JP4467188B2 - 多重特異的結合分子とその使用 - Google Patents
多重特異的結合分子とその使用 Download PDFInfo
- Publication number
- JP4467188B2 JP4467188B2 JP2000576861A JP2000576861A JP4467188B2 JP 4467188 B2 JP4467188 B2 JP 4467188B2 JP 2000576861 A JP2000576861 A JP 2000576861A JP 2000576861 A JP2000576861 A JP 2000576861A JP 4467188 B2 JP4467188 B2 JP 4467188B2
- Authority
- JP
- Japan
- Prior art keywords
- chain
- tcr
- binding
- cells
- protein
- 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.)
- Expired - Lifetime
Links
- 230000027455 binding Effects 0.000 title claims abstract description 285
- 238000000034 method Methods 0.000 claims abstract description 163
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 153
- 108091008874 T cell receptors Proteins 0.000 claims abstract description 22
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 claims abstract description 22
- 210000004027 cell Anatomy 0.000 claims description 246
- 108090000623 proteins and genes Proteins 0.000 claims description 171
- 108091008324 binding proteins Proteins 0.000 claims description 157
- 239000012634 fragment Substances 0.000 claims description 148
- 102000004169 proteins and genes Human genes 0.000 claims description 135
- 239000013598 vector Substances 0.000 claims description 114
- 210000001744 T-lymphocyte Anatomy 0.000 claims description 92
- 239000000427 antigen Substances 0.000 claims description 53
- 108091007433 antigens Proteins 0.000 claims description 53
- 102000036639 antigens Human genes 0.000 claims description 53
- 108091033319 polynucleotide Proteins 0.000 claims description 51
- 239000002157 polynucleotide Substances 0.000 claims description 51
- 102000040430 polynucleotide Human genes 0.000 claims description 51
- 108700018351 Major Histocompatibility Complex Proteins 0.000 claims description 49
- 230000020382 suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I Effects 0.000 claims description 49
- 230000009870 specific binding Effects 0.000 claims description 34
- 210000002865 immune cell Anatomy 0.000 claims description 31
- 150000001413 amino acids Chemical class 0.000 claims description 30
- 206010028980 Neoplasm Diseases 0.000 claims description 29
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 28
- 241000588724 Escherichia coli Species 0.000 claims description 25
- 229920001184 polypeptide Polymers 0.000 claims description 21
- 238000000338 in vitro Methods 0.000 claims description 19
- 210000004881 tumor cell Anatomy 0.000 claims description 17
- 241000701022 Cytomegalovirus Species 0.000 claims description 16
- 230000002147 killing effect Effects 0.000 claims description 16
- 201000011510 cancer Diseases 0.000 claims description 12
- 239000003550 marker Substances 0.000 claims description 12
- 238000004519 manufacturing process Methods 0.000 claims description 11
- 102100025064 Cellular tumor antigen p53 Human genes 0.000 claims description 9
- 101100084022 Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) lapA gene Proteins 0.000 claims description 8
- 101150009573 phoA gene Proteins 0.000 claims description 8
- 238000012258 culturing Methods 0.000 claims description 7
- 101100136076 Aspergillus oryzae (strain ATCC 42149 / RIB 40) pel1 gene Proteins 0.000 claims description 5
- 241000700605 Viruses Species 0.000 claims description 5
- 101150040383 pel2 gene Proteins 0.000 claims description 5
- 101150050446 pelB gene Proteins 0.000 claims description 5
- 239000003623 enhancer Substances 0.000 claims description 4
- 238000003384 imaging method Methods 0.000 claims description 3
- 238000002372 labelling Methods 0.000 claims description 3
- 101000914514 Homo sapiens T-cell-specific surface glycoprotein CD28 Proteins 0.000 claims description 2
- 108010033276 Peptide Fragments Proteins 0.000 claims description 2
- 102000007079 Peptide Fragments Human genes 0.000 claims description 2
- 102100027213 T-cell-specific surface glycoprotein CD28 Human genes 0.000 claims description 2
- 210000000265 leukocyte Anatomy 0.000 claims description 2
- 210000002540 macrophage Anatomy 0.000 claims description 2
- 102000023732 binding proteins Human genes 0.000 claims 25
- 230000003213 activating effect Effects 0.000 claims 2
- 239000008194 pharmaceutical composition Substances 0.000 claims 2
- 239000004480 active ingredient Substances 0.000 claims 1
- 210000000822 natural killer cell Anatomy 0.000 claims 1
- 230000014621 translational initiation Effects 0.000 claims 1
- 238000012360 testing method Methods 0.000 abstract description 12
- 239000000203 mixture Substances 0.000 abstract description 11
- 102000014914 Carrier Proteins Human genes 0.000 description 133
- 241001515965 unidentified phage Species 0.000 description 132
- 108020004414 DNA Proteins 0.000 description 130
- 235000018102 proteins Nutrition 0.000 description 123
- 108020001507 fusion proteins Proteins 0.000 description 101
- 102000037865 fusion proteins Human genes 0.000 description 101
- 238000003556 assay Methods 0.000 description 62
- 230000014509 gene expression Effects 0.000 description 61
- 210000004408 hybridoma Anatomy 0.000 description 55
- 230000004927 fusion Effects 0.000 description 41
- 108060003951 Immunoglobulin Proteins 0.000 description 28
- 102000018358 immunoglobulin Human genes 0.000 description 28
- 101710125418 Major capsid protein Proteins 0.000 description 27
- 235000001014 amino acid Nutrition 0.000 description 27
- 229940024606 amino acid Drugs 0.000 description 27
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 26
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 26
- 238000003752 polymerase chain reaction Methods 0.000 description 26
- 101710132601 Capsid protein Proteins 0.000 description 25
- 101710094648 Coat protein Proteins 0.000 description 25
- 102100021181 Golgi phosphoprotein 3 Human genes 0.000 description 25
- 101710141454 Nucleoprotein Proteins 0.000 description 25
- 101710083689 Probable capsid protein Proteins 0.000 description 25
- 241001529936 Murinae Species 0.000 description 24
- 239000013615 primer Substances 0.000 description 24
- 239000000412 dendrimer Substances 0.000 description 23
- 229920000736 dendritic polymer Polymers 0.000 description 23
- 108091028043 Nucleic acid sequence Proteins 0.000 description 21
- 230000000694 effects Effects 0.000 description 21
- 238000001727 in vivo Methods 0.000 description 20
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical group N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 19
- 241000124008 Mammalia Species 0.000 description 19
- 238000000159 protein binding assay Methods 0.000 description 18
- 238000000746 purification Methods 0.000 description 18
- 238000011282 treatment Methods 0.000 description 18
- 241000699670 Mus sp. Species 0.000 description 17
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 17
- 238000010367 cloning Methods 0.000 description 16
- 239000002299 complementary DNA Substances 0.000 description 16
- 238000012286 ELISA Assay Methods 0.000 description 15
- 102000000588 Interleukin-2 Human genes 0.000 description 15
- 108010002350 Interleukin-2 Proteins 0.000 description 15
- 230000000638 stimulation Effects 0.000 description 15
- 238000001262 western blot Methods 0.000 description 15
- 239000002609 medium Substances 0.000 description 14
- 102000017420 CD3 protein, epsilon/gamma/delta subunit Human genes 0.000 description 13
- 108050005493 CD3 protein, epsilon/gamma/delta subunit Proteins 0.000 description 13
- 238000002474 experimental method Methods 0.000 description 13
- 239000003446 ligand Substances 0.000 description 13
- 238000010276 construction Methods 0.000 description 12
- 239000013604 expression vector Substances 0.000 description 12
- 238000000684 flow cytometry Methods 0.000 description 12
- 210000004962 mammalian cell Anatomy 0.000 description 12
- 101710169873 Capsid protein G8P Proteins 0.000 description 11
- 239000003155 DNA primer Substances 0.000 description 11
- 102000004190 Enzymes Human genes 0.000 description 11
- 108090000790 Enzymes Proteins 0.000 description 11
- 230000004913 activation Effects 0.000 description 11
- 230000008901 benefit Effects 0.000 description 11
- 230000006378 damage Effects 0.000 description 11
- 229940088598 enzyme Drugs 0.000 description 11
- 239000013612 plasmid Substances 0.000 description 11
- 239000000523 sample Substances 0.000 description 11
- 239000006228 supernatant Substances 0.000 description 11
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 10
- 241000699666 Mus <mouse, genus> Species 0.000 description 10
- 238000004458 analytical method Methods 0.000 description 10
- 230000015572 biosynthetic process Effects 0.000 description 10
- 229960002685 biotin Drugs 0.000 description 10
- 235000020958 biotin Nutrition 0.000 description 10
- 239000011616 biotin Substances 0.000 description 10
- 239000011651 chromium Substances 0.000 description 10
- 238000004132 cross linking Methods 0.000 description 10
- 238000013461 design Methods 0.000 description 10
- 230000028993 immune response Effects 0.000 description 10
- 238000011534 incubation Methods 0.000 description 10
- 230000000813 microbial effect Effects 0.000 description 10
- 239000000126 substance Substances 0.000 description 10
- 238000002965 ELISA Methods 0.000 description 9
- 230000006052 T cell proliferation Effects 0.000 description 9
- 150000007523 nucleic acids Chemical class 0.000 description 9
- 239000000047 product Substances 0.000 description 9
- 102000005962 receptors Human genes 0.000 description 9
- 108020003175 receptors Proteins 0.000 description 9
- 230000003612 virological effect Effects 0.000 description 9
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 8
- 101710192393 Attachment protein G3P Proteins 0.000 description 8
- 108090001008 Avidin Proteins 0.000 description 8
- 101710179596 Gene 3 protein Proteins 0.000 description 8
- 241001465754 Metazoa Species 0.000 description 8
- 101100442582 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) spe-1 gene Proteins 0.000 description 8
- 230000003302 anti-idiotype Effects 0.000 description 8
- 238000013459 approach Methods 0.000 description 8
- 239000000872 buffer Substances 0.000 description 8
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 8
- 238000012512 characterization method Methods 0.000 description 8
- 238000001514 detection method Methods 0.000 description 8
- 238000010790 dilution Methods 0.000 description 8
- 239000012895 dilution Substances 0.000 description 8
- 230000004073 interleukin-2 production Effects 0.000 description 8
- 239000011159 matrix material Substances 0.000 description 8
- 239000002773 nucleotide Substances 0.000 description 8
- 125000003729 nucleotide group Chemical group 0.000 description 8
- 238000002360 preparation method Methods 0.000 description 8
- 238000001712 DNA sequencing Methods 0.000 description 7
- 102000012745 Immunoglobulin Subunits Human genes 0.000 description 7
- 108010079585 Immunoglobulin Subunits Proteins 0.000 description 7
- 241000283984 Rodentia Species 0.000 description 7
- 229920002684 Sepharose Polymers 0.000 description 7
- 238000001516 cell proliferation assay Methods 0.000 description 7
- 230000001413 cellular effect Effects 0.000 description 7
- 239000003153 chemical reaction reagent Substances 0.000 description 7
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 7
- 238000005516 engineering process Methods 0.000 description 7
- 239000012091 fetal bovine serum Substances 0.000 description 7
- 230000006870 function Effects 0.000 description 7
- 239000000499 gel Substances 0.000 description 7
- 230000012010 growth Effects 0.000 description 7
- 108020004999 messenger RNA Proteins 0.000 description 7
- 102000039446 nucleic acids Human genes 0.000 description 7
- 108020004707 nucleic acids Proteins 0.000 description 7
- 238000004091 panning Methods 0.000 description 7
- 239000013605 shuttle vector Substances 0.000 description 7
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 7
- 108020004705 Codon Proteins 0.000 description 6
- 241000282412 Homo Species 0.000 description 6
- 108091034117 Oligonucleotide Proteins 0.000 description 6
- 108020004511 Recombinant DNA Proteins 0.000 description 6
- 230000006044 T cell activation Effects 0.000 description 6
- 125000003275 alpha amino acid group Chemical group 0.000 description 6
- 230000003115 biocidal effect Effects 0.000 description 6
- 239000006143 cell culture medium Substances 0.000 description 6
- 238000007796 conventional method Methods 0.000 description 6
- 239000012636 effector Substances 0.000 description 6
- 230000001900 immune effect Effects 0.000 description 6
- 230000003993 interaction Effects 0.000 description 6
- 230000035755 proliferation Effects 0.000 description 6
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 5
- 101100328086 Caenorhabditis elegans cla-1 gene Proteins 0.000 description 5
- VYZAMTAEIAYCRO-UHFFFAOYSA-N Chromium Chemical compound [Cr] VYZAMTAEIAYCRO-UHFFFAOYSA-N 0.000 description 5
- 239000004471 Glycine Substances 0.000 description 5
- 102000025850 HLA-A2 Antigen Human genes 0.000 description 5
- 108010074032 HLA-A2 Antigen Proteins 0.000 description 5
- 241001494479 Pecora Species 0.000 description 5
- 239000002202 Polyethylene glycol Substances 0.000 description 5
- 241000288906 Primates Species 0.000 description 5
- 230000000903 blocking effect Effects 0.000 description 5
- 210000000234 capsid Anatomy 0.000 description 5
- 238000005119 centrifugation Methods 0.000 description 5
- 229910052804 chromium Inorganic materials 0.000 description 5
- 210000000987 immune system Anatomy 0.000 description 5
- 230000001965 increasing effect Effects 0.000 description 5
- 208000015181 infectious disease Diseases 0.000 description 5
- 238000003780 insertion Methods 0.000 description 5
- 230000037431 insertion Effects 0.000 description 5
- 238000002955 isolation Methods 0.000 description 5
- 239000012528 membrane Substances 0.000 description 5
- 239000002953 phosphate buffered saline Substances 0.000 description 5
- 229920001223 polyethylene glycol Polymers 0.000 description 5
- 238000003127 radioimmunoassay Methods 0.000 description 5
- 230000010076 replication Effects 0.000 description 5
- 102220080600 rs797046116 Human genes 0.000 description 5
- 210000004989 spleen cell Anatomy 0.000 description 5
- 238000010186 staining Methods 0.000 description 5
- 238000002560 therapeutic procedure Methods 0.000 description 5
- 238000005406 washing Methods 0.000 description 5
- OZFAFGSSMRRTDW-UHFFFAOYSA-N (2,4-dichlorophenyl) benzenesulfonate Chemical compound ClC1=CC(Cl)=CC=C1OS(=O)(=O)C1=CC=CC=C1 OZFAFGSSMRRTDW-UHFFFAOYSA-N 0.000 description 4
- 102000004127 Cytokines Human genes 0.000 description 4
- 108090000695 Cytokines Proteins 0.000 description 4
- 239000012591 Dulbecco’s Phosphate Buffered Saline Substances 0.000 description 4
- 108090000288 Glycoproteins Proteins 0.000 description 4
- 102000003886 Glycoproteins Human genes 0.000 description 4
- 102100024025 Heparanase Human genes 0.000 description 4
- 241000238631 Hexapoda Species 0.000 description 4
- 101001047819 Homo sapiens Heparanase Proteins 0.000 description 4
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 4
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 4
- 102000013463 Immunoglobulin Light Chains Human genes 0.000 description 4
- 108010065825 Immunoglobulin Light Chains Proteins 0.000 description 4
- 101000579647 Penaeus vannamei Penaeidin-2a Proteins 0.000 description 4
- 208000036142 Viral infection Diseases 0.000 description 4
- 230000003321 amplification Effects 0.000 description 4
- 230000000259 anti-tumor effect Effects 0.000 description 4
- 239000011324 bead Substances 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 238000010382 chemical cross-linking Methods 0.000 description 4
- 238000003776 cleavage reaction Methods 0.000 description 4
- 230000000295 complement effect Effects 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 210000003527 eukaryotic cell Anatomy 0.000 description 4
- 239000000284 extract Substances 0.000 description 4
- 238000001502 gel electrophoresis Methods 0.000 description 4
- 230000002068 genetic effect Effects 0.000 description 4
- 230000006698 induction Effects 0.000 description 4
- 230000000670 limiting effect Effects 0.000 description 4
- 238000003199 nucleic acid amplification method Methods 0.000 description 4
- 230000008488 polyadenylation Effects 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 230000002829 reductive effect Effects 0.000 description 4
- 230000007017 scission Effects 0.000 description 4
- 238000012216 screening Methods 0.000 description 4
- 238000012163 sequencing technique Methods 0.000 description 4
- 238000010561 standard procedure Methods 0.000 description 4
- UCSJYZPVAKXKNQ-HZYVHMACSA-N streptomycin Chemical compound CN[C@H]1[C@H](O)[C@@H](O)[C@H](CO)O[C@H]1O[C@@H]1[C@](C=O)(O)[C@H](C)O[C@H]1O[C@@H]1[C@@H](NC(N)=N)[C@H](O)[C@@H](NC(N)=N)[C@H](O)[C@H]1O UCSJYZPVAKXKNQ-HZYVHMACSA-N 0.000 description 4
- 231100000617 superantigen Toxicity 0.000 description 4
- 230000009385 viral infection Effects 0.000 description 4
- HKZAAJSTFUZYTO-LURJTMIESA-N (2s)-2-[[2-[[2-[[2-[(2-aminoacetyl)amino]acetyl]amino]acetyl]amino]acetyl]amino]-3-hydroxypropanoic acid Chemical compound NCC(=O)NCC(=O)NCC(=O)NCC(=O)N[C@@H](CO)C(O)=O HKZAAJSTFUZYTO-LURJTMIESA-N 0.000 description 3
- UZOVYGYOLBIAJR-UHFFFAOYSA-N 4-isocyanato-4'-methyldiphenylmethane Chemical compound C1=CC(C)=CC=C1CC1=CC=C(N=C=O)C=C1 UZOVYGYOLBIAJR-UHFFFAOYSA-N 0.000 description 3
- 108091026890 Coding region Proteins 0.000 description 3
- 241000699800 Cricetinae Species 0.000 description 3
- 102000018832 Cytochromes Human genes 0.000 description 3
- 108010052832 Cytochromes Proteins 0.000 description 3
- WSFSSNUMVMOOMR-UHFFFAOYSA-N Formaldehyde Chemical compound O=C WSFSSNUMVMOOMR-UHFFFAOYSA-N 0.000 description 3
- 101000946860 Homo sapiens T-cell surface glycoprotein CD3 epsilon chain Proteins 0.000 description 3
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 3
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 3
- 229930193140 Neomycin Natural products 0.000 description 3
- 238000012408 PCR amplification Methods 0.000 description 3
- 241000700159 Rattus Species 0.000 description 3
- 108010090804 Streptavidin Proteins 0.000 description 3
- 102100035794 T-cell surface glycoprotein CD3 epsilon chain Human genes 0.000 description 3
- 102100034922 T-cell surface glycoprotein CD8 alpha chain Human genes 0.000 description 3
- 102000006601 Thymidine Kinase Human genes 0.000 description 3
- 108020004440 Thymidine kinase Proteins 0.000 description 3
- 238000002835 absorbance Methods 0.000 description 3
- 238000001042 affinity chromatography Methods 0.000 description 3
- 125000000539 amino acid group Chemical group 0.000 description 3
- 238000007413 biotinylation Methods 0.000 description 3
- 230000006287 biotinylation Effects 0.000 description 3
- 229940098773 bovine serum albumin Drugs 0.000 description 3
- 230000022534 cell killing Effects 0.000 description 3
- 230000006037 cell lysis Effects 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 230000016396 cytokine production Effects 0.000 description 3
- 230000001472 cytotoxic effect Effects 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 230000013595 glycosylation Effects 0.000 description 3
- 238000006206 glycosylation reaction Methods 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- RAXXELZNTBOGNW-UHFFFAOYSA-N imidazole Natural products C1=CNC=N1 RAXXELZNTBOGNW-UHFFFAOYSA-N 0.000 description 3
- 238000003119 immunoblot Methods 0.000 description 3
- 238000000099 in vitro assay Methods 0.000 description 3
- 101150066555 lacZ gene Proteins 0.000 description 3
- 239000006166 lysate Substances 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 244000005700 microbiome Species 0.000 description 3
- 229960004927 neomycin Drugs 0.000 description 3
- 229920000768 polyamine Polymers 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 108091008146 restriction endonucleases Proteins 0.000 description 3
- 230000002441 reversible effect Effects 0.000 description 3
- 239000000243 solution Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 238000002198 surface plasmon resonance spectroscopy Methods 0.000 description 3
- 230000004083 survival effect Effects 0.000 description 3
- 239000000725 suspension Substances 0.000 description 3
- 238000001890 transfection Methods 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- NHBKXEKEPDILRR-UHFFFAOYSA-N 2,3-bis(butanoylsulfanyl)propyl butanoate Chemical compound CCCC(=O)OCC(SC(=O)CCC)CSC(=O)CCC NHBKXEKEPDILRR-UHFFFAOYSA-N 0.000 description 2
- 108020005345 3' Untranslated Regions Proteins 0.000 description 2
- 102100034540 Adenomatous polyposis coli protein Human genes 0.000 description 2
- 108010032595 Antibody Binding Sites Proteins 0.000 description 2
- 208000023275 Autoimmune disease Diseases 0.000 description 2
- 241000283690 Bos taurus Species 0.000 description 2
- 241000272201 Columbiformes Species 0.000 description 2
- 208000035473 Communicable disease Diseases 0.000 description 2
- 238000011537 Coomassie blue staining Methods 0.000 description 2
- 241000724791 Filamentous phage Species 0.000 description 2
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 2
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 2
- 108010051696 Growth Hormone Proteins 0.000 description 2
- 101000924577 Homo sapiens Adenomatous polyposis coli protein Proteins 0.000 description 2
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 2
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 2
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 2
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 2
- 108091036060 Linker DNA Proteins 0.000 description 2
- 101710156564 Major tail protein Gp23 Proteins 0.000 description 2
- 102000018697 Membrane Proteins Human genes 0.000 description 2
- 108010052285 Membrane Proteins Proteins 0.000 description 2
- 101000686985 Mouse mammary tumor virus (strain C3H) Protein PR73 Proteins 0.000 description 2
- 241000283973 Oryctolagus cuniculus Species 0.000 description 2
- 229910019142 PO4 Inorganic materials 0.000 description 2
- 241000282579 Pan Species 0.000 description 2
- 229930040373 Paraformaldehyde Natural products 0.000 description 2
- 229930182555 Penicillin Natural products 0.000 description 2
- JGSARLDLIJGVTE-MBNYWOFBSA-N Penicillin G Chemical compound N([C@H]1[C@H]2SC([C@@H](N2C1=O)C(O)=O)(C)C)C(=O)CC1=CC=CC=C1 JGSARLDLIJGVTE-MBNYWOFBSA-N 0.000 description 2
- 108091005804 Peptidases Proteins 0.000 description 2
- 239000004698 Polyethylene Substances 0.000 description 2
- 101710193132 Pre-hexon-linking protein VIII Proteins 0.000 description 2
- 239000004365 Protease Substances 0.000 description 2
- 239000012614 Q-Sepharose Substances 0.000 description 2
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 2
- 238000011579 SCID mouse model Methods 0.000 description 2
- -1 SPDP carbodiimide Chemical class 0.000 description 2
- UIIMBOGNXHQVGW-UHFFFAOYSA-M Sodium bicarbonate Chemical compound [Na+].OC([O-])=O UIIMBOGNXHQVGW-UHFFFAOYSA-M 0.000 description 2
- 102100038803 Somatotropin Human genes 0.000 description 2
- QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 2
- 206010052779 Transplant rejections Diseases 0.000 description 2
- 208000027418 Wounds and injury Diseases 0.000 description 2
- 230000001464 adherent effect Effects 0.000 description 2
- 235000004279 alanine Nutrition 0.000 description 2
- 125000003277 amino group Chemical group 0.000 description 2
- 230000003092 anti-cytokine Effects 0.000 description 2
- 210000000628 antibody-producing cell Anatomy 0.000 description 2
- 239000012062 aqueous buffer Substances 0.000 description 2
- 239000007864 aqueous solution Substances 0.000 description 2
- 210000001106 artificial yeast chromosome Anatomy 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 238000002306 biochemical method Methods 0.000 description 2
- 210000004899 c-terminal region Anatomy 0.000 description 2
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 2
- 230000020411 cell activation Effects 0.000 description 2
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 2
- 238000012875 competitive assay Methods 0.000 description 2
- 230000002860 competitive effect Effects 0.000 description 2
- 230000001268 conjugating effect Effects 0.000 description 2
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 2
- 230000009260 cross reactivity Effects 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 230000009089 cytolysis Effects 0.000 description 2
- 231100000433 cytotoxic Toxicity 0.000 description 2
- 238000002784 cytotoxicity assay Methods 0.000 description 2
- 231100000263 cytotoxicity test Toxicity 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 238000010586 diagram Methods 0.000 description 2
- 230000029087 digestion Effects 0.000 description 2
- 239000000975 dye Substances 0.000 description 2
- 238000001962 electrophoresis Methods 0.000 description 2
- 210000003743 erythrocyte Anatomy 0.000 description 2
- 239000011536 extraction buffer Substances 0.000 description 2
- 238000004108 freeze drying Methods 0.000 description 2
- 239000000122 growth hormone Substances 0.000 description 2
- 239000000833 heterodimer Substances 0.000 description 2
- 238000009396 hybridization Methods 0.000 description 2
- 238000003018 immunoassay Methods 0.000 description 2
- 229940072221 immunoglobulins Drugs 0.000 description 2
- 238000001114 immunoprecipitation Methods 0.000 description 2
- 239000012535 impurity Substances 0.000 description 2
- 230000000977 initiatory effect Effects 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 208000014674 injury Diseases 0.000 description 2
- 239000002502 liposome Substances 0.000 description 2
- 238000011068 loading method Methods 0.000 description 2
- 230000007774 longterm Effects 0.000 description 2
- 201000001441 melanoma Diseases 0.000 description 2
- 229910052751 metal Inorganic materials 0.000 description 2
- 239000002184 metal Substances 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 238000010172 mouse model Methods 0.000 description 2
- 239000002736 nonionic surfactant Substances 0.000 description 2
- 230000009871 nonspecific binding Effects 0.000 description 2
- 238000004806 packaging method and process Methods 0.000 description 2
- 229920002866 paraformaldehyde Polymers 0.000 description 2
- 239000002245 particle Substances 0.000 description 2
- 230000001717 pathogenic effect Effects 0.000 description 2
- 229940049954 penicillin Drugs 0.000 description 2
- 230000000144 pharmacologic effect Effects 0.000 description 2
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
- 239000010452 phosphate Substances 0.000 description 2
- 230000004962 physiological condition Effects 0.000 description 2
- 229920000642 polymer Polymers 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 210000001236 prokaryotic cell Anatomy 0.000 description 2
- 238000001742 protein purification Methods 0.000 description 2
- 230000012743 protein tagging Effects 0.000 description 2
- 239000001397 quillaja saponaria molina bark Substances 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 229930182490 saponin Natural products 0.000 description 2
- 150000007949 saponins Chemical class 0.000 description 2
- 125000003607 serino group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(O[H])([H])[H] 0.000 description 2
- 150000003384 small molecules Chemical class 0.000 description 2
- HHSGWIABCIVPJT-UHFFFAOYSA-M sodium;1-[4-[(2-iodoacetyl)amino]benzoyl]oxy-2,5-dioxopyrrolidine-3-sulfonate Chemical compound [Na+].O=C1C(S(=O)(=O)[O-])CC(=O)N1OC(=O)C1=CC=C(NC(=O)CI)C=C1 HHSGWIABCIVPJT-UHFFFAOYSA-M 0.000 description 2
- JUJBNYBVVQSIOU-UHFFFAOYSA-M sodium;4-[2-(4-iodophenyl)-3-(4-nitrophenyl)tetrazol-2-ium-5-yl]benzene-1,3-disulfonate Chemical compound [Na+].C1=CC([N+](=O)[O-])=CC=C1N1[N+](C=2C=CC(I)=CC=2)=NC(C=2C(=CC(=CC=2)S([O-])(=O)=O)S([O-])(=O)=O)=N1 JUJBNYBVVQSIOU-UHFFFAOYSA-M 0.000 description 2
- 238000001228 spectrum Methods 0.000 description 2
- 210000000952 spleen Anatomy 0.000 description 2
- 229960005322 streptomycin Drugs 0.000 description 2
- 238000001356 surgical procedure Methods 0.000 description 2
- 230000002194 synthesizing effect Effects 0.000 description 2
- 239000003053 toxin Substances 0.000 description 2
- 231100000765 toxin Toxicity 0.000 description 2
- 238000013518 transcription Methods 0.000 description 2
- 230000035897 transcription Effects 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- 230000004614 tumor growth Effects 0.000 description 2
- 230000005909 tumor killing Effects 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- 241000701447 unidentified baculovirus Species 0.000 description 2
- 238000011144 upstream manufacturing Methods 0.000 description 2
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 2
- BQWBEDSJTMWJAE-UHFFFAOYSA-N (2,5-dioxopyrrolidin-1-yl) 4-[(2-iodoacetyl)amino]benzoate Chemical compound C1=CC(NC(=O)CI)=CC=C1C(=O)ON1C(=O)CCC1=O BQWBEDSJTMWJAE-UHFFFAOYSA-N 0.000 description 1
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical compound OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- 101150084750 1 gene Proteins 0.000 description 1
- 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 1
- 101150090724 3 gene Proteins 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
- 101150014742 AGE1 gene Proteins 0.000 description 1
- 101100295756 Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / JCM 6841 / CCUG 19606 / CIP 70.34 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81) omp38 gene Proteins 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 244000063299 Bacillus subtilis Species 0.000 description 1
- 235000014469 Bacillus subtilis Nutrition 0.000 description 1
- 206010006187 Breast cancer Diseases 0.000 description 1
- 208000026310 Breast neoplasm Diseases 0.000 description 1
- 125000001433 C-terminal amino-acid group Chemical group 0.000 description 1
- 101100314454 Caenorhabditis elegans tra-1 gene Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 241000282472 Canis lupus familiaris Species 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 201000009030 Carcinoma Diseases 0.000 description 1
- 108010078791 Carrier Proteins Proteins 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 208000003322 Coinfection Diseases 0.000 description 1
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 1
- 108091035707 Consensus sequence Proteins 0.000 description 1
- 241000557626 Corvus corax Species 0.000 description 1
- 239000004971 Cross linker Substances 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 108010076804 DNA Restriction Enzymes Proteins 0.000 description 1
- 230000007018 DNA scission Effects 0.000 description 1
- 241000450599 DNA viruses Species 0.000 description 1
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 108010013369 Enteropeptidase Proteins 0.000 description 1
- 102100029727 Enteropeptidase Human genes 0.000 description 1
- 101710104662 Enterotoxin type C-3 Proteins 0.000 description 1
- 102100030844 Exocyst complex component 1 Human genes 0.000 description 1
- 108010074860 Factor Xa Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- 102000006395 Globulins Human genes 0.000 description 1
- 108010044091 Globulins Proteins 0.000 description 1
- 229920000209 Hexadimethrine bromide Polymers 0.000 description 1
- 108091006054 His-tagged proteins Proteins 0.000 description 1
- 101000740205 Homo sapiens Sal-like protein 1 Proteins 0.000 description 1
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 1
- 241000725303 Human immunodeficiency virus Species 0.000 description 1
- 206010020751 Hypersensitivity Diseases 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- 208000029462 Immunodeficiency disease Diseases 0.000 description 1
- 102000009786 Immunoglobulin Constant Regions Human genes 0.000 description 1
- 108010009817 Immunoglobulin Constant Regions Proteins 0.000 description 1
- 208000025814 Inflammatory myopathy with abundant macrophages Diseases 0.000 description 1
- 102100034343 Integrase Human genes 0.000 description 1
- 108091092195 Intron Proteins 0.000 description 1
- 208000011200 Kawasaki disease Diseases 0.000 description 1
- UGTHTQWIQKEDEH-BQBZGAKWSA-N L-alanyl-L-prolylglycine zwitterion Chemical compound C[C@H](N)C(=O)N1CCC[C@H]1C(=O)NCC(O)=O UGTHTQWIQKEDEH-BQBZGAKWSA-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
- 229930182816 L-glutamine Natural products 0.000 description 1
- 206010024229 Leprosy Diseases 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 108090001030 Lipoproteins Proteins 0.000 description 1
- 102000004895 Lipoproteins Human genes 0.000 description 1
- 208000016604 Lyme disease Diseases 0.000 description 1
- 102000007557 Melanoma-Specific Antigens Human genes 0.000 description 1
- 108010071463 Melanoma-Specific Antigens Proteins 0.000 description 1
- 241000699660 Mus musculus Species 0.000 description 1
- 101001106201 Mus musculus Ribonuclease 2B Proteins 0.000 description 1
- NIPNSKYNPDTRPC-UHFFFAOYSA-N N-[2-oxo-2-(2,4,6,7-tetrahydrotriazolo[4,5-c]pyridin-5-yl)ethyl]-2-[[3-(trifluoromethoxy)phenyl]methylamino]pyrimidine-5-carboxamide Chemical compound O=C(CNC(=O)C=1C=NC(=NC=1)NCC1=CC(=CC=C1)OC(F)(F)F)N1CC2=C(CC1)NN=N2 NIPNSKYNPDTRPC-UHFFFAOYSA-N 0.000 description 1
- 108091005461 Nucleic proteins Proteins 0.000 description 1
- 239000004677 Nylon Substances 0.000 description 1
- 108010079246 OMPA outer membrane proteins Proteins 0.000 description 1
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 1
- 101710160107 Outer membrane protein A Proteins 0.000 description 1
- 241001631646 Papillomaviridae Species 0.000 description 1
- 108010067902 Peptide Library Proteins 0.000 description 1
- 108010002747 Pfu DNA polymerase Proteins 0.000 description 1
- 241001505332 Polyomavirus sp. Species 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 239000012980 RPMI-1640 medium Substances 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 206010038997 Retroviral infections Diseases 0.000 description 1
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 1
- 102100037204 Sal-like protein 1 Human genes 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 101150052859 Slc9a1 gene Proteins 0.000 description 1
- 235000021355 Stearic acid Nutrition 0.000 description 1
- 241000194017 Streptococcus Species 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 230000005867 T cell response Effects 0.000 description 1
- 108700042075 T-Cell Receptor Genes 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
- 239000004473 Threonine Substances 0.000 description 1
- 108090000190 Thrombin Proteins 0.000 description 1
- 244000288561 Torulaspora delbrueckii Species 0.000 description 1
- 101710120037 Toxin CcdB Proteins 0.000 description 1
- 108700009124 Transcription Initiation Site Proteins 0.000 description 1
- 108091023040 Transcription factor Proteins 0.000 description 1
- 102000040945 Transcription factor Human genes 0.000 description 1
- 108700019146 Transgenes Proteins 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 102000015098 Tumor Suppressor Protein p53 Human genes 0.000 description 1
- 108010078814 Tumor Suppressor Protein p53 Proteins 0.000 description 1
- 102000001742 Tumor Suppressor Proteins Human genes 0.000 description 1
- 108010040002 Tumor Suppressor Proteins Proteins 0.000 description 1
- 206010067584 Type 1 diabetes mellitus Diseases 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 238000001261 affinity purification Methods 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 108010069020 alanyl-prolyl-glycine Proteins 0.000 description 1
- 125000003172 aldehyde group Chemical group 0.000 description 1
- 230000007815 allergy Effects 0.000 description 1
- 230000004075 alteration Effects 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 238000012197 amplification kit Methods 0.000 description 1
- 238000005349 anion exchange Methods 0.000 description 1
- 238000000137 annealing Methods 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000001093 anti-cancer Effects 0.000 description 1
- 229940124650 anti-cancer therapies Drugs 0.000 description 1
- 230000000840 anti-viral effect Effects 0.000 description 1
- 238000011319 anticancer therapy Methods 0.000 description 1
- 230000030741 antigen processing and presentation Effects 0.000 description 1
- 210000000612 antigen-presenting cell Anatomy 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 239000003443 antiviral agent Substances 0.000 description 1
- 101150042295 arfA gene Proteins 0.000 description 1
- 238000010420 art technique Methods 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 238000002820 assay format Methods 0.000 description 1
- 230000005784 autoimmunity Effects 0.000 description 1
- OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 102000005936 beta-Galactosidase Human genes 0.000 description 1
- 108010005774 beta-Galactosidase Proteins 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 101150031021 birA gene Proteins 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 108010006025 bovine growth hormone Proteins 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 125000000837 carbohydrate group Chemical group 0.000 description 1
- 230000015556 catabolic process Effects 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 239000003093 cationic surfactant Substances 0.000 description 1
- 238000000423 cell based assay Methods 0.000 description 1
- 230000005779 cell damage Effects 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 208000037887 cell injury Diseases 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 230000003196 chaotropic effect Effects 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
- 238000007385 chemical modification Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 238000002512 chemotherapy Methods 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 239000011248 coating agent Substances 0.000 description 1
- 238000000576 coating method Methods 0.000 description 1
- 238000004440 column chromatography Methods 0.000 description 1
- 230000000052 comparative effect Effects 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000005094 computer simulation Methods 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 238000007822 cytometric assay Methods 0.000 description 1
- 230000007812 deficiency Effects 0.000 description 1
- 230000002950 deficient Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 230000002939 deleterious effect Effects 0.000 description 1
- 238000004925 denaturation Methods 0.000 description 1
- 230000036425 denaturation Effects 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
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- 102000038379 digestive enzymes Human genes 0.000 description 1
- 108091007734 digestive enzymes Proteins 0.000 description 1
- 238000006471 dimerization reaction Methods 0.000 description 1
- 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 1
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
- 241001493065 dsRNA viruses Species 0.000 description 1
- 230000009977 dual effect Effects 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 230000006862 enzymatic digestion Effects 0.000 description 1
- 239000002532 enzyme inhibitor Substances 0.000 description 1
- 238000011156 evaluation Methods 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 238000000855 fermentation Methods 0.000 description 1
- 230000004151 fermentation Effects 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 238000000799 fluorescence microscopy Methods 0.000 description 1
- 125000000524 functional group Chemical group 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 102000054766 genetic haplotypes Human genes 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 108010067216 glycyl-glycyl-glycine Proteins 0.000 description 1
- XKUKSGPZAADMRA-UHFFFAOYSA-N glycyl-glycyl-glycine Natural products NCC(=O)NCC(=O)NCC(O)=O XKUKSGPZAADMRA-UHFFFAOYSA-N 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 210000002443 helper t lymphocyte Anatomy 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 239000000710 homodimer Substances 0.000 description 1
- 229940088597 hormone Drugs 0.000 description 1
- 239000005556 hormone Substances 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 229910052739 hydrogen Inorganic materials 0.000 description 1
- 239000001257 hydrogen Substances 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 230000005934 immune activation Effects 0.000 description 1
- 208000026278 immune system disease Diseases 0.000 description 1
- 230000000899 immune system response Effects 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 230000007813 immunodeficiency Effects 0.000 description 1
- 230000001506 immunosuppresive effect Effects 0.000 description 1
- 238000009169 immunotherapy Methods 0.000 description 1
- 238000002513 implantation Methods 0.000 description 1
- 238000005462 in vivo assay Methods 0.000 description 1
- 238000011503 in vivo imaging Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 230000002458 infectious effect Effects 0.000 description 1
- 206010022000 influenza Diseases 0.000 description 1
- 230000002401 inhibitory effect Effects 0.000 description 1
- 229910052816 inorganic phosphate Inorganic materials 0.000 description 1
- 239000002198 insoluble material Substances 0.000 description 1
- 238000007689 inspection Methods 0.000 description 1
- 238000007912 intraperitoneal administration Methods 0.000 description 1
- 238000010253 intravenous injection Methods 0.000 description 1
- 108010028930 invariant chain Proteins 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
- 238000005304 joining Methods 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- 239000004816 latex Substances 0.000 description 1
- 229920000126 latex Polymers 0.000 description 1
- 230000021633 leukocyte mediated immunity Effects 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 244000144972 livestock Species 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 238000011177 media preparation Methods 0.000 description 1
- 230000001404 mediated effect Effects 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 230000009149 molecular binding Effects 0.000 description 1
- 238000010369 molecular cloning Methods 0.000 description 1
- 238000012544 monitoring process Methods 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 208000001725 mucocutaneous lymph node syndrome Diseases 0.000 description 1
- 201000006417 multiple sclerosis Diseases 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 210000004897 n-terminal region Anatomy 0.000 description 1
- 230000009826 neoplastic cell growth Effects 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 238000013421 nuclear magnetic resonance imaging Methods 0.000 description 1
- 238000007899 nucleic acid hybridization Methods 0.000 description 1
- 238000011580 nude mouse model Methods 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- QIQXTHQIDYTFRH-UHFFFAOYSA-N octadecanoic acid Chemical compound CCCCCCCCCCCCCCCCCC(O)=O QIQXTHQIDYTFRH-UHFFFAOYSA-N 0.000 description 1
- OQCDKBAXFALNLD-UHFFFAOYSA-N octadecanoic acid Natural products CCCCCCCC(C)CCCCCCCCC(O)=O OQCDKBAXFALNLD-UHFFFAOYSA-N 0.000 description 1
- 239000002751 oligonucleotide probe Substances 0.000 description 1
- 150000002482 oligosaccharides Polymers 0.000 description 1
- 101150087557 omcB gene Proteins 0.000 description 1
- 101150115693 ompA gene Proteins 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 230000007170 pathology Effects 0.000 description 1
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 239000008196 pharmacological composition Substances 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 230000002062 proliferating effect Effects 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 230000000644 propagated effect Effects 0.000 description 1
- 235000004252 protein component Nutrition 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 230000005180 public health Effects 0.000 description 1
- 239000002510 pyrogen Substances 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000001177 retroviral effect Effects 0.000 description 1
- 206010039073 rheumatoid arthritis Diseases 0.000 description 1
- 108020004418 ribosomal RNA Proteins 0.000 description 1
- 238000003118 sandwich ELISA Methods 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 210000002027 skeletal muscle Anatomy 0.000 description 1
- 239000003998 snake venom Substances 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- 235000017557 sodium bicarbonate Nutrition 0.000 description 1
- CDBYLPFSWZWCQE-UHFFFAOYSA-L sodium carbonate Substances [Na+].[Na+].[O-]C([O-])=O CDBYLPFSWZWCQE-UHFFFAOYSA-L 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000011537 solubilization buffer Substances 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000000527 sonication Methods 0.000 description 1
- 125000006850 spacer group Chemical group 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 230000002269 spontaneous effect Effects 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 238000012289 standard assay Methods 0.000 description 1
- 239000008117 stearic acid Substances 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 238000012916 structural analysis Methods 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000004094 surface-active agent Substances 0.000 description 1
- 238000013268 sustained release Methods 0.000 description 1
- 239000012730 sustained-release form Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 230000001225 therapeutic effect Effects 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 210000001519 tissue Anatomy 0.000 description 1
- 230000001988 toxicity Effects 0.000 description 1
- 231100000419 toxicity Toxicity 0.000 description 1
- 230000005026 transcription initiation Effects 0.000 description 1
- 230000005030 transcription termination Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 239000003656 tris buffered saline Substances 0.000 description 1
- 210000003171 tumor-infiltrating lymphocyte Anatomy 0.000 description 1
- 208000035408 type 1 diabetes mellitus 1 Diseases 0.000 description 1
- 239000011534 wash buffer Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 238000002424 x-ray crystallography Methods 0.000 description 1
Images
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/28—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
- C07K16/2803—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 immunoglobulin superfamily
- C07K16/2809—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 immunoglobulin superfamily against the T-cell receptor (TcR)-CD3 complex
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
- C07K14/70503—Immunoglobulin superfamily
- C07K14/7051—T-cell receptor (TcR)-CD3 complex
-
- 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
-
- 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
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/31—Immunoglobulins specific features characterized by aspects of specificity or valency multispecific
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/30—Immunoglobulins specific features characterized by aspects of specificity or valency
- C07K2317/34—Identification of a linear epitope shorter than 20 amino acid residues or of a conformational epitope defined by amino acid residues
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2319/00—Fusion polypeptide
- C07K2319/30—Non-immunoglobulin-derived peptide or protein having an immunoglobulin constant or Fc region, or a fragment thereof, attached thereto
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Immunology (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Toxicology (AREA)
- General Chemical & Material Sciences (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Animal Behavior & Ethology (AREA)
- Cell Biology (AREA)
- Pharmacology & Pharmacy (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
- Polysaccharides And Polysaccharide Derivatives (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Saccharide Compounds (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US10516498P | 1998-10-21 | 1998-10-21 | |
| PCT/US1999/024645 WO2000023087A1 (en) | 1998-10-21 | 1999-10-21 | Polyspecific binding molecules and uses thereof |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2004537952A JP2004537952A (ja) | 2004-12-24 |
| JP2004537952A5 JP2004537952A5 (enExample) | 2009-08-20 |
| JP4467188B2 true JP4467188B2 (ja) | 2010-05-26 |
Family
ID=22304401
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2000576861A Expired - Lifetime JP4467188B2 (ja) | 1998-10-21 | 1999-10-21 | 多重特異的結合分子とその使用 |
Country Status (9)
| Country | Link |
|---|---|
| US (3) | US6534633B1 (enExample) |
| EP (1) | EP1124568B1 (enExample) |
| JP (1) | JP4467188B2 (enExample) |
| AT (1) | ATE370967T1 (enExample) |
| AU (1) | AU1218000A (enExample) |
| DE (1) | DE69936927T2 (enExample) |
| DK (1) | DK1124568T3 (enExample) |
| ES (1) | ES2293748T3 (enExample) |
| WO (1) | WO2000023087A1 (enExample) |
Families Citing this family (66)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20030144474A1 (en) * | 2000-06-05 | 2003-07-31 | Sunol Molecular Corporation | T cell receptor fusions and conjugates and methods of use thereof |
| JP4447456B2 (ja) | 2001-06-05 | 2010-04-07 | アルトール バイオサイエンス コーポレーション | Ｐ５３結合ｔ細胞受容体分子とその使用 |
| EP1567553A2 (en) * | 2002-12-03 | 2005-08-31 | Avidex Ltd. | Complexes of receptors |
| JP3803790B2 (ja) | 2003-02-17 | 2006-08-02 | 株式会社東北テクノアーチ | 新規なダイアボディ型二重特異性抗体 |
| US8772451B2 (en) | 2003-11-10 | 2014-07-08 | Altor Bioscience Corporation | Soluble TCR molecules and methods of use |
| US7964380B2 (en) * | 2005-01-21 | 2011-06-21 | Argylia Technologies | Nanoparticles for manipulation of biopolymers and methods of thereof |
| GB0507046D0 (en) * | 2005-04-06 | 2005-05-11 | Celltech R&D Ltd | Primers |
| US20080299137A1 (en) * | 2005-10-28 | 2008-12-04 | Novo Nordisk A/S | Fusion Proteins That Bind Effector Lymphocytes And Target Cells |
| WO2007085266A1 (en) * | 2006-01-30 | 2007-08-02 | Dako Denmark A/S | High-speed quantification of antigen specific t-cells in whole blood by flow cytometry |
| EP2505209A1 (en) | 2006-06-26 | 2012-10-03 | MacroGenics, Inc. | Fcgamma-RIIB-specific antibodies and methods of the use thereof |
| FR2902799B1 (fr) | 2006-06-27 | 2012-10-26 | Millipore Corp | Procede et unite de preparation d'un echantillon pour l'analyse microbiologique d'un liquide |
| US20100210478A1 (en) * | 2006-06-29 | 2010-08-19 | Xiaolian Gao | Make and use of surface molecules of varied densities |
| US8569464B2 (en) | 2006-12-21 | 2013-10-29 | Emd Millipore Corporation | Purification of proteins |
| US8163886B2 (en) | 2006-12-21 | 2012-04-24 | Emd Millipore Corporation | Purification of proteins |
| US8362217B2 (en) | 2006-12-21 | 2013-01-29 | Emd Millipore Corporation | Purification of proteins |
| EP2361930A3 (en) | 2007-03-26 | 2011-10-26 | Dako Denmark A/S | Multimers of MHC-peptide complexes and uses thereof in Borrelia infectious diseases |
| EP2167537A2 (en) | 2007-07-03 | 2010-03-31 | Dako Denmark A/S | Compiled methods for analysing and sorting samples |
| WO2009039854A2 (en) | 2007-09-27 | 2009-04-02 | Dako Denmark A/S | Mhc multimers in tuberculosis diagnostics, vaccine and therapeutics |
| US10968269B1 (en) | 2008-02-28 | 2021-04-06 | Agilent Technologies, Inc. | MHC multimers in borrelia diagnostics and disease |
| US20110070191A1 (en) * | 2008-03-19 | 2011-03-24 | Wong Hing C | T cell receptor fusions and conjugates and methods of use there of |
| WO2009151514A1 (en) * | 2008-06-11 | 2009-12-17 | Millipore Corporation | Stirred tank bioreactor |
| CN104800147A (zh) * | 2008-07-10 | 2015-07-29 | 德勒尼克斯治疗股份公司 | 用于大分子的增强的递送的方法和组合物 |
| WO2010009735A2 (en) * | 2008-07-23 | 2010-01-28 | Dako Denmark A/S | Combinatorial analysis and repair |
| GB0817244D0 (en) * | 2008-09-20 | 2008-10-29 | Univ Cardiff | Use of a protein kinase inhibitor to detect immune cells, such as T cells |
| US11992518B2 (en) | 2008-10-02 | 2024-05-28 | Agilent Technologies, Inc. | Molecular vaccines for infectious disease |
| US10369204B2 (en) | 2008-10-02 | 2019-08-06 | Dako Denmark A/S | Molecular vaccines for infectious disease |
| ES2749232T3 (es) * | 2008-12-16 | 2020-03-19 | Emd Millipore Corp | Reactor de tanque agitado y procedimiento |
| EP2258719A1 (en) | 2009-05-19 | 2010-12-08 | Max-Delbrück-Centrum für Molekulare Medizin (MDC) | Multiple target T cell receptor |
| GB0908613D0 (en) | 2009-05-20 | 2009-06-24 | Immunocore Ltd | T Cell Reseptors |
| SG10201804385YA (en) | 2010-05-17 | 2018-06-28 | Emd Millipore Corp | Stimulus responsive polymers for the purification of biomolecules |
| KR20130041843A (ko) * | 2010-06-08 | 2013-04-25 | 이엠디 밀리포어 코포레이션 | 바이오 분자의 정제에 사용되는 중합체의 잔량을 검출하는 방법 |
| AU2012316859A1 (en) * | 2011-09-29 | 2014-04-17 | Apo-T B.V. | Multi-specific binding molecules targeting aberrant cells |
| DK3369742T3 (da) | 2011-10-05 | 2020-10-19 | Univ Rockefeller | Dimere bakteriofaglysiner |
| KR101963230B1 (ko) | 2011-12-26 | 2019-03-29 | 삼성전자주식회사 | 복수개의 단일 항체를 포함하는 단백질 복합체 |
| EP2802356A1 (en) | 2012-01-13 | 2014-11-19 | Apo-T B.V. | Aberrant cell-restricted immunoglobulins provided with a toxic moiety |
| UA114108C2 (uk) | 2012-07-10 | 2017-04-25 | Борд Оф Ріджентс, Дзе Юніверсіті Оф Техас Сістем | Моноклональне антитіло для застосування в діагностиці і терапії злоякісних пухлин і аутоімунного захворювання |
| US20150183877A1 (en) * | 2012-07-18 | 2015-07-02 | Eli Lilly And Company | Multi-Specific IgG-(Fab)2 Constructs Containing T-Cell Receptor Constant Domains |
| KR101911438B1 (ko) * | 2012-10-31 | 2018-10-24 | 삼성전자주식회사 | 이중 특이 항원 결합 단백질 복합체 및 이중 특이 항체의 제조 방법 |
| US20150320799A1 (en) | 2012-12-20 | 2015-11-12 | Purdue Research Foundation | Chimeric antigen receptor-expressing t cells as anti-cancer therapeutics |
| EP3071594A4 (en) | 2013-11-22 | 2017-05-03 | The Board of Trustees of the University of Illionis | Engineered high-affinity human t cell receptors |
| US10816554B2 (en) * | 2014-04-04 | 2020-10-27 | The Board Of Trustees Of The Leland Stanford Junior University | Ligand discovery for T cell receptors |
| US9884921B2 (en) | 2014-07-01 | 2018-02-06 | Pfizer Inc. | Bispecific heterodimeric diabodies and uses thereof |
| JP7282521B2 (ja) | 2016-04-08 | 2023-05-29 | パーデュー・リサーチ・ファウンデイション | Ｃａｒ ｔ細胞療法のための方法および組成物 |
| US11827688B2 (en) | 2016-06-02 | 2023-11-28 | Immunocore Limited | Dosing regimen for GP100-specific TCR—anti-CD3 SCFV fusion protein |
| EP3579870A4 (en) | 2017-02-07 | 2020-12-30 | Seattle Children's Hospital (DBA Seattle Children's Research Institute) | PHOSPHOLIPID ETHER (PLE) T CAR-LYMPHOCYTE TUMOR (CTCT) TARGETING AGENTS |
| CN110944651A (zh) | 2017-02-08 | 2020-03-31 | 蜻蜓疗法股份有限公司 | 用于自然杀伤细胞激活的多特异性结合蛋白及其治疗癌症的治疗性用途 |
| ES2955074T3 (es) | 2017-02-20 | 2023-11-28 | Dragonfly Therapeutics Inc | Proteínas que se unen a HER2, NKG2D Y CD16 |
| WO2018160622A1 (en) | 2017-02-28 | 2018-09-07 | Endocyte, Inc. | Compositions and methods for car t cell therapy |
| WO2018166589A1 (en) | 2017-03-15 | 2018-09-20 | Biontech Cell & Gene Therapies Gmbh | Antigen receptors and uses thereof |
| WO2019046818A1 (en) | 2017-09-01 | 2019-03-07 | Dana-Farber Cancer Institute, Inc. | SPECIFIC IMMUNOGENIC PEPTIDES OF BCMA AND TACI ANTIGENS FOR THE TREATMENT OF CANCER |
| AU2019209432A1 (en) | 2018-01-22 | 2020-08-06 | Seattle Children's Hospital (dba Seattle Children's Research Institute) | Methods of use for CAR T cells |
| CN111936518A (zh) | 2018-02-06 | 2020-11-13 | 西雅图儿童医院（Dba西雅图儿童研究所） | 对fl-ple标记的肿瘤表现出最佳的t细胞功能的荧光素特异性car |
| CA3090236A1 (en) | 2018-02-08 | 2019-08-15 | Dragonfly Therapeutics, Inc. | Combination therapy of cancer involving multi-specific binding proteins that activate natural killer cells |
| SG11202007482WA (en) | 2018-02-08 | 2020-09-29 | Dragonfly Therapeutics Inc | Antibody variable domains targeting the nkg2d receptor |
| KR102832460B1 (ko) | 2018-02-20 | 2025-07-11 | 드래곤플라이 쎄라퓨틱스, 인크. | Cd33, nkg2d, 및 cd16에 결합하는 다중-특이적 결합 단백질, 및 이의 사용 방법 |
| WO2019165237A1 (en) | 2018-02-23 | 2019-08-29 | Endocyte, Inc. | Sequencing method for car t cell therapy |
| EA202091888A1 (ru) | 2018-08-08 | 2020-10-23 | Драгонфлай Терапьютикс, Инк. | Вариабельные домены антител, нацеленные на рецептор nkg2d |
| MX2021001527A (es) | 2018-08-08 | 2021-06-15 | Dragonfly Therapeutics Inc | Proteínas de unión a nkg2d, cd16 y a un antígeno asociado a tumor. |
| MA53293A (fr) | 2018-08-08 | 2021-11-17 | Dragonfly Therapeutics Inc | Protéines de liaison multi-spécifiques se liant à bcma, nkg2d et cd16, et méthodes d'utilisation |
| US12258373B2 (en) | 2018-12-17 | 2025-03-25 | Immudex Aps | Panel comprising Borrelia MHC multimers |
| CA3131138A1 (en) | 2019-03-06 | 2020-09-10 | Dana-Farber Cancer Institute, Inc. | T cell receptors specific to b-cell maturation antigen for treatment of cancer |
| MX2022013944A (es) | 2020-05-06 | 2022-11-30 | Dragonfly Therapeutics Inc | Proteinas que se unen al receptor activador de celulas asesinas naturales grupo 2 miembro d (nkg2d), cumulo de diferenciacion (cd16) y miembro a de la familia de dominios de lectina tipo c 12 (clec12a). |
| WO2022187539A1 (en) | 2021-03-03 | 2022-09-09 | Dragonfly Therapeutics, Inc. | Methods of treating cancer using multi-specific binding proteins that bind nkg2d, cd16 and a tumor-associated antigen |
| US12162940B2 (en) | 2021-05-05 | 2024-12-10 | Immatics Biotechnologies Gmbh | BMA031 antigen binding polypeptides |
| IL321737A (en) * | 2023-01-05 | 2025-08-01 | Angeles Therapeutics Inc | Methods and compositions for gene transformation and control of activity of synthetic and immune receptors |
| GB202320012D0 (en) * | 2023-12-22 | 2024-02-07 | Immunocore Ltd | Bispecific molecules |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE3853515T3 (de) * | 1987-05-21 | 2005-08-25 | Micromet Ag | Multifunktionelle proteine mit vorbestimmter zielsetzung. |
| DE3920358A1 (de) * | 1989-06-22 | 1991-01-17 | Behringwerke Ag | Bispezifische und oligospezifische, mono- und oligovalente antikoerperkonstrukte, ihre herstellung und verwendung |
| ES2098368T3 (es) | 1990-08-09 | 1997-05-01 | Nat Jewish Ct Immun & Respirat | Produccion de anticuerpos monoclonales contra un elemento vbeta humano de los receptores de las celulas t, utilizando vectores de adn recombinante. |
| AU643109B2 (en) * | 1990-12-14 | 1993-11-04 | Cell Genesys, Inc. | Chimeric chains for receptor-associated signal transduction pathways |
| US5637481A (en) | 1993-02-01 | 1997-06-10 | Bristol-Myers Squibb Company | Expression vectors encoding bispecific fusion proteins and methods of producing biologically active bispecific fusion proteins in a mammalian cell |
| US6399368B1 (en) | 1992-01-17 | 2002-06-04 | Board Of Regents, The University Of Texas System | Secretion of T cell receptor fragments from recombinant Escherichia coli cells |
| CA2118508A1 (en) | 1992-04-24 | 1993-11-11 | Elizabeth S. Ward | Recombinant production of immunoglobulin-like domains in prokaryotic cells |
| FR2698880B1 (fr) | 1992-11-25 | 1995-02-24 | Inst Nat Sante Rech Med | Procédé de production de récepteurs T solubles, produits ainsi obtenus et leur utilisation dans des compositions diagnostiques ou thérapeutiques. |
| WO1996018105A1 (en) * | 1994-12-06 | 1996-06-13 | The President And Fellows Of Harvard College | Single chain t-cell receptor |
| JPH11507843A (ja) * | 1996-03-28 | 1999-07-13 | ザ・ジョンズ・ホプキンス・ユニバーシティー | タンパク質の可溶性二価および多価ヘテロ二量体類縁体 |
| ATE533784T1 (de) * | 1997-10-02 | 2011-12-15 | Altor Bioscience Corp | Lösliche, einzelkettige proteine des t- zellrezeptors |
-
1999
- 1999-10-21 US US09/422,375 patent/US6534633B1/en not_active Expired - Lifetime
- 1999-10-21 AU AU12180/00A patent/AU1218000A/en not_active Abandoned
- 1999-10-21 AT AT99970601T patent/ATE370967T1/de active
- 1999-10-21 DE DE69936927T patent/DE69936927T2/de not_active Expired - Lifetime
- 1999-10-21 JP JP2000576861A patent/JP4467188B2/ja not_active Expired - Lifetime
- 1999-10-21 ES ES99970601T patent/ES2293748T3/es not_active Expired - Lifetime
- 1999-10-21 WO PCT/US1999/024645 patent/WO2000023087A1/en not_active Ceased
- 1999-10-21 EP EP99970601A patent/EP1124568B1/en not_active Expired - Lifetime
- 1999-10-21 DK DK99970601T patent/DK1124568T3/da active
-
2002
- 2002-11-05 US US10/287,941 patent/US8105830B2/en not_active Expired - Fee Related
-
2011
- 2011-12-22 US US13/335,362 patent/US20120230995A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| ATE370967T1 (de) | 2007-09-15 |
| DE69936927D1 (de) | 2007-10-04 |
| JP2004537952A (ja) | 2004-12-24 |
| WO2000023087A1 (en) | 2000-04-27 |
| US8105830B2 (en) | 2012-01-31 |
| EP1124568B1 (en) | 2007-08-22 |
| US6534633B1 (en) | 2003-03-18 |
| DE69936927T2 (de) | 2008-05-15 |
| ES2293748T3 (es) | 2008-03-16 |
| DK1124568T3 (da) | 2008-01-02 |
| EP1124568A1 (en) | 2001-08-22 |
| US20030171552A1 (en) | 2003-09-11 |
| US20120230995A1 (en) | 2012-09-13 |
| EP1124568A4 (en) | 2003-08-27 |
| AU1218000A (en) | 2000-05-08 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP4467188B2 (ja) | 多重特異的結合分子とその使用 | |
| JP7047172B2 (ja) | 融合タンパク質を用いたｔｃｒの再プログラミングのための組成物及び方法 | |
| US11560427B2 (en) | Heavy-chain antibodies (VHHs) against claudin 18A2 and use thereof | |
| KR100712256B1 (ko) | 가용성 단일쇄 ｔ-세포 수용체 단백질 | |
| US20040253250A1 (en) | Compositions and methods for regulating lymphocyte activation | |
| JPH08511420A (ja) | 抗 体 | |
| AU2004245038A1 (en) | De-immunized anti-CD3 antibody | |
| WO1998058965A2 (en) | B7-binding molecules for treating immune diseases | |
| RU2725807C2 (ru) | Растворимый универсальный усиливающий adcc синтетический слитный ген, пептидная технология и их применение | |
| EP1097210B1 (en) | Immunological reagent specifically interacting with the extracellular domain of the human zeta chain | |
| US20250302875A1 (en) | TARGETING MODULES AGAINST IL13R-alpha-2 AND/OR HER2 FOR USE IN A METHOD FOR STIMULATING A CHIMERIC ANTIGEN RECEPTOR-MEDIATED IMMUNE RESPONSE IN A MAMMAL | |
| AU773844B2 (en) | Compositions and methods for regulating lymphocyte activation | |
| JPH11509723A (ja) | 抗原特異的グリコシル化阻害因子の製法 | |
| AU1872902A (en) | Compositions and methods for regulating lymphocyte activation |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20050215 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20070703 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20070921 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20071001 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20071026 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20071102 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20071119 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20071127 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20080104 |
|
| RD13 | Notification of appointment of power of sub attorney |
Free format text: JAPANESE INTERMEDIATE CODE: A7433 Effective date: 20080104 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20080104 Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20080104 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20081216 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20090227 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20090306 |
|
| A601 | Written request for extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A601 Effective date: 20090511 |
|
| A602 | Written permission of extension of time |
Free format text: JAPANESE INTERMEDIATE CODE: A602 Effective date: 20090518 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20090616 |
|
| A524 | Written submission of copy of amendment under article 19 pct |
Free format text: JAPANESE INTERMEDIATE CODE: A524 Effective date: 20090616 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A821 Effective date: 20090618 |
|
| A131 | Notification of reasons for refusal |
Free format text: JAPANESE INTERMEDIATE CODE: A131 Effective date: 20091201 |
|
| A521 | Request for written amendment filed |
Free format text: JAPANESE INTERMEDIATE CODE: A523 Effective date: 20091214 |
|
| TRDD | Decision of grant or rejection written | ||
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 Effective date: 20100126 |
|
| A01 | Written decision to grant a patent or to grant a registration (utility model) |
Free format text: JAPANESE INTERMEDIATE CODE: A01 |
|
| A61 | First payment of annual fees (during grant procedure) |
Free format text: JAPANESE INTERMEDIATE CODE: A61 Effective date: 20100223 |
|
| R150 | Certificate of patent or registration of utility model |
Ref document number: 4467188 Country of ref document: JP Free format text: JAPANESE INTERMEDIATE CODE: R150 Free format text: JAPANESE INTERMEDIATE CODE: R150 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20130305 Year of fee payment: 3 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20130305 Year of fee payment: 3 |
|
| FPAY | Renewal fee payment (event date is renewal date of database) |
Free format text: PAYMENT UNTIL: 20140305 Year of fee payment: 4 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| R250 | Receipt of annual fees |
Free format text: JAPANESE INTERMEDIATE CODE: R250 |
|
| EXPY | Cancellation because of completion of term |