CA2857721C - Pdgf receptor beta binding polypeptides - Google Patents
Pdgf receptor beta binding polypeptides Download PDFInfo
- Publication number
- CA2857721C CA2857721C CA2857721A CA2857721A CA2857721C CA 2857721 C CA2857721 C CA 2857721C CA 2857721 A CA2857721 A CA 2857721A CA 2857721 A CA2857721 A CA 2857721A CA 2857721 C CA2857721 C CA 2857721C
- Authority
- CA
- Canada
- Prior art keywords
- amino acid
- binding
- seq
- binding polypeptide
- set forth
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 230000027455 binding Effects 0.000 title claims abstract description 246
- 108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 169
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 167
- 229920001184 polypeptide Polymers 0.000 title claims abstract description 164
- 108091008606 PDGF receptors Proteins 0.000 title description 18
- 102000011653 Platelet-Derived Growth Factor Receptors Human genes 0.000 title description 18
- 238000000034 method Methods 0.000 claims abstract description 63
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims abstract description 57
- 201000010099 disease Diseases 0.000 claims abstract description 33
- 239000013604 expression vector Substances 0.000 claims abstract description 19
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 19
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 18
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 18
- 239000008194 pharmaceutical composition Substances 0.000 claims abstract description 13
- 238000003259 recombinant expression Methods 0.000 claims abstract description 8
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 98
- 208000035475 disorder Diseases 0.000 claims description 24
- 230000000694 effects Effects 0.000 claims description 19
- 206010064930 age-related macular degeneration Diseases 0.000 claims description 15
- 208000002780 macular degeneration Diseases 0.000 claims description 15
- 239000000203 mixture Substances 0.000 claims description 15
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 claims description 12
- 206010028980 Neoplasm Diseases 0.000 claims description 8
- 239000003446 ligand Substances 0.000 claims description 7
- 230000003042 antagnostic effect Effects 0.000 claims description 5
- 201000011510 cancer Diseases 0.000 claims description 5
- 239000003937 drug carrier Substances 0.000 claims description 5
- 238000006471 dimerization reaction Methods 0.000 claims description 4
- 238000002844 melting Methods 0.000 claims description 4
- 230000008018 melting Effects 0.000 claims description 4
- 101000692455 Homo sapiens Platelet-derived growth factor receptor beta Proteins 0.000 claims description 3
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 claims description 3
- 230000026731 phosphorylation Effects 0.000 claims description 3
- 238000006366 phosphorylation reaction Methods 0.000 claims description 3
- 102100026547 Platelet-derived growth factor receptor beta Human genes 0.000 claims description 2
- 238000012258 culturing Methods 0.000 claims description 2
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 claims description 2
- 101000692457 Mus musculus Platelet-derived growth factor receptor beta Proteins 0.000 claims 1
- 244000126002 Ziziphus vulgaris Species 0.000 claims 1
- 102000047790 human PDGFRB Human genes 0.000 claims 1
- 239000012634 fragment Substances 0.000 abstract description 61
- 239000000427 antigen Substances 0.000 abstract description 59
- 108091007433 antigens Proteins 0.000 abstract description 59
- 102000036639 antigens Human genes 0.000 abstract description 59
- 210000004027 cell Anatomy 0.000 description 69
- 108090000623 proteins and genes Proteins 0.000 description 35
- 238000006467 substitution reaction Methods 0.000 description 31
- 238000011282 treatment Methods 0.000 description 29
- 108020004414 DNA Proteins 0.000 description 26
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 25
- 241000699666 Mus <mouse, genus> Species 0.000 description 24
- 239000013598 vector Substances 0.000 description 22
- 102000004169 proteins and genes Human genes 0.000 description 21
- 239000000243 solution Substances 0.000 description 18
- 108010038512 Platelet-Derived Growth Factor Proteins 0.000 description 17
- 102000010780 Platelet-Derived Growth Factor Human genes 0.000 description 17
- 101100112922 Candida albicans CDR3 gene Proteins 0.000 description 16
- 239000003814 drug Substances 0.000 description 15
- 238000000746 purification Methods 0.000 description 15
- 150000001413 amino acids Chemical class 0.000 description 14
- -1 antibodies Proteins 0.000 description 11
- 238000000338 in vitro Methods 0.000 description 11
- 230000001225 therapeutic effect Effects 0.000 description 11
- 239000012636 effector Substances 0.000 description 10
- 230000006870 function Effects 0.000 description 10
- 230000013595 glycosylation Effects 0.000 description 10
- 238000006206 glycosylation reaction Methods 0.000 description 10
- 102000005962 receptors Human genes 0.000 description 10
- 108020003175 receptors Proteins 0.000 description 10
- 230000002829 reductive effect Effects 0.000 description 10
- 125000000539 amino acid group Chemical group 0.000 description 9
- 238000003556 assay Methods 0.000 description 9
- 230000005012 migration Effects 0.000 description 9
- 238000013508 migration Methods 0.000 description 9
- 239000013612 plasmid Substances 0.000 description 9
- 239000013615 primer Substances 0.000 description 9
- 229940079593 drug Drugs 0.000 description 8
- 238000002360 preparation method Methods 0.000 description 8
- 230000000069 prophylactic effect Effects 0.000 description 8
- 102100026120 IgG receptor FcRn large subunit p51 Human genes 0.000 description 7
- 101710177940 IgG receptor FcRn large subunit p51 Proteins 0.000 description 7
- 108091034117 Oligonucleotide Proteins 0.000 description 7
- 238000004458 analytical method Methods 0.000 description 7
- 230000000295 complement effect Effects 0.000 description 7
- 238000001727 in vivo Methods 0.000 description 7
- 238000002347 injection Methods 0.000 description 7
- 239000007924 injection Substances 0.000 description 7
- 108020004999 messenger RNA Proteins 0.000 description 7
- 238000000159 protein binding assay Methods 0.000 description 7
- 210000002966 serum Anatomy 0.000 description 7
- 229940124597 therapeutic agent Drugs 0.000 description 7
- 230000014616 translation Effects 0.000 description 7
- 241000894006 Bacteria Species 0.000 description 6
- 102000009109 Fc receptors Human genes 0.000 description 6
- 108010087819 Fc receptors Proteins 0.000 description 6
- 241001465754 Metazoa Species 0.000 description 6
- 108091028043 Nucleic acid sequence Proteins 0.000 description 6
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 6
- 108010029485 Protein Isoforms Proteins 0.000 description 6
- 102000001708 Protein Isoforms Human genes 0.000 description 6
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 6
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 238000004113 cell culture Methods 0.000 description 6
- 238000010276 construction Methods 0.000 description 6
- 210000002950 fibroblast Anatomy 0.000 description 6
- 230000004927 fusion Effects 0.000 description 6
- 108020001507 fusion proteins Proteins 0.000 description 6
- 102000037865 fusion proteins Human genes 0.000 description 6
- 238000011534 incubation Methods 0.000 description 6
- 238000001990 intravenous administration Methods 0.000 description 6
- 238000004519 manufacturing process Methods 0.000 description 6
- 239000003550 marker Substances 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 210000003668 pericyte Anatomy 0.000 description 6
- 230000002441 reversible effect Effects 0.000 description 6
- 238000013519 translation Methods 0.000 description 6
- 102000053602 DNA Human genes 0.000 description 5
- 238000012286 ELISA Assay Methods 0.000 description 5
- 210000001744 T-lymphocyte Anatomy 0.000 description 5
- 241000700605 Viruses Species 0.000 description 5
- 230000004913 activation Effects 0.000 description 5
- 239000011324 bead Substances 0.000 description 5
- 230000037396 body weight Effects 0.000 description 5
- 239000003795 chemical substances by application Substances 0.000 description 5
- 238000001514 detection method Methods 0.000 description 5
- 210000003734 kidney Anatomy 0.000 description 5
- 229920001223 polyethylene glycol Polymers 0.000 description 5
- 238000012216 screening Methods 0.000 description 5
- 210000001519 tissue Anatomy 0.000 description 5
- 231100000765 toxin Toxicity 0.000 description 5
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 4
- 108010081589 Becaplermin Proteins 0.000 description 4
- 102000004190 Enzymes Human genes 0.000 description 4
- 108090000790 Enzymes Proteins 0.000 description 4
- 238000012408 PCR amplification Methods 0.000 description 4
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 4
- 230000001580 bacterial effect Effects 0.000 description 4
- 230000004071 biological effect Effects 0.000 description 4
- 230000003247 decreasing effect Effects 0.000 description 4
- 239000006185 dispersion Substances 0.000 description 4
- 238000010494 dissociation reaction Methods 0.000 description 4
- 230000005593 dissociations Effects 0.000 description 4
- 229940088598 enzyme Drugs 0.000 description 4
- 230000005847 immunogenicity Effects 0.000 description 4
- 230000005764 inhibitory process Effects 0.000 description 4
- 230000004807 localization Effects 0.000 description 4
- 244000005700 microbiome Species 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 239000000126 substance Substances 0.000 description 4
- 208000024891 symptom Diseases 0.000 description 4
- 239000003981 vehicle Substances 0.000 description 4
- 101100175449 Arabidopsis thaliana GILP gene Proteins 0.000 description 3
- 241000699802 Cricetulus griseus Species 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 102000016359 Fibronectins Human genes 0.000 description 3
- 108010067306 Fibronectins Proteins 0.000 description 3
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 102000016844 Immunoglobulin-like domains Human genes 0.000 description 3
- 108050006430 Immunoglobulin-like domains Proteins 0.000 description 3
- 108020004684 Internal Ribosome Entry Sites Proteins 0.000 description 3
- 241000124008 Mammalia Species 0.000 description 3
- 241001529936 Murinae Species 0.000 description 3
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 3
- 239000007864 aqueous solution Substances 0.000 description 3
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 3
- 210000001185 bone marrow Anatomy 0.000 description 3
- 210000004556 brain Anatomy 0.000 description 3
- 230000012292 cell migration Effects 0.000 description 3
- 230000007423 decrease Effects 0.000 description 3
- 239000008121 dextrose Substances 0.000 description 3
- 238000003384 imaging method Methods 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 238000002649 immunization Methods 0.000 description 3
- 239000004615 ingredient Substances 0.000 description 3
- 238000001361 intraarterial administration Methods 0.000 description 3
- 238000007918 intramuscular administration Methods 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 231100000252 nontoxic Toxicity 0.000 description 3
- 230000003000 nontoxic effect Effects 0.000 description 3
- 239000001048 orange dye Substances 0.000 description 3
- 239000002245 particle Substances 0.000 description 3
- 239000000843 powder Substances 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- 239000000651 prodrug Substances 0.000 description 3
- 229940002612 prodrug Drugs 0.000 description 3
- 230000010076 replication Effects 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 238000003998 size exclusion chromatography high performance liquid chromatography Methods 0.000 description 3
- 238000007920 subcutaneous administration Methods 0.000 description 3
- 239000003053 toxin Substances 0.000 description 3
- 108700012359 toxins Proteins 0.000 description 3
- 230000009466 transformation Effects 0.000 description 3
- 210000004881 tumor cell Anatomy 0.000 description 3
- 241001430294 unidentified retrovirus Species 0.000 description 3
- 230000002792 vascular Effects 0.000 description 3
- 239000013603 viral vector Substances 0.000 description 3
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- 230000003442 weekly effect Effects 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical compound COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 2
- 229920000936 Agarose Polymers 0.000 description 2
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 2
- 208000017667 Chronic Disease Diseases 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- 238000002965 ELISA Methods 0.000 description 2
- 108010093488 His-His-His-His-His-His Proteins 0.000 description 2
- 108060003951 Immunoglobulin Proteins 0.000 description 2
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 2
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 2
- 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 2
- UDCDOJQOXWCCSD-UHFFFAOYSA-N N,N-dimethyl-N'-p-tolylsulfamide Chemical compound CN(C)S(=O)(=O)NC1=CC=C(C)C=C1 UDCDOJQOXWCCSD-UHFFFAOYSA-N 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 239000002202 Polyethylene glycol Substances 0.000 description 2
- 108010076504 Protein Sorting Signals Proteins 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 238000010521 absorption reaction Methods 0.000 description 2
- 230000021736 acetylation Effects 0.000 description 2
- 238000006640 acetylation reaction Methods 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 239000004480 active ingredient Substances 0.000 description 2
- 239000013543 active substance Substances 0.000 description 2
- 238000001261 affinity purification Methods 0.000 description 2
- 230000004075 alteration Effects 0.000 description 2
- 239000005557 antagonist Substances 0.000 description 2
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 230000009831 antigen interaction Effects 0.000 description 2
- 230000001363 autoimmune Effects 0.000 description 2
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- 238000013357 binding ELISA Methods 0.000 description 2
- 239000012148 binding buffer Substances 0.000 description 2
- 230000015572 biosynthetic process Effects 0.000 description 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- 230000004663 cell proliferation Effects 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- OSASVXMJTNOKOY-UHFFFAOYSA-N chlorobutanol Chemical compound CC(C)(O)C(Cl)(Cl)Cl OSASVXMJTNOKOY-UHFFFAOYSA-N 0.000 description 2
- 238000004587 chromatography analysis Methods 0.000 description 2
- 239000002299 complementary DNA Substances 0.000 description 2
- 150000001875 compounds Chemical class 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 230000009089 cytolysis Effects 0.000 description 2
- 231100000433 cytotoxic Toxicity 0.000 description 2
- 231100000599 cytotoxic agent Toxicity 0.000 description 2
- 230000001472 cytotoxic effect Effects 0.000 description 2
- 239000002619 cytotoxin Substances 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 239000003085 diluting agent Substances 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 239000002612 dispersion medium Substances 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 239000012530 fluid Substances 0.000 description 2
- 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 2
- 210000003953 foreskin Anatomy 0.000 description 2
- 210000004602 germ cell Anatomy 0.000 description 2
- 150000004676 glycans Chemical class 0.000 description 2
- 102000018358 immunoglobulin Human genes 0.000 description 2
- 239000000367 immunologic factor Substances 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 238000004255 ion exchange chromatography Methods 0.000 description 2
- 238000002955 isolation Methods 0.000 description 2
- 230000000670 limiting effect Effects 0.000 description 2
- 150000002632 lipids Chemical class 0.000 description 2
- 239000006166 lysate Substances 0.000 description 2
- 230000005291 magnetic effect Effects 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 229910021645 metal ion Inorganic materials 0.000 description 2
- 238000010232 migration assay Methods 0.000 description 2
- 210000005170 neoplastic cell Anatomy 0.000 description 2
- 230000001613 neoplastic effect Effects 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 238000007911 parenteral administration Methods 0.000 description 2
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 2
- 239000008177 pharmaceutical agent Substances 0.000 description 2
- 239000008363 phosphate buffer Substances 0.000 description 2
- 239000003755 preservative agent Substances 0.000 description 2
- 230000002265 prevention Effects 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 230000002035 prolonged effect Effects 0.000 description 2
- 239000012857 radioactive material Substances 0.000 description 2
- 238000003127 radioimmunoassay Methods 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 230000002207 retinal effect Effects 0.000 description 2
- 102200072304 rs1057519530 Human genes 0.000 description 2
- 239000012679 serum free medium Substances 0.000 description 2
- 239000002904 solvent Substances 0.000 description 2
- 230000009870 specific binding Effects 0.000 description 2
- 239000004094 surface-active agent Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 238000013268 sustained release Methods 0.000 description 2
- 239000012730 sustained-release form Substances 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 230000004797 therapeutic response Effects 0.000 description 2
- 230000000699 topical effect Effects 0.000 description 2
- 231100000331 toxic Toxicity 0.000 description 2
- 230000002588 toxic effect Effects 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- 210000005166 vasculature Anatomy 0.000 description 2
- IIZPXYDJLKNOIY-JXPKJXOSSA-N 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC IIZPXYDJLKNOIY-JXPKJXOSSA-N 0.000 description 1
- PNDPGZBMCMUPRI-HVTJNCQCSA-N 10043-66-0 Chemical compound [131I][131I] PNDPGZBMCMUPRI-HVTJNCQCSA-N 0.000 description 1
- UAIUNKRWKOVEES-UHFFFAOYSA-N 3,3',5,5'-tetramethylbenzidine Chemical compound CC1=C(N)C(C)=CC(C=2C=C(C)C(N)=C(C)C=2)=C1 UAIUNKRWKOVEES-UHFFFAOYSA-N 0.000 description 1
- FVFVNNKYKYZTJU-UHFFFAOYSA-N 6-chloro-1,3,5-triazine-2,4-diamine Chemical compound NC1=NC(N)=NC(Cl)=N1 FVFVNNKYKYZTJU-UHFFFAOYSA-N 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
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 102000012440 Acetylcholinesterase Human genes 0.000 description 1
- 108010022752 Acetylcholinesterase Proteins 0.000 description 1
- 206010001052 Acute respiratory distress syndrome Diseases 0.000 description 1
- 108010000239 Aequorin Proteins 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 101100503323 Artemisia annua FPS1 gene Proteins 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 241001112741 Bacillaceae Species 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- 241000701822 Bovine papillomavirus Species 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 208000005590 Choroidal Neovascularization Diseases 0.000 description 1
- 206010060823 Choroidal neovascularisation Diseases 0.000 description 1
- 108091026890 Coding region Proteins 0.000 description 1
- RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 1
- 206010055665 Corneal neovascularisation Diseases 0.000 description 1
- 201000000054 Coronary Restenosis Diseases 0.000 description 1
- 201000000057 Coronary Stenosis Diseases 0.000 description 1
- 206010056489 Coronary artery restenosis Diseases 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 101710112752 Cytotoxin Proteins 0.000 description 1
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 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
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 1
- FBPFZTCFMRRESA-JGWLITMVSA-N D-glucitol Chemical compound OC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-JGWLITMVSA-N 0.000 description 1
- GUBGYTABKSRVRQ-WFVLMXAXSA-N DEAE-cellulose Chemical compound OC1C(O)C(O)C(CO)O[C@H]1O[C@@H]1C(CO)OC(O)C(O)C1O GUBGYTABKSRVRQ-WFVLMXAXSA-N 0.000 description 1
- 230000004544 DNA amplification Effects 0.000 description 1
- 239000003155 DNA primer Substances 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- 230000006820 DNA synthesis Effects 0.000 description 1
- XPDXVDYUQZHFPV-UHFFFAOYSA-N Dansyl Chloride Chemical compound C1=CC=C2C(N(C)C)=CC=CC2=C1S(Cl)(=O)=O XPDXVDYUQZHFPV-UHFFFAOYSA-N 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
- 241000702421 Dependoparvovirus Species 0.000 description 1
- 108700022150 Designed Ankyrin Repeat Proteins Proteins 0.000 description 1
- 102100024746 Dihydrofolate reductase Human genes 0.000 description 1
- 102000016607 Diphtheria Toxin Human genes 0.000 description 1
- 108010053187 Diphtheria Toxin Proteins 0.000 description 1
- LVGKNOAMLMIIKO-UHFFFAOYSA-N Elaidinsaeure-aethylester Natural products CCCCCCCCC=CCCCCCCCC(=O)OCC LVGKNOAMLMIIKO-UHFFFAOYSA-N 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000588921 Enterobacteriaceae Species 0.000 description 1
- 239000004593 Epoxy Substances 0.000 description 1
- 108010008177 Fd immunoglobulins Proteins 0.000 description 1
- 206010016654 Fibrosis Diseases 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
- 241000233866 Fungi Species 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 108700004714 Gelonium multiflorum GEL Proteins 0.000 description 1
- 101100503326 Gibberella fujikuroi FPPS gene Proteins 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 241000606768 Haemophilus influenzae Species 0.000 description 1
- 101710154606 Hemagglutinin Proteins 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 101001030232 Homo sapiens Myosin-9 Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 102000008100 Human Serum Albumin Human genes 0.000 description 1
- 108091006905 Human Serum Albumin Proteins 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 1
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 1
- SHZGCJCMOBCMKK-DHVFOXMCSA-N L-fucopyranose Chemical group C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O SHZGCJCMOBCMKK-DHVFOXMCSA-N 0.000 description 1
- 102000019298 Lipocalin Human genes 0.000 description 1
- 108050006654 Lipocalin Proteins 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 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
- 102000008072 Lymphokines Human genes 0.000 description 1
- 108010074338 Lymphokines Proteins 0.000 description 1
- 229930195725 Mannitol Natural products 0.000 description 1
- 241000713333 Mouse mammary tumor virus Species 0.000 description 1
- 101100519722 Mus musculus Pdgfrb gene Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 102100038938 Myosin-9 Human genes 0.000 description 1
- 230000004988 N-glycosylation Effects 0.000 description 1
- 108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 1
- 206010029113 Neovascularisation Diseases 0.000 description 1
- 108091093105 Nuclear DNA Proteins 0.000 description 1
- 101710093908 Outer capsid protein VP4 Proteins 0.000 description 1
- 101710135467 Outer capsid protein sigma-1 Proteins 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 206010072557 Peripheral artery restenosis Diseases 0.000 description 1
- 108010004729 Phycoerythrin Proteins 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 102000001393 Platelet-Derived Growth Factor alpha Receptor Human genes 0.000 description 1
- 108010068588 Platelet-Derived Growth Factor alpha Receptor Proteins 0.000 description 1
- 102000018967 Platelet-Derived Growth Factor beta Receptor Human genes 0.000 description 1
- 108010051742 Platelet-Derived Growth Factor beta Receptor Proteins 0.000 description 1
- 101710164680 Platelet-derived growth factor receptor beta Proteins 0.000 description 1
- 241001505332 Polyomavirus sp. Species 0.000 description 1
- 101710176177 Protein A56 Proteins 0.000 description 1
- 102000004022 Protein-Tyrosine Kinases Human genes 0.000 description 1
- 108090000412 Protein-Tyrosine Kinases Proteins 0.000 description 1
- 101000762949 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) Exotoxin A Proteins 0.000 description 1
- 208000013616 Respiratory Distress Syndrome Diseases 0.000 description 1
- 108010039491 Ricin Proteins 0.000 description 1
- 241000235070 Saccharomyces Species 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 206010039710 Scleroderma Diseases 0.000 description 1
- 244000309493 Soybean severe stunt virus Species 0.000 description 1
- 108010090804 Streptavidin Proteins 0.000 description 1
- 241000194017 Streptococcus Species 0.000 description 1
- 206010051379 Systemic Inflammatory Response Syndrome Diseases 0.000 description 1
- 101150006914 TRP1 gene Proteins 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 241000700618 Vaccinia virus Species 0.000 description 1
- 101150003160 X gene Proteins 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 229940022698 acetylcholinesterase Drugs 0.000 description 1
- 239000008186 active pharmaceutical agent Substances 0.000 description 1
- 230000009692 acute damage Effects 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 208000011341 adult acute respiratory distress syndrome Diseases 0.000 description 1
- 201000000028 adult respiratory distress syndrome Diseases 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 238000004220 aggregation Methods 0.000 description 1
- 230000001476 alcoholic effect Effects 0.000 description 1
- 208000026935 allergic disease Diseases 0.000 description 1
- 230000009435 amidation Effects 0.000 description 1
- 238000007112 amidation reaction Methods 0.000 description 1
- 238000002399 angioplasty Methods 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 230000000844 anti-bacterial effect Effects 0.000 description 1
- 230000003466 anti-cipated effect Effects 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 230000000259 anti-tumor effect Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 229940121375 antifungal agent Drugs 0.000 description 1
- 239000003429 antifungal agent Substances 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 235000006708 antioxidants Nutrition 0.000 description 1
- 239000008365 aqueous carrier Substances 0.000 description 1
- 239000003125 aqueous solvent Substances 0.000 description 1
- 229960005070 ascorbic acid Drugs 0.000 description 1
- 235000010323 ascorbic acid Nutrition 0.000 description 1
- 239000011668 ascorbic acid Substances 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 238000010256 biochemical assay Methods 0.000 description 1
- 230000003115 biocidal effect Effects 0.000 description 1
- 239000003139 biocide Substances 0.000 description 1
- 230000008512 biological response Effects 0.000 description 1
- 239000003131 biological toxin Substances 0.000 description 1
- 230000000903 blocking effect Effects 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 230000036765 blood level Effects 0.000 description 1
- 238000010322 bone marrow transplantation Methods 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 239000001506 calcium phosphate Substances 0.000 description 1
- 229910000389 calcium phosphate Inorganic materials 0.000 description 1
- 235000011010 calcium phosphates Nutrition 0.000 description 1
- BPKIGYQJPYCAOW-FFJTTWKXSA-I calcium;potassium;disodium;(2s)-2-hydroxypropanoate;dichloride;dihydroxide;hydrate Chemical compound O.[OH-].[OH-].[Na+].[Na+].[Cl-].[Cl-].[K+].[Ca+2].C[C@H](O)C([O-])=O BPKIGYQJPYCAOW-FFJTTWKXSA-I 0.000 description 1
- 230000030833 cell death Effects 0.000 description 1
- 230000007910 cell fusion Effects 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000000919 ceramic Substances 0.000 description 1
- 208000019065 cervical carcinoma Diseases 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 239000002975 chemoattractant Substances 0.000 description 1
- 238000002512 chemotherapy Methods 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 229960004926 chlorobutanol Drugs 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 239000007979 citrate buffer Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000003759 clinical diagnosis Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 230000004154 complement system Effects 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 229910052802 copper Inorganic materials 0.000 description 1
- 239000010949 copper Substances 0.000 description 1
- 201000000159 corneal neovascularization Diseases 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 239000000824 cytostatic agent Substances 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 230000001934 delay Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 230000001627 detrimental effect Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- UQLDLKMNUJERMK-UHFFFAOYSA-L di(octadecanoyloxy)lead Chemical compound [Pb+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O UQLDLKMNUJERMK-UHFFFAOYSA-L 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 239000000032 diagnostic agent Substances 0.000 description 1
- 229940039227 diagnostic agent Drugs 0.000 description 1
- 238000002059 diagnostic imaging Methods 0.000 description 1
- 108020001096 dihydrofolate reductase Proteins 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
- 239000002552 dosage form Substances 0.000 description 1
- 239000003792 electrolyte Substances 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 238000010828 elution Methods 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 238000003366 endpoint assay Methods 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 239000003623 enhancer Substances 0.000 description 1
- 230000007613 environmental effect Effects 0.000 description 1
- 210000000981 epithelium Anatomy 0.000 description 1
- 108010002591 epsilon receptor Proteins 0.000 description 1
- LVGKNOAMLMIIKO-QXMHVHEDSA-N ethyl oleate Chemical compound CCCCCCCC\C=C/CCCCCCCC(=O)OCC LVGKNOAMLMIIKO-QXMHVHEDSA-N 0.000 description 1
- 229940093471 ethyl oleate Drugs 0.000 description 1
- 210000003527 eukaryotic cell Anatomy 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 230000004761 fibrosis Effects 0.000 description 1
- 230000009795 fibrotic process Effects 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- MHMNJMPURVTYEJ-UHFFFAOYSA-N fluorescein-5-isothiocyanate Chemical compound O1C(=O)C2=CC(N=C=S)=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 MHMNJMPURVTYEJ-UHFFFAOYSA-N 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 230000022244 formylation Effects 0.000 description 1
- 238000006170 formylation reaction Methods 0.000 description 1
- 238000010230 functional analysis Methods 0.000 description 1
- 239000007789 gas Substances 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 229920000159 gelatin Polymers 0.000 description 1
- 235000019322 gelatine Nutrition 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 230000012010 growth Effects 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 229940047650 haemophilus influenzae Drugs 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 239000012510 hollow fiber Substances 0.000 description 1
- 235000003642 hunger Nutrition 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000009610 hypersensitivity Effects 0.000 description 1
- 210000002865 immune cell Anatomy 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000003018 immunoassay Methods 0.000 description 1
- 230000002163 immunogen Effects 0.000 description 1
- 230000016784 immunoglobulin production Effects 0.000 description 1
- 238000003364 immunohistochemistry Methods 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 230000002779 inactivation Effects 0.000 description 1
- 210000003000 inclusion body Anatomy 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 230000009405 individual cell migration Effects 0.000 description 1
- 239000011261 inert gas Substances 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 230000002757 inflammatory effect Effects 0.000 description 1
- 230000028709 inflammatory response Effects 0.000 description 1
- 206010022000 influenza Diseases 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000007972 injectable composition Substances 0.000 description 1
- 230000004068 intracellular signaling Effects 0.000 description 1
- 238000007917 intracranial administration Methods 0.000 description 1
- 238000010255 intramuscular injection Methods 0.000 description 1
- 239000007927 intramuscular injection Substances 0.000 description 1
- 230000005865 ionizing radiation Effects 0.000 description 1
- 230000001788 irregular Effects 0.000 description 1
- 239000007951 isotonicity adjuster Substances 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 230000003902 lesion Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 210000004185 liver Anatomy 0.000 description 1
- HWYHZTIRURJOHG-UHFFFAOYSA-N luminol Chemical compound O=C1NNC(=O)C2=C1C(N)=CC=C2 HWYHZTIRURJOHG-UHFFFAOYSA-N 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 238000012423 maintenance Methods 0.000 description 1
- 239000000594 mannitol Substances 0.000 description 1
- 235000010355 mannitol Nutrition 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 238000002483 medication Methods 0.000 description 1
- 239000002609 medium Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- 239000011325 microbead Substances 0.000 description 1
- 239000003094 microcapsule Substances 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 239000003226 mitogen Substances 0.000 description 1
- 230000002297 mitogenic effect Effects 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 210000005087 mononuclear cell Anatomy 0.000 description 1
- 238000010172 mouse model Methods 0.000 description 1
- 102000051367 mu Opioid Receptors Human genes 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- ZTLGJPIZUOVDMT-UHFFFAOYSA-N n,n-dichlorotriazin-4-amine Chemical compound ClN(Cl)C1=CC=NN=N1 ZTLGJPIZUOVDMT-UHFFFAOYSA-N 0.000 description 1
- 201000008383 nephritis Diseases 0.000 description 1
- 239000012457 nonaqueous media Substances 0.000 description 1
- 239000013631 noncovalent dimer Substances 0.000 description 1
- 239000000346 nonvolatile oil Substances 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 150000002482 oligosaccharides Polymers 0.000 description 1
- 239000004006 olive oil Substances 0.000 description 1
- 235000008390 olive oil Nutrition 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 150000002895 organic esters Chemical class 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000005298 paramagnetic effect Effects 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 230000006320 pegylation Effects 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 229960003742 phenol Drugs 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 230000004962 physiological condition Effects 0.000 description 1
- 230000035790 physiological processes and functions Effects 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 210000002826 placenta Anatomy 0.000 description 1
- 230000003169 placental effect Effects 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 229950008882 polysorbate Drugs 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 238000002600 positron emission tomography Methods 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000011533 pre-incubation Methods 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000004393 prognosis Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000002062 proliferating effect Effects 0.000 description 1
- 238000001243 protein synthesis Methods 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 210000001938 protoplast Anatomy 0.000 description 1
- 208000005069 pulmonary fibrosis Diseases 0.000 description 1
- 230000005855 radiation Effects 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 201000002793 renal fibrosis Diseases 0.000 description 1
- 208000037803 restenosis Diseases 0.000 description 1
- 210000001525 retina Anatomy 0.000 description 1
- 238000010839 reverse transcription Methods 0.000 description 1
- 238000003757 reverse transcription PCR Methods 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
- 238000013341 scale-up Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 239000004017 serum-free culture medium Substances 0.000 description 1
- 125000005629 sialic acid group Chemical group 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 230000037351 starvation Effects 0.000 description 1
- 230000001954 sterilising effect Effects 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 125000001424 substituent group Chemical group 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000005846 sugar alcohols Polymers 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 238000004114 suspension culture Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000012956 testing procedure Methods 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- RTKIYNMVFMVABJ-UHFFFAOYSA-L thimerosal Chemical compound [Na+].CC[Hg]SC1=CC=CC=C1C([O-])=O RTKIYNMVFMVABJ-UHFFFAOYSA-L 0.000 description 1
- 229940033663 thimerosal Drugs 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 230000002103 transcriptional effect Effects 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 238000012546 transfer Methods 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 230000004565 tumor cell growth Effects 0.000 description 1
- 229910052721 tungsten Inorganic materials 0.000 description 1
- 238000000108 ultra-filtration 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
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- 238000001291 vacuum drying Methods 0.000 description 1
- 238000009777 vacuum freeze-drying Methods 0.000 description 1
- 235000015112 vegetable and seed oil Nutrition 0.000 description 1
- 239000008158 vegetable oil Substances 0.000 description 1
- 210000002845 virion Anatomy 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 108020001612 μ-opioid receptors Proteins 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2863—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against receptors for growth factors, growth regulators
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/02—Ophthalmic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/475—Growth factors; Growth regulators
- C07K14/49—Platelet-derived growth factor [PDGF]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/71—Receptors; Cell surface antigens; Cell surface determinants for growth factors; for growth regulators
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/22—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against growth factors ; against growth regulators
-
- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/10—Processes for the isolation, preparation or purification of DNA or RNA
- C12N15/1034—Isolating an individual clone by screening libraries
- C12N15/1093—General methods of preparing gene libraries, not provided for in other subgroups
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P21/00—Preparation of peptides or proteins
- C12P21/005—Glycopeptides, glycoproteins
-
- 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
- A61K2039/505—Medicinal preparations containing antigens or antibodies comprising antibodies
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/60—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments
- C07K2317/62—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising only variable region components
- C07K2317/622—Single chain antibody (scFv)
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/76—Antagonist effect on antigen, e.g. neutralization or inhibition of binding
-
- 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
- C07K2317/92—Affinity (KD), association rate (Ka), dissociation rate (Kd) or EC50 value
-
- 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
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Immunology (AREA)
- Zoology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Biomedical Technology (AREA)
- Microbiology (AREA)
- Cell Biology (AREA)
- Crystallography & Structural Chemistry (AREA)
- Physics & Mathematics (AREA)
- Bioinformatics & Computational Biology (AREA)
- Plant Pathology (AREA)
- Ophthalmology & Optometry (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201161566778P | 2011-12-05 | 2011-12-05 | |
| US61/566,778 | 2011-12-05 | ||
| US201261610905P | 2012-03-14 | 2012-03-14 | |
| US61/610,905 | 2012-03-14 | ||
| PCT/US2012/067909 WO2013085972A1 (en) | 2011-12-05 | 2012-12-05 | Pdgf receptor beta binding polypeptides |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CA2857721A1 CA2857721A1 (en) | 2013-06-13 |
| CA2857721C true CA2857721C (en) | 2022-05-31 |
Family
ID=48574820
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2857721A Active CA2857721C (en) | 2011-12-05 | 2012-12-05 | Pdgf receptor beta binding polypeptides |
Country Status (9)
| Country | Link |
|---|---|
| US (4) | US9416179B2 (OSRAM) |
| EP (2) | EP3712173B1 (OSRAM) |
| JP (2) | JP6483442B2 (OSRAM) |
| CN (2) | CN107353342B (OSRAM) |
| AU (1) | AU2012347972B2 (OSRAM) |
| CA (1) | CA2857721C (OSRAM) |
| ES (1) | ES2784131T3 (OSRAM) |
| TW (2) | TWI640537B (OSRAM) |
| WO (1) | WO2013085972A1 (OSRAM) |
Families Citing this family (35)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| HUE054836T2 (hu) | 2010-01-28 | 2021-10-28 | Eagle Pharmaceuticals Inc | Bendamusztin kiszerelései |
| EP3798236B1 (en) * | 2011-03-15 | 2022-08-10 | X-Body, Inc. | Antibody screening methods |
| AU2012347972B2 (en) * | 2011-12-05 | 2018-05-10 | X-Body, Inc. | PDGF receptor beta binding polypeptides |
| JP6224064B2 (ja) | 2012-03-20 | 2017-11-01 | イーグル・ファーマシューティカルズ・インコーポレーテッド | 低減された投与容量を必要とする患者におけるベンダムスチン応答性症状の治療方法 |
| HRP20240056T1 (hr) | 2012-03-20 | 2024-03-29 | Eagle Pharmaceuticals, Inc. | Formulacije bendamustina |
| WO2015109898A1 (zh) * | 2014-01-24 | 2015-07-30 | 上海恒瑞医药有限公司 | VEGF与PDGFRβ双特异性融合蛋白及其用途 |
| ES2800674T3 (es) * | 2014-03-21 | 2021-01-04 | X Body Inc | Polipéptidos biespecíficos de unión a antígeno |
| CN118772278A (zh) | 2017-06-02 | 2024-10-15 | 辉瑞公司 | Flt3的特异性抗体及其用途 |
| AU2019352482A1 (en) | 2018-10-05 | 2021-05-13 | Seoul National University R&Db Foundation | PDGF receptor antibody and use thereof |
| JP2020146300A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146318A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146316A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146305A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146315A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146304A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146301A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146307A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146317A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146298A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146309A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146310A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146297A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146306A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146302A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146311A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146299A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146314A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146312A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146308A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| JP2020146303A (ja) * | 2019-03-14 | 2020-09-17 | 株式会社三洋物産 | 遊技機 |
| AU2020308463A1 (en) | 2019-06-26 | 2022-02-17 | Ap Biosciences, Inc. | Antibodies for T-cell activation |
| JP7774293B2 (ja) * | 2019-07-24 | 2025-11-21 | 国立研究開発法人科学技術振興機構 | 抗体酵素の革新的製造技術 |
| TW202146453A (zh) * | 2020-02-28 | 2021-12-16 | 美商埃派斯進有限公司 | 抗sirpa抗體及其使用方法 |
| CN114369163B (zh) * | 2022-02-18 | 2024-02-23 | 中国科学技术大学 | 与人血小板衍生生长因子受体β结合的羊驼源纳米抗体 |
| CN117986337B (zh) * | 2024-02-02 | 2024-08-16 | 杭州御寿生物科技有限公司 | 一种提高免疫力的益生菌组合物以及在治疗疾病中的应用 |
Family Cites Families (90)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4741900A (en) | 1982-11-16 | 1988-05-03 | Cytogen Corporation | Antibody-metal ion complexes |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US5807715A (en) | 1984-08-27 | 1998-09-15 | The Board Of Trustees Of The Leland Stanford Junior University | Methods and transformed mammalian lymphocyte cells for producing functional antigen-binding protein including chimeric immunoglobulin |
| US5225539A (en) | 1986-03-27 | 1993-07-06 | Medical Research Council | Recombinant altered antibodies and methods of making altered antibodies |
| GB8607679D0 (en) | 1986-03-27 | 1986-04-30 | Winter G P | Recombinant dna product |
| EP0307434B2 (en) | 1987-03-18 | 1998-07-29 | Scotgen Biopharmaceuticals, Inc. | Altered antibodies |
| ATE120454T1 (de) | 1988-06-14 | 1995-04-15 | Cetus Oncology Corp | Kupplungsmittel und sterisch gehinderte, mit disulfid gebundene konjugate daraus. |
| US6780613B1 (en) | 1988-10-28 | 2004-08-24 | Genentech, Inc. | Growth hormone variants |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| IE63847B1 (en) | 1989-05-05 | 1995-06-14 | Res Dev Foundation | A novel antibody delivery system for biological response modifiers |
| US5460785A (en) | 1989-08-09 | 1995-10-24 | Rhomed Incorporated | Direct labeling of antibodies and other protein with metal ions |
| GB8928874D0 (en) | 1989-12-21 | 1990-02-28 | Celltech Ltd | Humanised antibodies |
| US5314995A (en) | 1990-01-22 | 1994-05-24 | Oncogen | Therapeutic interleukin-2-antibody based fusion proteins |
| JP3319594B2 (ja) | 1990-03-20 | 2002-09-03 | ザ・トラスティーズ・オブ・コランビア・ユニバーシティー・イン・ザ・シティー・オブ・ニューヨーク | 定常領域の代わりに受容体結合性リガンドを有するキメラ抗体 |
| ATE218889T1 (de) | 1990-11-09 | 2002-06-15 | Stephen D Gillies | Cytokine immunokonjugate |
| DE69233482T2 (de) | 1991-05-17 | 2006-01-12 | Merck & Co., Inc. | Verfahren zur Verminderung der Immunogenität der variablen Antikörperdomänen |
| US5565332A (en) | 1991-09-23 | 1996-10-15 | Medical Research Council | Production of chimeric antibodies - a combinatorial approach |
| WO1993010805A1 (en) * | 1991-12-02 | 1993-06-10 | Cor Therapeutics, Inc. | Inhibitory immunoglobulin polypeptides to human pdgf beta receptor |
| US5817310A (en) | 1991-12-02 | 1998-10-06 | Cor Therapeutics, Inc. | Inhibitory immunoglobulin polypeptides to human PDGF beta receptor |
| US5639641A (en) | 1992-09-09 | 1997-06-17 | Immunogen Inc. | Resurfacing of rodent antibodies |
| US5922545A (en) | 1993-10-29 | 1999-07-13 | Affymax Technologies N.V. | In vitro peptide and antibody display libraries |
| GB9422383D0 (en) | 1994-11-05 | 1995-01-04 | Wellcome Found | Antibodies |
| US5869046A (en) | 1995-04-14 | 1999-02-09 | Genentech, Inc. | Altered polypeptides with increased half-life |
| US6096871A (en) | 1995-04-14 | 2000-08-01 | Genentech, Inc. | Polypeptides altered to contain an epitope from the Fc region of an IgG molecule for increased half-life |
| US6121022A (en) | 1995-04-14 | 2000-09-19 | Genentech, Inc. | Altered polypeptides with increased half-life |
| US5739277A (en) | 1995-04-14 | 1998-04-14 | Genentech Inc. | Altered polypeptides with increased half-life |
| GB9524973D0 (en) | 1995-12-06 | 1996-02-07 | Lynxvale Ltd | Viral vectors |
| CA2262405A1 (en) | 1996-08-02 | 1998-02-12 | Bristol-Myers Squibb Company | A method for inhibiting immunoglobulin-induced toxicity resulting from the use of immunoglobulins in therapy and in vivo diagnosis |
| WO1998023289A1 (en) | 1996-11-27 | 1998-06-04 | The General Hospital Corporation | MODULATION OF IgG BINDING TO FcRn |
| CA2278786C (en) | 1997-01-21 | 2010-07-20 | The General Hospital Corporation | Selection of proteins using rna-protein fusions |
| US6261804B1 (en) | 1997-01-21 | 2001-07-17 | The General Hospital Corporation | Selection of proteins using RNA-protein fusions |
| US6277375B1 (en) | 1997-03-03 | 2001-08-21 | Board Of Regents, The University Of Texas System | Immunoglobulin-like domains with increased half-lives |
| DE69834032T2 (de) | 1997-04-23 | 2006-12-07 | Universität Zürich | Verfahren zur erkennung von nucleinsäuremolekülen codierend für (poly)peptide, welche mit zielmolekülen interagieren |
| EP0983303B1 (en) | 1997-05-21 | 2006-03-08 | Biovation Limited | Method for the production of non-immunogenic proteins |
| DE69937291T2 (de) | 1998-04-02 | 2008-07-10 | Genentech, Inc., South San Francisco | Antikörpervarianten und fragmente davon |
| US6242195B1 (en) | 1998-04-02 | 2001-06-05 | Genentech, Inc. | Methods for determining binding of an analyte to a receptor |
| US6528624B1 (en) | 1998-04-02 | 2003-03-04 | Genentech, Inc. | Polypeptide variants |
| US6194551B1 (en) | 1998-04-02 | 2001-02-27 | Genentech, Inc. | Polypeptide variants |
| CA2323638A1 (en) | 1998-04-03 | 1999-10-14 | Phylos, Inc. | Addressable protein arrays |
| GB9809951D0 (en) | 1998-05-08 | 1998-07-08 | Univ Cambridge Tech | Binding molecules |
| US6846655B1 (en) | 1998-06-29 | 2005-01-25 | Phylos, Inc. | Methods for generating highly diverse libraries |
| EP1105516A4 (en) | 1998-08-17 | 2002-01-09 | Phylos Inc | METHODS FOR PRODUCING PRIVATE NUCLEIC ACIDS FROM 3 'NON-TRANSLATED REGIONS AND FOR OPTIMIZING THE FORMATION OF A CELL-PROTEIN RNA FUSION |
| WO2000009464A1 (en) | 1998-08-17 | 2000-02-24 | Phylos, Inc. | Identification of compound-protein interactions using libraries of protein-nucleic acid fusion molecules |
| WO2000009560A2 (en) | 1998-08-17 | 2000-02-24 | Abgenix, Inc. | Generation of modified molecules with increased serum half-lives |
| HK1039355B (en) | 1998-12-02 | 2007-09-21 | Bristol-Myers Squibb Company | Dna-protein fusions and uses thereof |
| EP1006183A1 (en) | 1998-12-03 | 2000-06-07 | Max-Planck-Gesellschaft zur Förderung der Wissenschaften e.V. | Recombinant soluble Fc receptors |
| ES2278463T3 (es) | 1998-12-08 | 2007-08-01 | Biovation Limited | Metodo para reducir la inmunogenicidad de proteinas. |
| US6737056B1 (en) | 1999-01-15 | 2004-05-18 | Genentech, Inc. | Polypeptide variants with altered effector function |
| KR101155191B1 (ko) | 1999-01-15 | 2012-06-13 | 제넨테크, 인크. | 효과기 기능이 변화된 폴리펩티드 변이체 |
| EP1187626A4 (en) | 1999-06-01 | 2006-07-19 | Compound Therapeutics Inc | PROCESS FOR THE PREPARATION OF 5'-NUCLEIC ACID PROTEIN CONJUGATES |
| AU778194B2 (en) | 1999-07-12 | 2004-11-18 | Bristol-Myers Squibb Company | C-terminal protein tagging |
| EP1196637B1 (en) | 1999-07-27 | 2007-04-25 | Adnexus Therapeutics, Inc. | Peptide acceptor ligation methods |
| AU779653B2 (en) | 1999-08-27 | 2005-02-03 | Bristol-Myers Squibb Company | Methods for encoding and sorting in vitro translated proteins |
| AU783689B2 (en) | 2000-01-24 | 2005-11-24 | Adnexus Therapeutics, Inc. | Sensitive, multiplexed diagnostic assays for protein analysis |
| US7022479B2 (en) | 2000-01-24 | 2006-04-04 | Compound Therapeutics, Inc. | Sensitive, multiplexed diagnostic assays for protein analysis |
| GB0029407D0 (en) | 2000-12-01 | 2001-01-17 | Affitech As | Product |
| DK1355919T3 (da) | 2000-12-12 | 2011-03-14 | Medimmune Llc | Molekyler med længere halveringstider, sammensætninger og anvendelser deraf |
| WO2002084277A1 (en) | 2001-04-17 | 2002-10-24 | Abmaxis, Inc. | Structure-based construction of human antibody library |
| US6951725B2 (en) | 2001-06-21 | 2005-10-04 | Compound Therapeutics, Inc. | In vitro protein interaction detection systems |
| JP2005289809A (ja) | 2001-10-24 | 2005-10-20 | Vlaams Interuniversitair Inst Voor Biotechnologie Vzw (Vib Vzw) | 突然変異重鎖抗体 |
| WO2003045975A2 (en) | 2001-11-27 | 2003-06-05 | Compound Therapeutics, Inc. | Solid-phase immobilization of proteins and peptides |
| US20040002587A1 (en) | 2002-02-20 | 2004-01-01 | Watkins Jeffry D. | Fc region variants |
| EP1487879B1 (en) | 2002-03-01 | 2012-12-26 | Immunomedics, Inc. | Bispecific antibody point mutations for enhancing rate of clearance |
| US20040132101A1 (en) | 2002-09-27 | 2004-07-08 | Xencor | Optimized Fc variants and methods for their generation |
| CA2495251C (en) | 2002-08-14 | 2018-03-06 | Macrogenics, Inc. | Fc.gamma.riib-specific antibodies and methods of use thereof |
| KR100980065B1 (ko) | 2002-09-27 | 2010-09-03 | 젠코어 인코포레이티드 | 최적화된 Ｆｃ 변이체 및 그의 제조 방법 |
| AU2003286467B2 (en) | 2002-10-15 | 2009-10-01 | Abbvie Biotherapeutics Inc. | Alteration of FcRn binding affinities or serum half-lives of antibodies by mutagenesis |
| GB0226729D0 (en) * | 2002-11-15 | 2002-12-24 | Medical Res Council | Intracellular antibodies |
| WO2004063351A2 (en) | 2003-01-09 | 2004-07-29 | Macrogenics, Inc. | IDENTIFICATION AND ENGINEERING OF ANTIBODIES WITH VARIANT Fc REGIONS AND METHODS OF USING SAME |
| CN1871259A (zh) | 2003-08-22 | 2006-11-29 | 比奥根艾迪克Ma公司 | 具有改变的效应物功能的经改进的抗体和制备它的方法 |
| GB0324368D0 (en) | 2003-10-17 | 2003-11-19 | Univ Cambridge Tech | Polypeptides including modified constant regions |
| WO2005047327A2 (en) | 2003-11-12 | 2005-05-26 | Biogen Idec Ma Inc. | NEONATAL Fc RECEPTOR (FcRn)-BINDING POLYPEPTIDE VARIANTS, DIMERIC Fc BINDING PROTEINS AND METHODS RELATED THERETO |
| EP1697520A2 (en) | 2003-12-22 | 2006-09-06 | Xencor, Inc. | Fc polypeptides with novel fc ligand binding sites |
| PT1706424E (pt) | 2004-01-12 | 2009-10-01 | Applied Molecular Evolution | Variantes da região fc |
| US7276585B2 (en) | 2004-03-24 | 2007-10-02 | Xencor, Inc. | Immunoglobulin variants outside the Fc region |
| WO2005123780A2 (en) | 2004-04-09 | 2005-12-29 | Protein Design Labs, Inc. | Alteration of fcrn binding affinities or serum half-lives of antibodies by mutagenesis |
| WO2006085967A2 (en) | 2004-07-09 | 2006-08-17 | Xencor, Inc. | OPTIMIZED ANTI-CD20 MONOCONAL ANTIBODIES HAVING Fc VARIANTS |
| EP2940043A1 (en) | 2004-07-15 | 2015-11-04 | Xencor, Inc. | Optimized fc variants |
| WO2006047350A2 (en) | 2004-10-21 | 2006-05-04 | Xencor, Inc. | IgG IMMUNOGLOBULIN VARIANTS WITH OPTIMIZED EFFECTOR FUNCTION |
| US8460364B2 (en) | 2006-07-20 | 2013-06-11 | Orbusneich Medical, Inc. | Bioabsorbable polymeric medical device |
| US20080206585A1 (en) * | 2007-02-22 | 2008-08-28 | Kennametal Inc. | Composite materials comprising a hard ceramic phase and a Cu-Ni-Mn infiltration alloy |
| US7740850B2 (en) * | 2007-04-17 | 2010-06-22 | ImClone, LLC | PDGFRβ-specific antibodies |
| US20110022149A1 (en) | 2007-06-04 | 2011-01-27 | Cox Brian J | Methods and devices for treatment of vascular defects |
| PL2274008T3 (pl) * | 2008-03-27 | 2014-07-31 | Zymogenetics Inc | Kompozycje i sposoby hamowania PDGFRbeta i VEGF-A |
| JP5924937B2 (ja) | 2008-07-25 | 2016-05-25 | エックス−ボディ インコーポレイテッド | タンパク質スクリーニング法 |
| WO2011056997A1 (en) * | 2009-11-04 | 2011-05-12 | Fabrus Llc | Methods for affinity maturation-based antibody optimization |
| EP3798236B1 (en) * | 2011-03-15 | 2022-08-10 | X-Body, Inc. | Antibody screening methods |
| CN102250249A (zh) * | 2011-06-18 | 2011-11-23 | 常州亚当生物技术有限公司 | 一种抗VEGF/PDGFRbeta双特异性抗体及其应用 |
| AU2012347972B2 (en) * | 2011-12-05 | 2018-05-10 | X-Body, Inc. | PDGF receptor beta binding polypeptides |
-
2012
- 2012-12-05 AU AU2012347972A patent/AU2012347972B2/en not_active Ceased
- 2012-12-05 CA CA2857721A patent/CA2857721C/en active Active
- 2012-12-05 EP EP20154280.0A patent/EP3712173B1/en active Active
- 2012-12-05 WO PCT/US2012/067909 patent/WO2013085972A1/en not_active Ceased
- 2012-12-05 US US13/705,978 patent/US9416179B2/en active Active
- 2012-12-05 ES ES12856569T patent/ES2784131T3/es active Active
- 2012-12-05 TW TW106112237A patent/TWI640537B/zh not_active IP Right Cessation
- 2012-12-05 CN CN201710700723.6A patent/CN107353342B/zh not_active Expired - Fee Related
- 2012-12-05 CN CN201280068404.3A patent/CN104105708B/zh active Active
- 2012-12-05 TW TW101145785A patent/TWI591074B/zh active
- 2012-12-05 EP EP12856569.4A patent/EP2788379B1/en active Active
- 2012-12-05 JP JP2014546016A patent/JP6483442B2/ja active Active
-
2016
- 2016-07-11 US US15/207,188 patent/US10604578B2/en active Active
-
2018
- 2018-11-19 JP JP2018216510A patent/JP6843816B2/ja not_active Expired - Fee Related
-
2020
- 2020-02-17 US US16/792,728 patent/US11136398B2/en not_active Expired - Fee Related
-
2021
- 2021-08-24 US US17/410,324 patent/US20220089748A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| TWI640537B (zh) | 2018-11-11 |
| TWI591074B (zh) | 2017-07-11 |
| US11136398B2 (en) | 2021-10-05 |
| WO2013085972A1 (en) | 2013-06-13 |
| CN104105708B (zh) | 2018-04-03 |
| EP2788379B1 (en) | 2020-02-05 |
| US20130177572A1 (en) | 2013-07-11 |
| JP2019047807A (ja) | 2019-03-28 |
| CN107353342A (zh) | 2017-11-17 |
| JP6483442B2 (ja) | 2019-03-13 |
| TW201333038A (zh) | 2013-08-16 |
| HK1202882A1 (en) | 2015-10-09 |
| US10604578B2 (en) | 2020-03-31 |
| US20200299390A1 (en) | 2020-09-24 |
| EP3712173B1 (en) | 2023-07-12 |
| CN104105708A (zh) | 2014-10-15 |
| US20170029510A1 (en) | 2017-02-02 |
| EP2788379A1 (en) | 2014-10-15 |
| CA2857721A1 (en) | 2013-06-13 |
| US9416179B2 (en) | 2016-08-16 |
| CN107353342B (zh) | 2021-08-10 |
| EP3712173A1 (en) | 2020-09-23 |
| EP2788379A4 (en) | 2015-05-06 |
| JP6843816B2 (ja) | 2021-03-17 |
| US20220089748A1 (en) | 2022-03-24 |
| JP2015501814A (ja) | 2015-01-19 |
| AU2012347972B2 (en) | 2018-05-10 |
| AU2012347972A1 (en) | 2014-06-19 |
| ES2784131T3 (es) | 2020-09-22 |
| TW201802117A (zh) | 2018-01-16 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US11136398B2 (en) | PDGF receptor beta binding polypeptides | |
| EP3246339A1 (en) | Antibodies to bradykinin b1 receptor ligands | |
| US11814441B2 (en) | Bi-specific antigen-binding polypeptides | |
| HK40037402A (en) | Pdgf receptor beta binding polypeptides | |
| HK1202882B (en) | Pdgf receptor beta binding polypeptides | |
| HK40035879A (en) | Bi-specific antigen-binding polypeptides | |
| OA17139A (en) | Antibodies to bradykinin B1 receptor ligands | |
| HK1233656A1 (en) | Bi-specific antigen-binding polypeptides |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request |
Effective date: 20171110 |