AU2012296961B2 - Modified proteins and peptides - Google Patents
Modified proteins and peptides Download PDFInfo
- Publication number
- AU2012296961B2 AU2012296961B2 AU2012296961A AU2012296961A AU2012296961B2 AU 2012296961 B2 AU2012296961 B2 AU 2012296961B2 AU 2012296961 A AU2012296961 A AU 2012296961A AU 2012296961 A AU2012296961 A AU 2012296961A AU 2012296961 B2 AU2012296961 B2 AU 2012296961B2
- Authority
- AU
- Australia
- Prior art keywords
- dab
- binding
- amino acid
- seq
- extension
- 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.)
- Ceased
Links
- 102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 41
- 108091005601 modified peptides Proteins 0.000 title abstract description 7
- 108091005573 modified proteins Proteins 0.000 title abstract description 7
- 102000035118 modified proteins Human genes 0.000 title abstract description 7
- 230000027455 binding Effects 0.000 claims abstract description 233
- 210000004899 c-terminal region Anatomy 0.000 claims abstract description 133
- 241000282414 Homo sapiens Species 0.000 claims abstract description 116
- 108060003951 Immunoglobulin Proteins 0.000 claims abstract description 89
- 102000018358 immunoglobulin Human genes 0.000 claims abstract description 89
- 230000002829 reductive effect Effects 0.000 claims abstract description 53
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 47
- 230000004927 fusion Effects 0.000 claims abstract description 30
- 235000001014 amino acid Nutrition 0.000 claims description 80
- 238000000034 method Methods 0.000 claims description 80
- 235000004279 alanine Nutrition 0.000 claims description 70
- 150000001413 amino acids Chemical group 0.000 claims description 65
- 239000000203 mixture Substances 0.000 claims description 63
- 210000004027 cell Anatomy 0.000 claims description 59
- 230000004048 modification Effects 0.000 claims description 54
- 238000012986 modification Methods 0.000 claims description 54
- 201000004681 Psoriasis Diseases 0.000 claims description 51
- 150000007523 nucleic acids Chemical class 0.000 claims description 47
- 102000039446 nucleic acids Human genes 0.000 claims description 42
- 108020004707 nucleic acids Proteins 0.000 claims description 42
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 claims description 38
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 38
- 239000003814 drug Substances 0.000 claims description 38
- 239000008194 pharmaceutical composition Substances 0.000 claims description 34
- 229920001184 polypeptide Polymers 0.000 claims description 30
- 208000035475 disorder Diseases 0.000 claims description 23
- 239000003085 diluting agent Substances 0.000 claims description 21
- 238000009472 formulation Methods 0.000 claims description 18
- 238000004519 manufacturing process Methods 0.000 claims description 17
- 239000013598 vector Substances 0.000 claims description 17
- 201000010099 disease Diseases 0.000 claims description 15
- IEMCJUJOHAEFFW-UHFFFAOYSA-M potassium 2-[(2-acetyloxybenzoyl)amino]ethanesulfonate Chemical compound CC(=O)OC1=CC=CC=C1C(=O)NCCS(=O)(=O)[O-].[K+] IEMCJUJOHAEFFW-UHFFFAOYSA-M 0.000 claims description 15
- 208000023504 respiratory system disease Diseases 0.000 claims description 13
- 208000027866 inflammatory disease Diseases 0.000 claims description 12
- 208000019693 Lung disease Diseases 0.000 claims description 11
- 206010035664 Pneumonia Diseases 0.000 claims description 11
- 206010069351 acute lung injury Diseases 0.000 claims description 11
- 206010001052 Acute respiratory distress syndrome Diseases 0.000 claims description 8
- 230000002685 pulmonary effect Effects 0.000 claims description 8
- 208000006545 Chronic Obstructive Pulmonary Disease Diseases 0.000 claims description 7
- 230000000241 respiratory effect Effects 0.000 claims description 7
- 241000588724 Escherichia coli Species 0.000 claims description 6
- 101000929495 Homo sapiens Adenosine deaminase Proteins 0.000 claims description 6
- 238000010254 subcutaneous injection Methods 0.000 claims description 6
- 210000001035 gastrointestinal tract Anatomy 0.000 claims description 5
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 5
- 239000005557 antagonist Substances 0.000 claims description 4
- 238000010255 intramuscular injection Methods 0.000 claims description 4
- 238000010253 intravenous injection Methods 0.000 claims description 4
- 238000013268 sustained release Methods 0.000 claims description 4
- 239000012730 sustained-release form Substances 0.000 claims description 4
- 208000022559 Inflammatory bowel disease Diseases 0.000 claims description 3
- 206010003246 arthritis Diseases 0.000 claims description 3
- 208000006673 asthma Diseases 0.000 claims description 3
- 239000007927 intramuscular injection Substances 0.000 claims description 3
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 2
- 239000006199 nebulizer Substances 0.000 claims description 2
- 102100033732 Tumor necrosis factor receptor superfamily member 1A Human genes 0.000 claims 2
- 101710187743 Tumor necrosis factor receptor superfamily member 1A Proteins 0.000 claims 2
- 101100114828 Drosophila melanogaster Orai gene Proteins 0.000 claims 1
- 125000003275 alpha amino acid group Chemical group 0.000 abstract description 98
- 238000006467 substitution reaction Methods 0.000 abstract description 56
- 102000004169 proteins and genes Human genes 0.000 abstract description 38
- 108090000623 proteins and genes Proteins 0.000 abstract description 38
- 239000000427 antigen Substances 0.000 abstract description 32
- 108091007433 antigens Proteins 0.000 abstract description 32
- 102000036639 antigens Human genes 0.000 abstract description 32
- 238000007792 addition Methods 0.000 abstract description 26
- 241000282836 Camelus dromedarius Species 0.000 abstract description 8
- 108010021625 Immunoglobulin Fragments Proteins 0.000 abstract description 6
- 102000008394 Immunoglobulin Fragments Human genes 0.000 abstract description 6
- 235000002198 Annona diversifolia Nutrition 0.000 abstract description 4
- 241000282842 Lama glama Species 0.000 abstract 1
- 238000003556 assay Methods 0.000 description 107
- 229940024606 amino acid Drugs 0.000 description 56
- 238000011282 treatment Methods 0.000 description 55
- 238000012360 testing method Methods 0.000 description 45
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 38
- 230000005764 inhibitory process Effects 0.000 description 38
- 235000018102 proteins Nutrition 0.000 description 35
- 238000002347 injection Methods 0.000 description 34
- 239000007924 injection Substances 0.000 description 34
- 229940120638 avastin Drugs 0.000 description 32
- 210000002966 serum Anatomy 0.000 description 32
- 101000611441 Solanum lycopersicum Pathogenesis-related leaf protein 6 Proteins 0.000 description 31
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 30
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 30
- 230000000694 effects Effects 0.000 description 30
- 102220274086 rs1379627026 Human genes 0.000 description 30
- 238000011191 terminal modification Methods 0.000 description 28
- 229940079593 drug Drugs 0.000 description 26
- 229960000397 bevacizumab Drugs 0.000 description 23
- 239000000463 material Substances 0.000 description 22
- 238000012790 confirmation Methods 0.000 description 21
- 125000005647 linker group Chemical group 0.000 description 21
- 230000035772 mutation Effects 0.000 description 21
- 238000012217 deletion Methods 0.000 description 17
- 230000037430 deletion Effects 0.000 description 17
- 108090001007 Interleukin-8 Proteins 0.000 description 16
- 102000004890 Interleukin-8 Human genes 0.000 description 16
- 238000011534 incubation Methods 0.000 description 16
- BYXHQQCXAJARLQ-ZLUOBGJFSA-N Ala-Ala-Ala Chemical compound C[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](C)C(O)=O BYXHQQCXAJARLQ-ZLUOBGJFSA-N 0.000 description 15
- 108700012920 TNF Proteins 0.000 description 14
- 239000005018 casein Substances 0.000 description 14
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 14
- 235000021240 caseins Nutrition 0.000 description 14
- NFGXHKASABOEEW-UHFFFAOYSA-N 1-methylethyl 11-methoxy-3,7,11-trimethyl-2,4-dodecadienoate Chemical group COC(C)(C)CCCC(C)CC=CC(C)=CC(=O)OC(C)C NFGXHKASABOEEW-UHFFFAOYSA-N 0.000 description 13
- 239000006228 supernatant Substances 0.000 description 12
- 239000011534 wash buffer Substances 0.000 description 12
- 108090000978 Interleukin-4 Proteins 0.000 description 11
- 102000004388 Interleukin-4 Human genes 0.000 description 11
- 239000000872 buffer Substances 0.000 description 11
- 150000001875 compounds Chemical class 0.000 description 11
- 239000003446 ligand Substances 0.000 description 11
- 108010090804 Streptavidin Proteins 0.000 description 10
- 210000004369 blood Anatomy 0.000 description 10
- 239000008280 blood Substances 0.000 description 10
- 239000012634 fragment Substances 0.000 description 10
- 238000001990 intravenous administration Methods 0.000 description 10
- 230000001225 therapeutic effect Effects 0.000 description 10
- 108090000176 Interleukin-13 Proteins 0.000 description 9
- 102000003816 Interleukin-13 Human genes 0.000 description 9
- 102100037792 Interleukin-6 receptor subunit alpha Human genes 0.000 description 9
- 241000282567 Macaca fascicularis Species 0.000 description 9
- 102000007562 Serum Albumin Human genes 0.000 description 9
- 108010071390 Serum Albumin Proteins 0.000 description 9
- 238000004458 analytical method Methods 0.000 description 9
- 230000036515 potency Effects 0.000 description 9
- 102220041804 rs550499593 Human genes 0.000 description 9
- 210000001519 tissue Anatomy 0.000 description 9
- 238000005406 washing Methods 0.000 description 9
- 241000282412 Homo Species 0.000 description 8
- 241000283984 Rodentia Species 0.000 description 8
- 238000007385 chemical modification Methods 0.000 description 8
- UQLDLKMNUJERMK-UHFFFAOYSA-L di(octadecanoyloxy)lead Chemical compound [Pb+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O UQLDLKMNUJERMK-UHFFFAOYSA-L 0.000 description 8
- 230000008030 elimination Effects 0.000 description 8
- 238000003379 elimination reaction Methods 0.000 description 8
- 238000011533 pre-incubation Methods 0.000 description 8
- 210000003491 skin Anatomy 0.000 description 8
- 241000282693 Cercopithecidae Species 0.000 description 7
- 102220548181 F-box-like/WD repeat-containing protein TBL1X_L108Q_mutation Human genes 0.000 description 7
- 101000611183 Homo sapiens Tumor necrosis factor Proteins 0.000 description 7
- 239000007983 Tris buffer Substances 0.000 description 7
- 238000010521 absorption reaction Methods 0.000 description 7
- 230000002500 effect on skin Effects 0.000 description 7
- 238000003018 immunoassay Methods 0.000 description 7
- 210000004072 lung Anatomy 0.000 description 7
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 7
- 238000002560 therapeutic procedure Methods 0.000 description 7
- 102000009027 Albumins Human genes 0.000 description 6
- 108010088751 Albumins Proteins 0.000 description 6
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 6
- 102000008100 Human Serum Albumin Human genes 0.000 description 6
- 108091006905 Human Serum Albumin Proteins 0.000 description 6
- 102100040247 Tumor necrosis factor Human genes 0.000 description 6
- 125000000539 amino acid group Chemical group 0.000 description 6
- -1 antibodies Proteins 0.000 description 6
- 239000012911 assay medium Substances 0.000 description 6
- 206010006451 bronchitis Diseases 0.000 description 6
- 150000005829 chemical entities Chemical class 0.000 description 6
- 238000010790 dilution Methods 0.000 description 6
- 239000012895 dilution Substances 0.000 description 6
- 239000013604 expression vector Substances 0.000 description 6
- 239000008240 homogeneous mixture Substances 0.000 description 6
- 210000004408 hybridoma Anatomy 0.000 description 6
- 238000000338 in vitro Methods 0.000 description 6
- 238000001727 in vivo Methods 0.000 description 6
- 210000004962 mammalian cell Anatomy 0.000 description 6
- 238000005259 measurement Methods 0.000 description 6
- 230000000813 microbial effect Effects 0.000 description 6
- 230000008569 process Effects 0.000 description 6
- 238000000159 protein binding assay Methods 0.000 description 6
- 102000005962 receptors Human genes 0.000 description 6
- 108020003175 receptors Proteins 0.000 description 6
- 230000009467 reduction Effects 0.000 description 6
- 102200083940 rs104894416 Human genes 0.000 description 6
- 208000024891 symptom Diseases 0.000 description 6
- 101150075175 Asgr1 gene Proteins 0.000 description 5
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 5
- 108010037897 DC-specific ICAM-3 grabbing nonintegrin Proteins 0.000 description 5
- 108010002616 Interleukin-5 Proteins 0.000 description 5
- 102000000743 Interleukin-5 Human genes 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 5
- 241000699666 Mus <mouse, genus> Species 0.000 description 5
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 5
- 102000025171 antigen binding proteins Human genes 0.000 description 5
- 108091000831 antigen binding proteins Proteins 0.000 description 5
- 230000000903 blocking effect Effects 0.000 description 5
- 238000004364 calculation method Methods 0.000 description 5
- 230000001419 dependent effect Effects 0.000 description 5
- 238000009826 distribution Methods 0.000 description 5
- 210000002889 endothelial cell Anatomy 0.000 description 5
- 238000005516 engineering process Methods 0.000 description 5
- 210000004602 germ cell Anatomy 0.000 description 5
- 102000043395 human ADA Human genes 0.000 description 5
- 230000006698 induction Effects 0.000 description 5
- 108040006732 interleukin-1 receptor activity proteins Proteins 0.000 description 5
- 102000014909 interleukin-1 receptor activity proteins Human genes 0.000 description 5
- 108040006858 interleukin-6 receptor activity proteins Proteins 0.000 description 5
- 239000002609 medium Substances 0.000 description 5
- 230000002265 prevention Effects 0.000 description 5
- 238000001525 receptor binding assay Methods 0.000 description 5
- 238000003860 storage Methods 0.000 description 5
- 238000002198 surface plasmon resonance spectroscopy Methods 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
- 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 4
- ODHCTXKNWHHXJC-VKHMYHEASA-N 5-oxo-L-proline Chemical compound OC(=O)[C@@H]1CCC(=O)N1 ODHCTXKNWHHXJC-VKHMYHEASA-N 0.000 description 4
- 206010006458 Bronchitis chronic Diseases 0.000 description 4
- 206010014561 Emphysema Diseases 0.000 description 4
- 101000599048 Homo sapiens Interleukin-6 receptor subunit alpha Proteins 0.000 description 4
- 101100425753 Homo sapiens TNFRSF1A gene Proteins 0.000 description 4
- 101000808011 Homo sapiens Vascular endothelial growth factor A Proteins 0.000 description 4
- 101000851007 Homo sapiens Vascular endothelial growth factor receptor 2 Proteins 0.000 description 4
- 206010020751 Hypersensitivity Diseases 0.000 description 4
- 239000004472 Lysine Substances 0.000 description 4
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 4
- 241000235648 Pichia Species 0.000 description 4
- 229920001213 Polysorbate 20 Polymers 0.000 description 4
- 208000010378 Pulmonary Embolism Diseases 0.000 description 4
- 241000700159 Rattus Species 0.000 description 4
- 208000013616 Respiratory Distress Syndrome Diseases 0.000 description 4
- 102100033177 Vascular endothelial growth factor receptor 2 Human genes 0.000 description 4
- 201000000028 adult respiratory distress syndrome Diseases 0.000 description 4
- 208000026935 allergic disease Diseases 0.000 description 4
- 230000009435 amidation Effects 0.000 description 4
- 238000007112 amidation reaction Methods 0.000 description 4
- 201000009267 bronchiectasis Diseases 0.000 description 4
- 238000006243 chemical reaction Methods 0.000 description 4
- 208000007451 chronic bronchitis Diseases 0.000 description 4
- 230000001684 chronic effect Effects 0.000 description 4
- 230000000295 complement effect Effects 0.000 description 4
- 230000006240 deamidation Effects 0.000 description 4
- 239000012537 formulation buffer Substances 0.000 description 4
- 230000013595 glycosylation Effects 0.000 description 4
- 238000006206 glycosylation reaction Methods 0.000 description 4
- 102000058223 human VEGFA Human genes 0.000 description 4
- 238000001802 infusion Methods 0.000 description 4
- 230000000873 masking effect Effects 0.000 description 4
- 239000002773 nucleotide Substances 0.000 description 4
- 125000003729 nucleotide group Chemical group 0.000 description 4
- 230000006320 pegylation Effects 0.000 description 4
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 4
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 4
- 230000003389 potentiating effect Effects 0.000 description 4
- 230000009257 reactivity Effects 0.000 description 4
- 102220392418 rs192256606 Human genes 0.000 description 4
- 102220246726 rs773397553 Human genes 0.000 description 4
- 238000012868 site-directed mutagenesis technique Methods 0.000 description 4
- 230000000638 stimulation Effects 0.000 description 4
- PZASAAIJIFDWSB-CKPDSHCKSA-N 8-[(1S)-1-[8-(trifluoromethyl)-7-[4-(trifluoromethyl)cyclohexyl]oxynaphthalen-2-yl]ethyl]-8-azabicyclo[3.2.1]octane-3-carboxylic acid Chemical compound FC(F)(F)C=1C2=CC([C@@H](N3C4CCC3CC(C4)C(O)=O)C)=CC=C2C=CC=1OC1CCC(C(F)(F)F)CC1 PZASAAIJIFDWSB-CKPDSHCKSA-N 0.000 description 3
- 244000303258 Annona diversifolia Species 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
- 239000004471 Glycine Substances 0.000 description 3
- 101001076430 Homo sapiens Interleukin-13 Proteins 0.000 description 3
- 241000699670 Mus sp. Species 0.000 description 3
- KJTLSVCANCCWHF-UHFFFAOYSA-N Ruthenium Chemical compound [Ru] KJTLSVCANCCWHF-UHFFFAOYSA-N 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 229930006000 Sucrose Natural products 0.000 description 3
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 3
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 3
- 108091008605 VEGF receptors Proteins 0.000 description 3
- 102000009484 Vascular Endothelial Growth Factor Receptors Human genes 0.000 description 3
- 108010017893 alanyl-alanyl-alanine Proteins 0.000 description 3
- 238000013459 approach Methods 0.000 description 3
- 230000006399 behavior Effects 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 239000000969 carrier Substances 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 210000004207 dermis Anatomy 0.000 description 3
- 239000008121 dextrose Substances 0.000 description 3
- 238000006911 enzymatic reaction Methods 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 239000012530 fluid Substances 0.000 description 3
- 238000004108 freeze drying Methods 0.000 description 3
- 125000000404 glutamine group Chemical group N[C@@H](CCC(N)=O)C(=O)* 0.000 description 3
- 102000019207 human interleukin-13 Human genes 0.000 description 3
- 230000002757 inflammatory effect Effects 0.000 description 3
- 230000001404 mediated effect Effects 0.000 description 3
- 108020004999 messenger RNA Proteins 0.000 description 3
- 235000015097 nutrients Nutrition 0.000 description 3
- 230000003647 oxidation Effects 0.000 description 3
- 238000007254 oxidation reaction Methods 0.000 description 3
- 230000036470 plasma concentration Effects 0.000 description 3
- 238000003752 polymerase chain reaction Methods 0.000 description 3
- 239000000244 polyoxyethylene sorbitan monooleate Substances 0.000 description 3
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 3
- 229920000053 polysorbate 80 Polymers 0.000 description 3
- 229940068968 polysorbate 80 Drugs 0.000 description 3
- 230000004481 post-translational protein modification Effects 0.000 description 3
- 230000035755 proliferation Effects 0.000 description 3
- 230000000069 prophylactic effect Effects 0.000 description 3
- 238000011321 prophylaxis Methods 0.000 description 3
- 108020001580 protein domains Proteins 0.000 description 3
- 230000001185 psoriatic effect Effects 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 238000012216 screening Methods 0.000 description 3
- 230000028327 secretion Effects 0.000 description 3
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 3
- 230000019491 signal transduction Effects 0.000 description 3
- 238000001542 size-exclusion chromatography Methods 0.000 description 3
- 239000011780 sodium chloride Substances 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- 239000005720 sucrose Substances 0.000 description 3
- 230000009885 systemic effect Effects 0.000 description 3
- 125000003396 thiol group Chemical group [H]S* 0.000 description 3
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 3
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 3
- 210000003606 umbilical vein Anatomy 0.000 description 3
- 108010047303 von Willebrand Factor Proteins 0.000 description 3
- 102100036537 von Willebrand factor Human genes 0.000 description 3
- 229960001134 von willebrand factor Drugs 0.000 description 3
- 230000003442 weekly effect Effects 0.000 description 3
- 206010001881 Alveolar proteinosis Diseases 0.000 description 2
- 208000033116 Asbestos intoxication Diseases 0.000 description 2
- 206010003487 Aspergilloma Diseases 0.000 description 2
- 201000002909 Aspergillosis Diseases 0.000 description 2
- 208000036641 Aspergillus infections Diseases 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 2
- 241000283707 Capra Species 0.000 description 2
- 206010009900 Colitis ulcerative Diseases 0.000 description 2
- 208000011231 Crohn disease Diseases 0.000 description 2
- 201000003883 Cystic fibrosis Diseases 0.000 description 2
- 206010014950 Eosinophilia Diseases 0.000 description 2
- 208000004248 Familial Primary Pulmonary Hypertension Diseases 0.000 description 2
- 208000009329 Graft vs Host Disease Diseases 0.000 description 2
- 206010072579 Granulomatosis with polyangiitis Diseases 0.000 description 2
- 101000851018 Homo sapiens Vascular endothelial growth factor receptor 1 Proteins 0.000 description 2
- 206010021133 Hypoventilation Diseases 0.000 description 2
- 201000009794 Idiopathic Pulmonary Fibrosis Diseases 0.000 description 2
- 208000029523 Interstitial Lung disease Diseases 0.000 description 2
- 241000235058 Komagataella pastoris Species 0.000 description 2
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 2
- 201000005099 Langerhans cell histiocytosis Diseases 0.000 description 2
- 206010058467 Lung neoplasm malignant Diseases 0.000 description 2
- 206010027406 Mesothelioma Diseases 0.000 description 2
- 206010029443 Nocardia Infections Diseases 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 102220517499 PAN2-PAN3 deadenylation complex subunit PAN3_L108A_mutation Human genes 0.000 description 2
- BELBBZDIHDAJOR-UHFFFAOYSA-N Phenolsulfonephthalein Chemical compound C1=CC(O)=CC=C1C1(C=2C=CC(O)=CC=2)C2=CC=CC=C2S(=O)(=O)O1 BELBBZDIHDAJOR-UHFFFAOYSA-N 0.000 description 2
- 208000002151 Pleural effusion Diseases 0.000 description 2
- 208000035109 Pneumococcal Infections Diseases 0.000 description 2
- 206010035667 Pneumonia anthrax Diseases 0.000 description 2
- 206010064911 Pulmonary arterial hypertension Diseases 0.000 description 2
- 208000029464 Pulmonary infiltrates Diseases 0.000 description 2
- 206010037423 Pulmonary oedema Diseases 0.000 description 2
- 239000012980 RPMI-1640 medium Substances 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 206010039085 Rhinitis allergic Diseases 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- 206010039491 Sarcoma Diseases 0.000 description 2
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- 108090000901 Transferrin Proteins 0.000 description 2
- 102000004338 Transferrin Human genes 0.000 description 2
- 206010052779 Transplant rejections Diseases 0.000 description 2
- 201000006704 Ulcerative Colitis Diseases 0.000 description 2
- 102100033178 Vascular endothelial growth factor receptor 1 Human genes 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- 201000007691 actinomycosis Diseases 0.000 description 2
- 230000004913 activation Effects 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 208000017304 adult pulmonary Langerhans cell histiocytosis Diseases 0.000 description 2
- 230000008484 agonism Effects 0.000 description 2
- 201000010105 allergic rhinitis Diseases 0.000 description 2
- 230000007815 allergy Effects 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 125000000637 arginyl group Chemical group N[C@@H](CCCNC(N)=N)C(=O)* 0.000 description 2
- 206010003441 asbestosis Diseases 0.000 description 2
- 235000003704 aspartic acid Nutrition 0.000 description 2
- 238000002820 assay format Methods 0.000 description 2
- 210000003719 b-lymphocyte Anatomy 0.000 description 2
- 239000007640 basal medium Substances 0.000 description 2
- 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 2
- 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 2
- 229960002685 biotin Drugs 0.000 description 2
- 235000020958 biotin Nutrition 0.000 description 2
- 239000011616 biotin Substances 0.000 description 2
- 150000001720 carbohydrates Chemical group 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- 238000001516 cell proliferation assay Methods 0.000 description 2
- 239000003153 chemical reaction reagent Substances 0.000 description 2
- 208000037976 chronic inflammation Diseases 0.000 description 2
- 208000037893 chronic inflammatory disorder Diseases 0.000 description 2
- 238000003776 cleavage reaction Methods 0.000 description 2
- 230000001186 cumulative effect Effects 0.000 description 2
- 238000006731 degradation reaction Methods 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000009792 diffusion process Methods 0.000 description 2
- 231100000673 dose–response relationship Toxicity 0.000 description 2
- 238000012377 drug delivery Methods 0.000 description 2
- 238000001035 drying Methods 0.000 description 2
- 239000012636 effector Substances 0.000 description 2
- 230000007613 environmental effect Effects 0.000 description 2
- 201000009580 eosinophilic pneumonia Diseases 0.000 description 2
- 210000002615 epidermis Anatomy 0.000 description 2
- 201000001155 extrinsic allergic alveolitis Diseases 0.000 description 2
- 210000002950 fibroblast Anatomy 0.000 description 2
- 229920000159 gelatin Polymers 0.000 description 2
- 235000019322 gelatine Nutrition 0.000 description 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
- 208000024908 graft versus host disease Diseases 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 229920000669 heparin Polymers 0.000 description 2
- ZFGMDIBRIDKWMY-PASTXAENSA-N heparin Chemical compound CC(O)=N[C@@H]1[C@@H](O)[C@H](O)[C@@H](COS(O)(=O)=O)O[C@@H]1O[C@@H]1[C@@H](C(O)=O)O[C@@H](O[C@H]2[C@@H]([C@@H](OS(O)(=O)=O)[C@@H](O[C@@H]3[C@@H](OC(O)[C@H](OS(O)(=O)=O)[C@H]3O)C(O)=O)O[C@@H]2O)CS(O)(=O)=O)[C@H](O)[C@H]1O ZFGMDIBRIDKWMY-PASTXAENSA-N 0.000 description 2
- 230000009610 hypersensitivity Effects 0.000 description 2
- 208000022098 hypersensitivity pneumonitis Diseases 0.000 description 2
- 208000000122 hyperventilation Diseases 0.000 description 2
- 230000000870 hyperventilation Effects 0.000 description 2
- 230000028993 immune response Effects 0.000 description 2
- 230000002163 immunogen Effects 0.000 description 2
- 230000005847 immunogenicity Effects 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- 206010022000 influenza Diseases 0.000 description 2
- 208000009449 inhalation anthrax Diseases 0.000 description 2
- 208000023372 inhalational anthrax Diseases 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 208000036971 interstitial lung disease 2 Diseases 0.000 description 2
- 238000006317 isomerization reaction Methods 0.000 description 2
- 238000002372 labelling Methods 0.000 description 2
- 238000012417 linear regression Methods 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 201000005202 lung cancer Diseases 0.000 description 2
- 208000020816 lung neoplasm Diseases 0.000 description 2
- 125000003588 lysine group Chemical group [H]N([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- 230000014759 maintenance of location Effects 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 210000001370 mediastinum Anatomy 0.000 description 2
- 201000006417 multiple sclerosis Diseases 0.000 description 2
- 230000037361 pathway Effects 0.000 description 2
- 230000000144 pharmacologic effect Effects 0.000 description 2
- 229960003531 phenolsulfonphthalein Drugs 0.000 description 2
- 210000004224 pleura Anatomy 0.000 description 2
- 206010035653 pneumoconiosis Diseases 0.000 description 2
- 201000008312 primary pulmonary hypertension Diseases 0.000 description 2
- 201000003489 pulmonary alveolar proteinosis Diseases 0.000 description 2
- 208000005333 pulmonary edema Diseases 0.000 description 2
- 201000009732 pulmonary eosinophilia Diseases 0.000 description 2
- 208000002815 pulmonary hypertension Diseases 0.000 description 2
- 201000003651 pulmonary sarcoidosis Diseases 0.000 description 2
- 208000008128 pulmonary tuberculosis Diseases 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000003127 radioimmunoassay Methods 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 208000021569 rheumatoid lung disease Diseases 0.000 description 2
- 229910052707 ruthenium Inorganic materials 0.000 description 2
- 230000007017 scission Effects 0.000 description 2
- 230000009919 sequestration Effects 0.000 description 2
- 230000011664 signaling Effects 0.000 description 2
- 231100000274 skin absorption Toxicity 0.000 description 2
- 230000037384 skin absorption Effects 0.000 description 2
- 208000017520 skin disease Diseases 0.000 description 2
- 201000002859 sleep apnea Diseases 0.000 description 2
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 2
- 239000001488 sodium phosphate Substances 0.000 description 2
- 229910000162 sodium phosphate Inorganic materials 0.000 description 2
- 235000011008 sodium phosphates Nutrition 0.000 description 2
- 230000006641 stabilisation Effects 0.000 description 2
- 239000008223 sterile water Substances 0.000 description 2
- 239000007929 subcutaneous injection Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 2
- 239000012581 transferrin Substances 0.000 description 2
- 238000011269 treatment regimen Methods 0.000 description 2
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 2
- 239000003981 vehicle Substances 0.000 description 2
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 2
- KIUKXJAPPMFGSW-DNGZLQJQSA-N (2S,3S,4S,5R,6R)-6-[(2S,3R,4R,5S,6R)-3-Acetamido-2-[(2S,3S,4R,5R,6R)-6-[(2R,3R,4R,5S,6R)-3-acetamido-2,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-2-carboxy-4,5-dihydroxyoxan-3-yl]oxy-5-hydroxy-6-(hydroxymethyl)oxan-4-yl]oxy-3,4,5-trihydroxyoxane-2-carboxylic acid Chemical compound CC(=O)N[C@H]1[C@H](O)O[C@H](CO)[C@@H](O)[C@@H]1O[C@H]1[C@H](O)[C@@H](O)[C@H](O[C@H]2[C@@H]([C@@H](O[C@H]3[C@@H]([C@@H](O)[C@H](O)[C@H](O3)C(O)=O)O)[C@H](O)[C@@H](CO)O2)NC(C)=O)[C@@H](C(O)=O)O1 KIUKXJAPPMFGSW-DNGZLQJQSA-N 0.000 description 1
- MZOFCQQQCNRIBI-VMXHOPILSA-N (3s)-4-[[(2s)-1-[[(2s)-1-[[(1s)-1-carboxy-2-hydroxyethyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-3-[[2-[[(2s)-2,6-diaminohexanoyl]amino]acetyl]amino]-4-oxobutanoic acid Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CCCCN MZOFCQQQCNRIBI-VMXHOPILSA-N 0.000 description 1
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 1
- 208000009304 Acute Kidney Injury Diseases 0.000 description 1
- 206010067484 Adverse reaction Diseases 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 108090001008 Avidin Proteins 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000282465 Canis Species 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 229920002134 Carboxymethyl cellulose Polymers 0.000 description 1
- 102000005367 Carboxypeptidases Human genes 0.000 description 1
- 108010006303 Carboxypeptidases Proteins 0.000 description 1
- 241000700198 Cavia Species 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- 108020004414 DNA Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 241000282324 Felis Species 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 108010010803 Gelatin Proteins 0.000 description 1
- 239000001828 Gelatine Substances 0.000 description 1
- 241000251152 Ginglymostoma cirratum Species 0.000 description 1
- 108090000288 Glycoproteins Proteins 0.000 description 1
- 102000003886 Glycoproteins Human genes 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101001055222 Homo sapiens Interleukin-8 Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 102000012745 Immunoglobulin Subunits Human genes 0.000 description 1
- 108010079585 Immunoglobulin Subunits Proteins 0.000 description 1
- XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical group SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-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
- 241000282852 Lama guanicoe Species 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 101000574441 Mus musculus Alkaline phosphatase, germ cell type Proteins 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 208000014777 Pulmonary venoocclusive disease Diseases 0.000 description 1
- 208000033626 Renal failure acute Diseases 0.000 description 1
- 102000013968 STAT6 Transcription Factor Human genes 0.000 description 1
- 108010011005 STAT6 Transcription Factor Proteins 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 102000003838 Sialyltransferases Human genes 0.000 description 1
- 108090000141 Sialyltransferases Proteins 0.000 description 1
- 108010033576 Transferrin Receptors Proteins 0.000 description 1
- 102000007238 Transferrin Receptors 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
- 108060008682 Tumor Necrosis Factor Proteins 0.000 description 1
- 102000000852 Tumor Necrosis Factor-alpha Human genes 0.000 description 1
- 101710187830 Tumor necrosis factor receptor superfamily member 1B Proteins 0.000 description 1
- 102100033733 Tumor necrosis factor receptor superfamily member 1B Human genes 0.000 description 1
- 241001416177 Vicugna pacos Species 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 201000011040 acute kidney failure Diseases 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 230000006838 adverse reaction Effects 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
- 235000010443 alginic acid Nutrition 0.000 description 1
- 229920000615 alginic acid Polymers 0.000 description 1
- 238000000540 analysis of variance Methods 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 238000012436 analytical size exclusion chromatography Methods 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 230000008485 antagonism Effects 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000003302 anti-idiotype Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 239000012131 assay buffer Substances 0.000 description 1
- QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
- 230000005784 autoimmunity Effects 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 238000002306 biochemical method Methods 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 239000006227 byproduct Substances 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
- 239000002775 capsule Substances 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 239000011545 carbonate/bicarbonate buffer Substances 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 230000006652 catabolic pathway Effects 0.000 description 1
- 238000000423 cell based assay Methods 0.000 description 1
- 230000030833 cell death Effects 0.000 description 1
- 239000013553 cell monolayer Substances 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 238000005119 centrifugation Methods 0.000 description 1
- 239000013522 chelant Substances 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 238000001311 chemical methods and process Methods 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 230000002860 competitive effect Effects 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 230000021615 conjugation Effects 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
- 230000009260 cross reactivity Effects 0.000 description 1
- 239000013078 crystal Substances 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 235000015872 dietary supplement Nutrition 0.000 description 1
- 238000010494 dissociation reaction Methods 0.000 description 1
- 230000005593 dissociations Effects 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 239000003792 electrolyte Substances 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 230000009881 electrostatic interaction Effects 0.000 description 1
- 239000000839 emulsion Substances 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 238000013265 extended release Methods 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 230000037433 frameshift Effects 0.000 description 1
- 230000005714 functional activity Effects 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 239000008273 gelatin Substances 0.000 description 1
- 235000011852 gelatine desserts Nutrition 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 230000024924 glomerular filtration Effects 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 239000001963 growth medium Substances 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 102000057041 human TNF Human genes 0.000 description 1
- 229920002674 hyaluronan Polymers 0.000 description 1
- 229960003160 hyaluronic acid Drugs 0.000 description 1
- 238000009396 hybridization Methods 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 229940072221 immunoglobulins Drugs 0.000 description 1
- 230000004957 immunoregulator effect Effects 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 239000011261 inert gas Substances 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000033001 locomotion Effects 0.000 description 1
- 238000004020 luminiscence type Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- VNWKTOKETHGBQD-UHFFFAOYSA-N methane Chemical compound C VNWKTOKETHGBQD-UHFFFAOYSA-N 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 239000004005 microsphere Substances 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 238000007479 molecular analysis Methods 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 229910000403 monosodium phosphate Inorganic materials 0.000 description 1
- 235000019799 monosodium phosphate Nutrition 0.000 description 1
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 108010087904 neutravidin Proteins 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 230000036542 oxidative stress Effects 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 206010033675 panniculitis Diseases 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 230000036961 partial effect Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 239000006187 pill Substances 0.000 description 1
- 239000013612 plasmid Substances 0.000 description 1
- 229920000036 polyvinylpyrrolidone Polymers 0.000 description 1
- 239000001267 polyvinylpyrrolidone Substances 0.000 description 1
- 235000013855 polyvinylpyrrolidone Nutrition 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 150000003141 primary amines Chemical class 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 230000002035 prolonged effect Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 229940043131 pyroglutamate Drugs 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 239000003642 reactive oxygen metabolite Substances 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 230000008929 regeneration Effects 0.000 description 1
- 238000011069 regeneration method Methods 0.000 description 1
- 230000013878 renal filtration Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 102200085014 rs4149117 Human genes 0.000 description 1
- 239000012146 running buffer Substances 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000007423 screening assay Methods 0.000 description 1
- 238000007789 sealing Methods 0.000 description 1
- 238000002864 sequence alignment Methods 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 230000009450 sialylation Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 229940126586 small molecule drug Drugs 0.000 description 1
- AJPJDKMHJJGVTQ-UHFFFAOYSA-M sodium dihydrogen phosphate Chemical compound [Na+].OP(O)([O-])=O AJPJDKMHJJGVTQ-UHFFFAOYSA-M 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 238000001694 spray drying Methods 0.000 description 1
- 239000012089 stop solution Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 230000002459 sustained effect Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 239000006188 syrup Substances 0.000 description 1
- 235000020357 syrup Nutrition 0.000 description 1
- 239000003826 tablet Substances 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- 231100000041 toxicology testing Toxicity 0.000 description 1
- 238000001890 transfection Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 230000009261 transgenic effect Effects 0.000 description 1
- 238000003146 transient transfection Methods 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- 238000002604 ultrasonography Methods 0.000 description 1
- 210000003954 umbilical cord Anatomy 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 210000001364 upper extremity Anatomy 0.000 description 1
- 210000000689 upper leg Anatomy 0.000 description 1
- 238000010200 validation analysis Methods 0.000 description 1
- 238000002424 x-ray crystallography Methods 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/42—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against immunoglobulins
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/04—Drugs for disorders of the alimentary tract or the digestive system for ulcers, gastritis or reflux esophagitis, e.g. antacids, inhibitors of acid secretion, mucosal protectants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- A61P11/02—Nasal agents, e.g. decongestants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
- A61P11/06—Antiasthmatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
- A61P17/06—Antipsoriatics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P19/00—Drugs for skeletal disorders
- A61P19/02—Drugs for skeletal disorders for joint disorders, e.g. arthritis, arthrosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/04—Antibacterial agents
- A61P31/06—Antibacterial agents for tuberculosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/10—Antimycotics
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- A61P31/14—Antivirals for RNA viruses
- A61P31/16—Antivirals for RNA viruses for influenza or rhinoviruses
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P33/00—Antiparasitic 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
- 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
- A61P37/06—Immunosuppressants, e.g. drugs for graft rejection
-
- 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
- A61P37/08—Antiallergic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/10—Drugs for disorders of the cardiovascular system for treating ischaemic or atherosclerotic diseases, e.g. antianginal drugs, coronary vasodilators, drugs for myocardial infarction, retinopathy, cerebrovascula insufficiency, renal arteriosclerosis
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
- A61P9/12—Antihypertensives
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal 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
- C07K16/22—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against growth factors ; against 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
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2878—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the NGF-receptor/TNF-receptor superfamily, e.g. CD27, CD30, CD40, CD95
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
-
- 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
- C07K2317/567—Framework region [FR]
-
- 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
- C07K2317/569—Single domain, e.g. dAb, sdAb, VHH, VNAR or nanobody®
-
- 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
-
- 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
- C07K2317/64—Immunoglobulins specific features characterized by non-natural combinations of immunoglobulin fragments comprising a combination of variable region and constant region components
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Public Health (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Pulmonology (AREA)
- Communicable Diseases (AREA)
- Oncology (AREA)
- Virology (AREA)
- Cardiology (AREA)
- Heart & Thoracic Surgery (AREA)
- Dermatology (AREA)
- Rheumatology (AREA)
- Otolaryngology (AREA)
- Pain & Pain Management (AREA)
- Biomedical Technology (AREA)
- Neurology (AREA)
- Neurosurgery (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Tropical Medicine & Parasitology (AREA)
- Vascular Medicine (AREA)
- Urology & Nephrology (AREA)
- Physical Education & Sports Medicine (AREA)
- Transplantation (AREA)
Priority Applications (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| AU2016277685A AU2016277685B2 (en) | 2011-08-17 | 2016-12-22 | Modified proteins and peptides |
| AU2019201505A AU2019201505A1 (en) | 2011-08-17 | 2019-03-05 | Modified proteins and peptides |
Applications Claiming Priority (11)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201161524488P | 2011-08-17 | 2011-08-17 | |
| US61/524,488 | 2011-08-17 | ||
| GB1121236.2 | 2011-12-12 | ||
| GBGB1121226.3A GB201121226D0 (en) | 2011-12-12 | 2011-12-12 | Modified proteins and peptides |
| GBGB1121233.9A GB201121233D0 (en) | 2011-12-12 | 2011-12-12 | Modified proteins and peptides |
| GBGB1121236.2A GB201121236D0 (en) | 2011-12-12 | 2011-12-12 | Proteins and peptides |
| GB1121233.9 | 2011-12-12 | ||
| GB1121226.3 | 2011-12-12 | ||
| PCT/EP2012/064632 WO2013014208A2 (en) | 2011-07-27 | 2012-07-25 | Antigen binding constructs |
| AUPCT/EP2012/064632 | 2012-07-25 | ||
| PCT/EP2012/065782 WO2013024059A2 (en) | 2011-08-17 | 2012-08-13 | Modified proteins and peptides |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2016277685A Division AU2016277685B2 (en) | 2011-08-17 | 2016-12-22 | Modified proteins and peptides |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| AU2012296961A1 AU2012296961A1 (en) | 2014-03-13 |
| AU2012296961B2 true AU2012296961B2 (en) | 2017-02-16 |
Family
ID=47715521
Family Applications (3)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2012296961A Ceased AU2012296961B2 (en) | 2011-08-17 | 2012-08-13 | Modified proteins and peptides |
| AU2016277685A Ceased AU2016277685B2 (en) | 2011-08-17 | 2016-12-22 | Modified proteins and peptides |
| AU2019201505A Abandoned AU2019201505A1 (en) | 2011-08-17 | 2019-03-05 | Modified proteins and peptides |
Family Applications After (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| AU2016277685A Ceased AU2016277685B2 (en) | 2011-08-17 | 2016-12-22 | Modified proteins and peptides |
| AU2019201505A Abandoned AU2019201505A1 (en) | 2011-08-17 | 2019-03-05 | Modified proteins and peptides |
Country Status (25)
Families Citing this family (96)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ES2860453T3 (es) | 2009-10-30 | 2021-10-05 | Novartis Ag | Bibliotecas universales del dominio de unión del lado inferior de la fibronectina de tipo III |
| EP2621953B1 (en) | 2010-09-30 | 2017-04-05 | Ablynx N.V. | Biological materials related to c-met |
| US11644471B2 (en) | 2010-09-30 | 2023-05-09 | Ablynx N.V. | Techniques for predicting, detecting and reducing aspecific protein interference in assays involving immunoglobulin single variable domains |
| EP2944654A1 (en) * | 2011-06-23 | 2015-11-18 | Ablynx N.V. | Techniques for predicting, detecting and reducing aspecific protein interference in assays involving immunoglobin single variable domains |
| ES2759936T3 (es) | 2011-06-23 | 2020-05-12 | Ablynx Nv | Proteínas de unión a albúmina sérica |
| EP4350345A3 (en) * | 2011-06-23 | 2024-07-24 | Ablynx N.V. | Techniques for predicting, detecting and reducing aspecific protein interference in assays involving immunoglobin single variable domains |
| IL250396B (en) | 2011-06-23 | 2022-06-01 | Ablynx Nv | Techniques for predicting, detecting and reducing aspecific protein interference in assays involving immunoglobulin single variable domains |
| KR102162413B1 (ko) * | 2011-08-17 | 2020-10-07 | 글락소 그룹 리미티드 | 변형된 단백질 및 펩티드 |
| US9346884B2 (en) | 2011-09-30 | 2016-05-24 | Ablynx N.V. | Biological materials related to c-Met |
| US9328174B2 (en) | 2012-05-09 | 2016-05-03 | Novartis Ag | Chemokine receptor binding polypeptides |
| US20140161796A1 (en) * | 2012-09-13 | 2014-06-12 | Andreas Loew | Single chain proteins with c-terminal modifications |
| WO2014111550A1 (en) * | 2013-01-17 | 2014-07-24 | Glaxosmithkline Intellectual Property Development Limited | Modified anti-serum albumin binding proteins |
| WO2015104322A1 (en) * | 2014-01-09 | 2015-07-16 | Glaxosmithkline Intellectual Property Development Limited | Treatment of inflammatory diseases with non-competitive tnfr1 antagonists |
| US11009511B2 (en) | 2014-05-16 | 2021-05-18 | Ablynx N.V. | Methods for detecting and/or measuring anti-drug antibodies, in particular treatment-emergent anti-drug antibodies |
| DK3143042T3 (da) * | 2014-05-16 | 2020-08-31 | Ablynx Nv | Forbedrede variable immunoglobulindomæner |
| KR20250099289A (ko) | 2014-05-16 | 2025-07-01 | 아블린쓰 엔.브이. | 개선된 면역글로불린 가변 도메인 |
| NL2013007B1 (en) | 2014-06-16 | 2016-07-05 | Ablynx Nv | Methods of treating TTP with immunoglobulin single variable domains and uses thereof. |
| CN107484416A (zh) * | 2014-09-26 | 2017-12-15 | 宏观基因有限公司 | 能够结合cd19和cd3的双特异性单价双抗体及其用途 |
| US10526397B2 (en) | 2015-01-21 | 2020-01-07 | Inhibrx, Inc. | Non-immunogenic single domain antibodies |
| EP3271391A1 (en) * | 2015-03-20 | 2018-01-24 | Ablynx N.V. | Glycosylated immunoglobulin single variable domains |
| ES2973042T3 (es) | 2015-03-31 | 2024-06-18 | Sorriso Pharmaceuticals Inc | Polipéptidos |
| WO2016156468A1 (en) | 2015-03-31 | 2016-10-06 | Vhsquared Limited | Polypeptides |
| CN107427577A (zh) | 2015-03-31 | 2017-12-01 | 韦斯夸尔德有限公司 | 具有蛋白酶可切割接头的肽构建体 |
| RS61062B1 (sr) | 2015-07-16 | 2020-12-31 | Inhibrx Inc | Multivalentni i multispecifični dr5-vezujući fuzioni proteini |
| EP4218833A1 (en) | 2015-10-01 | 2023-08-02 | Whitehead Institute for Biomedical Research | Labeling of antibodies |
| EP4036120A1 (en) * | 2015-10-30 | 2022-08-03 | F. Hoffmann-La Roche AG | Hinge modified antibody fragments and methods of making |
| JP6936797B2 (ja) | 2015-10-30 | 2021-09-22 | アブリンクス エン.ヴェー. | Il−23に対するポリペプチド |
| HK1258507A1 (zh) | 2015-11-12 | 2019-11-15 | Ablynx Nv | 改进的p2x7受体结合剂和包含其的多肽 |
| NO2768984T3 (cg-RX-API-DMAC7.html) * | 2015-11-12 | 2018-06-09 | ||
| PL3374392T3 (pl) | 2015-11-13 | 2022-03-28 | Ablynx Nv | Ulepszone domeny zmienne immunoglobuliny wiążące albuminę surowicy |
| KR102220275B1 (ko) * | 2015-11-18 | 2021-02-26 | 머크 샤프 앤드 돔 코포레이션 | Pd1 및/또는 lag3 결합제 |
| CA3003777A1 (en) | 2015-11-18 | 2017-05-26 | Merck Sharp & Dohme Corp. | Pd1/ctla4 binders |
| JP7046804B2 (ja) * | 2015-11-18 | 2022-04-04 | アブリンクス エン.ヴェー. | 改良された血清アルブミン結合剤 |
| CA3004900C (en) | 2015-11-18 | 2021-08-10 | Merck Sharp & Dohme Corp. | Ctla4 binders |
| JP7256011B2 (ja) | 2015-11-27 | 2023-04-11 | アブリンクス エン.ヴェー. | Cd40lを阻害するポリペプチド |
| US10597449B2 (en) | 2015-12-04 | 2020-03-24 | Boehringer Ingelheim International Gmbh | Biparatopic polypeptides antagonizing Wnt signaling in tumor cells |
| GB201522539D0 (en) | 2015-12-21 | 2016-02-03 | Hexcel Composites Ltd | Improvements in or relating to electrically conducting materials |
| KR102374912B1 (ko) * | 2016-06-23 | 2022-03-16 | 아블린쓰 엔.브이. | 면역글로불린 단일 가변 도메인에 대한 개선된 약동학적 어세이 |
| EP3519438A1 (en) | 2016-09-30 | 2019-08-07 | VHsquared Limited | Compositions |
| IL310340A (en) | 2016-12-07 | 2024-03-01 | Ablynx Nv | Improved serum albumin binding immunoglobulin single variable domains |
| US11414481B2 (en) | 2017-01-17 | 2022-08-16 | Ablynx N.V. | Serum albumin binders |
| LT3571224T (lt) | 2017-01-17 | 2024-11-11 | Ablynx Nv | Patobulintos serumo albumino rišamosios medžiagos |
| SG11201908154RA (en) | 2017-03-31 | 2019-10-30 | Ablynx Nv | Improved immunogenicity assays |
| MX2019014331A (es) | 2017-05-31 | 2020-01-27 | Boehringer Ingelheim Int | Polipeptidos que antagonizan la se?alizacion wnt en celulas tumorales. |
| IL317013A (en) | 2017-09-08 | 2025-01-01 | Takeda Pharmaceuticals Co | Binding proteins are activated under limited conditions |
| EP3688030B1 (en) * | 2017-09-27 | 2024-12-11 | Elasmogen Ltd | Specific binding molecules |
| CA3089211A1 (en) * | 2018-02-06 | 2019-08-15 | Ablynx Nv | Methods of treating initial episode of ttp with immunoglobulin single variable domains |
| EP3569618A1 (en) | 2018-05-19 | 2019-11-20 | Boehringer Ingelheim International GmbH | Antagonizing cd73 antibody |
| TWI848953B (zh) | 2018-06-09 | 2024-07-21 | 德商百靈佳殷格翰國際股份有限公司 | 針對癌症治療之多特異性結合蛋白 |
| EP3820891A1 (en) * | 2018-07-10 | 2021-05-19 | Regeneron Pharmaceuticals, Inc. | Modifying binding molecules to minimize pre-existing interactions |
| CN109096394B (zh) * | 2018-09-21 | 2021-11-05 | 成都阿帕克生物科技有限公司 | 一种抗葡萄球菌蛋白a的b亚单位的纳米抗体及核酸分子和应用 |
| FR3088640A1 (fr) | 2018-10-14 | 2020-05-22 | Smart Diagnostix Pharma | Nouveau polypeptide se liant specifiquement a la proteine p16 |
| WO2020089811A1 (en) | 2018-10-31 | 2020-05-07 | Novartis Ag | Dc-sign antibody drug conjugates |
| GB201818460D0 (en) * | 2018-11-13 | 2018-12-26 | Crescendo Biologics Ltd | Single domain antibodies that bind human serum albumin |
| CN114390938B (zh) | 2019-03-05 | 2025-03-21 | 武田药品工业有限公司 | 受约束的条件性活化的结合蛋白 |
| AU2020296979A1 (en) | 2019-06-21 | 2022-02-24 | Sorriso Pharmaceuticals, Inc. | Polypeptides |
| CN114466864B (zh) | 2019-06-21 | 2024-12-27 | 索瑞索制药公司 | 多肽 |
| TWI878355B (zh) | 2019-10-02 | 2025-04-01 | 德商百靈佳殷格翰國際股份有限公司 | 用於癌症治療之多重專一性結合蛋白 |
| GB201914468D0 (en) | 2019-10-07 | 2019-11-20 | Crescendo Biologics Ltd | Binding Molecules |
| AU2020403153A1 (en) * | 2019-12-11 | 2022-06-30 | Cullinan Oncology, Inc. | Anti-serum albumin antibodies |
| WO2021119551A1 (en) * | 2019-12-11 | 2021-06-17 | Cullinan Oncology, Inc. | Anti-cd19 antibodies and multi-specific binding proteins |
| AR121706A1 (es) * | 2020-04-01 | 2022-06-29 | Hoffmann La Roche | Moléculas de unión a antígeno biespecíficas dirigidas a ox40 y fap |
| CA3191431A1 (en) | 2020-08-17 | 2022-02-24 | Takeda Pharmaceutical Company Limited | Constrained conditionally activated binding proteins |
| CN114075282B (zh) * | 2020-08-20 | 2024-01-02 | 南京融捷康生物科技有限公司 | Il-5的结合分子及其制备方法和应用 |
| CN116847887A (zh) * | 2020-08-27 | 2023-10-03 | 伊诺西治疗公司 | 治疗自身免疫性疾病和癌症的方法和组合物 |
| WO2022051647A2 (en) | 2020-09-04 | 2022-03-10 | Maverick Therapeutics, Inc. | Constrained conditionally activated binding protein constructs with human serum albumin domains |
| WO2022081460A1 (en) * | 2020-10-12 | 2022-04-21 | Janssen Biotech, Inc. | Biosynthetic materials and methods for multidirectional biotransportation |
| CN112225807B (zh) * | 2020-10-30 | 2021-09-07 | 上海洛启生物医药技术有限公司 | 抗il5纳米抗体及其应用 |
| KR20230131210A (ko) | 2020-12-14 | 2023-09-12 | 다케다 야쿠힌 고교 가부시키가이샤 | 조건부 이중특이성 결합 단백질 |
| CN112341543B (zh) * | 2021-01-11 | 2021-04-23 | 广东赛尔生物科技有限公司 | 包含间充质干细胞外泌体的药物组合物在治疗疾病中的应用 |
| US20240199744A1 (en) | 2021-04-06 | 2024-06-20 | Takeda Pharmaceutical Company Limited | Therapeutic methods using constrained conditionally activated binding proteins |
| CN118339179A (zh) * | 2021-11-29 | 2024-07-12 | 江苏恒瑞医药股份有限公司 | 经修饰的蛋白或多肽 |
| WO2023110190A1 (en) | 2021-12-13 | 2023-06-22 | Heraeus Medical Gmbh | Tests and methods for detecting bacterial infection |
| KR20240135660A (ko) * | 2022-01-27 | 2024-09-11 | 얀센 바이오테크 인코포레이티드 | 향상된 단백질 조성물 |
| TW202342521A (zh) | 2022-02-23 | 2023-11-01 | 日商武田藥品工業股份有限公司 | 條件性雙特異性結合蛋白 |
| JP2025526384A (ja) | 2022-07-27 | 2025-08-13 | アブリンクス エン.ヴェー. | 新生児型Fc受容体の特異的エピトープに結合するポリペプチド |
| EP4357778A1 (en) | 2022-10-20 | 2024-04-24 | Heraeus Medical GmbH | Treatment of microbial infections diagnosed using the biomarker d-lactate |
| CN115819599B (zh) * | 2022-11-29 | 2024-01-16 | 江苏耀海生物制药有限公司 | 一种利用重组大肠杆菌分泌表达纳米抗体Cablivi的方法 |
| CN120529914A (zh) | 2023-01-09 | 2025-08-22 | 奥德赛治疗股份有限公司 | 抗tnfr2抗原结合蛋白及其用途 |
| KR20250151445A (ko) | 2023-02-17 | 2025-10-21 | 아블린쓰 엔.브이. | 신생아 fc 수용체에 결합하는 폴리펩티드 |
| TW202444757A (zh) | 2023-03-14 | 2024-11-16 | 美商奧迪希治療公司 | 抗cd25抗原結合蛋白及其用途 |
| WO2024220763A1 (en) * | 2023-04-20 | 2024-10-24 | Xentria, Inc. | Methods for detecting an anti-drug antibody (ada) against an anti-tnf alpha antibody |
| AR132699A1 (es) * | 2023-05-17 | 2025-07-23 | Odyssey Therapeutics Inc | Anticuerpos de dominio único modificados |
| WO2025006846A2 (en) | 2023-06-29 | 2025-01-02 | Odyssey Therapeutics, Inc. | Anti-trailr2 antigen-binding proteins and uses thereof |
| AR133188A1 (es) | 2023-07-05 | 2025-09-03 | Ablynx Nv | ANTAGONISTAS DE FcRn MEJORADOS PARA EL TRATAMIENTO DE ENFERMEDADES Y TRASTORNOS RELACIONADOS CON IgG |
| TW202525838A (zh) | 2023-08-30 | 2025-07-01 | 美商艾希利歐發展股份有限公司 | 經遮蔽il-2細胞介素及其使用方法 |
| WO2025049750A1 (en) | 2023-08-30 | 2025-03-06 | Xilio Development, Inc. | Vhh masked cytokines and methods of use thereof |
| WO2025061919A1 (en) | 2023-09-22 | 2025-03-27 | Ablynx Nv | Bi- and multivalent albumin binders |
| TW202530265A (zh) | 2023-10-13 | 2025-08-01 | 美商奧迪希治療公司 | 抗cdh17抗原結合蛋白及其用途 |
| CN119173537A (zh) * | 2024-01-03 | 2024-12-20 | 苏州智核生物医药科技有限公司 | 经修饰的免疫球蛋白单一可变结构域 |
| US20250250314A1 (en) | 2024-01-10 | 2025-08-07 | Xilio Development, Inc. | Masked il-2 cytokines and methods of use thereof |
| WO2025167664A1 (zh) * | 2024-02-07 | 2025-08-14 | 原启生物科技(上海)有限责任公司 | Ror1抗原结合蛋白及其用途 |
| WO2025189977A1 (zh) * | 2024-03-13 | 2025-09-18 | 寻济生物科技(北京)有限公司 | 一种抗vegfa融合构建体及其制备方法和应用 |
| WO2025217240A1 (en) | 2024-04-10 | 2025-10-16 | Odyssey Therapeutics, Inc. | Anti-tnfr2 antigen-binding proteins and uses thereof |
| WO2025255558A2 (en) | 2024-06-07 | 2025-12-11 | Odyssey Therapeutics, Inc. | Anti-thymic stromal lymphopoietin (tslp) antigen-binding proteins and uses thereof |
| WO2025255435A2 (en) | 2024-06-07 | 2025-12-11 | Odyssey Therapeutics, Inc. | Antigen-binding proteins against serum albumin and uses thereof |
Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004003019A2 (en) * | 2002-06-28 | 2004-01-08 | Domantis Limited | Immunoglobin single variant antigen-binding domains and dual-specific constructs |
| WO2006129843A2 (en) * | 2005-05-31 | 2006-12-07 | Canon Kabushiki Kaisha | Bispecific capturing molecule |
| WO2007063311A2 (en) * | 2005-12-01 | 2007-06-07 | Domantis Limited | Competitive domain antibody formats that bind interleukin 1 receptor type 1 |
| WO2007063308A2 (en) * | 2005-12-01 | 2007-06-07 | Domantis Limited | Noncompetitive domain antibody formats that bind interleukin 1 receptor type 1 |
| WO2009068627A2 (en) * | 2007-11-27 | 2009-06-04 | Ablynx N.V. | Amino acid sequences directed against heterodimeric cytokines and/or their receptors and polypeptides comprising the same |
| WO2012042026A1 (en) * | 2010-09-30 | 2012-04-05 | Ablynx Nv | Biological materials related to c-met |
Family Cites Families (35)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU8507191A (en) | 1990-08-29 | 1992-03-30 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
| PT1589107E (pt) | 1992-08-21 | 2010-03-29 | Univ Bruxelles | Imunoglobulinas desprovidas de cadeias leves |
| FR2708622B1 (fr) | 1993-08-02 | 1997-04-18 | Raymond Hamers | Vecteur recombinant contenant une séquence d'un gène de lipoprotéine de structure pour l'expression de séquences de nucléotides. |
| IL127127A0 (en) * | 1998-11-18 | 1999-09-22 | Peptor Ltd | Small functional units of antibody heavy chain variable regions |
| US20050271663A1 (en) | 2001-06-28 | 2005-12-08 | Domantis Limited | Compositions and methods for treating inflammatory disorders |
| US20060073141A1 (en) | 2001-06-28 | 2006-04-06 | Domantis Limited | Compositions and methods for treating inflammatory disorders |
| CA2492671C (en) | 2002-03-22 | 2012-04-17 | Aprogen, Inc. | Humanized antibody and process for preparing same |
| US7563443B2 (en) * | 2004-09-17 | 2009-07-21 | Domantis Limited | Monovalent anti-CD40L antibody polypeptides and compositions thereof |
| GB0521621D0 (en) | 2005-10-24 | 2005-11-30 | Domantis Ltd | Tumor necrosis factor receptor 1 antagonists for treating respiratory diseases |
| BRPI0609797B8 (pt) * | 2005-05-20 | 2021-05-25 | Ablynx Nv | nanocorpos melhorados para o tratamento de desordens mediadas por agregação |
| DE102005023617A1 (de) * | 2005-05-21 | 2006-11-23 | Aspre Ag | Verfahren zum Mischen von Farben in einem Display |
| JP2007008925A (ja) * | 2005-05-31 | 2007-01-18 | Canon Inc | 標的物質捕捉分子 |
| JP2009508521A (ja) | 2005-09-23 | 2009-03-05 | アカデミッシュ ジーケンハイス レイデン | タンパク凝集に関連する疾患の診断予防及び治療のためのvhh |
| EP1976991A1 (en) * | 2006-01-24 | 2008-10-08 | Domantis Limited | Fusion proteins that contain natural junctions |
| US8629244B2 (en) | 2006-08-18 | 2014-01-14 | Ablynx N.V. | Interleukin-6 receptor binding polypeptides |
| US20100143340A1 (en) * | 2006-12-13 | 2010-06-10 | Schering Corporation | Methods and compositions for treating cancer |
| AU2008254951A1 (en) | 2007-05-14 | 2008-11-27 | Biogen Idec Ma Inc. | Single-chain Fc (ScFc) regions, binding polypeptides comprising same, and methods related thereto |
| JP2010528647A (ja) | 2007-06-06 | 2010-08-26 | ドマンティス リミテッド | ポリペプチド、抗体可変ドメインおよびアンタゴニスト |
| CA2688434A1 (en) * | 2007-06-06 | 2008-12-11 | Domantis Limited | Polypeptides, antibody variable domains and antagonists |
| GB0724331D0 (en) * | 2007-12-13 | 2008-01-23 | Domantis Ltd | Compositions for pulmonary delivery |
| AR069495A1 (es) | 2007-11-30 | 2010-01-27 | Glaxo Group Ltd | Construcciones de union de antigenos para el tratamiento de cancer o enfermedades inflamatorias (asma, artritis o artrosis) |
| TW200938222A (en) | 2007-12-13 | 2009-09-16 | Glaxo Group Ltd | Compositions for pulmonary delivery |
| CN101977654A (zh) | 2008-03-21 | 2011-02-16 | 埃博灵克斯股份有限公司 | 冯威勒布兰特因子特异性结合物及其应用方法 |
| US8020937B2 (en) * | 2008-07-31 | 2011-09-20 | Lear Corporation | Layered technology for energy management of vehicle seating |
| WO2010017595A1 (en) * | 2008-08-14 | 2010-02-18 | Arana Therapeutics Limited | Variant domain antibodies |
| KR101593285B1 (ko) | 2008-10-29 | 2016-02-11 | 아블린쓰 엔.브이. | 단일 도메인 항원 결합 분자의 제형 |
| US10005830B2 (en) | 2009-03-05 | 2018-06-26 | Ablynx N.V. | Antigen binding dimer-complexes, methods of making/avoiding and uses thereof |
| SG174862A1 (en) * | 2009-04-10 | 2011-11-28 | Ablynx Nv | Improved amino acid sequences directed against il-6r and polypeptides comprising the same for the treatment of il-6r related diseases and disorder |
| HUE051430T2 (hu) * | 2009-07-10 | 2021-03-01 | Ablynx Nv | Eljárás variábilis domének elõállítására |
| GB201005063D0 (en) * | 2010-03-25 | 2010-05-12 | Ucb Pharma Sa | Biological products |
| TW201132759A (en) * | 2009-12-18 | 2011-10-01 | Sanofi Aventis | Novel antagonist antibodies and their FaB fragments against GPVI and uses thereof |
| IL250396B (en) * | 2011-06-23 | 2022-06-01 | Ablynx Nv | Techniques for predicting, detecting and reducing aspecific protein interference in assays involving immunoglobulin single variable domains |
| EP2944654A1 (en) * | 2011-06-23 | 2015-11-18 | Ablynx N.V. | Techniques for predicting, detecting and reducing aspecific protein interference in assays involving immunoglobin single variable domains |
| KR102162413B1 (ko) * | 2011-08-17 | 2020-10-07 | 글락소 그룹 리미티드 | 변형된 단백질 및 펩티드 |
| WO2014111550A1 (en) | 2013-01-17 | 2014-07-24 | Glaxosmithkline Intellectual Property Development Limited | Modified anti-serum albumin binding proteins |
-
2012
- 2012-08-13 KR KR1020147006909A patent/KR102162413B1/ko active Active
- 2012-08-13 ES ES12746095T patent/ES2813432T3/es active Active
- 2012-08-13 EP EP17191815.4A patent/EP3339322A3/en active Pending
- 2012-08-13 MX MX2014001883A patent/MX2014001883A/es unknown
- 2012-08-13 CN CN201810128962.3A patent/CN108178800B/zh active Active
- 2012-08-13 EA EA201490262A patent/EA027160B1/ru not_active IP Right Cessation
- 2012-08-13 SG SG10201605891TA patent/SG10201605891TA/en unknown
- 2012-08-13 AU AU2012296961A patent/AU2012296961B2/en not_active Ceased
- 2012-08-13 US US14/239,196 patent/US10808040B2/en active Active
- 2012-08-13 CN CN201280051150.4A patent/CN103917557B/zh active Active
- 2012-08-13 CA CA2845029A patent/CA2845029A1/en active Pending
- 2012-08-13 KR KR1020197027997A patent/KR102143506B1/ko active Active
- 2012-08-13 UA UAA201401344A patent/UA118833C2/uk unknown
- 2012-08-13 PE PE2014000214A patent/PE20141522A1/es active IP Right Grant
- 2012-08-13 JP JP2014525418A patent/JP6297976B2/ja active Active
- 2012-08-13 UY UY0001034254A patent/UY34254A/es not_active Application Discontinuation
- 2012-08-13 TW TW101129262A patent/TW201321405A/zh unknown
- 2012-08-13 EP EP12746095.4A patent/EP2744822B1/en active Active
- 2012-08-13 BR BR112014003679-9A patent/BR112014003679B1/pt active IP Right Grant
- 2012-08-13 MY MYPI2014700336A patent/MY167125A/en unknown
- 2012-08-13 AR ARP120102955A patent/AR087521A1/es unknown
- 2012-08-13 EP EP15180982.9A patent/EP2987806A3/en active Pending
- 2012-08-13 PH PH1/2014/500380A patent/PH12014500380A1/en unknown
- 2012-08-13 WO PCT/EP2012/065782 patent/WO2013024059A2/en not_active Ceased
- 2012-08-13 SG SG2014010482A patent/SG2014010482A/en unknown
-
2014
- 2014-02-11 IL IL230918A patent/IL230918A0/en unknown
- 2014-02-12 CO CO14029997A patent/CO7020851A2/es unknown
- 2014-02-17 DO DO2014000029A patent/DOP2014000029A/es unknown
- 2014-03-06 MA MA36807A patent/MA35428B1/fr unknown
- 2014-06-26 HK HK16102229.1A patent/HK1214281A1/en unknown
-
2016
- 2016-12-22 AU AU2016277685A patent/AU2016277685B2/en not_active Ceased
-
2018
- 2018-02-22 JP JP2018029267A patent/JP2018117623A/ja not_active Withdrawn
-
2019
- 2019-03-05 AU AU2019201505A patent/AU2019201505A1/en not_active Abandoned
- 2019-12-09 JP JP2019222041A patent/JP6979446B2/ja active Active
-
2020
- 2020-09-08 US US17/014,441 patent/US20210017293A1/en not_active Abandoned
-
2024
- 2024-09-23 US US18/893,457 patent/US20250136721A1/en active Pending
Patent Citations (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004003019A2 (en) * | 2002-06-28 | 2004-01-08 | Domantis Limited | Immunoglobin single variant antigen-binding domains and dual-specific constructs |
| WO2006129843A2 (en) * | 2005-05-31 | 2006-12-07 | Canon Kabushiki Kaisha | Bispecific capturing molecule |
| WO2007063311A2 (en) * | 2005-12-01 | 2007-06-07 | Domantis Limited | Competitive domain antibody formats that bind interleukin 1 receptor type 1 |
| WO2007063308A2 (en) * | 2005-12-01 | 2007-06-07 | Domantis Limited | Noncompetitive domain antibody formats that bind interleukin 1 receptor type 1 |
| WO2009068627A2 (en) * | 2007-11-27 | 2009-06-04 | Ablynx N.V. | Amino acid sequences directed against heterodimeric cytokines and/or their receptors and polypeptides comprising the same |
| WO2012042026A1 (en) * | 2010-09-30 | 2012-04-05 | Ablynx Nv | Biological materials related to c-met |
Also Published As
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US20250136721A1 (en) | Modified proteins and peptides | |
| KR102662499B1 (ko) | 개선된 혈청 알부민 결합제 | |
| KR102653724B1 (ko) | 개선된 혈청 알부민 결합제 | |
| WO2014111550A1 (en) | Modified anti-serum albumin binding proteins | |
| JP2016007218A (ja) | 改善された抗tnfr1ポリペプチド、抗体可変ドメインおよびアンタゴニスト | |
| KR20120101417A (ko) | 안정한 항?tnfr1 폴리펩티드,항체 가변 도메인 및 길항제 | |
| EP2742068A1 (en) | New antibodies against phosphorylcholine | |
| NZ621203B2 (en) | Modified proteins and peptides | |
| RU2789495C2 (ru) | Усовершенствованные связывающиеся с сывороточным альбумином вещества | |
| WO2023288078A1 (en) | Coronavirus antibodies and uses thereof | |
| WO2025223473A1 (zh) | 抗gdf-15抗体及其应用 | |
| WO2022012639A1 (zh) | Pd-1抗原结合蛋白及其应用 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| FGA | Letters patent sealed or granted (standard patent) | ||
| MK14 | Patent ceased section 143(a) (annual fees not paid) or expired |