MXPA06007514A - Vacuna para mejorar el crecimiento a base de epitopes neutralizantes. - Google Patents
Vacuna para mejorar el crecimiento a base de epitopes neutralizantes.Info
- Publication number
- MXPA06007514A MXPA06007514A MXPA06007514A MXPA06007514A MXPA06007514A MX PA06007514 A MXPA06007514 A MX PA06007514A MX PA06007514 A MXPA06007514 A MX PA06007514A MX PA06007514 A MXPA06007514 A MX PA06007514A MX PA06007514 A MXPA06007514 A MX PA06007514A
- Authority
- MX
- Mexico
- Prior art keywords
- peptide
- gdfd
- amino acid
- gdf8
- antibody
- Prior art date
Links
- 229960005486 vaccine Drugs 0.000 title claims abstract description 32
- 230000003472 neutralizing effect Effects 0.000 title description 14
- 230000012010 growth Effects 0.000 title description 7
- 230000002708 enhancing effect Effects 0.000 title 1
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 138
- 101000886562 Homo sapiens Growth/differentiation factor 8 Proteins 0.000 claims abstract description 135
- 102100039939 Growth/differentiation factor 8 Human genes 0.000 claims abstract description 83
- 241001465754 Metazoa Species 0.000 claims abstract description 58
- 238000000034 method Methods 0.000 claims abstract description 49
- 108020001507 fusion proteins Proteins 0.000 claims abstract description 30
- 102000037865 fusion proteins Human genes 0.000 claims abstract description 30
- 230000000694 effects Effects 0.000 claims abstract description 24
- 230000000890 antigenic effect Effects 0.000 claims abstract description 9
- 210000004027 cell Anatomy 0.000 claims description 56
- 241000283707 Capra Species 0.000 claims description 42
- 125000000539 amino acid group Chemical group 0.000 claims description 36
- 239000002243 precursor Substances 0.000 claims description 33
- 150000007523 nucleic acids Chemical class 0.000 claims description 31
- 108020004707 nucleic acids Proteins 0.000 claims description 25
- 102000039446 nucleic acids Human genes 0.000 claims description 25
- 239000000203 mixture Substances 0.000 claims description 24
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 23
- 238000006467 substitution reaction Methods 0.000 claims description 21
- 239000012634 fragment Substances 0.000 claims description 20
- 239000002773 nucleotide Substances 0.000 claims description 16
- 125000003729 nucleotide group Chemical group 0.000 claims description 16
- 238000006386 neutralization reaction Methods 0.000 claims description 15
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 13
- 239000002671 adjuvant Substances 0.000 claims description 12
- 230000028993 immune response Effects 0.000 claims description 10
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims description 9
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims description 9
- 230000002222 downregulating effect Effects 0.000 claims description 4
- 210000003527 eukaryotic cell Anatomy 0.000 claims description 4
- 238000004519 manufacturing process Methods 0.000 claims description 4
- 238000012216 screening Methods 0.000 claims description 3
- 238000012258 culturing Methods 0.000 claims description 2
- 239000003814 drug Substances 0.000 claims description 2
- 239000013599 cloning vector Substances 0.000 claims 3
- 102000004196 processed proteins & peptides Human genes 0.000 abstract description 62
- 108090000623 proteins and genes Proteins 0.000 description 63
- 235000018102 proteins Nutrition 0.000 description 51
- 102000004169 proteins and genes Human genes 0.000 description 51
- 235000001014 amino acid Nutrition 0.000 description 33
- 241000282414 Homo sapiens Species 0.000 description 29
- 230000014509 gene expression Effects 0.000 description 26
- 239000013598 vector Substances 0.000 description 24
- 229940024606 amino acid Drugs 0.000 description 21
- 150000001413 amino acids Chemical class 0.000 description 19
- 108020004414 DNA Proteins 0.000 description 18
- 229920001184 polypeptide Polymers 0.000 description 17
- 210000002966 serum Anatomy 0.000 description 15
- 108091026890 Coding region Proteins 0.000 description 14
- 241000700159 Rattus Species 0.000 description 14
- 239000000427 antigen Substances 0.000 description 14
- 108091007433 antigens Proteins 0.000 description 14
- 102000036639 antigens Human genes 0.000 description 14
- 230000027455 binding Effects 0.000 description 14
- 239000000463 material Substances 0.000 description 14
- 238000002965 ELISA Methods 0.000 description 11
- 238000003018 immunoassay Methods 0.000 description 11
- 238000000746 purification Methods 0.000 description 11
- 241000251468 Actinopterygii Species 0.000 description 10
- 238000003556 assay Methods 0.000 description 10
- 239000013604 expression vector Substances 0.000 description 10
- 239000013612 plasmid Substances 0.000 description 10
- 230000009257 reactivity Effects 0.000 description 10
- 108020004705 Codon Proteins 0.000 description 9
- 235000019688 fish Nutrition 0.000 description 9
- 230000006870 function Effects 0.000 description 9
- 230000004927 fusion Effects 0.000 description 9
- 241000972773 Aulopiformes Species 0.000 description 8
- 241000269817 Centrarchidae Species 0.000 description 8
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 8
- 230000003053 immunization Effects 0.000 description 8
- 235000019515 salmon Nutrition 0.000 description 8
- 238000013518 transcription Methods 0.000 description 8
- 230000035897 transcription Effects 0.000 description 8
- 241000283690 Bos taurus Species 0.000 description 7
- 238000007796 conventional method Methods 0.000 description 7
- -1 for example Proteins 0.000 description 7
- 238000002649 immunization Methods 0.000 description 7
- 238000000338 in vitro Methods 0.000 description 7
- 241000894007 species Species 0.000 description 7
- 108091029865 Exogenous DNA Proteins 0.000 description 6
- 241000238631 Hexapoda Species 0.000 description 6
- 241000283973 Oryctolagus cuniculus Species 0.000 description 6
- 241001494479 Pecora Species 0.000 description 6
- 241000269799 Perca fluviatilis Species 0.000 description 6
- 241000277331 Salmonidae Species 0.000 description 6
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 6
- 230000003828 downregulation Effects 0.000 description 6
- 239000002953 phosphate buffered saline Substances 0.000 description 6
- 230000010076 replication Effects 0.000 description 6
- 230000003612 virological effect Effects 0.000 description 6
- 102000004190 Enzymes Human genes 0.000 description 5
- 108090000790 Enzymes Proteins 0.000 description 5
- 108010070675 Glutathione transferase Proteins 0.000 description 5
- 102100029100 Hematopoietic prostaglandin D synthase Human genes 0.000 description 5
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 5
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 5
- 241000283984 Rodentia Species 0.000 description 5
- 241000282898 Sus scrofa Species 0.000 description 5
- 238000004587 chromatography analysis Methods 0.000 description 5
- 229940088598 enzyme Drugs 0.000 description 5
- 230000005764 inhibitory process Effects 0.000 description 5
- 239000011159 matrix material Substances 0.000 description 5
- 238000003786 synthesis reaction Methods 0.000 description 5
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 4
- 241000282693 Cercopithecidae Species 0.000 description 4
- 241000272201 Columbiformes Species 0.000 description 4
- 241000275449 Diplectrum formosum Species 0.000 description 4
- 241000283086 Equidae Species 0.000 description 4
- 241000287828 Gallus gallus Species 0.000 description 4
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 4
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 4
- 239000005089 Luciferase Substances 0.000 description 4
- 108010056852 Myostatin Proteins 0.000 description 4
- 102000004472 Myostatin Human genes 0.000 description 4
- 102000007659 Protein Deglycase DJ-1 Human genes 0.000 description 4
- 241000277284 Salvelinus fontinalis Species 0.000 description 4
- 102000004887 Transforming Growth Factor beta Human genes 0.000 description 4
- 108090001012 Transforming Growth Factor beta Proteins 0.000 description 4
- 230000004913 activation Effects 0.000 description 4
- 238000001042 affinity chromatography Methods 0.000 description 4
- 230000015572 biosynthetic process Effects 0.000 description 4
- 238000010494 dissociation reaction Methods 0.000 description 4
- 230000005593 dissociations Effects 0.000 description 4
- 235000013305 food Nutrition 0.000 description 4
- 210000004408 hybridoma Anatomy 0.000 description 4
- 108020004999 messenger RNA Proteins 0.000 description 4
- 239000007790 solid phase Substances 0.000 description 4
- ZRKFYGHZFMAOKI-QMGMOQQFSA-N tgfbeta Chemical compound C([C@H](NC(=O)[C@H](C(C)C)NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CC(C)C)NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CCSC)C(C)C)[C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)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](CC(C)C)C(O)=O)C1=CC=C(O)C=C1 ZRKFYGHZFMAOKI-QMGMOQQFSA-N 0.000 description 4
- 241000701447 unidentified baculovirus Species 0.000 description 4
- 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 description 3
- 229920000936 Agarose Polymers 0.000 description 3
- 241000272517 Anseriformes Species 0.000 description 3
- 241000473391 Archosargus rhomboidalis Species 0.000 description 3
- 241000271566 Aves Species 0.000 description 3
- 241000894006 Bacteria Species 0.000 description 3
- 241000282472 Canis lupus familiaris Species 0.000 description 3
- 102000014914 Carrier Proteins Human genes 0.000 description 3
- 241000283073 Equus caballus Species 0.000 description 3
- 108010054218 Factor VIII Proteins 0.000 description 3
- 102000001690 Factor VIII Human genes 0.000 description 3
- 241000701024 Human betaherpesvirus 5 Species 0.000 description 3
- 108060003951 Immunoglobulin Proteins 0.000 description 3
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 3
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 3
- 241000124008 Mammalia Species 0.000 description 3
- 241000699666 Mus <mouse, genus> Species 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 241000286209 Phasianidae Species 0.000 description 3
- 241000287530 Psittaciformes Species 0.000 description 3
- 241000700605 Viruses Species 0.000 description 3
- 238000004166 bioassay Methods 0.000 description 3
- 235000013330 chicken meat Nutrition 0.000 description 3
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- 230000008878 coupling Effects 0.000 description 3
- 238000010168 coupling process Methods 0.000 description 3
- 238000005859 coupling reaction Methods 0.000 description 3
- 230000004069 differentiation Effects 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 238000001502 gel electrophoresis Methods 0.000 description 3
- 238000004128 high performance liquid chromatography Methods 0.000 description 3
- 102000018358 immunoglobulin Human genes 0.000 description 3
- 238000002347 injection Methods 0.000 description 3
- 239000007924 injection Substances 0.000 description 3
- 239000003446 ligand Substances 0.000 description 3
- 230000007246 mechanism Effects 0.000 description 3
- 238000010369 molecular cloning Methods 0.000 description 3
- 229920000642 polymer Polymers 0.000 description 3
- 238000003752 polymerase chain reaction Methods 0.000 description 3
- 238000001556 precipitation Methods 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 230000009870 specific binding Effects 0.000 description 3
- 210000001519 tissue Anatomy 0.000 description 3
- 238000013519 translation Methods 0.000 description 3
- 241000252349 Acipenser transmontanus Species 0.000 description 2
- 241000272525 Anas platyrhynchos Species 0.000 description 2
- 241000272809 Anser anser Species 0.000 description 2
- 241000272814 Anser sp. Species 0.000 description 2
- 101710145634 Antigen 1 Proteins 0.000 description 2
- 241000282465 Canis Species 0.000 description 2
- 241000276616 Cichlidae Species 0.000 description 2
- 241000272205 Columba livia Species 0.000 description 2
- 102000053602 DNA Human genes 0.000 description 2
- 241000588724 Escherichia coli Species 0.000 description 2
- 108010046276 FLP recombinase Proteins 0.000 description 2
- 241000282324 Felis Species 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 241000288105 Grus Species 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 2
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 2
- 241000408747 Lepomis gibbosus Species 0.000 description 2
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
- 108060001084 Luciferase Proteins 0.000 description 2
- 239000004472 Lysine Substances 0.000 description 2
- 241000699670 Mus sp. Species 0.000 description 2
- 241000277275 Oncorhynchus mykiss Species 0.000 description 2
- 241001280377 Oncorhynchus tshawytscha Species 0.000 description 2
- 102000007079 Peptide Fragments Human genes 0.000 description 2
- 108010033276 Peptide Fragments Proteins 0.000 description 2
- 102000003992 Peroxidases Human genes 0.000 description 2
- 206010035226 Plasma cell myeloma Diseases 0.000 description 2
- 102000010752 Plasminogen Inactivators Human genes 0.000 description 2
- 241000288906 Primates Species 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 208000030555 Pygmy Diseases 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- 241000277289 Salmo salar Species 0.000 description 2
- 229920002684 Sepharose Polymers 0.000 description 2
- 241001417495 Serranidae Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 229920002125 Sokalan® Polymers 0.000 description 2
- 241000269788 Sparidae Species 0.000 description 2
- 241000269809 Sparus aurata Species 0.000 description 2
- 241000282887 Suidae Species 0.000 description 2
- 241000276707 Tilapia Species 0.000 description 2
- 101710120037 Toxin CcdB Proteins 0.000 description 2
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 description 2
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 2
- 238000004458 analytical method Methods 0.000 description 2
- 239000005557 antagonist Substances 0.000 description 2
- 210000000628 antibody-producing cell Anatomy 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 108091008324 binding proteins Proteins 0.000 description 2
- 210000004369 blood Anatomy 0.000 description 2
- 239000008280 blood Substances 0.000 description 2
- 238000009395 breeding Methods 0.000 description 2
- 230000001488 breeding effect Effects 0.000 description 2
- 244000309464 bull Species 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 230000009920 chelation Effects 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 210000000349 chromosome Anatomy 0.000 description 2
- 239000000356 contaminant Substances 0.000 description 2
- 235000013601 eggs Nutrition 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 101150004578 gdf-8 gene Proteins 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 239000003102 growth factor Substances 0.000 description 2
- 230000002163 immunogen Effects 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 229960000310 isoleucine Drugs 0.000 description 2
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 235000013336 milk Nutrition 0.000 description 2
- 239000008267 milk Substances 0.000 description 2
- 210000004080 milk Anatomy 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 210000003205 muscle Anatomy 0.000 description 2
- 201000000050 myeloid neoplasm Diseases 0.000 description 2
- 230000006263 negative regulation of skeletal muscle tissue growth Effects 0.000 description 2
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 description 2
- 108040007629 peroxidase activity proteins Proteins 0.000 description 2
- 235000020030 perry Nutrition 0.000 description 2
- 239000002797 plasminogen activator inhibitor Substances 0.000 description 2
- 229920002704 polyhistidine Polymers 0.000 description 2
- 108091033319 polynucleotide Proteins 0.000 description 2
- 102000040430 polynucleotide Human genes 0.000 description 2
- 239000002157 polynucleotide Substances 0.000 description 2
- 238000003127 radioimmunoassay Methods 0.000 description 2
- 238000011160 research Methods 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 239000011435 rock Substances 0.000 description 2
- 239000012266 salt solution Substances 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 230000009897 systematic effect Effects 0.000 description 2
- 238000012360 testing method Methods 0.000 description 2
- 230000005030 transcription termination Effects 0.000 description 2
- 238000001890 transfection Methods 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 238000002255 vaccination Methods 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- 230000004584 weight gain Effects 0.000 description 2
- 235000019786 weight gain Nutrition 0.000 description 2
- ASWBNKHCZGQVJV-UHFFFAOYSA-N (3-hexadecanoyloxy-2-hydroxypropyl) 2-(trimethylazaniumyl)ethyl phosphate Chemical compound CCCCCCCCCCCCCCCC(=O)OCC(O)COP([O-])(=O)OCC[N+](C)(C)C ASWBNKHCZGQVJV-UHFFFAOYSA-N 0.000 description 1
- 125000003088 (fluoren-9-ylmethoxy)carbonyl group Chemical group 0.000 description 1
- FJLUATLTXUNBOT-UHFFFAOYSA-N 1-Hexadecylamine Chemical compound CCCCCCCCCCCCCCCCN FJLUATLTXUNBOT-UHFFFAOYSA-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
- PYAFUXYGTYWWBP-UHFFFAOYSA-N 19-methoxynonadecane-1,2,3-triol Chemical compound COCCCCCCCCCCCCCCCCC(O)C(O)CO PYAFUXYGTYWWBP-UHFFFAOYSA-N 0.000 description 1
- MGADZUXDNSDTHW-UHFFFAOYSA-N 2H-pyran Chemical compound C1OC=CC=C1 MGADZUXDNSDTHW-UHFFFAOYSA-N 0.000 description 1
- GNMSJGSGAXHQRC-UHFFFAOYSA-N 3,3-diamino-2-methylpropan-1-ol Chemical compound OCC(C)C(N)N GNMSJGSGAXHQRC-UHFFFAOYSA-N 0.000 description 1
- 102100031126 6-phosphogluconolactonase Human genes 0.000 description 1
- 108010029731 6-phosphogluconolactonase Proteins 0.000 description 1
- CJIJXIFQYOPWTF-UHFFFAOYSA-N 7-hydroxycoumarin Natural products O1C(=O)C=CC2=CC(O)=CC=C21 CJIJXIFQYOPWTF-UHFFFAOYSA-N 0.000 description 1
- 241001519451 Abramis brama Species 0.000 description 1
- 108010042708 Acetylmuramyl-Alanyl-Isoglutamine Proteins 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 241001559555 Ambloplites rupestris Species 0.000 description 1
- 241000272521 Anatidae Species 0.000 description 1
- 241000271362 Andinoacara latifrons Species 0.000 description 1
- 241000264349 Archosargus probatocephalus Species 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- QXOPPIDJKPEKCW-GUBZILKMSA-N Asn-Pro-Arg Chemical compound C1C[C@H](N(C1)C(=O)[C@H](CC(=O)N)N)C(=O)N[C@@H](CCCN=C(N)N)C(=O)O QXOPPIDJKPEKCW-GUBZILKMSA-N 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 241000283705 Capra hircus Species 0.000 description 1
- 240000000606 Cardamine pratensis Species 0.000 description 1
- 235000008474 Cardamine pratensis Nutrition 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- 241001155433 Centrarchus macropterus Species 0.000 description 1
- 241001085785 Centropristis Species 0.000 description 1
- 241000758604 Centropristis ocyurus Species 0.000 description 1
- 241001085763 Centropristis striata Species 0.000 description 1
- 241001155440 Chaenobryttus gulosus Species 0.000 description 1
- 241000272470 Circus Species 0.000 description 1
- 235000008733 Citrus aurantifolia Nutrition 0.000 description 1
- 241000252203 Clupea harengus Species 0.000 description 1
- 241000272202 Columbidae Species 0.000 description 1
- 241001125817 Coregonus Species 0.000 description 1
- 241000611752 Coregonus clupeaformis Species 0.000 description 1
- 241000202327 Coturnix chinensis Species 0.000 description 1
- 108010069514 Cyclic Peptides Proteins 0.000 description 1
- 102000001189 Cyclic Peptides Human genes 0.000 description 1
- IQXSTXKVEMRMMB-XAVMHZPKSA-N Cys-Thr-Pro Chemical compound C[C@H]([C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@H](CS)N)O IQXSTXKVEMRMMB-XAVMHZPKSA-N 0.000 description 1
- 241000701022 Cytomegalovirus Species 0.000 description 1
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 description 1
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 1
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 1
- 241000252212 Danio rerio Species 0.000 description 1
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 108090000204 Dipeptidase 1 Proteins 0.000 description 1
- 241001020588 Diplectrum bivittatum Species 0.000 description 1
- 238000012286 ELISA Assay Methods 0.000 description 1
- 238000008157 ELISA kit Methods 0.000 description 1
- 241001236162 Elassoma evergladei Species 0.000 description 1
- 241001236173 Elassoma okefenokee Species 0.000 description 1
- 241001236171 Elassoma zonatum Species 0.000 description 1
- 241001155417 Enneacanthus gloriosus Species 0.000 description 1
- 241001236175 Enneacanthus obesus Species 0.000 description 1
- 241000357439 Epinephelus Species 0.000 description 1
- 241000206602 Eukaryota Species 0.000 description 1
- 108010074860 Factor Xa Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 description 1
- 102000016970 Follistatin Human genes 0.000 description 1
- 108010014612 Follistatin Proteins 0.000 description 1
- 241000947653 Fontinalis Species 0.000 description 1
- 241000287826 Gallus Species 0.000 description 1
- 108010018962 Glucosephosphate Dehydrogenase Proteins 0.000 description 1
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- QSQXZZCGPXQBPP-BQBZGAKWSA-N Gly-Pro-Cys Chemical compound C1C[C@H](N(C1)C(=O)CN)C(=O)N[C@@H](CS)C(=O)O QSQXZZCGPXQBPP-BQBZGAKWSA-N 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241000282575 Gorilla Species 0.000 description 1
- 241001417516 Haemulidae Species 0.000 description 1
- 241000353340 Helicolenus percoides Species 0.000 description 1
- 101000983944 Homo sapiens CDK2-associated and cullin domain-containing protein 1 Proteins 0.000 description 1
- 101000605403 Homo sapiens Plasminogen Proteins 0.000 description 1
- 101000869690 Homo sapiens Protein S100-A8 Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- GRRNUXAQVGOGFE-UHFFFAOYSA-N Hygromycin-B Natural products OC1C(NC)CC(N)C(O)C1OC1C2OC3(C(C(O)C(O)C(C(N)CO)O3)O)OC2C(O)C(CO)O1 GRRNUXAQVGOGFE-UHFFFAOYSA-N 0.000 description 1
- 241000321408 Hyporthodus flavolimbatus Species 0.000 description 1
- 241000252498 Ictalurus punctatus Species 0.000 description 1
- 108010058683 Immobilized Proteins Proteins 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- AHLPHDHHMVZTML-BYPYZUCNSA-N L-Ornithine Chemical compound NCCC[C@H](N)C(O)=O AHLPHDHHMVZTML-BYPYZUCNSA-N 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- 229930182816 L-glutamine Natural products 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 1
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 241000489982 Lagodon rhomboides Species 0.000 description 1
- 241000721656 Lepomis Species 0.000 description 1
- 241001155465 Lepomis auritus Species 0.000 description 1
- 241001155442 Lepomis cyanellus Species 0.000 description 1
- 241000721654 Lepomis macrochirus Species 0.000 description 1
- 241000408783 Lepomis megalotis Species 0.000 description 1
- 241000283987 Lepus capensis Species 0.000 description 1
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 description 1
- 241000282567 Macaca fascicularis Species 0.000 description 1
- 241000829100 Macaca mulatta polyomavirus 1 Species 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
- 241000288147 Meleagris gallopavo Species 0.000 description 1
- 241000290125 Micropterus coosae Species 0.000 description 1
- 241001328758 Micropterus dolomieu Species 0.000 description 1
- 241001125889 Micropterus salmoides Species 0.000 description 1
- 241000237852 Mollusca Species 0.000 description 1
- 241000202240 Morone americana Species 0.000 description 1
- 241000202236 Morone chrysops Species 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- FFDGPVCHZBVARC-UHFFFAOYSA-N N,N-dimethylglycine Chemical compound CN(C)CC(O)=O FFDGPVCHZBVARC-UHFFFAOYSA-N 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 108091005461 Nucleic proteins Proteins 0.000 description 1
- 241001455619 Numenius Species 0.000 description 1
- REYJJPSVUYRZGE-UHFFFAOYSA-N Octadecylamine Chemical compound CCCCCCCCCCCCCCCCCCN REYJJPSVUYRZGE-UHFFFAOYSA-N 0.000 description 1
- 108091034117 Oligonucleotide Proteins 0.000 description 1
- 241001417899 Oncorhynchus clarkii Species 0.000 description 1
- 241000277326 Oncorhynchus gorbuscha Species 0.000 description 1
- 241000277329 Oncorhynchus keta Species 0.000 description 1
- 241000277338 Oncorhynchus kisutch Species 0.000 description 1
- 241000277269 Oncorhynchus masou Species 0.000 description 1
- 241000277277 Oncorhynchus nerka Species 0.000 description 1
- 241000276719 Oreochromis Species 0.000 description 1
- 241000276701 Oreochromis mossambicus Species 0.000 description 1
- AHLPHDHHMVZTML-UHFFFAOYSA-N Orn-delta-NH2 Natural products NCCCC(N)C(O)=O AHLPHDHHMVZTML-UHFFFAOYSA-N 0.000 description 1
- UTJLXEIPEHZYQJ-UHFFFAOYSA-N Ornithine Natural products OC(=O)C(C)CCCN UTJLXEIPEHZYQJ-UHFFFAOYSA-N 0.000 description 1
- 241001282110 Pagrus major Species 0.000 description 1
- 241000282515 Papio hamadryas Species 0.000 description 1
- 241001396961 Parapristipoma trilineatum Species 0.000 description 1
- 241000237988 Patellidae Species 0.000 description 1
- 235000019483 Peanut oil Nutrition 0.000 description 1
- 229930182555 Penicillin Natural products 0.000 description 1
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 241000269801 Perca Species 0.000 description 1
- 241000276618 Perciformes Species 0.000 description 1
- 241000288049 Perdix perdix Species 0.000 description 1
- 102100029251 Phagocytosis-stimulating peptide Human genes 0.000 description 1
- 108010077971 Plasminogen Inactivators Proteins 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 241001155420 Pomoxis annularis Species 0.000 description 1
- 241000269816 Pomoxis nigromaculatus Species 0.000 description 1
- 241000767458 Prosopium cylindraceum Species 0.000 description 1
- 102100032442 Protein S100-A8 Human genes 0.000 description 1
- 241000125945 Protoparvovirus Species 0.000 description 1
- 241000287531 Psittacidae Species 0.000 description 1
- 108020005067 RNA Splice Sites Proteins 0.000 description 1
- 241000700157 Rattus norvegicus Species 0.000 description 1
- 241000277288 Salmo trutta Species 0.000 description 1
- 241000277299 Salmoniformes Species 0.000 description 1
- 241000277293 Salvelinus alpinus Species 0.000 description 1
- 241000277282 Salvelinus confluentus Species 0.000 description 1
- 241000277297 Salvelinus leucomaenis Species 0.000 description 1
- 241000277279 Salvelinus malma Species 0.000 description 1
- 241000276448 Salvelinus namaycush Species 0.000 description 1
- 241000276677 Sarotherodon Species 0.000 description 1
- 241000675916 Serranus phoebe Species 0.000 description 1
- 241000675264 Serranus tortugarum Species 0.000 description 1
- BQCADISMDOOEFD-UHFFFAOYSA-N Silver Chemical compound [Ag] BQCADISMDOOEFD-UHFFFAOYSA-N 0.000 description 1
- 108020004682 Single-Stranded DNA Proteins 0.000 description 1
- 241000519995 Stachys sylvatica Species 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 241001494106 Stenotomus chrysops Species 0.000 description 1
- 241000271567 Struthioniformes Species 0.000 description 1
- DCRHJDRLCFMEBI-RHYQMDGZSA-N Thr-Lys-Met Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCSC)C(O)=O DCRHJDRLCFMEBI-RHYQMDGZSA-N 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 241001489531 Thymallus thymallus Species 0.000 description 1
- 235000011941 Tilia x europaea Nutrition 0.000 description 1
- 102100022241 Transmembrane protein 54 Human genes 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 108010084754 Tuftsin Proteins 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- SDSCOOZQQGUQFC-GVXVVHGQSA-N Val-His-Gln Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC1=CN=CN1)C(=O)N[C@@H](CCC(=O)N)C(=O)O)N SDSCOOZQQGUQFC-GVXVVHGQSA-N 0.000 description 1
- LUXUAZKGQZPOBZ-SAXJAHGMSA-N [(3S,4S,5S,6R)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl] (Z)-octadec-9-enoate Chemical compound CCCCCCCC\C=C/CCCCCCCC(=O)OC1O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]1O LUXUAZKGQZPOBZ-SAXJAHGMSA-N 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000003463 adsorbent Substances 0.000 description 1
- 238000005377 adsorption chromatography Methods 0.000 description 1
- 150000001299 aldehydes Chemical class 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 229940037003 alum Drugs 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- ILRRQNADMUWWFW-UHFFFAOYSA-K aluminium phosphate Chemical compound O1[Al]2OP1(=O)O2 ILRRQNADMUWWFW-UHFFFAOYSA-K 0.000 description 1
- DIZPMCHEQGEION-UHFFFAOYSA-H aluminium sulfate (anhydrous) Chemical compound [Al+3].[Al+3].[O-]S([O-])(=O)=O.[O-]S([O-])(=O)=O.[O-]S([O-])(=O)=O DIZPMCHEQGEION-UHFFFAOYSA-H 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 230000008485 antagonism Effects 0.000 description 1
- 239000003146 anticoagulant agent Substances 0.000 description 1
- 229940127219 anticoagulant drug Drugs 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 150000001483 arginine derivatives Chemical class 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 235000015278 beef Nutrition 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 102000006635 beta-lactamase Human genes 0.000 description 1
- 230000001588 bifunctional effect Effects 0.000 description 1
- 150000001718 carbodiimides Chemical class 0.000 description 1
- 241001233037 catfish Species 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 210000004671 cell-free system Anatomy 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 108091006116 chimeric peptides Proteins 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 238000009833 condensation Methods 0.000 description 1
- 230000005494 condensation Effects 0.000 description 1
- 239000003636 conditioned culture medium Substances 0.000 description 1
- 239000007822 coupling agent Substances 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 108010004073 cysteinylcysteine Proteins 0.000 description 1
- 235000013365 dairy product Nutrition 0.000 description 1
- 125000001295 dansyl group Chemical group [H]C1=C([H])C(N(C([H])([H])[H])C([H])([H])[H])=C2C([H])=C([H])C([H])=C(C2=C1[H])S(*)(=O)=O 0.000 description 1
- 238000010511 deprotection reaction Methods 0.000 description 1
- 238000001514 detection method Methods 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 229960000633 dextran sulfate Drugs 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- IWEDIXLBFLAXBO-UHFFFAOYSA-N dicamba Chemical compound COC1=C(Cl)C=CC(Cl)=C1C(O)=O IWEDIXLBFLAXBO-UHFFFAOYSA-N 0.000 description 1
- UGMCXQCYOVCMTB-UHFFFAOYSA-K dihydroxy(stearato)aluminium Chemical compound CCCCCCCCCCCCCCCCCC(=O)O[Al](O)O UGMCXQCYOVCMTB-UHFFFAOYSA-K 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 239000000539 dimer Substances 0.000 description 1
- PSLWZOIUBRXAQW-UHFFFAOYSA-M dimethyl(dioctadecyl)azanium;bromide Chemical compound [Br-].CCCCCCCCCCCCCCCCCC[N+](C)(C)CCCCCCCCCCCCCCCCCC PSLWZOIUBRXAQW-UHFFFAOYSA-M 0.000 description 1
- 108700003601 dimethylglycine Proteins 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 210000003743 erythrocyte Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000001400 expression cloning Methods 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 210000003746 feather Anatomy 0.000 description 1
- 239000012091 fetal bovine serum Substances 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
- 238000001641 gel filtration chromatography Methods 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000003292 glue Substances 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 108060003552 hemocyanin Proteins 0.000 description 1
- 235000019514 herring Nutrition 0.000 description 1
- 229920001519 homopolymer Polymers 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 125000001165 hydrophobic group Chemical group 0.000 description 1
- 238000012872 hydroxylapatite chromatography Methods 0.000 description 1
- GRRNUXAQVGOGFE-NZSRVPFOSA-N hygromycin B Chemical compound O[C@@H]1[C@@H](NC)C[C@@H](N)[C@H](O)[C@H]1O[C@H]1[C@H]2O[C@@]3([C@@H]([C@@H](O)[C@@H](O)[C@@H](C(N)CO)O3)O)O[C@H]2[C@@H](O)[C@@H](CO)O1 GRRNUXAQVGOGFE-NZSRVPFOSA-N 0.000 description 1
- 229940097277 hygromycin b Drugs 0.000 description 1
- 150000002463 imidates Chemical class 0.000 description 1
- 230000037451 immune surveillance Effects 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 230000017730 intein-mediated protein splicing Effects 0.000 description 1
- 238000004255 ion exchange chromatography Methods 0.000 description 1
- 238000001155 isoelectric focusing Methods 0.000 description 1
- 210000004731 jugular vein Anatomy 0.000 description 1
- 210000003292 kidney cell Anatomy 0.000 description 1
- 238000011813 knockout mouse model Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 239000010985 leather Substances 0.000 description 1
- 239000004571 lime Substances 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 239000007791 liquid phase Substances 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 238000003670 luciferase enzyme activity assay Methods 0.000 description 1
- 210000001165 lymph node Anatomy 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- BSOQXXWZTUDTEL-ZUYCGGNHSA-N muramyl dipeptide Chemical compound OC(=O)CC[C@H](C(N)=O)NC(=O)[C@H](C)NC(=O)[C@@H](C)O[C@H]1[C@H](O)[C@@H](CO)O[C@@H](O)[C@@H]1NC(C)=O BSOQXXWZTUDTEL-ZUYCGGNHSA-N 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- 235000019198 oils Nutrition 0.000 description 1
- 229960003104 ornithine Drugs 0.000 description 1
- 238000004810 partition chromatography Methods 0.000 description 1
- 239000000312 peanut oil Substances 0.000 description 1
- 229940049954 penicillin Drugs 0.000 description 1
- 229940023041 peptide vaccine Drugs 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 238000002616 plasmapheresis Methods 0.000 description 1
- 229920001983 poloxamer Polymers 0.000 description 1
- 239000004584 polyacrylic acid Substances 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 229920000447 polyanionic polymer Polymers 0.000 description 1
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 244000144977 poultry Species 0.000 description 1
- 238000009374 poultry farming Methods 0.000 description 1
- 235000013594 poultry meat Nutrition 0.000 description 1
- 238000002360 preparation method Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000009465 prokaryotic expression Effects 0.000 description 1
- 125000006239 protecting group Chemical group 0.000 description 1
- 230000004952 protein activity Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 230000012743 protein tagging Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 235000020236 pumpkin seed Nutrition 0.000 description 1
- 239000013014 purified material Substances 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 230000022532 regulation of transcription, DNA-dependent Effects 0.000 description 1
- 239000011347 resin Substances 0.000 description 1
- 229920005989 resin Polymers 0.000 description 1
- 230000004043 responsiveness Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 238000004366 reverse phase liquid chromatography Methods 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- PYWVYCXTNDRMGF-UHFFFAOYSA-N rhodamine B Chemical compound [Cl-].C=12C=CC(=[N+](CC)CC)C=C2OC2=CC(N(CC)CC)=CC=C2C=1C1=CC=CC=C1C(O)=O PYWVYCXTNDRMGF-UHFFFAOYSA-N 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 239000012679 serum free medium Substances 0.000 description 1
- 229910052709 silver Inorganic materials 0.000 description 1
- 239000004332 silver Substances 0.000 description 1
- 210000002027 skeletal muscle Anatomy 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 238000010532 solid phase synthesis reaction Methods 0.000 description 1
- 210000004989 spleen cell Anatomy 0.000 description 1
- 238000005507 spraying Methods 0.000 description 1
- 229960005322 streptomycin Drugs 0.000 description 1
- KZNICNPSHKQLFF-UHFFFAOYSA-N succinimide Chemical class O=C1CCC(=O)N1 KZNICNPSHKQLFF-UHFFFAOYSA-N 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 238000004114 suspension culture Methods 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 239000012096 transfection reagent Substances 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
- IESDGNYHXIOKRW-LEOABGAYSA-N tuftsin Chemical compound C[C@@H](O)[C@H](N)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@H](CCCNC(N)=N)C(O)=O IESDGNYHXIOKRW-LEOABGAYSA-N 0.000 description 1
- 229940035670 tuftsin Drugs 0.000 description 1
- 208000001072 type 2 diabetes mellitus Diseases 0.000 description 1
- 238000005199 ultracentrifugation Methods 0.000 description 1
- ORHBXUUXSCNDEV-UHFFFAOYSA-N umbelliferone Chemical compound C1=CC(=O)OC2=CC(O)=CC=C21 ORHBXUUXSCNDEV-UHFFFAOYSA-N 0.000 description 1
- HFTAFOQKODTIJY-UHFFFAOYSA-N umbelliferone Natural products Cc1cc2C=CC(=O)Oc2cc1OCC=CC(C)(C)O HFTAFOQKODTIJY-UHFFFAOYSA-N 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 238000010200 validation analysis Methods 0.000 description 1
- 239000004474 valine Substances 0.000 description 1
- 239000003981 vehicle Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 238000001262 western blot Methods 0.000 description 1
- 210000002268 wool Anatomy 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
-
- 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
-
- 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
- A61K38/18—Growth factors; Growth regulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P21/00—Drugs for disorders of the muscular or neuromuscular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P21/00—Drugs for disorders of the muscular or neuromuscular system
- A61P21/06—Anabolic 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P3/00—Drugs for disorders of the metabolism
- A61P3/08—Drugs for disorders of the metabolism for glucose homeostasis
- A61P3/10—Drugs for disorders of the metabolism for glucose homeostasis for hyperglycaemia, e.g. antidiabetics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
-
- 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
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Veterinary Medicine (AREA)
- Engineering & Computer Science (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Pharmacology & Pharmacy (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Immunology (AREA)
- Diabetes (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Gastroenterology & Hepatology (AREA)
- Zoology (AREA)
- Endocrinology (AREA)
- Genetics & Genomics (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Physical Education & Sports Medicine (AREA)
- Toxicology (AREA)
- Obesity (AREA)
- Hematology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Neurology (AREA)
- Molecular Biology (AREA)
- Epidemiology (AREA)
- Emergency Medicine (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US53371903P | 2003-12-31 | 2003-12-31 | |
| PCT/US2004/043125 WO2005066204A2 (en) | 2003-12-31 | 2004-12-21 | Neutralizing epitope-based growth enhancing vaccine |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| MXPA06007514A true MXPA06007514A (es) | 2006-08-31 |
Family
ID=34748944
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| MXPA06007514A MXPA06007514A (es) | 2003-12-31 | 2004-12-21 | Vacuna para mejorar el crecimiento a base de epitopes neutralizantes. |
Country Status (21)
| Country | Link |
|---|---|
| US (3) | US7371726B2 (https=) |
| EP (1) | EP1699820A2 (https=) |
| JP (2) | JP2007535912A (https=) |
| KR (1) | KR20060120229A (https=) |
| CN (1) | CN1902221A (https=) |
| AR (1) | AR047345A1 (https=) |
| AU (1) | AU2004312411B8 (https=) |
| BR (1) | BRPI0418317A (https=) |
| CA (1) | CA2551877A1 (https=) |
| EC (1) | ECSP066683A (https=) |
| IL (1) | IL176494A0 (https=) |
| MX (1) | MXPA06007514A (https=) |
| NO (1) | NO20063478L (https=) |
| NZ (1) | NZ547593A (https=) |
| PE (1) | PE20051050A1 (https=) |
| RU (1) | RU2422460C2 (https=) |
| SG (1) | SG153874A1 (https=) |
| TW (1) | TWI357906B (https=) |
| UA (1) | UA93855C2 (https=) |
| WO (1) | WO2005066204A2 (https=) |
| ZA (1) | ZA200605227B (https=) |
Families Citing this family (37)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8460864B2 (en) | 2003-01-21 | 2013-06-11 | Ptc Therapeutics, Inc. | Methods for identifying compounds that modulate untranslated region-dependent gene expression and methods of using same |
| US9068234B2 (en) * | 2003-01-21 | 2015-06-30 | Ptc Therapeutics, Inc. | Methods and agents for screening for compounds capable of modulating gene expression |
| US8426194B2 (en) * | 2003-01-21 | 2013-04-23 | Ptc Therapeutics, Inc. | Methods and agents for screening for compounds capable of modulating VEGF expression |
| EP1699820A2 (en) * | 2003-12-31 | 2006-09-13 | Schering-Plough Ltd. | Neutralizing epitope-based growth enhancing vaccine |
| EP1799709B1 (en) * | 2004-09-30 | 2012-04-04 | ORICO Limited | Myostatin isoform |
| CA2594276A1 (en) * | 2004-12-30 | 2006-07-13 | Schering-Plough Ltd. | Neutralizing epitope-based growth enhancing vaccine |
| EP1951756B1 (en) | 2005-10-06 | 2015-01-07 | Eli Lilly And Company | Anti-myostatin antibodies |
| UA92504C2 (en) * | 2005-10-12 | 2010-11-10 | Эли Лилли Энд Компани | Anti-myostatin monoclonal antibody |
| CN104761637B (zh) | 2006-03-31 | 2021-10-15 | 中外制药株式会社 | 调控抗体血液动力学的方法 |
| AU2013231037B2 (en) * | 2006-08-03 | 2016-05-12 | Myostin Therapeutics Pty Ltd | Myostatin antagonists |
| CN101522707B (zh) * | 2006-08-03 | 2013-08-28 | 莫约斯汀医疗有限公司 | 肌肉生长抑制素拮抗剂 |
| BRPI0716249A2 (pt) | 2006-09-05 | 2013-09-03 | Lilly Co Eli | anticorpos antimiostatina |
| US8283115B1 (en) | 2007-06-20 | 2012-10-09 | Ptc Therapeutics, Inc. | Methods of screening for compounds for treating muscular dystrophy using UTRN mRNA translation regulation |
| US8283116B1 (en) | 2007-06-22 | 2012-10-09 | Ptc Therapeutics, Inc. | Methods of screening for compounds for treating spinal muscular atrophy using SMN mRNA translation regulation |
| ES2595638T3 (es) | 2007-09-26 | 2017-01-02 | Chugai Seiyaku Kabushiki Kaisha | Método para modificar el punto isoeléctrico de un anticuerpo mediante la sustitución de aminoácidos en una CDR |
| KR102057826B1 (ko) | 2008-04-11 | 2019-12-20 | 추가이 세이야쿠 가부시키가이샤 | 복수 분자의 항원에 반복 결합하는 항원 결합 분자 |
| JO3340B1 (ar) | 2010-05-26 | 2019-03-13 | Regeneron Pharma | مضادات حيوية لـعامل تمايز النمو 8 البشري |
| AR081556A1 (es) * | 2010-06-03 | 2012-10-03 | Glaxo Group Ltd | Proteinas de union al antigeno humanizadas |
| SG187867A1 (en) | 2010-08-16 | 2013-03-28 | Amgen Inc | Antibodies that bind myostatin, compositions and methods |
| EP2647706B1 (en) | 2010-11-30 | 2023-05-17 | Chugai Seiyaku Kabushiki Kaisha | Antigen-binding molecule capable of binding to plurality of antigen molecules repeatedly |
| DK2780368T3 (en) | 2011-11-14 | 2018-02-05 | Regeneron Pharma | COMPOSITIONS AND PROCEDURES FOR INCREASING MUSCLE MASS AND MUSCLE STRENGTH BY SPECIFIC ANTAGONIZATION OF GDF8 AND / OR ACTIVIN A |
| WO2014030750A1 (ja) | 2012-08-24 | 2014-02-27 | 中外製薬株式会社 | マウスFcγRII特異的Fc抗体 |
| CN105246914B (zh) | 2013-04-02 | 2021-08-27 | 中外制药株式会社 | Fc区变体 |
| RS61778B1 (sr) | 2013-05-06 | 2021-06-30 | Scholar Rock Inc | Kompozicije i postupci za modulaciju faktora rasta |
| TW201920262A (zh) | 2013-07-30 | 2019-06-01 | 美商再生元醫藥公司 | 抗活化素ａ之抗體及其用途 |
| EP3215175A4 (en) | 2014-11-06 | 2018-06-27 | Scholar Rock, Inc. | Anti-pro/latent-myostatin antibodies and uses thereof |
| KR101860280B1 (ko) | 2014-12-19 | 2018-05-21 | 추가이 세이야쿠 가부시키가이샤 | 항-마이오스타틴 항체, 변이체 Fc 영역을 함유하는 폴리펩타이드, 및 사용 방법 |
| KR102605798B1 (ko) | 2015-02-05 | 2023-11-23 | 추가이 세이야쿠 가부시키가이샤 | 이온 농도 의존적 항원 결합 도메인을 포함하는 항체, Fc 영역 개변체, IL-8에 결합하는 항체, 및 그들의 사용 |
| KR20170135967A (ko) | 2015-04-15 | 2017-12-08 | 리제너론 파마슈티칼스 인코포레이티드 | Gdf8 억제제를 사용하여 강도 및 기능을 증가시키는 방법 |
| HRP20211081T1 (hr) * | 2015-09-15 | 2021-10-15 | Scholar Rock, Inc. | Anti-pro/latentna miostatinska protutijela i njihove uporabe |
| WO2017110981A1 (en) | 2015-12-25 | 2017-06-29 | Chugai Seiyaku Kabushiki Kaisha | Anti-myostatin antibodies and methods of use |
| CN115814077A (zh) | 2016-01-08 | 2023-03-21 | 供石公司 | 抗-原肌生长抑制素/潜伏肌生长抑制素抗体及其使用方法 |
| NZ789269A (en) | 2016-06-13 | 2026-01-30 | Scholar Rock Inc | Use of myostatin inhibitors and combination therapies |
| EP3494991A4 (en) | 2016-08-05 | 2020-07-29 | Chugai Seiyaku Kabushiki Kaisha | COMPOSITION FOR THE PROPHYLAXIS OR TREATMENT OF IL-8 RELATED DISEASES |
| EP4218817A3 (en) | 2017-01-06 | 2023-09-06 | Scholar Rock, Inc. | Methods for treating metabolic diseases by inhibiting myostatin activation |
| MX2020008991A (es) | 2018-03-01 | 2020-12-10 | Regeneron Pharma | Metodos para alterar la composicion corporal. |
| EP4638496A1 (en) | 2022-12-22 | 2025-10-29 | Scholar Rock, Inc. | Selective and potent inhibitory antibodies of myostatin activation |
Family Cites Families (28)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5977438A (en) | 1988-02-26 | 1999-11-02 | Biosource Technologies, Inc. | Production of peptides in plants as viral coat protein fusions |
| CA2014033C (en) | 1989-04-07 | 1993-02-09 | Stephen D. Acres | Compositions and treatments for pneumonia in animals |
| WO1993008290A1 (en) | 1991-10-16 | 1993-04-29 | University Of Saskatchewan | Enhanced immunogenicity using leukotoxin chimeras |
| US5422110A (en) | 1991-10-16 | 1995-06-06 | University Of Saskatchewan | Enhanced immunogenicity using leukotoxin chimeras |
| DK0690873T3 (da) | 1993-03-19 | 2003-09-29 | Univ Johns Hopkins Med | Vækstdifferentieringsfaktor-8 |
| US6607884B1 (en) | 1993-03-19 | 2003-08-19 | The Johns Hopkins University School Of Medicine | Methods of detecting growth differentiation factor-8 |
| US20030074680A1 (en) | 1993-03-19 | 2003-04-17 | Johns Hopkins University School Of Medicine | Growth differentiation factor-8 |
| US5994618A (en) | 1997-02-05 | 1999-11-30 | Johns Hopkins University School Of Medicine | Growth differentiation factor-8 transgenic mice |
| US6042832A (en) | 1996-08-28 | 2000-03-28 | Thomas Jefferson University | Polypeptides fused with alfalfa mosaic virus or ilarvirus capsid proteins |
| AU6274298A (en) | 1997-02-05 | 1998-08-25 | Johns Hopkins University School Of Medicine, The | Growth differentiation factor-8 |
| CA2279826A1 (en) | 1997-02-05 | 1998-08-13 | Biostar Inc. | Immunization against endogenous molecules |
| US6656475B1 (en) | 1997-08-01 | 2003-12-02 | The Johns Hopkins University School Of Medicine | Growth differentiation factor receptors, agonists and antagonists thereof, and methods of using same |
| GB2333706A (en) | 1998-02-02 | 1999-08-04 | Merck & Co Inc | Method for increasing muscle mass in animals |
| US6369201B1 (en) * | 1998-02-19 | 2002-04-09 | Metamorphix International, Inc. | Myostatin multimers |
| US6004937A (en) | 1998-03-09 | 1999-12-21 | Genetics Institute, Inc. | Use of follistatin to modulate growth and differentiation factor 8 [GDF-8] and bone morphogenic protein 11 [BMP-11] |
| JP4544742B2 (ja) * | 1998-05-06 | 2010-09-15 | メタモーフイクス・インコーポレーテツド | Ｇｄｆ−８の阻害による糖尿病の処置法 |
| US6284882B1 (en) | 1999-06-10 | 2001-09-04 | Abbott Laboratories | Myostatin gene promoter and inhibition of activation thereof |
| TR200400621T2 (tr) * | 1999-07-20 | 2004-08-23 | Pharmexa A/S | GDF-8 aktivitesinin aşağı doğru düzenlenmesi için bir yöntem. |
| US6617440B1 (en) | 1999-07-30 | 2003-09-09 | Pfizer, Inc. | Myostatin regulatory region, nucleotide sequence determination and methods for its use |
| EP1221961A4 (en) | 1999-10-13 | 2004-03-31 | Roswell Park Memorial Inst | INDUCTION OF A STRONG IMMUNE RESPONSE TO A TUMOR-RELATED SELF-ANTIGEN |
| US6730306B1 (en) | 2000-03-08 | 2004-05-04 | Large Scale Biology Corporation | Parvovirus vaccine as viral coat protein fusions |
| US7037501B2 (en) * | 2001-01-04 | 2006-05-02 | Regents Of The University Of Minnesota | Myostatin immnoconjugate |
| US7320789B2 (en) | 2001-09-26 | 2008-01-22 | Wyeth | Antibody inhibitors of GDF-8 and uses thereof |
| MXPA05006113A (es) | 2002-12-11 | 2005-09-30 | Pharmexa As | Epitopos sencillos objetivo. |
| BR0317538A (pt) | 2002-12-20 | 2005-11-29 | Amgen Inc | Agente ligante, sequência de polinucleotìdeo, vetor de expressão, célula hospedeira, composição farmacêutica, e, métodos de inibir a atividade de miostatina, de aumentar a massa muscular magra e a razão de massa muscular magra para gordura, de tratar uma doença de emaciação muscular e um distúrbio metabólico relacionado com miostatina em um indivìduo, de detectar e medir miostatina em uma amostra, e, de diagnosticar um distúrbio relacionado com miostatina em um indivìduo |
| EP1699820A2 (en) * | 2003-12-31 | 2006-09-13 | Schering-Plough Ltd. | Neutralizing epitope-based growth enhancing vaccine |
| US20060281075A1 (en) * | 2004-12-22 | 2006-12-14 | Large Scale Biology Corporation | Purification of viruses, proteins and nucleic acids |
| CA2594276A1 (en) | 2004-12-30 | 2006-07-13 | Schering-Plough Ltd. | Neutralizing epitope-based growth enhancing vaccine |
-
2004
- 2004-12-21 EP EP04815235A patent/EP1699820A2/en not_active Withdrawn
- 2004-12-21 RU RU2006127314/10A patent/RU2422460C2/ru not_active IP Right Cessation
- 2004-12-21 JP JP2006547309A patent/JP2007535912A/ja not_active Withdrawn
- 2004-12-21 BR BRPI0418317-7A patent/BRPI0418317A/pt not_active IP Right Cessation
- 2004-12-21 WO PCT/US2004/043125 patent/WO2005066204A2/en not_active Ceased
- 2004-12-21 SG SG200904421-5A patent/SG153874A1/en unknown
- 2004-12-21 UA UAA200608516A patent/UA93855C2/ru unknown
- 2004-12-21 US US11/019,001 patent/US7371726B2/en not_active Expired - Fee Related
- 2004-12-21 MX MXPA06007514A patent/MXPA06007514A/es active IP Right Grant
- 2004-12-21 NZ NZ547593A patent/NZ547593A/en not_active IP Right Cessation
- 2004-12-21 CA CA002551877A patent/CA2551877A1/en not_active Abandoned
- 2004-12-21 CN CNA2004800395458A patent/CN1902221A/zh active Pending
- 2004-12-21 AU AU2004312411A patent/AU2004312411B8/en not_active Ceased
- 2004-12-21 KR KR1020067013214A patent/KR20060120229A/ko not_active Abandoned
- 2004-12-22 TW TW093140145A patent/TWI357906B/zh not_active IP Right Cessation
- 2004-12-22 AR ARP040104868A patent/AR047345A1/es active IP Right Grant
-
2005
- 2005-01-03 PE PE2005000029A patent/PE20051050A1/es not_active Application Discontinuation
-
2006
- 2006-06-22 IL IL176494A patent/IL176494A0/en unknown
- 2006-06-23 ZA ZA200605227A patent/ZA200605227B/xx unknown
- 2006-06-29 EC EC2006006683A patent/ECSP066683A/es unknown
- 2006-07-28 NO NO20063478A patent/NO20063478L/no not_active Application Discontinuation
-
2008
- 2008-04-02 US US12/061,012 patent/US7585648B2/en not_active Expired - Fee Related
-
2009
- 2009-08-04 US US12/535,298 patent/US7892561B2/en not_active Expired - Fee Related
-
2011
- 2011-01-20 JP JP2011010279A patent/JP2011083290A/ja active Pending
Also Published As
| Publication number | Publication date |
|---|---|
| WO2005066204A3 (en) | 2005-08-11 |
| WO2005066204A2 (en) | 2005-07-21 |
| CN1902221A (zh) | 2007-01-24 |
| BRPI0418317A (pt) | 2007-05-02 |
| TWI357906B (en) | 2012-02-11 |
| IL176494A0 (en) | 2006-10-05 |
| AU2004312411B2 (en) | 2011-11-03 |
| AU2004312411A1 (en) | 2005-07-21 |
| PE20051050A1 (es) | 2005-12-12 |
| UA93855C2 (ru) | 2011-03-25 |
| NZ547593A (en) | 2009-09-25 |
| RU2006127314A (ru) | 2008-02-10 |
| EP1699820A2 (en) | 2006-09-13 |
| KR20060120229A (ko) | 2006-11-24 |
| ZA200605227B (en) | 2007-03-28 |
| US7371726B2 (en) | 2008-05-13 |
| US20050143306A1 (en) | 2005-06-30 |
| ECSP066683A (es) | 2006-10-25 |
| AR047345A1 (es) | 2006-01-18 |
| US7892561B2 (en) | 2011-02-22 |
| AU2004312411B8 (en) | 2011-11-24 |
| US20090311282A1 (en) | 2009-12-17 |
| US7585648B2 (en) | 2009-09-08 |
| JP2011083290A (ja) | 2011-04-28 |
| US20080227156A1 (en) | 2008-09-18 |
| JP2007535912A (ja) | 2007-12-13 |
| TW200526683A (en) | 2005-08-16 |
| RU2422460C2 (ru) | 2011-06-27 |
| CA2551877A1 (en) | 2005-07-21 |
| NO20063478L (no) | 2006-08-28 |
| SG153874A1 (en) | 2009-07-29 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US7892561B2 (en) | Neutralizing GDF8 epitope-based growth enhancing vaccine | |
| CN1191491A (zh) | 结缔组织生长因子 | |
| JP2001512492A (ja) | Ｌｓｒ受容体、その活性、そのクローニングならびにその肥満および関連する危険性または合併症の診断、予防および／または治療への応用 | |
| US20010006942A1 (en) | Chemokine receptor peptide vaccines for treatment and prevention of diabetes | |
| US9493519B2 (en) | Toxin in type A Clostridium perfringens | |
| US20090208522A1 (en) | Neutralizing Epitope-Based Growth Enhancing Vaccine | |
| WO1995017205A1 (en) | Recombinant human thymopoietin proteins and uses therefor | |
| EA010405B1 (ru) | Семейство секретируемых белков | |
| KR20060129229A (ko) | 표면에 위치한 빈창자캄필로박터 폴리펩티드 | |
| JP2003501013A (ja) | ローソニア由来の遺伝子及び関連ＳｏｄＣポリペプチド、ぺプチド及びタンパク質並びにそれらの使用 | |
| JP2003520594A (ja) | 精子特異的タンパク質 | |
| Rodríguez et al. | Neutralization of black widow spider (Latrodectus mactans) venom with rabbit polyclonal serum hyperimmunized with recombinant alpha-latrotoxin fragments | |
| Seabrook et al. | Recognition of pertussis toxin by antibodies to synthetic peptides | |
| CN1287171A (zh) | 人神经元钙传感蛋白及其编码序列、以及制法和用途 | |
| US20020098546A1 (en) | Canine TAg1 proteins, nucleic acid molecules, and uses thereof | |
| CN1120315A (zh) | 溶组织内阿米巴粘附外源凝集素的35/31千道尔顿亚基 | |
| CN1289848A (zh) | 一种人白介素增强子结合因子蛋白异构体及其编码序列 | |
| CN1281895A (zh) | 一种人线粒体溶质载体蛋白异构体及其编码序列 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FG | Grant or registration |