GB2528401A - Anti-nerve growth factor antibodies and methods of preparing and using the same - Google Patents
Anti-nerve growth factor antibodies and methods of preparing and using the same Download PDFInfo
- Publication number
- GB2528401A GB2528401A GB1517547.4A GB201517547A GB2528401A GB 2528401 A GB2528401 A GB 2528401A GB 201517547 A GB201517547 A GB 201517547A GB 2528401 A GB2528401 A GB 2528401A
- Authority
- GB
- United Kingdom
- Prior art keywords
- amino acid
- seq
- antibody
- acid sequence
- canine
- 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.)
- Withdrawn
Links
- 238000000034 method Methods 0.000 title claims abstract description 146
- 229940053128 nerve growth factor Drugs 0.000 title claims description 230
- 241000282465 Canis Species 0.000 claims abstract description 235
- 208000002193 Pain Diseases 0.000 claims abstract description 110
- 230000036407 pain Effects 0.000 claims abstract description 90
- 125000000539 amino acid group Chemical group 0.000 claims abstract description 67
- 150000001413 amino acids Chemical class 0.000 claims abstract description 56
- 206010003246 arthritis Diseases 0.000 claims abstract description 22
- 241000894007 species Species 0.000 claims abstract description 13
- 101150111783 NTRK1 gene Proteins 0.000 claims abstract description 8
- 108091008604 NGF receptors Proteins 0.000 claims abstract description 7
- 102000007339 Nerve Growth Factor Receptors Human genes 0.000 claims abstract description 7
- 230000027455 binding Effects 0.000 claims description 264
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 249
- 108010025020 Nerve Growth Factor Proteins 0.000 claims description 229
- 102000015336 Nerve Growth Factor Human genes 0.000 claims description 227
- 239000012634 fragment Substances 0.000 claims description 158
- 239000000427 antigen Substances 0.000 claims description 81
- 102000036639 antigens Human genes 0.000 claims description 81
- 108091007433 antigens Proteins 0.000 claims description 81
- 238000006467 substitution reaction Methods 0.000 claims description 48
- 206010028980 Neoplasm Diseases 0.000 claims description 27
- 230000006870 function Effects 0.000 claims description 20
- 239000008194 pharmaceutical composition Substances 0.000 claims description 20
- 201000008482 osteoarthritis Diseases 0.000 claims description 17
- 206010039073 rheumatoid arthritis Diseases 0.000 claims description 17
- 239000012636 effector Substances 0.000 claims description 14
- 230000001404 mediated effect Effects 0.000 claims description 14
- 230000002401 inhibitory effect Effects 0.000 claims description 12
- 206010036030 Polyarthritis Diseases 0.000 claims description 9
- 208000030428 polyarticular arthritis Diseases 0.000 claims description 9
- 230000005764 inhibitory process Effects 0.000 claims description 8
- 239000003085 diluting agent Substances 0.000 claims description 6
- 239000003937 drug carrier Substances 0.000 claims description 6
- 238000012217 deletion Methods 0.000 claims description 5
- 230000037430 deletion Effects 0.000 claims description 5
- 239000000546 pharmaceutical excipient Substances 0.000 claims description 4
- 102220585298 Serine/threonine-protein kinase STK11_E16G_mutation Human genes 0.000 claims 2
- 102220005320 rs33945546 Human genes 0.000 claims 2
- 102220126689 rs886044337 Human genes 0.000 claims 2
- 102220509400 E3 ubiquitin-protein ligase HUWE1_T27V_mutation Human genes 0.000 claims 1
- 102220486979 Sodium-dependent phosphate transport protein 1_S76N_mutation Human genes 0.000 claims 1
- 102220590621 Spindlin-1_T19R_mutation Human genes 0.000 claims 1
- 102220519680 Transcription factor E2F1_E14D_mutation Human genes 0.000 claims 1
- 102220281547 rs1555514410 Human genes 0.000 claims 1
- 102220039281 rs199473357 Human genes 0.000 claims 1
- 102220046945 rs267608437 Human genes 0.000 claims 1
- 102200021640 rs2722372 Human genes 0.000 claims 1
- 102200027728 rs62642916 Human genes 0.000 claims 1
- 150000007523 nucleic acids Chemical class 0.000 abstract description 50
- 102000039446 nucleic acids Human genes 0.000 abstract description 47
- 108020004707 nucleic acids Proteins 0.000 abstract description 47
- 239000003102 growth factor Substances 0.000 abstract description 2
- 230000007514 neuronal growth Effects 0.000 abstract description 2
- 235000001014 amino acid Nutrition 0.000 description 85
- 229940024606 amino acid Drugs 0.000 description 59
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 37
- 210000004027 cell Anatomy 0.000 description 33
- 230000003472 neutralizing effect Effects 0.000 description 33
- 229910052740 iodine Inorganic materials 0.000 description 32
- 108090000765 processed proteins & peptides Proteins 0.000 description 30
- 108090000623 proteins and genes Proteins 0.000 description 30
- 235000018102 proteins Nutrition 0.000 description 28
- 102000004169 proteins and genes Human genes 0.000 description 28
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 27
- 229920001184 polypeptide Polymers 0.000 description 27
- 102000004196 processed proteins & peptides Human genes 0.000 description 27
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 26
- 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 25
- 241000282472 Canis lupus familiaris Species 0.000 description 23
- 229910052731 fluorine Inorganic materials 0.000 description 23
- 239000000203 mixture Substances 0.000 description 23
- 230000000295 complement effect Effects 0.000 description 22
- 239000003814 drug Substances 0.000 description 22
- 229910052717 sulfur Inorganic materials 0.000 description 22
- 239000013604 expression vector Substances 0.000 description 21
- 230000014509 gene expression Effects 0.000 description 20
- 241000282414 Homo sapiens Species 0.000 description 19
- 229910052757 nitrogen Inorganic materials 0.000 description 19
- 239000006228 supernatant Substances 0.000 description 18
- 229910052739 hydrogen Inorganic materials 0.000 description 17
- 238000004519 manufacturing process Methods 0.000 description 17
- 229910052700 potassium Inorganic materials 0.000 description 17
- 208000000094 Chronic Pain Diseases 0.000 description 16
- 229910052698 phosphorus Inorganic materials 0.000 description 16
- 230000037396 body weight Effects 0.000 description 14
- 239000003795 chemical substances by application Substances 0.000 description 14
- 108091033319 polynucleotide Proteins 0.000 description 14
- 102000040430 polynucleotide Human genes 0.000 description 14
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 13
- 239000002157 polynucleotide Substances 0.000 description 13
- 208000004550 Postoperative Pain Diseases 0.000 description 12
- 238000005571 anion exchange chromatography Methods 0.000 description 12
- 230000004048 modification Effects 0.000 description 12
- 238000012986 modification Methods 0.000 description 12
- 238000002360 preparation method Methods 0.000 description 12
- 239000013598 vector Substances 0.000 description 12
- 229940124597 therapeutic agent Drugs 0.000 description 11
- 206010065390 Inflammatory pain Diseases 0.000 description 10
- 238000000746 purification Methods 0.000 description 10
- 238000001542 size-exclusion chromatography Methods 0.000 description 10
- 108020004414 DNA Proteins 0.000 description 9
- 108060003951 Immunoglobulin Proteins 0.000 description 9
- 206010061218 Inflammation Diseases 0.000 description 9
- 239000002253 acid Substances 0.000 description 9
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 9
- 102000018358 immunoglobulin Human genes 0.000 description 9
- 230000004054 inflammatory process Effects 0.000 description 9
- 241001465754 Metazoa Species 0.000 description 8
- 241000700159 Rattus Species 0.000 description 8
- 230000010056 antibody-dependent cellular cytotoxicity Effects 0.000 description 8
- 230000002917 arthritic effect Effects 0.000 description 8
- 230000004071 biological effect Effects 0.000 description 8
- 239000000872 buffer Substances 0.000 description 8
- 229910052805 deuterium Inorganic materials 0.000 description 8
- 230000013595 glycosylation Effects 0.000 description 8
- 238000006206 glycosylation reaction Methods 0.000 description 8
- 208000030175 lameness Diseases 0.000 description 8
- 208000004296 neuralgia Diseases 0.000 description 8
- 210000002966 serum Anatomy 0.000 description 8
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 8
- 102100036220 PC4 and SFRS1-interacting protein Human genes 0.000 description 7
- 239000005557 antagonist Substances 0.000 description 7
- 230000000694 effects Effects 0.000 description 7
- 238000009472 formulation Methods 0.000 description 7
- 230000002163 immunogen Effects 0.000 description 7
- 208000021722 neuropathic pain Diseases 0.000 description 7
- 229940021182 non-steroidal anti-inflammatory drug Drugs 0.000 description 7
- 201000008968 osteosarcoma Diseases 0.000 description 7
- 239000002953 phosphate buffered saline Substances 0.000 description 7
- 230000002265 prevention Effects 0.000 description 7
- -1 such as an antibody Proteins 0.000 description 7
- 238000001356 surgical procedure Methods 0.000 description 7
- 108010076504 Protein Sorting Signals Proteins 0.000 description 6
- 230000004913 activation Effects 0.000 description 6
- 239000003638 chemical reducing agent Substances 0.000 description 6
- 230000008021 deposition Effects 0.000 description 6
- 239000000499 gel Substances 0.000 description 6
- 238000001727 in vivo Methods 0.000 description 6
- 238000012829 orthopaedic surgery Methods 0.000 description 6
- 230000001823 pruritic effect Effects 0.000 description 6
- 210000004872 soft tissue Anatomy 0.000 description 6
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 5
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 5
- 239000013543 active substance Substances 0.000 description 5
- 238000001042 affinity chromatography Methods 0.000 description 5
- 230000008901 benefit Effects 0.000 description 5
- 201000011510 cancer Diseases 0.000 description 5
- 239000013019 capto adhere Substances 0.000 description 5
- 230000005847 immunogenicity Effects 0.000 description 5
- 239000012071 phase Substances 0.000 description 5
- 230000001105 regulatory effect Effects 0.000 description 5
- 150000003431 steroids Chemical class 0.000 description 5
- 102000015533 trkA Receptor Human genes 0.000 description 5
- 108010064884 trkA Receptor Proteins 0.000 description 5
- 239000003981 vehicle Substances 0.000 description 5
- 238000002965 ELISA Methods 0.000 description 4
- 101100404651 Mus musculus Ngf gene Proteins 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 208000005298 acute pain Diseases 0.000 description 4
- 230000000202 analgesic effect Effects 0.000 description 4
- 230000003305 autocrine Effects 0.000 description 4
- 208000010877 cognitive disease Diseases 0.000 description 4
- 239000003246 corticosteroid Substances 0.000 description 4
- 238000010790 dilution Methods 0.000 description 4
- 239000012895 dilution Substances 0.000 description 4
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 4
- 238000005516 engineering process Methods 0.000 description 4
- 230000005714 functional activity Effects 0.000 description 4
- 108020001507 fusion proteins Proteins 0.000 description 4
- 102000037865 fusion proteins Human genes 0.000 description 4
- 230000028993 immune response Effects 0.000 description 4
- 210000000987 immune system Anatomy 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- 230000007774 longterm Effects 0.000 description 4
- 210000004962 mammalian cell Anatomy 0.000 description 4
- 239000000041 non-steroidal anti-inflammatory agent Substances 0.000 description 4
- 230000003076 paracrine Effects 0.000 description 4
- 238000003752 polymerase chain reaction Methods 0.000 description 4
- 102000005962 receptors Human genes 0.000 description 4
- 108020003175 receptors Proteins 0.000 description 4
- 230000001225 therapeutic effect Effects 0.000 description 4
- 210000001519 tissue Anatomy 0.000 description 4
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 3
- 239000005995 Aluminium silicate Substances 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 102000009109 Fc receptors Human genes 0.000 description 3
- 108010087819 Fc receptors Proteins 0.000 description 3
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 208000004454 Hyperalgesia Diseases 0.000 description 3
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 3
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 3
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 3
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 3
- 241001529936 Murinae Species 0.000 description 3
- 229920001213 Polysorbate 20 Polymers 0.000 description 3
- 208000003251 Pruritus Diseases 0.000 description 3
- 238000007792 addition Methods 0.000 description 3
- 235000012211 aluminium silicate Nutrition 0.000 description 3
- 229940035676 analgesics Drugs 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 239000000730 antalgic agent Substances 0.000 description 3
- 230000008827 biological function Effects 0.000 description 3
- 210000004899 c-terminal region Anatomy 0.000 description 3
- 229910052799 carbon Inorganic materials 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 238000010367 cloning Methods 0.000 description 3
- 239000002299 complementary DNA Substances 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 238000012258 culturing Methods 0.000 description 3
- 230000001419 dependent effect Effects 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 230000002255 enzymatic effect Effects 0.000 description 3
- 230000002209 hydrophobic effect Effects 0.000 description 3
- 230000001900 immune effect Effects 0.000 description 3
- 238000001802 infusion Methods 0.000 description 3
- 238000001990 intravenous administration Methods 0.000 description 3
- 238000004255 ion exchange chromatography Methods 0.000 description 3
- NLYAJNPCOHFWQQ-UHFFFAOYSA-N kaolin Chemical compound O.O.O=[Al]O[Si](=O)O[Si](=O)O[Al]=O NLYAJNPCOHFWQQ-UHFFFAOYSA-N 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 239000013642 negative control Substances 0.000 description 3
- 238000011017 operating method Methods 0.000 description 3
- 208000035824 paresthesia Diseases 0.000 description 3
- 238000010647 peptide synthesis reaction Methods 0.000 description 3
- 230000036470 plasma concentration Effects 0.000 description 3
- 239000013612 plasmid Substances 0.000 description 3
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 3
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 3
- 230000002980 postoperative effect Effects 0.000 description 3
- 239000000047 product Substances 0.000 description 3
- 230000035755 proliferation Effects 0.000 description 3
- 230000011664 signaling Effects 0.000 description 3
- 239000000126 substance Substances 0.000 description 3
- 239000004094 surface-active agent Substances 0.000 description 3
- 238000003786 synthesis reaction Methods 0.000 description 3
- 238000005406 washing Methods 0.000 description 3
- 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 2
- FTOAOBMCPZCFFF-UHFFFAOYSA-N 5,5-diethylbarbituric acid Chemical compound CCC1(CC)C(=O)NC(=O)NC1=O FTOAOBMCPZCFFF-UHFFFAOYSA-N 0.000 description 2
- 239000005541 ACE inhibitor Substances 0.000 description 2
- RZVAJINKPMORJF-UHFFFAOYSA-N Acetaminophen Chemical compound CC(=O)NC1=CC=C(O)C=C1 RZVAJINKPMORJF-UHFFFAOYSA-N 0.000 description 2
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 2
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 2
- BPYKTIZUTYGOLE-IFADSCNNSA-N Bilirubin Chemical compound N1C(=O)C(C)=C(C=C)\C1=C\C1=C(C)C(CCC(O)=O)=C(CC2=C(C(C)=C(\C=C/3C(=C(C=C)C(=O)N\3)C)N2)CCC(O)=O)N1 BPYKTIZUTYGOLE-IFADSCNNSA-N 0.000 description 2
- 229940127291 Calcium channel antagonist Drugs 0.000 description 2
- 208000028698 Cognitive impairment Diseases 0.000 description 2
- 108020004635 Complementary DNA Proteins 0.000 description 2
- PMATZTZNYRCHOR-CGLBZJNRSA-N Cyclosporin A Chemical compound CC[C@@H]1NC(=O)[C@H]([C@H](O)[C@H](C)C\C=C\C)N(C)C(=O)[C@H](C(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](CC(C)C)N(C)C(=O)[C@@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)N(C)C(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)N(C)C(=O)CN(C)C1=O PMATZTZNYRCHOR-CGLBZJNRSA-N 0.000 description 2
- 108010036949 Cyclosporine Proteins 0.000 description 2
- SRBFZHDQGSBBOR-IOVATXLUSA-N D-xylopyranose Chemical compound O[C@@H]1COC(O)[C@H](O)[C@H]1O SRBFZHDQGSBBOR-IOVATXLUSA-N 0.000 description 2
- 238000009007 Diagnostic Kit Methods 0.000 description 2
- 238000012286 ELISA Assay Methods 0.000 description 2
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 2
- 108010010803 Gelatin Proteins 0.000 description 2
- 229940121710 HMGCoA reductase inhibitor Drugs 0.000 description 2
- 241000282412 Homo Species 0.000 description 2
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 2
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 2
- 108700005091 Immunoglobulin Genes Proteins 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 102000007072 Nerve Growth Factors Human genes 0.000 description 2
- 108090000189 Neuropeptides Proteins 0.000 description 2
- 108091028043 Nucleic acid sequence Proteins 0.000 description 2
- 108020004511 Recombinant DNA Proteins 0.000 description 2
- 239000008156 Ringer's lactate solution Substances 0.000 description 2
- 240000005578 Rivina humilis Species 0.000 description 2
- 108010003723 Single-Domain Antibodies Proteins 0.000 description 2
- 241000191940 Staphylococcus Species 0.000 description 2
- 239000004473 Threonine Substances 0.000 description 2
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- 230000002378 acidificating effect Effects 0.000 description 2
- 239000000674 adrenergic antagonist Substances 0.000 description 2
- 239000000556 agonist Substances 0.000 description 2
- 206010053552 allodynia Diseases 0.000 description 2
- 230000003042 antagnostic effect Effects 0.000 description 2
- 239000003242 anti bacterial agent Substances 0.000 description 2
- 230000000843 anti-fungal effect Effects 0.000 description 2
- 230000003276 anti-hypertensive effect Effects 0.000 description 2
- 230000003110 anti-inflammatory effect Effects 0.000 description 2
- 230000000842 anti-protozoal effect Effects 0.000 description 2
- 230000000840 anti-viral effect Effects 0.000 description 2
- 229940121375 antifungal agent Drugs 0.000 description 2
- 239000003904 antiprotozoal agent Substances 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 230000005784 autoimmunity Effects 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 102000012740 beta Adrenergic Receptors Human genes 0.000 description 2
- 108010079452 beta Adrenergic Receptors Proteins 0.000 description 2
- 238000013357 binding ELISA Methods 0.000 description 2
- 230000003115 biocidal effect Effects 0.000 description 2
- 230000000903 blocking effect Effects 0.000 description 2
- 239000000480 calcium channel blocker Substances 0.000 description 2
- 150000001720 carbohydrates Chemical group 0.000 description 2
- 230000004706 cardiovascular dysfunction Effects 0.000 description 2
- 239000000969 carrier Substances 0.000 description 2
- 238000004113 cell culture Methods 0.000 description 2
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 2
- 229960001265 ciclosporin Drugs 0.000 description 2
- 239000007819 coupling partner Substances 0.000 description 2
- DDRJAANPRJIHGJ-UHFFFAOYSA-N creatinine Chemical compound CN1CC(=O)NC1=N DDRJAANPRJIHGJ-UHFFFAOYSA-N 0.000 description 2
- 229930182912 cyclosporin Natural products 0.000 description 2
- 230000007423 decrease Effects 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 208000035475 disorder Diseases 0.000 description 2
- 238000010494 dissociation reaction Methods 0.000 description 2
- 230000005593 dissociations Effects 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 239000002934 diuretic Substances 0.000 description 2
- 230000001882 diuretic effect Effects 0.000 description 2
- 230000008030 elimination Effects 0.000 description 2
- 238000003379 elimination reaction Methods 0.000 description 2
- 210000003527 eukaryotic cell Anatomy 0.000 description 2
- 125000000524 functional group Chemical group 0.000 description 2
- 239000008273 gelatin Substances 0.000 description 2
- 229920000159 gelatin Polymers 0.000 description 2
- 235000019322 gelatine Nutrition 0.000 description 2
- 235000011852 gelatine desserts Nutrition 0.000 description 2
- 239000003862 glucocorticoid Substances 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 239000002471 hydroxymethylglutaryl coenzyme A reductase inhibitor Substances 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 230000016784 immunoglobulin production Effects 0.000 description 2
- 229940072221 immunoglobulins Drugs 0.000 description 2
- 239000003018 immunosuppressive agent Substances 0.000 description 2
- 229940125721 immunosuppressive agent Drugs 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- 208000015181 infectious disease Diseases 0.000 description 2
- 239000003112 inhibitor Substances 0.000 description 2
- 238000003780 insertion Methods 0.000 description 2
- 230000037431 insertion Effects 0.000 description 2
- 238000010253 intravenous injection Methods 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 239000007791 liquid phase Substances 0.000 description 2
- 239000012931 lyophilized formulation Substances 0.000 description 2
- 238000007726 management method Methods 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- BQJCRHHNABKAKU-KBQPJGBKSA-N morphine Chemical compound O([C@H]1[C@H](C=C[C@H]23)O)C4=C5[C@@]12CCN(C)[C@@H]3CC5=CC=C4O BQJCRHHNABKAKU-KBQPJGBKSA-N 0.000 description 2
- 230000035772 mutation Effects 0.000 description 2
- 210000005036 nerve Anatomy 0.000 description 2
- 238000006386 neutralization reaction Methods 0.000 description 2
- 239000000816 peptidomimetic Substances 0.000 description 2
- 125000001151 peptidyl group Chemical group 0.000 description 2
- 229940068977 polysorbate 20 Drugs 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 239000000651 prodrug Substances 0.000 description 2
- 229940002612 prodrug Drugs 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 239000002464 receptor antagonist Substances 0.000 description 2
- 229940044551 receptor antagonist Drugs 0.000 description 2
- 230000009467 reduction Effects 0.000 description 2
- 230000002829 reductive effect Effects 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 230000000717 retained effect Effects 0.000 description 2
- 230000001177 retroviral effect Effects 0.000 description 2
- 230000035945 sensitivity Effects 0.000 description 2
- 230000001953 sensory effect Effects 0.000 description 2
- 210000001044 sensory neuron Anatomy 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000001509 sodium citrate Substances 0.000 description 2
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 2
- 239000007790 solid phase Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000007920 subcutaneous administration Methods 0.000 description 2
- 230000008685 targeting Effects 0.000 description 2
- 230000000451 tissue damage Effects 0.000 description 2
- 231100000827 tissue damage Toxicity 0.000 description 2
- 206010044652 trigeminal neuralgia Diseases 0.000 description 2
- 230000003827 upregulation Effects 0.000 description 2
- 229940124549 vasodilator Drugs 0.000 description 2
- 239000003071 vasodilator agent Substances 0.000 description 2
- 230000000007 visual effect Effects 0.000 description 2
- KYBXNPIASYUWLN-WUCPZUCCSA-N (2s)-5-hydroxypyrrolidine-2-carboxylic acid Chemical compound OC1CC[C@@H](C(O)=O)N1 KYBXNPIASYUWLN-WUCPZUCCSA-N 0.000 description 1
- 102000040650 (ribonucleotides)n+m Human genes 0.000 description 1
- 125000000979 2-amino-2-oxoethyl group Chemical group [H]C([*])([H])C(=O)N([H])[H] 0.000 description 1
- GOJUJUVQIVIZAV-UHFFFAOYSA-N 2-amino-4,6-dichloropyrimidine-5-carbaldehyde Chemical group NC1=NC(Cl)=C(C=O)C(Cl)=N1 GOJUJUVQIVIZAV-UHFFFAOYSA-N 0.000 description 1
- 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
- QFVHZQCOUORWEI-UHFFFAOYSA-N 4-[(4-anilino-5-sulfonaphthalen-1-yl)diazenyl]-5-hydroxynaphthalene-2,7-disulfonic acid Chemical compound C=12C(O)=CC(S(O)(=O)=O)=CC2=CC(S(O)(=O)=O)=CC=1N=NC(C1=CC=CC(=C11)S(O)(=O)=O)=CC=C1NC1=CC=CC=C1 QFVHZQCOUORWEI-UHFFFAOYSA-N 0.000 description 1
- 102100033400 4F2 cell-surface antigen heavy chain Human genes 0.000 description 1
- 229940117976 5-hydroxylysine Drugs 0.000 description 1
- ODHCTXKNWHHXJC-VKHMYHEASA-N 5-oxo-L-proline Chemical group OC(=O)[C@@H]1CCC(=O)N1 ODHCTXKNWHHXJC-VKHMYHEASA-N 0.000 description 1
- BSYNRYMUTXBXSQ-FOQJRBATSA-N 59096-14-9 Chemical compound CC(=O)OC1=CC=CC=C1[14C](O)=O BSYNRYMUTXBXSQ-FOQJRBATSA-N 0.000 description 1
- 102000014777 Adipokines Human genes 0.000 description 1
- 108010078606 Adipokines Proteins 0.000 description 1
- 102100036475 Alanine aminotransferase 1 Human genes 0.000 description 1
- 108010082126 Alanine transaminase Proteins 0.000 description 1
- 108010088751 Albumins Proteins 0.000 description 1
- 102000009027 Albumins Human genes 0.000 description 1
- 102100034112 Alkyldihydroxyacetonephosphate synthase, peroxisomal Human genes 0.000 description 1
- 208000000044 Amnesia Diseases 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 102000013142 Amylases Human genes 0.000 description 1
- 108010065511 Amylases Proteins 0.000 description 1
- 102100034282 Ankyrin repeat domain-containing protein 23 Human genes 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 206010058019 Cancer Pain Diseases 0.000 description 1
- 241000824799 Canis lupus dingo Species 0.000 description 1
- 206010007559 Cardiac failure congestive Diseases 0.000 description 1
- 206010057248 Cell death Diseases 0.000 description 1
- VEXZGXHMUGYJMC-UHFFFAOYSA-M Chloride anion Chemical compound [Cl-] VEXZGXHMUGYJMC-UHFFFAOYSA-M 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 241000699662 Cricetomys gambianus Species 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 108700022150 Designed Ankyrin Repeat Proteins Proteins 0.000 description 1
- 208000032131 Diabetic Neuropathies Diseases 0.000 description 1
- 101000617550 Dictyostelium discoideum Presenilin-A Proteins 0.000 description 1
- 102100022317 Dihydropteridine reductase Human genes 0.000 description 1
- 206010013886 Dysaesthesia Diseases 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- 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 1
- 101710113304 Glutathione S-transferase class-mu 28 kDa isozyme Proteins 0.000 description 1
- 101100082540 Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) pcp gene Proteins 0.000 description 1
- 206010019280 Heart failures Diseases 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000800023 Homo sapiens 4F2 cell-surface antigen heavy chain Proteins 0.000 description 1
- 101000799143 Homo sapiens Alkyldihydroxyacetonephosphate synthase, peroxisomal Proteins 0.000 description 1
- 101000780120 Homo sapiens Ankyrin repeat domain-containing protein 23 Proteins 0.000 description 1
- 208000035154 Hyperesthesia Diseases 0.000 description 1
- 206010020772 Hypertension Diseases 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 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
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- LRQKBLKVPFOOQJ-YFKPBYRVSA-N L-norleucine Chemical compound CCCC[C@H]([NH3+])C([O-])=O LRQKBLKVPFOOQJ-YFKPBYRVSA-N 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- ZRVUJXDFFKFLMG-UHFFFAOYSA-N Meloxicam Chemical compound OC=1C2=CC=CC=C2S(=O)(=O)N(C)C=1C(=O)NC1=NC=C(C)S1 ZRVUJXDFFKFLMG-UHFFFAOYSA-N 0.000 description 1
- 208000026139 Memory disease Diseases 0.000 description 1
- 230000004988 N-glycosylation Effects 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 108010087702 Penicillinase Proteins 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 241000276498 Pollachius virens Species 0.000 description 1
- 229920001219 Polysorbate 40 Polymers 0.000 description 1
- 229920001214 Polysorbate 60 Polymers 0.000 description 1
- 229920002642 Polysorbate 65 Polymers 0.000 description 1
- 229920002651 Polysorbate 85 Polymers 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 102000008866 Prostaglandin E receptors Human genes 0.000 description 1
- 108010088540 Prostaglandin E receptors Proteins 0.000 description 1
- 102000004022 Protein-Tyrosine Kinases Human genes 0.000 description 1
- 108090000412 Protein-Tyrosine Kinases Proteins 0.000 description 1
- 206010037660 Pyrexia Diseases 0.000 description 1
- 108010039491 Ricin Proteins 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 108700011201 Streptococcus IgG Fc-binding Proteins 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 101710088929 Voltage-dependent L-type calcium channel subunit alpha-1S Proteins 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000008351 acetate buffer Substances 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 239000000478 adipokine Substances 0.000 description 1
- 210000000577 adipose tissue Anatomy 0.000 description 1
- 239000002671 adjuvant Substances 0.000 description 1
- 239000000443 aerosol Substances 0.000 description 1
- 230000000172 allergic effect Effects 0.000 description 1
- WQZGKKKJIJFFOK-PHYPRBDBSA-N alpha-D-galactose Chemical compound OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-PHYPRBDBSA-N 0.000 description 1
- 235000019418 amylase Nutrition 0.000 description 1
- 229940124326 anaesthetic agent Drugs 0.000 description 1
- 230000003444 anaesthetic effect Effects 0.000 description 1
- 239000012491 analyte Substances 0.000 description 1
- 238000009175 antibody therapy Methods 0.000 description 1
- 102000025171 antigen binding proteins Human genes 0.000 description 1
- 108091000831 antigen binding proteins Proteins 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 238000013459 approach Methods 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- PYMYPHUHKUWMLA-UHFFFAOYSA-N arabinose Natural products OCC(O)C(O)C(O)C=O PYMYPHUHKUWMLA-UHFFFAOYSA-N 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
- 208000010668 atopic eczema Diseases 0.000 description 1
- 229960002319 barbital Drugs 0.000 description 1
- 230000006399 behavior Effects 0.000 description 1
- SRBFZHDQGSBBOR-UHFFFAOYSA-N beta-D-Pyranose-Lyxose Natural products OC1COC(O)C(O)C1O SRBFZHDQGSBBOR-UHFFFAOYSA-N 0.000 description 1
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 1
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 1
- 230000008275 binding mechanism Effects 0.000 description 1
- 238000002306 biochemical method Methods 0.000 description 1
- 230000036782 biological activation Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 238000005460 biophysical method Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 229960002685 biotin Drugs 0.000 description 1
- 235000020958 biotin Nutrition 0.000 description 1
- 239000011616 biotin Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 230000036760 body temperature Effects 0.000 description 1
- 238000009529 body temperature measurement Methods 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- RMRJXGBAOAMLHD-IHFGGWKQSA-N buprenorphine Chemical compound C([C@]12[C@H]3OC=4C(O)=CC=C(C2=4)C[C@@H]2[C@]11CC[C@]3([C@H](C1)[C@](C)(O)C(C)(C)C)OC)CN2CC1CC1 RMRJXGBAOAMLHD-IHFGGWKQSA-N 0.000 description 1
- 229960001736 buprenorphine Drugs 0.000 description 1
- IFKLAQQSCNILHL-QHAWAJNXSA-N butorphanol Chemical compound N1([C@@H]2CC3=CC=C(C=C3[C@@]3([C@]2(CCCC3)O)CC1)O)CC1CCC1 IFKLAQQSCNILHL-QHAWAJNXSA-N 0.000 description 1
- 229960001113 butorphanol Drugs 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 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
- BMLSTPRTEKLIPM-UHFFFAOYSA-I calcium;potassium;disodium;hydrogen carbonate;dichloride;dihydroxide;hydrate Chemical compound O.[OH-].[OH-].[Na+].[Na+].[Cl-].[Cl-].[K+].[Ca+2].OC([O-])=O BMLSTPRTEKLIPM-UHFFFAOYSA-I 0.000 description 1
- 239000004202 carbamide Substances 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- IVUMCTKHWDRRMH-UHFFFAOYSA-N carprofen Chemical compound C1=CC(Cl)=C[C]2C3=CC=C(C(C(O)=O)C)C=C3N=C21 IVUMCTKHWDRRMH-UHFFFAOYSA-N 0.000 description 1
- 229960003184 carprofen Drugs 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 230000005889 cellular cytotoxicity Effects 0.000 description 1
- 230000005754 cellular signaling Effects 0.000 description 1
- 239000003153 chemical reaction reagent Substances 0.000 description 1
- 235000012000 cholesterol Nutrition 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 230000004186 co-expression Effects 0.000 description 1
- 238000002648 combination therapy Methods 0.000 description 1
- 230000024203 complement activation Effects 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 238000007796 conventional method Methods 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
- 229940109239 creatinine Drugs 0.000 description 1
- 230000009260 cross reactivity Effects 0.000 description 1
- 239000012228 culture supernatant Substances 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000016396 cytokine production Effects 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000006735 deficit Effects 0.000 description 1
- 230000003111 delayed effect Effects 0.000 description 1
- YSMODUONRAFBET-UHFFFAOYSA-N delta-DL-hydroxylysine Natural products NCC(O)CCC(N)C(O)=O YSMODUONRAFBET-UHFFFAOYSA-N 0.000 description 1
- WAZQAZKAZLXFMK-UHFFFAOYSA-N deracoxib Chemical compound C1=C(F)C(OC)=CC=C1C1=CC(C(F)F)=NN1C1=CC=C(S(N)(=O)=O)C=C1 WAZQAZKAZLXFMK-UHFFFAOYSA-N 0.000 description 1
- 229960003314 deracoxib Drugs 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 230000004069 differentiation Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 230000003292 diminished effect Effects 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 230000009429 distress Effects 0.000 description 1
- 238000011833 dog model Methods 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 238000012377 drug delivery Methods 0.000 description 1
- 230000036267 drug metabolism Effects 0.000 description 1
- 230000002996 emotional effect Effects 0.000 description 1
- YSMODUONRAFBET-UHNVWZDZSA-N erythro-5-hydroxy-L-lysine Chemical compound NC[C@H](O)CC[C@H](N)C(O)=O YSMODUONRAFBET-UHNVWZDZSA-N 0.000 description 1
- XFBVBWWRPKNWHW-UHFFFAOYSA-N etodolac Chemical compound C1COC(CC)(CC(O)=O)C2=N[C]3C(CC)=CC=CC3=C21 XFBVBWWRPKNWHW-UHFFFAOYSA-N 0.000 description 1
- 229960005293 etodolac Drugs 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- 229960002428 fentanyl Drugs 0.000 description 1
- PJMPHNIQZUBGLI-UHFFFAOYSA-N fentanyl Chemical compound C=1C=CC=CC=1N(C(=O)CC)C(CC1)CCN1CCC1=CC=CC=C1 PJMPHNIQZUBGLI-UHFFFAOYSA-N 0.000 description 1
- 230000027950 fever generation Effects 0.000 description 1
- FULAPETWGIGNMT-UHFFFAOYSA-N firocoxib Chemical compound C=1C=C(S(C)(=O)=O)C=CC=1C=1C(C)(C)OC(=O)C=1OCC1CC1 FULAPETWGIGNMT-UHFFFAOYSA-N 0.000 description 1
- 229960002524 firocoxib Drugs 0.000 description 1
- 239000012530 fluid Substances 0.000 description 1
- MGCCHNLNRBULBU-WZTVWXICSA-N flunixin meglumine Chemical compound CNC[C@H](O)[C@@H](O)[C@H](O)[C@H](O)CO.C1=CC=C(C(F)(F)F)C(C)=C1NC1=NC=CC=C1C(O)=O MGCCHNLNRBULBU-WZTVWXICSA-N 0.000 description 1
- 229960000469 flunixin meglumine Drugs 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 229930182830 galactose Natural products 0.000 description 1
- 210000004602 germ cell Anatomy 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 description 1
- PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
- 239000010931 gold Substances 0.000 description 1
- 229910052737 gold Inorganic materials 0.000 description 1
- 108010067006 heat stable toxin (E coli) Proteins 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- OAKJQQAXSVQMHS-UHFFFAOYSA-N hydrazine Substances NN OAKJQQAXSVQMHS-UHFFFAOYSA-N 0.000 description 1
- WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 description 1
- 125000002349 hydroxyamino group Chemical group [H]ON([H])[*] 0.000 description 1
- 230000003100 immobilizing effect Effects 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 229940127121 immunoconjugate Drugs 0.000 description 1
- 229940027941 immunoglobulin g Drugs 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 230000006882 induction of apoptosis Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000028709 inflammatory response Effects 0.000 description 1
- 239000007972 injectable composition Substances 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 238000001361 intraarterial administration Methods 0.000 description 1
- 230000004068 intracellular signaling Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- DKYWVDODHFEZIM-UHFFFAOYSA-N ketoprofen Chemical compound OC(=O)C(C)C1=CC=CC(C(=O)C=2C=CC=CC=2)=C1 DKYWVDODHFEZIM-UHFFFAOYSA-N 0.000 description 1
- 229960000991 ketoprofen Drugs 0.000 description 1
- 210000003292 kidney cell Anatomy 0.000 description 1
- 230000002147 killing effect Effects 0.000 description 1
- 238000012933 kinetic analysis Methods 0.000 description 1
- 230000003902 lesion Effects 0.000 description 1
- 239000003446 ligand Substances 0.000 description 1
- 230000000670 limiting effect Effects 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 239000002502 liposome Substances 0.000 description 1
- 239000012669 liquid formulation Substances 0.000 description 1
- 239000006193 liquid solution Substances 0.000 description 1
- 230000005923 long-lasting effect Effects 0.000 description 1
- 210000003141 lower extremity Anatomy 0.000 description 1
- 101150074251 lpp gene Proteins 0.000 description 1
- 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 1
- 230000014759 maintenance of location Effects 0.000 description 1
- 230000003211 malignant effect Effects 0.000 description 1
- 229960001929 meloxicam Drugs 0.000 description 1
- 230000006984 memory degeneration Effects 0.000 description 1
- 208000023060 memory loss Diseases 0.000 description 1
- 230000002503 metabolic effect Effects 0.000 description 1
- 239000004005 microsphere Substances 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 229960005181 morphine Drugs 0.000 description 1
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 208000031225 myocardial ischemia Diseases 0.000 description 1
- 229960000805 nalbuphine Drugs 0.000 description 1
- NETZHAKZCGBWSS-CEDHKZHLSA-N nalbuphine Chemical compound C([C@]12[C@H]3OC=4C(O)=CC=C(C2=4)C[C@@H]2[C@]1(O)CC[C@@H]3O)CN2CC1CCC1 NETZHAKZCGBWSS-CEDHKZHLSA-N 0.000 description 1
- 210000002569 neuron Anatomy 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 230000001473 noxious effect Effects 0.000 description 1
- 230000000771 oncological effect Effects 0.000 description 1
- 239000000014 opioid analgesic Substances 0.000 description 1
- 229940005483 opioid analgesics Drugs 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 210000001672 ovary Anatomy 0.000 description 1
- 230000008058 pain sensation Effects 0.000 description 1
- 230000008533 pain sensitivity Effects 0.000 description 1
- 229960005489 paracetamol Drugs 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 229950009506 penicillinase Drugs 0.000 description 1
- 230000008447 perception Effects 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 239000000244 polyoxyethylene sorbitan monooleate Substances 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 239000000249 polyoxyethylene sorbitan monopalmitate Substances 0.000 description 1
- 235000010483 polyoxyethylene sorbitan monopalmitate Nutrition 0.000 description 1
- 239000001818 polyoxyethylene sorbitan monostearate Substances 0.000 description 1
- 235000010989 polyoxyethylene sorbitan monostearate Nutrition 0.000 description 1
- 239000001816 polyoxyethylene sorbitan tristearate Substances 0.000 description 1
- 235000010988 polyoxyethylene sorbitan tristearate Nutrition 0.000 description 1
- 229940101027 polysorbate 40 Drugs 0.000 description 1
- 229940113124 polysorbate 60 Drugs 0.000 description 1
- 229940099511 polysorbate 65 Drugs 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- 229940068968 polysorbate 80 Drugs 0.000 description 1
- 229940113171 polysorbate 85 Drugs 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 238000000159 protein binding assay Methods 0.000 description 1
- 230000002797 proteolythic effect Effects 0.000 description 1
- 230000002685 pulmonary effect Effects 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000006798 recombination Effects 0.000 description 1
- 238000005215 recombination Methods 0.000 description 1
- 238000011084 recovery Methods 0.000 description 1
- 230000008439 repair process Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 238000007363 ring formation reaction Methods 0.000 description 1
- ZEXGDYFACFXQPF-UHFFFAOYSA-N robenacoxib Chemical compound OC(=O)CC1=CC(CC)=CC=C1NC1=C(F)C(F)=CC(F)=C1F ZEXGDYFACFXQPF-UHFFFAOYSA-N 0.000 description 1
- 229960000205 robenacoxib Drugs 0.000 description 1
- 238000013391 scatchard analysis Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000013077 scoring method Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000035807 sensation Effects 0.000 description 1
- 230000020341 sensory perception of pain Effects 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 238000004904 shortening Methods 0.000 description 1
- 231100000161 signs of toxicity Toxicity 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 238000003998 size exclusion chromatography high performance liquid chromatography Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 239000008354 sodium chloride injection Substances 0.000 description 1
- 230000003238 somatosensory effect Effects 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 239000008362 succinate buffer Substances 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 238000013268 sustained release Methods 0.000 description 1
- 239000012730 sustained-release form Substances 0.000 description 1
- 230000002889 sympathetic effect Effects 0.000 description 1
- 229940037128 systemic glucocorticoids Drugs 0.000 description 1
- 238000002560 therapeutic procedure Methods 0.000 description 1
- 229940104230 thymidine Drugs 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 108010087967 type I signal peptidase Proteins 0.000 description 1
- 241000701447 unidentified baculovirus Species 0.000 description 1
- 125000002987 valine group Chemical group [H]N([H])C([H])(C(*)=O)C([H])(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 238000011179 visual inspection Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 210000000636 white adipocyte Anatomy 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K39/00—Medicinal preparations containing antigens or antibodies
- A61K39/395—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum
- A61K39/39533—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals
- A61K39/3955—Antibodies; Immunoglobulins; Immune serum, e.g. antilymphocytic serum against materials from animals against proteinaceous materials, e.g. enzymes, hormones, lymphokines
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K45/00—Medicinal preparations containing active ingredients not provided for in groups A61K31/00 - A61K41/00
- A61K45/06—Mixtures of active ingredients without chemical characterisation, e.g. antiphlogistics and cardiaca
-
- 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
- A61P25/00—Drugs for disorders of the nervous system
- A61P25/04—Centrally acting analgesics, e.g. opioids
-
- 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
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C07K1/14—Extraction; Separation; Purification
- C07K1/16—Extraction; Separation; Purification by chromatography
- C07K1/165—Extraction; Separation; Purification by chromatography mixed-mode chromatography
-
- 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
- C07K16/2887—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against CD20
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/46—Hybrid immunoglobulins
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/46—Hybrid immunoglobulins
- C07K16/461—Igs containing Ig-regions, -domains or -residues form different species
- C07K16/467—Igs with modifications in the FR-residues only
-
- 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
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/24—Immunoglobulins specific features characterized by taxonomic origin containing regions, domains or residues from different species, e.g. chimeric, humanized or veneered
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/40—Immunoglobulins specific features characterized by post-translational modification
- C07K2317/41—Glycosylation, sialylation, or fucosylation
-
- 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
-
- 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
- C07K2317/71—Decreased effector function due to an Fc-modification
-
- 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
- C07K2317/72—Increased effector function due to an Fc-modification
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/70—Immunoglobulins specific features characterized by effect upon binding to a cell or to an antigen
- C07K2317/73—Inducing cell death, e.g. apoptosis, necrosis or inhibition of cell proliferation
- C07K2317/734—Complement-dependent cytotoxicity [CDC]
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- 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
- C07K2319/00—Fusion polypeptide
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- General Health & Medical Sciences (AREA)
- Immunology (AREA)
- Veterinary Medicine (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Epidemiology (AREA)
- Pain & Pain Management (AREA)
- Neurosurgery (AREA)
- Rheumatology (AREA)
- Biomedical Technology (AREA)
- Neurology (AREA)
- Analytical Chemistry (AREA)
- Microbiology (AREA)
- Mycology (AREA)
- Endocrinology (AREA)
- Orthopedic Medicine & Surgery (AREA)
- Oncology (AREA)
- Communicable Diseases (AREA)
- Physical Education & Sports Medicine (AREA)
- Peptides Or Proteins (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (4)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201161483481P | 2011-05-06 | 2011-05-06 | |
| GBGB1114858.2A GB201114858D0 (en) | 2011-08-29 | 2011-08-29 | Anti-nerve growth factor antibodies and methods of using the same |
| US201161531439P | 2011-09-06 | 2011-09-06 | |
| GB1320045.6A GB2505352B (en) | 2011-05-06 | 2012-05-08 | Anti-nerve growth factor antibodies and methods of preparing and using the same |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| GB201517547D0 GB201517547D0 (en) | 2015-11-18 |
| GB2528401A true GB2528401A (en) | 2016-01-20 |
Family
ID=50931152
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| GB1517547.4A Withdrawn GB2528401A (en) | 2011-05-06 | 2012-05-08 | Anti-nerve growth factor antibodies and methods of preparing and using the same |
Country Status (3)
| Country | Link |
|---|---|
| US (3) | US9580496B2 (enExample) |
| JP (3) | JP5969102B2 (enExample) |
| GB (1) | GB2528401A (enExample) |
Families Citing this family (24)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US8587771B2 (en) * | 2010-07-16 | 2013-11-19 | Microsoft Corporation | Method and system for multi-phase dynamic calibration of three-dimensional (3D) sensors in a time-of-flight system |
| US10704021B2 (en) | 2012-03-15 | 2020-07-07 | Flodesign Sonics, Inc. | Acoustic perfusion devices |
| PE20160953A1 (es) * | 2013-12-12 | 2016-09-26 | Shanghai hengrui pharmaceutical co ltd | Anticuerpo pd-1, fragmento de union al antigeno de este y uso medico de este |
| CA2932515C (en) | 2013-12-20 | 2023-08-01 | Intervet International B.V. | Caninized antibodies |
| CA2935960C (en) | 2014-01-08 | 2023-01-10 | Bart Lipkens | Acoustophoresis device with dual acoustophoretic chamber |
| ES2853823T3 (es) | 2014-09-30 | 2021-09-17 | Intervet Int Bv | Anticuerpos de PD-L1 que se unen a PD-L1 canino |
| US9758575B2 (en) * | 2015-04-06 | 2017-09-12 | Yung Shin Pharmaceutical Industrial Co. Ltd. | Antibodies which specifically bind to canine vascular endothelial growth factor and uses thereof |
| US11708572B2 (en) | 2015-04-29 | 2023-07-25 | Flodesign Sonics, Inc. | Acoustic cell separation techniques and processes |
| US11377651B2 (en) | 2016-10-19 | 2022-07-05 | Flodesign Sonics, Inc. | Cell therapy processes utilizing acoustophoresis |
| US20190292250A1 (en) * | 2015-08-31 | 2019-09-26 | The Trustees Of The University Of Pennsylvania | Aav-anti-vegf for treating cancer in companion animals |
| US11091556B2 (en) | 2015-12-18 | 2021-08-17 | Intervet Inc. | Caninized human antibodies to human IL-4R alpha |
| JP7008020B2 (ja) | 2015-12-18 | 2022-01-25 | インターベット インターナショナル ベー． フェー． | ヒトおよびイヌｉｌ－４ｒアルファに対するイヌ化ヒト抗体 |
| KR102293753B1 (ko) | 2016-01-06 | 2021-08-24 | 오더-메이드 메디컬 리서치 인코포레이티드 | Vegf 와 nrp1 의 결합을 저해하는 항체 |
| EP3401331B1 (en) | 2016-01-06 | 2022-04-06 | Order-Made Medical Research Inc. | High-affinity anti-vegf antibody |
| US11214789B2 (en) | 2016-05-03 | 2022-01-04 | Flodesign Sonics, Inc. | Concentration and washing of particles with acoustics |
| US10928489B2 (en) * | 2017-04-06 | 2021-02-23 | Microsoft Technology Licensing, Llc | Time of flight camera |
| US10215856B1 (en) | 2017-11-27 | 2019-02-26 | Microsoft Technology Licensing, Llc | Time of flight camera |
| US10901087B2 (en) | 2018-01-15 | 2021-01-26 | Microsoft Technology Licensing, Llc | Time of flight camera |
| US10942274B2 (en) | 2018-04-11 | 2021-03-09 | Microsoft Technology Licensing, Llc | Time of flight and picture camera |
| US10895925B2 (en) | 2018-10-03 | 2021-01-19 | Microsoft Technology Licensing, Llc | Touch display alignment |
| US11435476B2 (en) | 2018-10-12 | 2022-09-06 | Microsoft Technology Licensing, Llc | Time-of-flight RGB-IR image sensor |
| JP2021059499A (ja) | 2019-10-03 | 2021-04-15 | 日本全薬工業株式会社 | イヌｃｄ２０に対するモノクローナル抗体又は抗体フラグメント |
| US11079515B2 (en) | 2019-12-18 | 2021-08-03 | Microsoft Technology Licensing, Llc | Micro lens time-of-flight sensor having micro lens heights that vary based on image height |
| US20240018481A1 (en) | 2021-07-30 | 2024-01-18 | Chengdu Unovel Biopharma Co., Ltd. | Recombinant cho cell, construction method therefor, and detection system and method using same |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2003060080A2 (en) * | 2001-12-21 | 2003-07-24 | Idexx Laboratories, Inc. | Canine immunoglobulin variable domains, caninized antibodies, and methods for making and using them |
| WO2005061540A2 (en) * | 2003-12-24 | 2005-07-07 | Lay Line Genomics S.P.A. | Method for the humanization of antibodies and humanized antibodies thereby obtained |
Family Cites Families (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP2837240B2 (ja) * | 1990-06-07 | 1998-12-14 | 財団法人化学及血清療法研究所 | イヌ免疫グロブリンγ鎖の定常領域をコードする遺伝子断片およびマウス×イヌキメラ抗体 |
| GB9202796D0 (en) | 1992-02-11 | 1992-03-25 | Wellcome Found | Antiviral antibody |
| EP1268794A2 (en) * | 2000-04-07 | 2003-01-02 | Heska Corporation | Compositions and methods related to canine igg and canine il-13 receptors |
| US7321026B2 (en) | 2001-06-27 | 2008-01-22 | Skytech Technology Limited | Framework-patched immunoglobulins |
| US20030190705A1 (en) | 2001-10-29 | 2003-10-09 | Sunol Molecular Corporation | Method of humanizing immune system molecules |
| PL379983A1 (pl) * | 2003-02-19 | 2006-11-27 | Rinat Neuroscience Corp. | Sposoby leczenia bólu polegające na podaniu antagonisty czynnika wzrostu nerwów i niesteroidowego leku przeciwzapalnego oraz zawierające je kompozycje |
| JP2005104936A (ja) * | 2003-10-01 | 2005-04-21 | Nippon Zenyaku Kogyo Kk | イヌｔａｒｃ抗体 |
| JP2005143436A (ja) * | 2003-11-18 | 2005-06-09 | Nippon Zenyaku Kogyo Kk | イヌｍｄｃ |
| US7462697B2 (en) * | 2004-11-08 | 2008-12-09 | Epitomics, Inc. | Methods for antibody engineering |
| ITRM20050290A1 (it) | 2005-06-07 | 2006-12-08 | Lay Line Genomics Spa | Uso di molecole in grado di inibire il legame tra ngf e il suo recettore trka come analgesici ad effetto prolungato. |
| EP2185589B1 (en) * | 2007-06-01 | 2016-01-06 | University of Maryland, Baltimore | Immunoglobulin constant region fc receptor binding agents |
| US8337842B2 (en) | 2008-09-04 | 2012-12-25 | Vet Therapeutics, Inc. | Monoclonal antibodies |
| US8569460B2 (en) | 2009-03-25 | 2013-10-29 | Vet Therapeutics, Inc. | Antibody constant domain regions and uses thereof |
| WO2010117448A2 (en) * | 2009-04-05 | 2010-10-14 | Provenance Biopharmaceuticals Corp. | Chimeric immunocytokines and methods of use thereof |
| CA2808577C (en) | 2010-08-19 | 2018-09-25 | Abbott Laboratories | Anti-ngf antibodies and their use |
| KR20170070272A (ko) | 2011-05-06 | 2017-06-21 | 넥스베트 오스트레일리아 피티와이 리미티드 | 항신경성 성장 인자 항체 및 그의 제조방법과 이용방법 |
-
2012
- 2012-05-08 GB GB1517547.4A patent/GB2528401A/en not_active Withdrawn
- 2012-05-08 US US14/115,779 patent/US9580496B2/en active Active
-
2015
- 2015-12-09 JP JP2015239920A patent/JP5969102B2/ja active Active
-
2017
- 2017-01-24 US US15/413,808 patent/US20170369565A1/en not_active Abandoned
- 2017-02-23 JP JP2017031939A patent/JP2017101064A/ja active Pending
-
2018
- 2018-06-28 US US16/022,405 patent/US20190161540A1/en not_active Abandoned
-
2019
- 2019-03-29 JP JP2019067955A patent/JP6732990B2/ja active Active
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2003060080A2 (en) * | 2001-12-21 | 2003-07-24 | Idexx Laboratories, Inc. | Canine immunoglobulin variable domains, caninized antibodies, and methods for making and using them |
| WO2005061540A2 (en) * | 2003-12-24 | 2005-07-07 | Lay Line Genomics S.P.A. | Method for the humanization of antibodies and humanized antibodies thereby obtained |
Non-Patent Citations (3)
| Title |
|---|
| Database Geneseq [Online] 8 September 2005, Humanized alpha D11 antibody heavy chain variable region SEQ ID No. 17, retrieved from EBI accession no. GSP:AEB12537. * |
| MABS, vol. 1, no. 4, July 2009, PELAT THIBAUT ET AL, "Non-human primate immune libraries combined with germline humanization: an (almost) new, and powerful approach for the isolation of therapeutic antibodies", pages 377-381. * |
| Seminars in Immunology 2, 1990, Gorman and Clark, "Humanisation if monoclonal antibodies for therapy', pages 457-466. * |
Also Published As
| Publication number | Publication date |
|---|---|
| US20150056183A9 (en) | 2015-02-26 |
| JP6732990B2 (ja) | 2020-07-29 |
| JP2017101064A (ja) | 2017-06-08 |
| US20190161540A1 (en) | 2019-05-30 |
| GB201517547D0 (en) | 2015-11-18 |
| JP2016041750A (ja) | 2016-03-31 |
| US20140170137A1 (en) | 2014-06-19 |
| JP2019147801A (ja) | 2019-09-05 |
| JP5969102B2 (ja) | 2016-08-10 |
| US9580496B2 (en) | 2017-02-28 |
| US20170369565A1 (en) | 2017-12-28 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| EP2705054B1 (en) | Anti-nerve growth factor antibodies and methods of preparing and using the same | |
| US20190161540A1 (en) | Anti-nerve growth factor antibodies and methods of preparing and using the same | |
| CA2834983C (en) | Anti-nerve growth factor antibodies and methods of preparing and using the same | |
| AU2012252152B2 (en) | Anti-nerve growth factor antibodies and methods of preparing and using the same | |
| CA2835094C (en) | Anti-nerve growth factor antibodies and methods of preparing and using the same | |
| GB2528811A (en) | Anti-nerve growth factor antibodies and methods of preparing and using the same | |
| HK1195571B (en) | Anti-nerve growth factor antibodies and methods of preparing and using the same | |
| HK1195571A (en) | Anti-nerve growth factor antibodies and methods of preparing and using the same | |
| NZ617446B2 (en) | Anti-nerve growth factor antibodies and methods of preparing and using the same | |
| EP4026845A1 (en) | Anti-nerve growth factor antibodies and methods of preparing and using the same | |
| HK1195781B (en) | Anti-nerve growth factor antibodies and methods of preparing and using the same | |
| HK1195781A (en) | Anti-nerve growth factor antibodies and methods of preparing and using the same |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| WAP | Application withdrawn, taken to be withdrawn or refused ** after publication under section 16(1) |