverativ Therapeutics Inc. | Zmniejszenie immunogenności przeciwko czynnikowi viii u osób poddawanych terapii czynnikiem viii |
| LT2822577T (lt) | 2012-02-15 | 2019-03-25 | Bioverativ Therapeutics Inc. | Rekombinantiniai faktoriaus viii baltymai |
| HRP20221531T1 (hr) | 2012-02-15 | 2023-02-17 | Bioverativ Therapeutics Inc. | Pripravci faktora viii i postupci dobivanja i korištenja istih |
| US9878056B2 (en) | 2012-04-02 | 2018-01-30 | Modernatx, Inc. | Modified polynucleotides for the production of cosmetic proteins and peptides |
| US9572897B2 (en) | 2012-04-02 | 2017-02-21 | Modernatx, Inc. | Modified polynucleotides for the production of cytoplasmic and cytoskeletal proteins |
| US9283287B2 (en) | 2012-04-02 | 2016-03-15 | Moderna Therapeutics, Inc. | Modified polynucleotides for the production of nuclear proteins |
| DE18200782T1 (de) | 2012-04-02 | 2021-10-21 | Modernatx, Inc. | Modifizierte polynukleotide zur herstellung von proteinen im zusammenhang mit erkrankungen beim menschen |
| EP2836518B1 (en) | 2012-04-11 | 2019-01-02 | Bioverativ Therapeutics Inc. | Methods of detecting glycosaminoglycans |
| CA2875246A1 (en) | 2012-06-08 | 2013-12-12 | Biogen Idec Ma Inc. | Procoagulant compounds |
| AU2013270683A1 (en) | 2012-06-08 | 2014-12-11 | Biogen Ma Inc. | Chimeric clotting factors |
| EP3970738A1 (en) | 2012-07-25 | 2022-03-23 | Bioverativ Therapeutics Inc. | Blood factor monitoring assay and uses thereof |
| TW201427685A (zh) * | 2012-09-25 | 2014-07-16 | Biogen Idec Inc | Fix多肽的應用 |
| CA2888806A1 (en) * | 2012-10-18 | 2014-04-24 | Biogen Idec Ma Inc. | Methods of using a fixed dose of a clotting factor |
| AU2013348029A1 (en) * | 2012-11-20 | 2015-07-02 | The University Of North Carolina At Chapel Hill | Methods and compositions for modified factor IX proteins |
| CA2892529C (en) | 2012-11-26 | 2023-04-25 | Moderna Therapeutics, Inc. | Terminally modified rna |
| US10717965B2 (en) | 2013-01-10 | 2020-07-21 | Gloriana Therapeutics, Inc. | Mammalian cell culture-produced neublastin antibodies |
| LT2956477T (lt) | 2013-02-15 | 2021-02-10 | Bioverativ Therapeutics Inc. | Optimizuotas faktoriaus viii genas |
| US8980864B2 (en) | 2013-03-15 | 2015-03-17 | Moderna Therapeutics, Inc. | Compositions and methods of altering cholesterol levels |
| EP3033097B1 (en) | 2013-08-14 | 2021-03-10 | Bioverativ Therapeutics Inc. | Factor viii-xten fusions and uses thereof |
| HUE057005T2 (hu) | 2013-09-25 | 2022-04-28 | Bioverativ Therapeutics Inc | Oszlopon történõ vírusinaktiváló eljárások |
| EA201690675A1 (ru) | 2013-10-03 | 2016-08-31 | Модерна Терапьютикс, Инк. | Полинуклеотиды, кодирующие рецептор липопротеинов низкой плотности |
| EP3082848B1 (en) | 2013-12-06 | 2023-10-18 | Bioverativ Therapeutics Inc. | Population pharmacokinetics tools and uses thereof |
| US20160289633A1 (en) | 2013-12-20 | 2016-10-06 | Biogen Ma Inc. | Use of Perfusion Seed Cultures to Improve Biopharmaceutical Fed-Batch Production Capacity and Product Quality |
| KR102382402B1 (ko) | 2014-02-04 | 2022-04-01 | 바이오젠 엠에이 인코포레이티드 | 번역 후 변형을 강화시키기 위한 통류 방식 양이온 교환 크로마토그래피의 용도 |
| EP3160478A4 (en) | 2014-06-30 | 2018-05-16 | Bioverativ Therapeutics Inc. | Optimized factor ix gene |
| MA40864A (fr) | 2014-10-31 | 2017-09-05 | Biogen Ma Inc | Hypotaurine, gaba, bêta-alanine et choline pour la régulation de l'accumulation de sous-produits résiduaires dans des procédés de culture de cellules mammifères |
| PL3411478T3 (pl) | 2016-02-01 | 2022-10-03 | Bioverativ Therapeutics Inc. | Geny zoptymalizowanego czynnika VIII |
| SG11201808475XA (en) | 2016-04-15 | 2018-10-30 | Baxalta Inc | Method and apparatus for providing a pharmacokinetic drug dosing regiment |
| TW201739448A (zh) * | 2016-05-06 | 2017-11-16 | 安成生物科技股份有限公司 | 用於治療及/或預防血液相關疾病之方法及配方 |
| EP3481416B1 (en) | 2016-07-08 | 2020-09-09 | CSL Behring Lengnau AG | Subcutaneous administration of long-acting factor ix in humans |
| CN107759694B (zh) * | 2016-08-19 | 2023-01-13 | 安源医药科技(上海)有限公司 | 双特异性抗体及其制备方法与用途 |
| CN106279437B (zh) | 2016-08-19 | 2017-10-31 | 安源医药科技(上海)有限公司 | 高糖基化人凝血因子viii融合蛋白及其制备方法与用途 |
| EP3502143A4 (en) | 2016-08-19 | 2020-07-15 | Ampsource Biopharma Shanghai Inc. | BINDING PEPTIDE FOR THE CONSTRUCTION OF A FUSION PROTEIN |
| WO2018102743A1 (en) | 2016-12-02 | 2018-06-07 | Bioverativ Therapeutics Inc. | Methods of treating hemophilic arthropathy using chimeric clotting factors |
| BR112019011198A2 (pt) | 2016-12-02 | 2019-12-17 | Bioverativ Therapeutics Inc | métodos de indução de tolerância imune a fatores de coagulação |
| US10896749B2 (en) | 2017-01-27 | 2021-01-19 | Shire Human Genetic Therapies, Inc. | Drug monitoring tool |
| EA201991768A1 (ru) | 2017-01-31 | 2020-01-22 | Байоверетив Терапьютикс Инк. | Слитые белки на основе фактора ix и способы их получения и пути применения |
| US11045128B2 (en) | 2017-06-03 | 2021-06-29 | Sentinel Medical Technologies, LLC | Catheter for monitoring intra-abdominal pressure |
| US10813589B2 (en) | 2017-06-03 | 2020-10-27 | Sentinel Medical Technologies, LLC | Catheter for monitoring uterine contraction pressure |
| US11045143B2 (en) | 2017-06-03 | 2021-06-29 | Sentinel Medical Technologies, LLC | Catheter with connectable hub for monitoring pressure |
| US10799131B2 (en) | 2017-06-03 | 2020-10-13 | Sentinel Medical Technologies, LLC | Catheter for monitoring intrauterine pressure to protect the fallopian tubes |
| US11185245B2 (en) | 2017-06-03 | 2021-11-30 | Sentinel Medical Technologies, Llc. | Catheter for monitoring pressure for muscle compartment syndrome |
| CN110799209A (zh) * | 2017-06-29 | 2020-02-14 | 康诺贝林伦瑙有限公司 | 用于预防性治疗血友病的包含因子ix和人白蛋白的融合蛋白的21天给药方案及其方法 |
| JP7374883B2 (ja) | 2017-08-09 | 2023-11-07 | バイオベラティブ セラピューティクス インコーポレイテッド | 核酸分子およびその使用 |
| US20200263196A1 (en) | 2017-09-27 | 2020-08-20 | Sigilon Therapeutics, Inc. | Methods, compositions, and implantable elements comprising active cells |
| WO2019195056A1 (en) | 2018-04-04 | 2019-10-10 | Sigilon Therapeutics, Inc. | Methods, compositions, and implantable elements comprising stem cells |
| TW202014181A (zh) | 2018-04-04 | 2020-04-16 | 美商希吉隆醫療公司 | 可植入顆粒及相關方法 |
| RS66972B1 (sr) | 2018-05-18 | 2025-07-31 | Bioverativ Therapeutics Inc | Metode lečenja hemofilije a |
| CN119955796A (zh) | 2018-08-09 | 2025-05-09 | 比奥维拉迪维治疗股份有限公司 | 核酸分子及其用于非病毒基因疗法的用途 |
| UY38389A (es) | 2018-09-27 | 2020-04-30 | Sigilon Therapeutics Inc | Dispositivos implantables para terapia celular y métodos relacionados |
| US11672457B2 (en) | 2018-11-24 | 2023-06-13 | Sentinel Medical Technologies, Llc. | Catheter for monitoring pressure |
| US11779263B2 (en) | 2019-02-08 | 2023-10-10 | Sentinel Medical Technologies, Llc. | Catheter for monitoring intra-abdominal pressure for assessing preeclampsia |
| WO2020187969A1 (en) | 2019-03-19 | 2020-09-24 | CSL Behring Lengnau AG | Factor ix variants and uses thereof in therapy |
| EP3956456A1 (en) | 2019-04-17 | 2022-02-23 | Codiak BioSciences, Inc. | Compositions of exosomes and aav |
| CN112175088B (zh) * | 2019-07-02 | 2023-03-28 | 江苏晟斯生物制药有限公司 | 改进的fix融合蛋白、缀合物及其应用 |
| WO2021026020A1 (en) | 2019-08-08 | 2021-02-11 | Sentinel Medical Technologies, LLC | Cable for use with pressure monitoring catheters |
| CN115279896A (zh) | 2019-09-30 | 2022-11-01 | 比奥维拉迪维治疗股份有限公司 | 慢病毒载体配制品 |
| US11617543B2 (en) | 2019-12-30 | 2023-04-04 | Sentinel Medical Technologies, Llc. | Catheter for monitoring pressure |
| US11981718B2 (en) | 2020-05-27 | 2024-05-14 | Ampsource Biopharma Shanghai Inc. | Dual-function protein for lipid and blood glucose regulation |
| MX2023000156A (es) | 2020-06-24 | 2023-02-16 | Bioverativ Therapeutics Inc | Metodos para la eliminacion de factor viii libre de preparaciones de vectores lentivirales modificados para expresar dicha proteina. |
| EP4362971A1 (en) * | 2021-07-01 | 2024-05-08 | CSL Behring Lengnau AG | Factor ix subcutaneous administration with enhanced safety |
| EP4602155A1 (en) | 2022-10-11 | 2025-08-20 | Sigilon Therapeutics, Inc. | Engineered cells and implantable elements for treatment of disease |
| WO2024081310A1 (en) | 2022-10-11 | 2024-04-18 | Sigilon Therapeutics, Inc. | Engineered cells and implantable elements for treatment of disease |
Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2009130602A2 (en) * | 2008-04-24 | 2009-10-29 | Celtic Pharma Peg Ltd. | Factor ix conjugates with extended half-lives |
| WO2010020690A1 (en) * | 2008-08-21 | 2010-02-25 | Octapharma Ag | Recombinantly produced human factor viii and ix |
| JP2010063462A (ja) * | 1997-02-14 | 2010-03-25 | American Red Cross | トランスジェニック動物乳房組織における活性ヒト第ix因子の発現 |
Family Cites Families (91)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4786726A (en) * | 1986-01-06 | 1988-11-22 | Blood Systems, Inc. | Factor IX therapeutic blood product, means and methods of preparing same |
| AU600575B2 (en) | 1987-03-18 | 1990-08-16 | Sb2, Inc. | Altered antibodies |
| US4994371A (en) | 1987-08-28 | 1991-02-19 | Davie Earl W | DNA preparation of Christmas factor and use of DNA sequences |
| US5336603A (en) | 1987-10-02 | 1994-08-09 | Genentech, Inc. | CD4 adheson variants |
| KR900005995A (ko) | 1988-10-31 | 1990-05-07 | 우메모또 요시마사 | 변형 인터류킨-2 및 그의 제조방법 |
| US6406697B1 (en) | 1989-02-23 | 2002-06-18 | Genentech, Inc. | Hybrid immunoglobulins |
| EP0394827A1 (en) | 1989-04-26 | 1990-10-31 | F. Hoffmann-La Roche Ag | Chimaeric CD4-immunoglobulin polypeptides |
| ATE92107T1 (de) | 1989-04-29 | 1993-08-15 | Delta Biotechnology Ltd | N-terminale fragmente von menschliches serumalbumin enthaltenden fusionsproteinen. |
| US5766883A (en) | 1989-04-29 | 1998-06-16 | Delta Biotechnology Limited | Polypeptides |
| US5112946A (en) | 1989-07-06 | 1992-05-12 | Repligen Corporation | Modified pf4 compositions and methods of use |
| DE10399023I2 (de) | 1989-09-12 | 2006-11-23 | Ahp Mfg B V | TFN-bindende Proteine |
| WO1991006570A1 (en) | 1989-10-25 | 1991-05-16 | The University Of Melbourne | HYBRID Fc RECEPTOR MOLECULES |
| US5349053A (en) | 1990-06-01 | 1994-09-20 | Protein Design Labs, Inc. | Chimeric ligand/immunoglobulin molecules and their uses |
| AU643109B2 (en) | 1990-12-14 | 1993-11-04 | Cell Genesys, Inc. | Chimeric chains for receptor-associated signal transduction pathways |
| US5844095A (en) | 1991-06-27 | 1998-12-01 | Bristol-Myers Squibb Company | CTLA4 Ig fusion proteins |
| US5622929A (en) | 1992-01-23 | 1997-04-22 | Bristol-Myers Squibb Company | Thioether conjugates |
| FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| 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 |
| US6037452A (en) | 1992-04-10 | 2000-03-14 | Alpha Therapeutic Corporation | Poly(alkylene oxide)-Factor VIII or Factor IX conjugate |
| WO1993024135A1 (en) | 1992-05-26 | 1993-12-09 | Immunex Corporation | Novel cytokine that binds cd30 |
| US6277975B1 (en) | 1992-10-23 | 2001-08-21 | Genetics Institute, Inc. | Fusions of P-selectin ligand protein and polynucleotides encoding same |
| US5621039A (en) | 1993-06-08 | 1997-04-15 | Hallahan; Terrence W. | Factor IX- polymeric conjugates |
| WO1995021258A1 (en) | 1994-02-01 | 1995-08-10 | United States Of America, Represented By The Secretary, Department Of Health And Human Services | Fusion proteins that include antibody and nonantibody portions |
| AU3382595A (en) | 1994-07-29 | 1996-03-04 | Smithkline Beecham Corporation | Novel compounds |
| GB9415379D0 (en) | 1994-07-29 | 1994-09-21 | Smithkline Beecham Plc | Novel compounds |
| ATE238668T1 (de) | 1995-01-17 | 2003-05-15 | Brigham & Womens Hospital | Rezeptorspezifischer transepithelialer transport von immunogenen |
| US6030613A (en) | 1995-01-17 | 2000-02-29 | The Brigham And Women's Hospital, Inc. | Receptor specific transepithelial transport of therapeutics |
| 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 |
| WO1997034631A1 (en) | 1996-03-18 | 1997-09-25 | Board Of Regents, The University Of Texas System | Immunoglobin-like domains with increased half lives |
| BR9815975A (pt) | 1998-07-31 | 2001-12-04 | Wallace E Carroll | Método e aparelho para a determinação defatores de terapia anticoagulante |
| US20010031721A1 (en) | 1999-05-05 | 2001-10-18 | Chandra Webb | Highly concentrated, lyophilized, and liquid factor IX formulations |
| US20030096355A1 (en) * | 1999-07-09 | 2003-05-22 | Ke Zhang | Isolation, identification and characterization of ymkz5, a novel member of the TNF-receptor supergene family |
| ATE336514T1 (de) | 2000-02-11 | 2006-09-15 | Merck Patent Gmbh | Steigerung der zirkulierenden halbwertzeit von auf antikörpern basierenden fusionsproteinen |
| CA2405550A1 (en) | 2000-04-12 | 2001-10-25 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| DK1278763T3 (da) | 2000-04-28 | 2007-06-11 | Inflazyme Pharm Ltd | 3-Nitrogen-6,7-dioxygensteroider og anvendelser relateret dertil |
| AU2002226028A1 (en) | 2000-11-14 | 2002-05-27 | Board Of Regents, Unversity Of Texas Systems | Mutant human factor ix with an increased resistance to inhibition by heparin |
| US20030203845A1 (en) | 2001-02-05 | 2003-10-30 | Knudsen Jens Bjerre | Combined use of factor VII polypeptides and factor IX polypeptides |
| CN1547608A (zh) | 2001-09-04 | 2004-11-17 | Ĭ��ר������˾ | 经修饰的因子ix |
| ES2561985T3 (es) | 2001-10-10 | 2016-03-01 | Ratiopharm Gmbh | Remodelación y glicoconjugación de anticuerpos |
| AU2002364586A1 (en) | 2001-12-21 | 2003-07-30 | Delta Biotechnology Limited | Albumin fusion proteins |
| CA2484556A1 (en) | 2001-12-21 | 2003-07-24 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| KR101204712B1 (ko) * | 2003-03-18 | 2012-11-27 | 노보 노르디스크 헬스 케어 악티엔게젤샤프트 | Gla-잔기 함유 세린 프로테아제의 제조 방법 |
| JP2007524607A (ja) | 2003-04-09 | 2007-08-30 | ワイス | 凝固因子の吸入による血友病処置 |
| TWI353991B (en) | 2003-05-06 | 2011-12-11 | Syntonix Pharmaceuticals Inc | Immunoglobulin chimeric monomer-dimer hybrids |
| US7348004B2 (en) | 2003-05-06 | 2008-03-25 | Syntonix Pharmaceuticals, Inc. | Immunoglobulin chimeric monomer-dimer hybrids |
| DE602004031390D1 (de) | 2003-05-06 | 2011-03-24 | Syntonix Pharmaceuticals Inc | Gerinnungsfaktor VII-Fc chimäre Proteine zur Behandlung von hämostatischen Krankheiten |
| US7212798B1 (en) * | 2003-07-17 | 2007-05-01 | Cisco Technology, Inc. | Adaptive AGC in a wireless network receiver |
| EP1654004A2 (en) | 2003-08-08 | 2006-05-10 | Novo Nordisk A/S | Synthesis and application of new structural well defined branched polymers as conjugating agents for peptides |
| EP1673395A1 (en) * | 2003-10-15 | 2006-06-28 | PDL BioPharma, Inc. | Alteration of fc-fusion protein serum half-lives by mutagenesis of positions 250, 314 and/or 428 of the heavy chain constant region of ig |
| NZ546733A (en) | 2003-12-03 | 2009-07-31 | Novo Nordisk As | Glycopegylated factor IX |
| JP2008509688A (ja) | 2004-08-17 | 2008-04-03 | ツェー・エス・エル・ベーリング・ゲー・エム・ベー・ハー | 改変ビタミンk依存性ポリペプチド |
| US8367805B2 (en) | 2004-11-12 | 2013-02-05 | Xencor, Inc. | Fc variants with altered binding to FcRn |
| US20090100533A1 (en) | 2004-12-21 | 2009-04-16 | Novo Nordisk Health Care Ag | Expression of gamma-carboxylated polypeptides in gamma-carboxylation deficient host sytems |
| US20060162552A1 (en) | 2005-01-26 | 2006-07-27 | Mohawk Valley Energy Solutions, Inc. | Systems and methods for controlling room air quality |
| EP1891231A4 (en) | 2005-05-25 | 2011-06-22 | Novo Nordisk As | GLYCOPEGYLATED FACTOR IX |
| US7855279B2 (en) | 2005-09-27 | 2010-12-21 | Amunix Operating, Inc. | Unstructured recombinant polymers and uses thereof |
| ES2749574T3 (es) | 2005-11-01 | 2020-03-23 | Wyeth Llc | Solución de cloruro sódico para la reconstitución de fármacos |
| US8759292B2 (en) | 2006-02-03 | 2014-06-24 | Prolor Biotech, Llc | Long-acting coagulation factors and methods of producing same |
| EP1816201A1 (en) | 2006-02-06 | 2007-08-08 | CSL Behring GmbH | Modified coagulation factor VIIa with extended half-life |
| EP1996937A4 (en) | 2006-03-06 | 2009-04-08 | Amunix Inc | GENETIC PACKS AND USES THEREOF |
| HUE067285T2 (hu) | 2006-03-24 | 2024-10-28 | Bioverativ Therapeutics Inc | PC5 mint IX-es faktor propeptidet feldolgozó enzim |
| DE602007007923D1 (de) * | 2006-04-11 | 2010-09-02 | Csl Behring Gmbh | Verfahren zur erhöhung der in-vivo-gewinnung therapeutischer polypeptide |
| BRPI0712008A2 (pt) | 2006-05-24 | 2012-01-10 | Novo Nordisk Healthcare Ag | derivados e análogos de fix prolongados |
| EP2032607B2 (en) | 2006-06-14 | 2017-02-22 | CSL Behring GmbH | Proteolytically cleavable fusion protein comprising a blood coagulation factor |
| US7939632B2 (en) | 2006-06-14 | 2011-05-10 | Csl Behring Gmbh | Proteolytically cleavable fusion proteins with high molar specific activity |
| TW200804416A (en) | 2006-06-19 | 2008-01-16 | Nautilus Technology Llc | Modified coagulation factor IX polypeptides and use thereof for treatment |
| JP5122562B2 (ja) | 2006-07-17 | 2013-01-16 | ノボ ノルディスク ヘルス ケア アーゲー | 増加した活性を有する第viia因子アナログの新規用途 |
| WO2008022151A1 (en) | 2006-08-15 | 2008-02-21 | Inspiration Biopharmaceuticals, Inc. | Prophylactic treatment of hemophilia |
| AU2007293614A1 (en) * | 2006-09-08 | 2008-03-13 | Ablynx N.V. | Serum albumin binding proteins with long half-lives |
| US7700734B2 (en) | 2007-01-09 | 2010-04-20 | Shu-Wha Lin | Recombinant human factor IX and use thereof |
| WO2008119815A1 (en) | 2007-04-02 | 2008-10-09 | Novo Nordisk A/S | Subcutaneous administration of coagulation factor ix |
| BRPI0815416A2 (pt) | 2007-08-15 | 2014-10-21 | Amunix Inc | Composições e métodos para modificar propriedades de polipeptídeos biologicamente ativos |
| CN104004739A (zh) | 2007-10-15 | 2014-08-27 | 北卡罗来纳-查佩尔山大学 | 半衰期延长的人因子ix变体 |
| AU2009244633A1 (en) | 2008-04-16 | 2009-11-12 | Bayer Healthcare Llc | Modified Factor IX polypeptides and uses thereof |
| WO2009140015A2 (en) | 2008-04-16 | 2009-11-19 | Bayer Healthcare Llc | Site-directed modification of factor ix |
| EP2444491B1 (en) | 2008-04-21 | 2016-11-16 | Novo Nordisk Healthcare Ag | Hyperglycosylated human coagulation factor IX |
| US20090282865A1 (en) | 2008-05-16 | 2009-11-19 | Ortloff Engineers, Ltd. | Liquefied Natural Gas and Hydrocarbon Gas Processing |
| GB2479069B (en) | 2008-09-24 | 2012-07-25 | Stabilitech Ltd | Method for preserving polypeptides using a sugar and polyethyleneimine |
| WO2010091122A1 (en) | 2009-02-03 | 2010-08-12 | Amunix, Inc. | Extended recombinant polypeptides and compositions comprising same |
| KR101722961B1 (ko) | 2009-02-11 | 2017-04-04 | 알부메딕스 에이/에스 | 알부민 변이체 및 접합체 |
| WO2011030641A1 (ja) | 2009-09-08 | 2011-03-17 | コニカミノルタホールディングス株式会社 | 身体用装具 |
| MX2012004793A (es) | 2009-10-30 | 2012-07-20 | Novozymes Biopharma Dk As | Variantes de albumina. |
| EP2353588B1 (en) | 2010-01-21 | 2015-04-15 | Agricultural Technology Research Institute | A sustained release preparation of factor IX |
| JP5969458B2 (ja) | 2010-04-09 | 2016-08-17 | アルブミディクス アクティーゼルスカブ | アルブミン誘導体及び変異体 |
| CN103140237A (zh) * | 2010-07-09 | 2013-06-05 | 比奥根艾迪克依蒙菲利亚公司 | 因子ix多肽及其使用方法 |
| CA2830660A1 (en) | 2011-05-05 | 2012-11-08 | Novozymes Biopharma Dk A/S | Albumin variants |
| US20140315817A1 (en) | 2011-11-18 | 2014-10-23 | Eleven Biotherapeutics, Inc. | Variant serum albumin with improved half-life and other properties |
| TW201427685A (zh) | 2012-09-25 | 2014-07-16 | Biogen Idec Inc | Fix多肽的應用 |
| CN105007722A (zh) | 2013-02-16 | 2015-10-28 | 诺维信生物制药丹麦公司 | 药代动力学动物模型 |
| EA037906B1 (ru) | 2013-03-15 | 2021-06-04 | Биовератив Терапьютикс Инк. | Препараты полипептида фактора ix |
| CA2934081A1 (en) | 2013-12-23 | 2015-07-02 | Csl Limited | Fusion proteins comprising factor ix for prophylactic treatment of hemophilia and methods thereof |
-
2011
- 2011-07-11 CN CN2011800375149A patent/CN103140237A/zh active Pending
- 2011-07-11 EP EP11804476.7A patent/EP2590668A4/en not_active Withdrawn
- 2011-07-11 LT LTEP19156074.7T patent/LT3552619T/lt unknown
- 2011-07-11 AU AU2011274414A patent/AU2011274414B2/en active Active
- 2011-07-11 DK DK19156074.7T patent/DK3552619T3/da active
- 2011-07-11 SG SG2012096053A patent/SG186856A1/en unknown
- 2011-07-11 MX MX2017008224A patent/MX375112B/es unknown
- 2011-07-11 KR KR1020237037701A patent/KR20230156435A/ko not_active Ceased
- 2011-07-11 NZ NZ605348A patent/NZ605348A/en unknown
- 2011-07-11 KR KR1020137003411A patent/KR20140017480A/ko not_active Ceased
- 2011-07-11 WO PCT/US2011/043569 patent/WO2012006624A2/en not_active Ceased
- 2011-07-11 SG SG10201913700SA patent/SG10201913700SA/en unknown
- 2011-07-11 MY MYPI2013000037A patent/MY166954A/en unknown
- 2011-07-11 KR KR1020197025541A patent/KR20190104442A/ko not_active Ceased
- 2011-07-11 UA UAA201701696A patent/UA126265C2/uk unknown
- 2011-07-11 RS RS20251092A patent/RS67366B1/sr unknown
- 2011-07-11 EP EP25189951.4A patent/EP4653528A2/en active Pending
- 2011-07-11 EP EP19156074.7A patent/EP3552619B1/en active Active
- 2011-07-11 EA EA201291480A patent/EA028067B1/ru unknown
- 2011-07-11 FI FIEP19156074.7T patent/FI3552619T3/fi active
- 2011-07-11 BR BR112013000650A patent/BR112013000650A8/pt not_active Application Discontinuation
- 2011-07-11 JP JP2013518876A patent/JP2013534426A/ja active Pending
- 2011-07-11 PT PT191560747T patent/PT3552619T/pt unknown
- 2011-07-11 MY MYPI2017000477A patent/MY192639A/en unknown
- 2011-07-11 MX MX2013000281A patent/MX356527B/es active IP Right Grant
- 2011-07-11 UA UAA201301039A patent/UA115120C2/uk unknown
- 2011-07-11 PL PL19156074.7T patent/PL3552619T3/pl unknown
- 2011-07-11 SG SG10201505218YA patent/SG10201505218YA/en unknown
- 2011-07-11 EA EA201790876A patent/EA037095B1/ru unknown
- 2011-07-11 KR KR1020227020222A patent/KR20220097518A/ko not_active Ceased
- 2011-07-11 KR KR1020187030651A patent/KR20180118808A/ko not_active Ceased
- 2011-07-11 CA CA2804274A patent/CA2804274A1/en active Pending
- 2011-07-11 US US13/809,276 patent/US9670475B2/en active Active
-
2012
- 2012-12-30 IL IL223990A patent/IL223990B/en active IP Right Grant
-
2013
- 2013-01-08 CL CL2013000058A patent/CL2013000058A1/es unknown
- 2013-01-08 MX MX2020009702A patent/MX2020009702A/es unknown
- 2013-03-11 US US13/793,796 patent/US9233145B2/en active Active
-
2015
- 2015-11-17 JP JP2015224436A patent/JP2016034973A/ja active Pending
- 2015-12-29 US US14/982,934 patent/US9867873B2/en active Active
-
2016
- 2016-02-12 US US15/043,445 patent/US9675676B2/en active Active
- 2016-02-12 US US15/043,455 patent/US9623091B2/en active Active
- 2016-02-12 US US15/043,457 patent/US9629903B2/en active Active
- 2016-09-15 AU AU2016228243A patent/AU2016228243B2/en active Active
- 2016-11-09 JP JP2016218597A patent/JP2017036328A/ja not_active Withdrawn
-
2017
- 2017-11-21 US US15/820,080 patent/US20180207244A1/en not_active Abandoned
- 2017-11-30 AU AU2017268650A patent/AU2017268650B2/en active Active
-
2018
- 2018-02-06 US US15/890,284 patent/US10561714B2/en active Active
- 2018-02-06 US US15/890,290 patent/US20180228879A1/en not_active Abandoned
- 2018-11-21 JP JP2018218122A patent/JP2019023242A/ja not_active Withdrawn
-
2019
- 2019-02-08 US US16/271,689 patent/US10548954B2/en active Active
- 2019-02-08 US US16/271,686 patent/US10568943B2/en active Active
-
2020
- 2020-01-08 AU AU2020200118A patent/AU2020200118B2/en active Active
- 2020-06-22 US US16/907,985 patent/US20210008178A1/en not_active Abandoned
- 2020-09-17 IL IL277432A patent/IL277432B/en unknown
- 2020-09-25 US US17/032,354 patent/US10898554B1/en active Active
-
2021
- 2021-06-24 IL IL284368A patent/IL284368A/en unknown
-
2022
- 2022-01-31 JP JP2022012817A patent/JP2022044828A/ja active Pending
- 2022-06-29 AU AU2022204643A patent/AU2022204643B2/en active Active
Patent Citations (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2010063462A (ja) * | 1997-02-14 | 2010-03-25 | American Red Cross | トランスジェニック動物乳房組織における活性ヒト第ix因子の発現 |
| WO2009130602A2 (en) * | 2008-04-24 | 2009-10-29 | Celtic Pharma Peg Ltd. | Factor ix conjugates with extended half-lives |
| WO2010020690A1 (en) * | 2008-08-21 | 2010-02-25 | Octapharma Ag | Recombinantly produced human factor viii and ix |
Non-Patent Citations (2)
| Title |
|---|
| JPN6015025910; Blood 115(10), 201003, p.2057-2064 * |
| JPN6015025911; BioDrugs 20(3), 2006, p.151-160 * |
Cited By (12)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US11642398B2 (en) | 2013-03-15 | 2023-05-09 | Bioverativ Therapeutics Inc. | Factor IX polypeptide formulations |
| JP2017502036A (ja) * | 2013-12-23 | 2017-01-19 | シーエスエル、リミテッド | 血友病の予防的処置のための第ix因子を含む融合タンパク質およびその方法 |
| KR20160137577A (ko) * | 2014-03-24 | 2016-11-30 | 바이오젠 엠에이 인코포레이티드 | 동결건조된 ix 인자 제형 |
| JP2017510585A (ja) * | 2014-03-24 | 2017-04-13 | バイオジェン・エムエイ・インコーポレイテッドBiogen MA Inc. | 凍結乾燥第ix因子製剤 |
| JP2022044689A (ja) * | 2014-03-24 | 2022-03-17 | バイオベラティブ セラピューティクス インコーポレイテッド | 凍結乾燥第ix因子製剤 |
| KR102385372B1 (ko) * | 2014-03-24 | 2022-04-11 | 바이오버라티브 테라퓨틱스 인크. | 동결건조된 ix 인자 제형 |
| JP7058940B2 (ja) | 2014-03-24 | 2022-04-25 | バイオベラティブ セラピューティクス インコーポレイテッド | 凍結乾燥第ix因子製剤 |
| JP7503583B2 (ja) | 2014-03-24 | 2024-06-20 | バイオベラティブ セラピューティクス インコーポレイテッド | 凍結乾燥第ix因子製剤 |
| US12128092B2 (en) | 2014-03-24 | 2024-10-29 | Bioverativ Therapeutics Inc. | Lyophilized factor IX formulations |
| JP2018522563A (ja) * | 2015-08-03 | 2018-08-16 | バイオベラティブ セラピューティクス インコーポレイテッド | 第ix因子融合タンパク質及びそれらの製造方法及び使用方法 |
| JP2022171790A (ja) * | 2015-08-03 | 2022-11-11 | バイオベラティブ セラピューティクス インコーポレイテッド | 第ix因子融合タンパク質及びそれらの製造方法及び使用方法 |
| JP7418519B2 (ja) | 2015-08-03 | 2024-01-19 | バイオベラティブ セラピューティクス インコーポレイテッド | 第ix因子融合タンパク質及びそれらの製造方法及び使用方法 |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US10898554B1 (en) | Factor IX polypeptides and methods of use thereof | |
| JP6641340B2 (ja) | 第VIII−Fc因子キメラおよびハイブリッドポリペプチドならびにその使用法 | |
| TWI764092B (zh) | 因子viii嵌合及雜交多肽,及其使用方法 | |
| HK40015680A (en) | Factor ix polypeptides and methods of use thereof |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20140710 |
|
| A621 | Written request for application examination |
Free format text: JAPANESE INTERMEDIATE CODE: A621 Effective date: 20140710 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20150626 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20150925 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20151023 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20151117 |
|
| A02 | Decision of refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A02 Effective date: 20160223 |