CA2829606C - Methods and reagents for creating monoclonal antibodies - Google Patents
Methods and reagents for creating monoclonal antibodies Download PDFInfo
- Publication number
- CA2829606C CA2829606C CA2829606A CA2829606A CA2829606C CA 2829606 C CA2829606 C CA 2829606C CA 2829606 A CA2829606 A CA 2829606A CA 2829606 A CA2829606 A CA 2829606A CA 2829606 C CA2829606 C CA 2829606C
- Authority
- CA
- Canada
- Prior art keywords
- antigen
- immunoglobulin
- nucleic acid
- acid sequences
- animal
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Active
Links
- 238000000034 method Methods 0.000 title claims abstract description 220
- 239000003153 chemical reaction reagent Substances 0.000 title claims description 46
- 239000000427 antigen Substances 0.000 claims abstract description 358
- 108091007433 antigens Proteins 0.000 claims abstract description 358
- 102000036639 antigens Human genes 0.000 claims abstract description 358
- 108060003951 Immunoglobulin Proteins 0.000 claims abstract description 270
- 102000018358 immunoglobulin Human genes 0.000 claims abstract description 270
- 150000007523 nucleic acids Chemical class 0.000 claims abstract description 239
- 241001465754 Metazoa Species 0.000 claims abstract description 181
- 238000001819 mass spectrum Methods 0.000 claims abstract description 121
- 102000039446 nucleic acids Human genes 0.000 claims abstract description 95
- 108020004707 nucleic acids Proteins 0.000 claims abstract description 95
- 229940072221 immunoglobulins Drugs 0.000 claims abstract description 84
- 102000007079 Peptide Fragments Human genes 0.000 claims abstract description 70
- 108010033276 Peptide Fragments Proteins 0.000 claims abstract description 61
- 102000012745 Immunoglobulin Subunits Human genes 0.000 claims abstract description 45
- 108010079585 Immunoglobulin Subunits Proteins 0.000 claims abstract description 45
- 125000003275 alpha amino acid group Chemical group 0.000 claims abstract 29
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 213
- 108090000623 proteins and genes Proteins 0.000 claims description 162
- 102000004169 proteins and genes Human genes 0.000 claims description 125
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 106
- 230000027455 binding Effects 0.000 claims description 67
- 241000282414 Homo sapiens Species 0.000 claims description 65
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 64
- 108020004414 DNA Proteins 0.000 claims description 62
- 108091032973 (ribonucleotides)n+m Proteins 0.000 claims description 55
- 238000001228 spectrum Methods 0.000 claims description 50
- 239000004365 Protease Substances 0.000 claims description 44
- 241000283973 Oryctolagus cuniculus Species 0.000 claims description 42
- 238000000746 purification Methods 0.000 claims description 42
- 102000035195 Peptidases Human genes 0.000 claims description 41
- 108091005804 Peptidases Proteins 0.000 claims description 41
- 230000003321 amplification Effects 0.000 claims description 38
- 238000003199 nucleic acid amplification method Methods 0.000 claims description 38
- 238000002965 ELISA Methods 0.000 claims description 37
- 238000001262 western blot Methods 0.000 claims description 33
- 238000003556 assay Methods 0.000 claims description 27
- 210000004369 blood Anatomy 0.000 claims description 26
- 239000008280 blood Substances 0.000 claims description 26
- 239000000126 substance Substances 0.000 claims description 26
- 230000007026 protein scission Effects 0.000 claims description 19
- 241000894007 species Species 0.000 claims description 15
- 101710120037 Toxin CcdB Proteins 0.000 claims description 13
- 238000000684 flow cytometry Methods 0.000 claims description 13
- 102000040430 polynucleotide Human genes 0.000 claims description 13
- 108091033319 polynucleotide Proteins 0.000 claims description 13
- 239000002157 polynucleotide Substances 0.000 claims description 13
- 238000003018 immunoassay Methods 0.000 claims description 11
- 238000010839 reverse transcription Methods 0.000 claims description 11
- 210000000265 leukocyte Anatomy 0.000 claims description 10
- 238000012216 screening Methods 0.000 claims description 10
- 230000015572 biosynthetic process Effects 0.000 claims description 9
- 238000010166 immunofluorescence Methods 0.000 claims description 9
- 235000013336 milk Nutrition 0.000 claims description 9
- 210000004080 milk Anatomy 0.000 claims description 9
- 239000008267 milk Substances 0.000 claims description 9
- 238000003364 immunohistochemistry Methods 0.000 claims description 8
- 238000001823 molecular biology technique Methods 0.000 claims description 8
- 108700005091 Immunoglobulin Genes Proteins 0.000 claims description 7
- 238000001261 affinity purification Methods 0.000 claims description 7
- 238000000338 in vitro Methods 0.000 claims description 7
- 210000001124 body fluid Anatomy 0.000 claims description 6
- 239000010839 body fluid Substances 0.000 claims description 6
- 238000006386 neutralization reaction Methods 0.000 claims description 6
- 238000003786 synthesis reaction Methods 0.000 claims description 6
- 230000028327 secretion Effects 0.000 claims description 5
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 claims description 4
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 claims description 4
- 238000001114 immunoprecipitation Methods 0.000 claims description 4
- 238000000159 protein binding assay Methods 0.000 claims description 4
- 238000003127 radioimmunoassay Methods 0.000 claims description 4
- 210000001179 synovial fluid Anatomy 0.000 claims description 4
- 210000003296 saliva Anatomy 0.000 claims description 3
- 210000003567 ascitic fluid Anatomy 0.000 claims description 2
- 210000001175 cerebrospinal fluid Anatomy 0.000 claims description 2
- 210000004748 cultured cell Anatomy 0.000 claims description 2
- 210000003097 mucus Anatomy 0.000 claims description 2
- 210000001138 tear Anatomy 0.000 claims description 2
- 101100112922 Candida albicans CDR3 gene Proteins 0.000 claims 4
- 238000000730 protein immunoprecipitation Methods 0.000 claims 1
- 210000004027 cell Anatomy 0.000 description 124
- 210000003719 b-lymphocyte Anatomy 0.000 description 113
- 238000003752 polymerase chain reaction Methods 0.000 description 85
- 150000001413 amino acids Chemical group 0.000 description 83
- 239000011324 bead Substances 0.000 description 82
- 239000000203 mixture Substances 0.000 description 81
- 238000012163 sequencing technique Methods 0.000 description 72
- 235000018102 proteins Nutrition 0.000 description 66
- 108010047041 Complementarity Determining Regions Proteins 0.000 description 65
- 239000012634 fragment Substances 0.000 description 62
- 238000004949 mass spectrometry Methods 0.000 description 59
- 238000006243 chemical reaction Methods 0.000 description 50
- 239000002299 complementary DNA Substances 0.000 description 43
- 108091093088 Amplicon Proteins 0.000 description 42
- 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 42
- 239000002953 phosphate buffered saline Substances 0.000 description 42
- 201000010099 disease Diseases 0.000 description 40
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 40
- 238000007481 next generation sequencing Methods 0.000 description 39
- 210000002966 serum Anatomy 0.000 description 36
- 210000002381 plasma Anatomy 0.000 description 35
- 239000002773 nucleotide Substances 0.000 description 34
- 125000003729 nucleotide group Chemical group 0.000 description 34
- 239000000872 buffer Substances 0.000 description 33
- 238000004458 analytical method Methods 0.000 description 32
- 230000002441 reversible effect Effects 0.000 description 32
- 238000004885 tandem mass spectrometry Methods 0.000 description 32
- 239000000523 sample Substances 0.000 description 31
- 229920001184 polypeptide Polymers 0.000 description 30
- 238000005516 engineering process Methods 0.000 description 29
- 230000000670 limiting effect Effects 0.000 description 29
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 27
- 150000002500 ions Chemical class 0.000 description 27
- 241000699666 Mus <mouse, genus> Species 0.000 description 24
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 24
- 102100024952 Protein CBFA2T1 Human genes 0.000 description 23
- 230000000694 effects Effects 0.000 description 22
- 241000699670 Mus sp. Species 0.000 description 21
- 235000001014 amino acid Nutrition 0.000 description 20
- 235000019419 proteases Nutrition 0.000 description 20
- 238000002955 isolation Methods 0.000 description 19
- 238000003757 reverse transcription PCR Methods 0.000 description 19
- 108090000631 Trypsin Proteins 0.000 description 18
- 102000004142 Trypsin Human genes 0.000 description 18
- 238000013459 approach Methods 0.000 description 18
- 239000012588 trypsin Substances 0.000 description 18
- 229960001322 trypsin Drugs 0.000 description 18
- 239000000047 product Substances 0.000 description 17
- 230000029087 digestion Effects 0.000 description 16
- 239000000839 emulsion Substances 0.000 description 16
- 238000001294 liquid chromatography-tandem mass spectrometry Methods 0.000 description 16
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 15
- 230000004927 fusion Effects 0.000 description 15
- 238000012408 PCR amplification Methods 0.000 description 14
- 230000002068 genetic effect Effects 0.000 description 14
- 108020004999 messenger RNA Proteins 0.000 description 14
- 210000004988 splenocyte Anatomy 0.000 description 14
- 239000004471 Glycine Substances 0.000 description 13
- 125000000539 amino acid group Chemical group 0.000 description 13
- 230000000692 anti-sense effect Effects 0.000 description 13
- 230000037396 body weight Effects 0.000 description 13
- 230000002596 correlated effect Effects 0.000 description 13
- 230000001225 therapeutic effect Effects 0.000 description 13
- 210000001519 tissue Anatomy 0.000 description 13
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 12
- 108090000284 Pepsin A Proteins 0.000 description 12
- 102000057297 Pepsin A Human genes 0.000 description 12
- BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 12
- 229940111202 pepsin Drugs 0.000 description 12
- 229920000136 polysorbate Polymers 0.000 description 12
- 238000002360 preparation method Methods 0.000 description 12
- 238000010561 standard procedure Methods 0.000 description 12
- 238000011282 treatment Methods 0.000 description 12
- 108090000317 Chymotrypsin Proteins 0.000 description 11
- 102000004190 Enzymes Human genes 0.000 description 11
- 108090000790 Enzymes Proteins 0.000 description 11
- 229960002376 chymotrypsin Drugs 0.000 description 11
- 238000003776 cleavage reaction Methods 0.000 description 11
- 229940088598 enzyme Drugs 0.000 description 11
- 239000002502 liposome Substances 0.000 description 11
- 230000009257 reactivity Effects 0.000 description 11
- 210000000952 spleen Anatomy 0.000 description 11
- 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 10
- 239000007983 Tris buffer Substances 0.000 description 10
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 10
- 241000700605 Viruses Species 0.000 description 10
- 210000000349 chromosome Anatomy 0.000 description 10
- 230000004048 modification Effects 0.000 description 10
- 238000012986 modification Methods 0.000 description 10
- 239000013642 negative control Substances 0.000 description 10
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 10
- 230000008569 process Effects 0.000 description 10
- 230000007017 scission Effects 0.000 description 10
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 10
- 102000007260 Deoxyribonuclease I Human genes 0.000 description 9
- 108010008532 Deoxyribonuclease I Proteins 0.000 description 9
- 206010028980 Neoplasm Diseases 0.000 description 9
- 238000010828 elution Methods 0.000 description 9
- 230000003053 immunization Effects 0.000 description 9
- 239000006166 lysate Substances 0.000 description 9
- 239000007787 solid Substances 0.000 description 9
- 239000006228 supernatant Substances 0.000 description 9
- 102220497176 Small vasohibin-binding protein_T47D_mutation Human genes 0.000 description 8
- 238000002835 absorbance Methods 0.000 description 8
- 238000010804 cDNA synthesis Methods 0.000 description 8
- 239000013604 expression vector Substances 0.000 description 8
- 238000002649 immunization Methods 0.000 description 8
- 238000000126 in silico method Methods 0.000 description 8
- 210000001806 memory b lymphocyte Anatomy 0.000 description 8
- 239000002245 particle Substances 0.000 description 8
- 239000011347 resin Substances 0.000 description 8
- 229920005989 resin Polymers 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 7
- 238000010847 SEQUEST Methods 0.000 description 7
- 229920002684 Sepharose Polymers 0.000 description 7
- 108010090804 Streptavidin Proteins 0.000 description 7
- 239000002253 acid Substances 0.000 description 7
- 238000004811 liquid chromatography Methods 0.000 description 7
- 238000012552 review Methods 0.000 description 7
- 230000009261 transgenic effect Effects 0.000 description 7
- OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 6
- 102100027207 CD27 antigen Human genes 0.000 description 6
- -1 CD78 Proteins 0.000 description 6
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 6
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 6
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 6
- 101000914511 Homo sapiens CD27 antigen Proteins 0.000 description 6
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 6
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 6
- 102100034343 Integrase Human genes 0.000 description 6
- 241000288906 Primates Species 0.000 description 6
- 238000002123 RNA extraction Methods 0.000 description 6
- 241000283984 Rodentia Species 0.000 description 6
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 6
- 239000013592 cell lysate Substances 0.000 description 6
- 230000005754 cellular signaling Effects 0.000 description 6
- 238000012512 characterization method Methods 0.000 description 6
- 238000010367 cloning Methods 0.000 description 6
- 230000000295 complement effect Effects 0.000 description 6
- 230000000875 corresponding effect Effects 0.000 description 6
- ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 6
- 239000003937 drug carrier Substances 0.000 description 6
- 238000001962 electrophoresis Methods 0.000 description 6
- 238000002474 experimental method Methods 0.000 description 6
- 235000019253 formic acid Nutrition 0.000 description 6
- 238000013467 fragmentation Methods 0.000 description 6
- 238000006062 fragmentation reaction Methods 0.000 description 6
- 230000028993 immune response Effects 0.000 description 6
- 108010045069 keyhole-limpet hemocyanin Proteins 0.000 description 6
- 238000004519 manufacturing process Methods 0.000 description 6
- 239000000463 material Substances 0.000 description 6
- 244000052769 pathogen Species 0.000 description 6
- 230000001717 pathogenic effect Effects 0.000 description 6
- 239000002243 precursor Substances 0.000 description 6
- 108010090371 progesterone receptor B Proteins 0.000 description 6
- 239000011541 reaction mixture Substances 0.000 description 6
- 239000002904 solvent Substances 0.000 description 6
- 229940043517 specific immunoglobulins Drugs 0.000 description 6
- 238000002255 vaccination Methods 0.000 description 6
- 102100024222 B-lymphocyte antigen CD19 Human genes 0.000 description 5
- 102100035360 Cerebellar degeneration-related antigen 1 Human genes 0.000 description 5
- 102000053602 DNA Human genes 0.000 description 5
- 101000980825 Homo sapiens B-lymphocyte antigen CD19 Proteins 0.000 description 5
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 5
- 108010067372 Pancreatic elastase Proteins 0.000 description 5
- 102000016387 Pancreatic elastase Human genes 0.000 description 5
- 108090000526 Papain Proteins 0.000 description 5
- 210000001744 T-lymphocyte Anatomy 0.000 description 5
- RTAQQCXQSZGOHL-UHFFFAOYSA-N Titanium Chemical compound [Ti] RTAQQCXQSZGOHL-UHFFFAOYSA-N 0.000 description 5
- 230000002378 acidificating effect Effects 0.000 description 5
- 239000011543 agarose gel Substances 0.000 description 5
- 229960002685 biotin Drugs 0.000 description 5
- 235000020958 biotin Nutrition 0.000 description 5
- 239000011616 biotin Substances 0.000 description 5
- 210000001185 bone marrow Anatomy 0.000 description 5
- 239000004202 carbamide Substances 0.000 description 5
- 239000000969 carrier Substances 0.000 description 5
- 238000012350 deep sequencing Methods 0.000 description 5
- 238000011161 development Methods 0.000 description 5
- 238000010790 dilution Methods 0.000 description 5
- 239000012895 dilution Substances 0.000 description 5
- 210000004408 hybridoma Anatomy 0.000 description 5
- 230000002163 immunogen Effects 0.000 description 5
- 238000002347 injection Methods 0.000 description 5
- 239000007924 injection Substances 0.000 description 5
- 244000144972 livestock Species 0.000 description 5
- 210000001165 lymph node Anatomy 0.000 description 5
- 210000005259 peripheral blood Anatomy 0.000 description 5
- 239000011886 peripheral blood Substances 0.000 description 5
- 108010090388 progesterone receptor A Proteins 0.000 description 5
- 230000002829 reductive effect Effects 0.000 description 5
- 230000001105 regulatory effect Effects 0.000 description 5
- 230000009870 specific binding Effects 0.000 description 5
- 229910052719 titanium Inorganic materials 0.000 description 5
- 239000010936 titanium Substances 0.000 description 5
- JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 4
- 230000006820 DNA synthesis Effects 0.000 description 4
- 241000282412 Homo Species 0.000 description 4
- 241000124008 Mammalia Species 0.000 description 4
- 241001529936 Murinae Species 0.000 description 4
- ZYFVNVRFVHJEIU-UHFFFAOYSA-N PicoGreen Chemical compound CN(C)CCCN(CCCN(C)C)C1=CC(=CC2=[N+](C3=CC=CC=C3S2)C)C2=CC=CC=C2N1C1=CC=CC=C1 ZYFVNVRFVHJEIU-UHFFFAOYSA-N 0.000 description 4
- 108010026552 Proteome Proteins 0.000 description 4
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 4
- 241000700159 Rattus Species 0.000 description 4
- 239000002671 adjuvant Substances 0.000 description 4
- 210000000628 antibody-producing cell Anatomy 0.000 description 4
- 238000003149 assay kit Methods 0.000 description 4
- 239000012620 biological material Substances 0.000 description 4
- 201000011510 cancer Diseases 0.000 description 4
- 238000013461 design Methods 0.000 description 4
- 238000010586 diagram Methods 0.000 description 4
- 238000009826 distribution Methods 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 238000001077 electron transfer detection Methods 0.000 description 4
- 238000005538 encapsulation Methods 0.000 description 4
- 238000000605 extraction Methods 0.000 description 4
- 210000004602 germ cell Anatomy 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- 238000000816 matrix-assisted laser desorption--ionisation Methods 0.000 description 4
- 239000003094 microcapsule Substances 0.000 description 4
- 229940055729 papain Drugs 0.000 description 4
- 235000019834 papain Nutrition 0.000 description 4
- 229920000642 polymer Polymers 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 238000012175 pyrosequencing Methods 0.000 description 4
- 239000011535 reaction buffer Substances 0.000 description 4
- 230000008707 rearrangement Effects 0.000 description 4
- 230000009467 reduction Effects 0.000 description 4
- 238000011160 research Methods 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 238000012360 testing method Methods 0.000 description 4
- 238000002560 therapeutic procedure Methods 0.000 description 4
- 238000001890 transfection Methods 0.000 description 4
- 238000013519 translation Methods 0.000 description 4
- 229960005486 vaccine Drugs 0.000 description 4
- 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 3
- 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 3
- 235000002198 Annona diversifolia Nutrition 0.000 description 3
- 108091008875 B cell receptors Proteins 0.000 description 3
- 102000004506 Blood Proteins Human genes 0.000 description 3
- 108010017384 Blood Proteins Proteins 0.000 description 3
- 241000283690 Bos taurus Species 0.000 description 3
- 241000283707 Capra Species 0.000 description 3
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 3
- 108010017826 DNA Polymerase I Proteins 0.000 description 3
- 102000004594 DNA Polymerase I Human genes 0.000 description 3
- 238000000018 DNA microarray Methods 0.000 description 3
- 102000016911 Deoxyribonucleases Human genes 0.000 description 3
- 108010053770 Deoxyribonucleases Proteins 0.000 description 3
- 241000287828 Gallus gallus Species 0.000 description 3
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 3
- 241000700721 Hepatitis B virus Species 0.000 description 3
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 3
- 101001018085 Lysobacter enzymogenes Lysyl endopeptidase Proteins 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 108091034117 Oligonucleotide Proteins 0.000 description 3
- 241001494479 Pecora Species 0.000 description 3
- 241000276498 Pollachius virens Species 0.000 description 3
- 229920002873 Polyethylenimine Polymers 0.000 description 3
- 229920001213 Polysorbate 20 Polymers 0.000 description 3
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 3
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 3
- 239000007984 Tris EDTA buffer Substances 0.000 description 3
- 230000009824 affinity maturation Effects 0.000 description 3
- 235000013330 chicken meat Nutrition 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 238000001360 collision-induced dissociation Methods 0.000 description 3
- 150000001875 compounds Chemical class 0.000 description 3
- 230000001419 dependent effect Effects 0.000 description 3
- 238000001514 detection method Methods 0.000 description 3
- 230000004069 differentiation Effects 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 230000006870 function Effects 0.000 description 3
- 239000000499 gel Substances 0.000 description 3
- 230000005484 gravity Effects 0.000 description 3
- 230000012010 growth Effects 0.000 description 3
- 210000005260 human cell Anatomy 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 210000005210 lymphoid organ Anatomy 0.000 description 3
- 239000011159 matrix material Substances 0.000 description 3
- 238000005259 measurement Methods 0.000 description 3
- 230000007246 mechanism Effects 0.000 description 3
- 239000004005 microsphere Substances 0.000 description 3
- 230000003287 optical effect Effects 0.000 description 3
- 230000036961 partial effect Effects 0.000 description 3
- 238000000955 peptide mass fingerprinting Methods 0.000 description 3
- 238000013081 phylogenetic analysis Methods 0.000 description 3
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 3
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 3
- 210000001948 pro-b lymphocyte Anatomy 0.000 description 3
- 230000035945 sensitivity Effects 0.000 description 3
- 238000000926 separation method Methods 0.000 description 3
- 239000007790 solid phase Substances 0.000 description 3
- 230000003595 spectral effect Effects 0.000 description 3
- 238000003860 storage Methods 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 150000003608 titanium Chemical class 0.000 description 3
- 241000712461 unidentified influenza virus Species 0.000 description 3
- 239000013598 vector Substances 0.000 description 3
- 230000003612 virological effect Effects 0.000 description 3
- WEVYNIUIFUYDGI-UHFFFAOYSA-N 3-[6-[4-(trifluoromethoxy)anilino]-4-pyrimidinyl]benzamide Chemical compound NC(=O)C1=CC=CC(C=2N=CN=C(NC=3C=CC(OC(F)(F)F)=CC=3)C=2)=C1 WEVYNIUIFUYDGI-UHFFFAOYSA-N 0.000 description 2
- 208000030507 AIDS Diseases 0.000 description 2
- 102100027211 Albumin Human genes 0.000 description 2
- 108010088751 Albumins Proteins 0.000 description 2
- 244000303258 Annona diversifolia Species 0.000 description 2
- 102100022005 B-lymphocyte antigen CD20 Human genes 0.000 description 2
- BXTVQNYQYUTQAZ-UHFFFAOYSA-N BNPS-skatole Chemical compound N=1C2=CC=CC=C2C(C)(Br)C=1SC1=CC=CC=C1[N+]([O-])=O BXTVQNYQYUTQAZ-UHFFFAOYSA-N 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- HEDRZPFGACZZDS-UHFFFAOYSA-N Chloroform Chemical compound ClC(Cl)Cl HEDRZPFGACZZDS-UHFFFAOYSA-N 0.000 description 2
- 108091026890 Coding region Proteins 0.000 description 2
- 206010009944 Colon cancer Diseases 0.000 description 2
- 102100032768 Complement receptor type 2 Human genes 0.000 description 2
- 108020004394 Complementary RNA Proteins 0.000 description 2
- 241000699800 Cricetinae Species 0.000 description 2
- FBPFZTCFMRRESA-KVTDHHQDSA-N D-Mannitol Chemical compound OC[C@@H](O)[C@@H](O)[C@H](O)[C@H](O)CO FBPFZTCFMRRESA-KVTDHHQDSA-N 0.000 description 2
- 238000001712 DNA sequencing Methods 0.000 description 2
- 229920002307 Dextran Polymers 0.000 description 2
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 2
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 2
- 101150086096 Eif2ak3 gene Proteins 0.000 description 2
- 241000289669 Erinaceus europaeus Species 0.000 description 2
- 241000282326 Felis catus Species 0.000 description 2
- 229920001917 Ficoll Polymers 0.000 description 2
- ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
- 239000007995 HEPES buffer Substances 0.000 description 2
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 2
- 101000897405 Homo sapiens B-lymphocyte antigen CD20 Proteins 0.000 description 2
- 101000574060 Homo sapiens Progesterone receptor Proteins 0.000 description 2
- 101000874179 Homo sapiens Syndecan-1 Proteins 0.000 description 2
- 241000725303 Human immunodeficiency virus Species 0.000 description 2
- 206010061218 Inflammation Diseases 0.000 description 2
- 101710203526 Integrase Proteins 0.000 description 2
- 108091092195 Intron Proteins 0.000 description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 2
- 241000283953 Lagomorpha Species 0.000 description 2
- 229930195725 Mannitol Natural products 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 239000012807 PCR reagent Substances 0.000 description 2
- ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
- 238000011530 RNeasy Mini Kit Methods 0.000 description 2
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 2
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N Silicium dioxide Chemical compound O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 2
- 229930006000 Sucrose Natural products 0.000 description 2
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 2
- 102100035721 Syndecan-1 Human genes 0.000 description 2
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 2
- 238000005903 acid hydrolysis reaction Methods 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 230000000996 additive effect Effects 0.000 description 2
- 230000001464 adherent effect Effects 0.000 description 2
- 230000029936 alkylation Effects 0.000 description 2
- 238000005804 alkylation reaction Methods 0.000 description 2
- 238000000137 annealing Methods 0.000 description 2
- WQZGKKKJIJFFOK-VFUOTHLCSA-N beta-D-glucose Chemical compound OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-VFUOTHLCSA-N 0.000 description 2
- 239000011230 binding agent Substances 0.000 description 2
- 239000012472 biological sample Substances 0.000 description 2
- 150000001720 carbohydrates Chemical class 0.000 description 2
- 235000014633 carbohydrates Nutrition 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 210000004978 chinese hamster ovary cell Anatomy 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
- 239000003593 chromogenic compound Substances 0.000 description 2
- 239000011248 coating agent Substances 0.000 description 2
- 238000000576 coating method Methods 0.000 description 2
- 239000003184 complementary RNA Substances 0.000 description 2
- 239000012228 culture supernatant Substances 0.000 description 2
- 238000012258 culturing Methods 0.000 description 2
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 2
- 235000018417 cysteine Nutrition 0.000 description 2
- 239000003398 denaturant Substances 0.000 description 2
- 239000003599 detergent Substances 0.000 description 2
- 238000000502 dialysis Methods 0.000 description 2
- 239000000539 dimer Substances 0.000 description 2
- 238000010494 dissociation reaction Methods 0.000 description 2
- 230000005593 dissociations Effects 0.000 description 2
- 229940079593 drug Drugs 0.000 description 2
- 210000003743 erythrocyte Anatomy 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- XUFQPHANEAPEMJ-UHFFFAOYSA-N famotidine Chemical compound NC(N)=NC1=NC(CSCCC(N)=NS(N)(=O)=O)=CS1 XUFQPHANEAPEMJ-UHFFFAOYSA-N 0.000 description 2
- 235000013861 fat-free Nutrition 0.000 description 2
- 210000004700 fetal blood Anatomy 0.000 description 2
- 239000012091 fetal bovine serum Substances 0.000 description 2
- 230000001605 fetal effect Effects 0.000 description 2
- 239000012997 ficoll-paque Substances 0.000 description 2
- 238000001914 filtration Methods 0.000 description 2
- 239000005350 fused silica glass Substances 0.000 description 2
- 239000008103 glucose Substances 0.000 description 2
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 2
- 239000003102 growth factor Substances 0.000 description 2
- 230000036541 health Effects 0.000 description 2
- 238000010438 heat treatment Methods 0.000 description 2
- 229960002897 heparin Drugs 0.000 description 2
- 229920000669 heparin Polymers 0.000 description 2
- 230000001900 immune effect Effects 0.000 description 2
- 210000000987 immune system Anatomy 0.000 description 2
- 238000010185 immunofluorescence analysis Methods 0.000 description 2
- 238000001727 in vivo Methods 0.000 description 2
- 230000004054 inflammatory process Effects 0.000 description 2
- 206010022000 influenza Diseases 0.000 description 2
- 230000002401 inhibitory effect Effects 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- 238000007912 intraperitoneal administration Methods 0.000 description 2
- 238000001990 intravenous administration Methods 0.000 description 2
- 210000004185 liver Anatomy 0.000 description 2
- 239000012139 lysis buffer Substances 0.000 description 2
- HQKMJHAJHXVSDF-UHFFFAOYSA-L magnesium stearate Chemical compound [Mg+2].CCCCCCCCCCCCCCCCCC([O-])=O.CCCCCCCCCCCCCCCCCC([O-])=O HQKMJHAJHXVSDF-UHFFFAOYSA-L 0.000 description 2
- 238000002826 magnetic-activated cell sorting Methods 0.000 description 2
- 235000010355 mannitol Nutrition 0.000 description 2
- 239000000594 mannitol Substances 0.000 description 2
- 238000013507 mapping Methods 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 238000012544 monitoring process Methods 0.000 description 2
- 210000005087 mononuclear cell Anatomy 0.000 description 2
- 238000011587 new zealand white rabbit Methods 0.000 description 2
- IFPHDUVGLXEIOQ-UHFFFAOYSA-N ortho-iodosylbenzoic acid Chemical compound OC(=O)C1=CC=CC=C1I=O IFPHDUVGLXEIOQ-UHFFFAOYSA-N 0.000 description 2
- 238000012856 packing Methods 0.000 description 2
- 239000012188 paraffin wax Substances 0.000 description 2
- 238000007911 parenteral administration Methods 0.000 description 2
- 230000010412 perfusion Effects 0.000 description 2
- 239000008194 pharmaceutical composition Substances 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- 238000004321 preservation Methods 0.000 description 2
- 108090000468 progesterone receptors Proteins 0.000 description 2
- 102000003998 progesterone receptors Human genes 0.000 description 2
- 230000002797 proteolythic effect Effects 0.000 description 2
- 238000000575 proteomic method Methods 0.000 description 2
- 102000005962 receptors Human genes 0.000 description 2
- 108020003175 receptors Proteins 0.000 description 2
- 230000006798 recombination Effects 0.000 description 2
- 238000005215 recombination Methods 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 230000000979 retarding effect Effects 0.000 description 2
- 230000003248 secreting effect Effects 0.000 description 2
- 238000010187 selection method Methods 0.000 description 2
- 239000002002 slurry Substances 0.000 description 2
- UNFWWIHTNXNPBV-WXKVUWSESA-N spectinomycin Chemical compound O([C@@H]1[C@@H](NC)[C@@H](O)[C@H]([C@@H]([C@H]1O1)O)NC)[C@]2(O)[C@H]1O[C@H](C)CC2=O UNFWWIHTNXNPBV-WXKVUWSESA-N 0.000 description 2
- 239000007858 starting material Substances 0.000 description 2
- 230000003068 static effect Effects 0.000 description 2
- 239000012089 stop solution Substances 0.000 description 2
- 239000005720 sucrose Substances 0.000 description 2
- 238000003146 transient transfection Methods 0.000 description 2
- 238000012176 true single molecule sequencing Methods 0.000 description 2
- 210000003171 tumor-infiltrating lymphocyte Anatomy 0.000 description 2
- 238000011144 upstream manufacturing Methods 0.000 description 2
- 230000009385 viral infection Effects 0.000 description 2
- 238000005406 washing Methods 0.000 description 2
- FPYJSJDOHRDAMT-KQWNVCNZSA-N 1h-indole-5-sulfonamide, n-(3-chlorophenyl)-3-[[3,5-dimethyl-4-[(4-methyl-1-piperazinyl)carbonyl]-1h-pyrrol-2-yl]methylene]-2,3-dihydro-n-methyl-2-oxo-, (3z)- Chemical compound C=1C=C2NC(=O)\C(=C/C3=C(C(C(=O)N4CCN(C)CC4)=C(C)N3)C)C2=CC=1S(=O)(=O)N(C)C1=CC=CC(Cl)=C1 FPYJSJDOHRDAMT-KQWNVCNZSA-N 0.000 description 1
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 1
- 102100031585 ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 Human genes 0.000 description 1
- 206010063409 Acarodermatitis Diseases 0.000 description 1
- 241000251468 Actinopterygii Species 0.000 description 1
- 229920000936 Agarose Polymers 0.000 description 1
- GUBGYTABKSRVRQ-XLOQQCSPSA-N Alpha-Lactose Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@H](O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-XLOQQCSPSA-N 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 241000271566 Aves Species 0.000 description 1
- 102100027205 B-cell antigen receptor complex-associated protein alpha chain Human genes 0.000 description 1
- 102100027203 B-cell antigen receptor complex-associated protein beta chain Human genes 0.000 description 1
- 102100025218 B-cell differentiation antigen CD72 Human genes 0.000 description 1
- 102100038080 B-cell receptor CD22 Human genes 0.000 description 1
- 208000032791 BCR-ABL1 positive chronic myelogenous leukemia Diseases 0.000 description 1
- 208000035143 Bacterial infection Diseases 0.000 description 1
- 108010082845 Bacteriorhodopsins Proteins 0.000 description 1
- 102100029945 Beta-galactoside alpha-2,6-sialyltransferase 1 Human genes 0.000 description 1
- 206010006187 Breast cancer Diseases 0.000 description 1
- 208000026310 Breast neoplasm Diseases 0.000 description 1
- CPELXLSAUQHCOX-UHFFFAOYSA-M Bromide Chemical compound [Br-] CPELXLSAUQHCOX-UHFFFAOYSA-M 0.000 description 1
- 101150013553 CD40 gene Proteins 0.000 description 1
- 102100035793 CD83 antigen Human genes 0.000 description 1
- 102100037904 CD9 antigen Human genes 0.000 description 1
- 241000282832 Camelidae Species 0.000 description 1
- 241000282836 Camelus dromedarius Species 0.000 description 1
- 102100032145 Carbohydrate sulfotransferase 10 Human genes 0.000 description 1
- 201000006082 Chickenpox Diseases 0.000 description 1
- 102100029172 Choline-phosphate cytidylyltransferase A Human genes 0.000 description 1
- 101710100763 Choline-phosphate cytidylyltransferase A Proteins 0.000 description 1
- 241000251730 Chondrichthyes Species 0.000 description 1
- 108020004635 Complementary DNA Proteins 0.000 description 1
- 241000689227 Cora <basidiomycete fungus> Species 0.000 description 1
- 241000557626 Corvus corax Species 0.000 description 1
- 102000004127 Cytokines Human genes 0.000 description 1
- 108090000695 Cytokines Proteins 0.000 description 1
- WQZGKKKJIJFFOK-QTVWNMPRSA-N D-mannopyranose Chemical compound OC[C@H]1OC(O)[C@@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-QTVWNMPRSA-N 0.000 description 1
- 102000012410 DNA Ligases Human genes 0.000 description 1
- 108010061982 DNA Ligases Proteins 0.000 description 1
- 102000004163 DNA-directed RNA polymerases Human genes 0.000 description 1
- 108090000626 DNA-directed RNA polymerases Proteins 0.000 description 1
- 102100025012 Dipeptidyl peptidase 4 Human genes 0.000 description 1
- 241000271571 Dromaius novaehollandiae Species 0.000 description 1
- 101150059079 EBNA1 gene Proteins 0.000 description 1
- 241000611421 Elia Species 0.000 description 1
- 102000005593 Endopeptidases Human genes 0.000 description 1
- 108010059378 Endopeptidases Proteins 0.000 description 1
- 241000283086 Equidae Species 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 206010015548 Euthanasia Diseases 0.000 description 1
- 108060002716 Exonuclease Proteins 0.000 description 1
- 238000004252 FT/ICR mass spectrometry Methods 0.000 description 1
- 108010058643 Fungal Proteins Proteins 0.000 description 1
- 108010024636 Glutathione Proteins 0.000 description 1
- JZNWSCPGTDBMEW-UHFFFAOYSA-N Glycerophosphorylethanolamin Natural products NCCOP(O)(=O)OCC(O)CO JZNWSCPGTDBMEW-UHFFFAOYSA-N 0.000 description 1
- 206010069767 H1N1 influenza Diseases 0.000 description 1
- 102100030595 HLA class II histocompatibility antigen gamma chain Human genes 0.000 description 1
- 101710088172 HTH-type transcriptional regulator RipA Proteins 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101000777636 Homo sapiens ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 Proteins 0.000 description 1
- 101000914489 Homo sapiens B-cell antigen receptor complex-associated protein alpha chain Proteins 0.000 description 1
- 101000914491 Homo sapiens B-cell antigen receptor complex-associated protein beta chain Proteins 0.000 description 1
- 101000934359 Homo sapiens B-cell differentiation antigen CD72 Proteins 0.000 description 1
- 101000884305 Homo sapiens B-cell receptor CD22 Proteins 0.000 description 1
- 101000863864 Homo sapiens Beta-galactoside alpha-2,6-sialyltransferase 1 Proteins 0.000 description 1
- 101000946856 Homo sapiens CD83 antigen Proteins 0.000 description 1
- 101100275686 Homo sapiens CR2 gene Proteins 0.000 description 1
- 101000775595 Homo sapiens Carbohydrate sulfotransferase 10 Proteins 0.000 description 1
- 101000941929 Homo sapiens Complement receptor type 2 Proteins 0.000 description 1
- 101000908391 Homo sapiens Dipeptidyl peptidase 4 Proteins 0.000 description 1
- 101001082627 Homo sapiens HLA class II histocompatibility antigen gamma chain Proteins 0.000 description 1
- 101001078133 Homo sapiens Integrin alpha-2 Proteins 0.000 description 1
- 101000994378 Homo sapiens Integrin alpha-3 Proteins 0.000 description 1
- 101001076422 Homo sapiens Interleukin-1 receptor type 2 Proteins 0.000 description 1
- 101001055144 Homo sapiens Interleukin-2 receptor subunit alpha Proteins 0.000 description 1
- 101000777628 Homo sapiens Leukocyte antigen CD37 Proteins 0.000 description 1
- 101000878605 Homo sapiens Low affinity immunoglobulin epsilon Fc receptor Proteins 0.000 description 1
- 101000738977 Homo sapiens Reverse transcriptase/ribonuclease H Proteins 0.000 description 1
- 101000884271 Homo sapiens Signal transducer CD24 Proteins 0.000 description 1
- 101000716124 Homo sapiens T-cell surface glycoprotein CD1c Proteins 0.000 description 1
- 101000914484 Homo sapiens T-lymphocyte activation antigen CD80 Proteins 0.000 description 1
- 101000851376 Homo sapiens Tumor necrosis factor receptor superfamily member 8 Proteins 0.000 description 1
- 108090000144 Human Proteins Proteins 0.000 description 1
- 102000003839 Human Proteins Human genes 0.000 description 1
- 241000701085 Human alphaherpesvirus 3 Species 0.000 description 1
- 102000006496 Immunoglobulin Heavy Chains Human genes 0.000 description 1
- 108010019476 Immunoglobulin Heavy Chains Proteins 0.000 description 1
- 102100025305 Integrin alpha-2 Human genes 0.000 description 1
- 102100032819 Integrin alpha-3 Human genes 0.000 description 1
- 238000012695 Interfacial polymerization Methods 0.000 description 1
- 102100026017 Interleukin-1 receptor type 2 Human genes 0.000 description 1
- 102100026878 Interleukin-2 receptor subunit alpha Human genes 0.000 description 1
- 102000011782 Keratins Human genes 0.000 description 1
- 108010076876 Keratins Proteins 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 241000282838 Lama Species 0.000 description 1
- 241000283986 Lepus Species 0.000 description 1
- 102100031586 Leukocyte antigen CD37 Human genes 0.000 description 1
- 102100038007 Low affinity immunoglobulin epsilon Fc receptor Human genes 0.000 description 1
- 241000406668 Loxodonta cyclotis Species 0.000 description 1
- 108060001084 Luciferase Proteins 0.000 description 1
- 239000005089 Luciferase Substances 0.000 description 1
- 102000043136 MAP kinase family Human genes 0.000 description 1
- 108091054455 MAP kinase family Proteins 0.000 description 1
- 229940125895 MET kinase inhibitor Drugs 0.000 description 1
- 239000004907 Macro-emulsion Substances 0.000 description 1
- 108700018351 Major Histocompatibility Complex Proteins 0.000 description 1
- PEEHTFAAVSWFBL-UHFFFAOYSA-N Maleimide Chemical compound O=C1NC(=O)C=C1 PEEHTFAAVSWFBL-UHFFFAOYSA-N 0.000 description 1
- 206010027476 Metastases Diseases 0.000 description 1
- 102100024193 Mitogen-activated protein kinase 1 Human genes 0.000 description 1
- 101100275687 Mus musculus Cr2 gene Proteins 0.000 description 1
- 101100370002 Mus musculus Tnfsf14 gene Proteins 0.000 description 1
- CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
- 108091007491 NSP3 Papain-like protease domains Proteins 0.000 description 1
- 241000282579 Pan Species 0.000 description 1
- 241000282577 Pan troglodytes Species 0.000 description 1
- 208000030852 Parasitic disease Diseases 0.000 description 1
- 108010030544 Peptidyl-Lys metalloendopeptidase Proteins 0.000 description 1
- 241000009328 Perro Species 0.000 description 1
- 241001674048 Phthiraptera Species 0.000 description 1
- 239000004793 Polystyrene Substances 0.000 description 1
- 101800003414 Pro-elastase Proteins 0.000 description 1
- 206010060862 Prostate cancer Diseases 0.000 description 1
- 208000000236 Prostatic Neoplasms Diseases 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 239000012083 RIPA buffer Substances 0.000 description 1
- 239000012979 RPMI medium Substances 0.000 description 1
- 238000010240 RT-PCR analysis Methods 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 108091028664 Ribonucleotide Proteins 0.000 description 1
- 241000447727 Scabies Species 0.000 description 1
- 102100038081 Signal transducer CD24 Human genes 0.000 description 1
- 229920002472 Starch Polymers 0.000 description 1
- 241000272534 Struthio camelus Species 0.000 description 1
- 241000282887 Suidae Species 0.000 description 1
- 102100036014 T-cell surface glycoprotein CD1c Human genes 0.000 description 1
- 102100027222 T-lymphocyte activation antigen CD80 Human genes 0.000 description 1
- 108010006785 Taq Polymerase Proteins 0.000 description 1
- 241000906446 Theraps Species 0.000 description 1
- 108090001109 Thermolysin Proteins 0.000 description 1
- 241001648840 Thosea asigna virus Species 0.000 description 1
- 102100040245 Tumor necrosis factor receptor superfamily member 5 Human genes 0.000 description 1
- 102100036857 Tumor necrosis factor receptor superfamily member 8 Human genes 0.000 description 1
- 206010067584 Type 1 diabetes mellitus Diseases 0.000 description 1
- 206010046980 Varicella Diseases 0.000 description 1
- 208000036142 Viral infection Diseases 0.000 description 1
- 208000027418 Wounds and injury Diseases 0.000 description 1
- 238000012452 Xenomouse strains Methods 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- 230000002159 abnormal effect Effects 0.000 description 1
- 150000007513 acids Chemical class 0.000 description 1
- 239000004480 active ingredient Substances 0.000 description 1
- 239000000443 aerosol Substances 0.000 description 1
- 238000001042 affinity chromatography Methods 0.000 description 1
- 208000026935 allergic disease Diseases 0.000 description 1
- WNROFYMDJYEPJX-UHFFFAOYSA-K aluminium hydroxide Chemical compound [OH-].[OH-].[OH-].[Al+3] WNROFYMDJYEPJX-UHFFFAOYSA-K 0.000 description 1
- 150000001408 amides Chemical class 0.000 description 1
- 210000000612 antigen-presenting cell Anatomy 0.000 description 1
- 239000003963 antioxidant agent Substances 0.000 description 1
- 210000001106 artificial yeast chromosome Anatomy 0.000 description 1
- 230000002238 attenuated effect Effects 0.000 description 1
- 230000001363 autoimmune Effects 0.000 description 1
- 208000022362 bacterial infectious disease Diseases 0.000 description 1
- 108010058966 bacteriophage T7 induced DNA polymerase Proteins 0.000 description 1
- 102000004441 bcr-abl Fusion Proteins Human genes 0.000 description 1
- 108010056708 bcr-abl Fusion Proteins Proteins 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000033228 biological regulation Effects 0.000 description 1
- 210000000601 blood cell Anatomy 0.000 description 1
- 210000004556 brain Anatomy 0.000 description 1
- 201000008275 breast carcinoma Diseases 0.000 description 1
- GEHJBWKLJVFKPS-UHFFFAOYSA-N bromochloroacetic acid Chemical compound OC(=O)C(Cl)Br GEHJBWKLJVFKPS-UHFFFAOYSA-N 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- 210000004899 c-terminal region Anatomy 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 235000012000 cholesterol Nutrition 0.000 description 1
- 229940043292 chymotrypsin / trypsin Drugs 0.000 description 1
- 238000005354 coacervation Methods 0.000 description 1
- 208000029742 colonic neoplasm Diseases 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 239000003636 conditioned culture medium Substances 0.000 description 1
- 238000012790 confirmation Methods 0.000 description 1
- 230000021615 conjugation Effects 0.000 description 1
- 239000000470 constituent Substances 0.000 description 1
- 239000000356 contaminant Substances 0.000 description 1
- 238000007796 conventional method Methods 0.000 description 1
- 230000001086 cytosolic effect Effects 0.000 description 1
- SUYVUBYJARFZHO-RRKCRQDMSA-N dATP Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-RRKCRQDMSA-N 0.000 description 1
- SUYVUBYJARFZHO-UHFFFAOYSA-N dATP Natural products C1=NC=2C(N)=NC=NC=2N1C1CC(O)C(COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 SUYVUBYJARFZHO-UHFFFAOYSA-N 0.000 description 1
- RGWHQCVHVJXOKC-SHYZEUOFSA-J dCTP(4-) Chemical compound O=C1N=C(N)C=CN1[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)C1 RGWHQCVHVJXOKC-SHYZEUOFSA-J 0.000 description 1
- HAAZLUGHYHWQIW-KVQBGUIXSA-N dGTP Chemical compound C1=NC=2C(=O)NC(N)=NC=2N1[C@H]1C[C@H](O)[C@@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)O1 HAAZLUGHYHWQIW-KVQBGUIXSA-N 0.000 description 1
- NHVNXKFIZYSCEB-XLPZGREQSA-N dTTP Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)C1 NHVNXKFIZYSCEB-XLPZGREQSA-N 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000034994 death Effects 0.000 description 1
- 238000000354 decomposition reaction Methods 0.000 description 1
- 239000003405 delayed action preparation Substances 0.000 description 1
- 239000005547 deoxyribonucleotide Substances 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 238000003795 desorption Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 239000003085 diluting agent Substances 0.000 description 1
- SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
- 229940090124 dipeptidyl peptidase 4 (dpp-4) inhibitors for blood glucose lowering Drugs 0.000 description 1
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical compound [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 description 1
- 235000011180 diphosphates Nutrition 0.000 description 1
- 239000012153 distilled water Substances 0.000 description 1
- 238000012377 drug delivery Methods 0.000 description 1
- 210000004667 early pro-b cell Anatomy 0.000 description 1
- 230000005684 electric field Effects 0.000 description 1
- 230000005672 electromagnetic field Effects 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000000132 electrospray ionisation Methods 0.000 description 1
- 230000008030 elimination Effects 0.000 description 1
- 238000003379 elimination reaction Methods 0.000 description 1
- 210000002472 endoplasmic reticulum Anatomy 0.000 description 1
- 230000006862 enzymatic digestion Effects 0.000 description 1
- 238000001976 enzyme digestion Methods 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- DNJIEGIFACGWOD-UHFFFAOYSA-N ethyl mercaptane Natural products CCS DNJIEGIFACGWOD-UHFFFAOYSA-N 0.000 description 1
- 238000001704 evaporation Methods 0.000 description 1
- 102000013165 exonuclease Human genes 0.000 description 1
- 239000010408 film Substances 0.000 description 1
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 210000001035 gastrointestinal tract Anatomy 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 210000001102 germinal center b cell Anatomy 0.000 description 1
- 229960003180 glutathione Drugs 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 208000002672 hepatitis B Diseases 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 238000012165 high-throughput sequencing Methods 0.000 description 1
- 238000007625 higher-energy collisional dissociation Methods 0.000 description 1
- 210000000688 human artificial chromosome Anatomy 0.000 description 1
- 235000020256 human milk Nutrition 0.000 description 1
- 210000004251 human milk Anatomy 0.000 description 1
- 229920001600 hydrophobic polymer Polymers 0.000 description 1
- 229920003063 hydroxymethyl cellulose Polymers 0.000 description 1
- 229940031574 hydroxymethyl cellulose Drugs 0.000 description 1
- 210000003297 immature b lymphocyte Anatomy 0.000 description 1
- 210000002865 immune cell Anatomy 0.000 description 1
- 238000010820 immunofluorescence microscopy Methods 0.000 description 1
- 238000002991 immunohistochemical analysis Methods 0.000 description 1
- 239000012133 immunoprecipitate Substances 0.000 description 1
- 238000012606 in vitro cell culture Methods 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 239000004615 ingredient Substances 0.000 description 1
- 208000014674 injury Diseases 0.000 description 1
- 238000007917 intracranial administration Methods 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000007852 inverse PCR Methods 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- PGLTVOMIXTUURA-UHFFFAOYSA-N iodoacetamide Chemical compound NC(=O)CI PGLTVOMIXTUURA-UHFFFAOYSA-N 0.000 description 1
- 238000005040 ion trap Methods 0.000 description 1
- FZWBNHMXJMCXLU-BLAUPYHCSA-N isomaltotriose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1OC[C@@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@@H](OC[C@@H](O)[C@@H](O)[C@H](O)[C@@H](O)C=O)O1 FZWBNHMXJMCXLU-BLAUPYHCSA-N 0.000 description 1
- 230000000155 isotopic effect Effects 0.000 description 1
- 238000011005 laboratory method Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 210000000014 large pre-b cell Anatomy 0.000 description 1
- 210000002202 late pro-b cell Anatomy 0.000 description 1
- 208000032839 leukemia Diseases 0.000 description 1
- 150000002632 lipids Chemical class 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 230000033001 locomotion Effects 0.000 description 1
- 235000019689 luncheon sausage Nutrition 0.000 description 1
- 210000004698 lymphocyte Anatomy 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- ZLNQQNXFFQJAID-UHFFFAOYSA-L magnesium carbonate Chemical compound [Mg+2].[O-]C([O-])=O ZLNQQNXFFQJAID-UHFFFAOYSA-L 0.000 description 1
- 239000001095 magnesium carbonate Substances 0.000 description 1
- 229910000021 magnesium carbonate Inorganic materials 0.000 description 1
- 235000019359 magnesium stearate Nutrition 0.000 description 1
- 210000004379 membrane Anatomy 0.000 description 1
- 239000004530 micro-emulsion Substances 0.000 description 1
- 239000011859 microparticle Substances 0.000 description 1
- 238000013508 migration Methods 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 229940126619 mouse monoclonal antibody Drugs 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- 210000004897 n-terminal region Anatomy 0.000 description 1
- 239000002088 nanocapsule Substances 0.000 description 1
- 239000002105 nanoparticle Substances 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 230000003472 neutralizing effect Effects 0.000 description 1
- 230000009871 nonspecific binding Effects 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 238000012758 nuclear staining Methods 0.000 description 1
- 210000000056 organ Anatomy 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 210000002741 palatine tonsil Anatomy 0.000 description 1
- 238000010647 peptide synthesis reaction Methods 0.000 description 1
- 230000002093 peripheral effect Effects 0.000 description 1
- 210000001986 peyer's patch Anatomy 0.000 description 1
- 238000002823 phage display Methods 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- 210000004214 philadelphia chromosome Anatomy 0.000 description 1
- WTJKGGKOPKCXLL-RRHRGVEJSA-N phosphatidylcholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCC=CCCCCCCCC WTJKGGKOPKCXLL-RRHRGVEJSA-N 0.000 description 1
- 150000008104 phosphatidylethanolamines Chemical class 0.000 description 1
- 210000003720 plasmablast Anatomy 0.000 description 1
- 210000004180 plasmocyte Anatomy 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- 229920002223 polystyrene Polymers 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- 235000008476 powdered milk Nutrition 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 238000002203 pretreatment Methods 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000001915 proofreading effect Effects 0.000 description 1
- 238000012514 protein characterization Methods 0.000 description 1
- 108020001580 protein domains Proteins 0.000 description 1
- 230000009145 protein modification Effects 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 229940024999 proteolytic enzymes for treatment of wounds and ulcers Drugs 0.000 description 1
- 238000010814 radioimmunoprecipitation assay Methods 0.000 description 1
- 239000012132 radioimmunoprecipitation assay buffer Substances 0.000 description 1
- 238000009790 rate-determining step (RDS) Methods 0.000 description 1
- 238000003259 recombinant expression Methods 0.000 description 1
- 230000001177 retroviral effect Effects 0.000 description 1
- 206010039073 rheumatoid arthritis Diseases 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 125000002652 ribonucleotide group Chemical group 0.000 description 1
- 210000003705 ribosome Anatomy 0.000 description 1
- CVHZOJJKTDOEJC-UHFFFAOYSA-N saccharin Chemical compound C1=CC=C2C(=O)NS(=O)(=O)C2=C1 CVHZOJJKTDOEJC-UHFFFAOYSA-N 0.000 description 1
- 208000005687 scabies Diseases 0.000 description 1
- 201000004409 schistosomiasis Diseases 0.000 description 1
- 238000007841 sequencing by ligation Methods 0.000 description 1
- 210000000345 small pre-b cell Anatomy 0.000 description 1
- 230000003393 splenic effect Effects 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 238000012289 standard assay Methods 0.000 description 1
- 239000008107 starch Substances 0.000 description 1
- 235000019698 starch Nutrition 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 238000010254 subcutaneous injection Methods 0.000 description 1
- 239000007929 subcutaneous injection Substances 0.000 description 1
- 239000013595 supernatant sample Substances 0.000 description 1
- 230000020382 suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I Effects 0.000 description 1
- 230000002459 sustained effect Effects 0.000 description 1
- 238000013268 sustained release Methods 0.000 description 1
- 239000012730 sustained-release form Substances 0.000 description 1
- 201000010740 swine influenza Diseases 0.000 description 1
- 208000024891 symptom Diseases 0.000 description 1
- 238000001308 synthesis method Methods 0.000 description 1
- 238000007910 systemic administration Methods 0.000 description 1
- 230000009885 systemic effect Effects 0.000 description 1
- 239000000454 talc Substances 0.000 description 1
- 235000012222 talc Nutrition 0.000 description 1
- 229910052623 talc Inorganic materials 0.000 description 1
- 229940126622 therapeutic monoclonal antibody Drugs 0.000 description 1
- 239000003104 tissue culture media Substances 0.000 description 1
- 238000011200 topical administration Methods 0.000 description 1
- 230000000699 topical effect Effects 0.000 description 1
- 239000003053 toxin Substances 0.000 description 1
- 231100000765 toxin Toxicity 0.000 description 1
- 238000013518 transcription Methods 0.000 description 1
- 230000035897 transcription Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- 230000005945 translocation Effects 0.000 description 1
- 201000008827 tuberculosis Diseases 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 238000003260 vortexing Methods 0.000 description 1
- 239000003643 water by type Substances 0.000 description 1
- 239000001993 wax Substances 0.000 description 1
- 239000000080 wetting agent Substances 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/08—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses
- C07K16/081—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from viruses from DNA viruses
- C07K16/082—Hepadnaviridae, e.g. hepatitis B virus
-
- 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
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/44—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material not provided for elsewhere, e.g. haptens, metals, DNA, RNA, amino acids
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/20—Immunoglobulins specific features characterized by taxonomic origin
- C07K2317/21—Immunoglobulins specific features characterized by taxonomic origin from primates, e.g. man
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K2317/00—Immunoglobulins specific features
- C07K2317/50—Immunoglobulins specific features characterized by immunoglobulin fragments
- C07K2317/56—Immunoglobulins specific features characterized by immunoglobulin fragments variable (Fv) region, i.e. VH and/or VL
- C07K2317/565—Complementarity determining region [CDR]
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- General Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Immunology (AREA)
- Virology (AREA)
- Communicable Diseases (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Pharmaceuticals Containing Other Organic And Inorganic Compounds (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (9)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201161450922P | 2011-03-09 | 2011-03-09 | |
| US61/450,922 | 2011-03-09 | ||
| US201161560006P | 2011-11-15 | 2011-11-15 | |
| US61/560,006 | 2011-11-15 | ||
| US201161566876P | 2011-12-05 | 2011-12-05 | |
| US61/566,876 | 2011-12-05 | ||
| US201261594729P | 2012-02-03 | 2012-02-03 | |
| US61/594,729 | 2012-02-03 | ||
| PCT/US2012/028501 WO2012122484A1 (en) | 2011-03-09 | 2012-03-09 | Methods and reagents for creating monoclonal antibodies |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CA2829606A1 CA2829606A1 (en) | 2012-09-13 |
| CA2829606C true CA2829606C (en) | 2020-06-02 |
Family
ID=45922811
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA2829606A Active CA2829606C (en) | 2011-03-09 | 2012-03-09 | Methods and reagents for creating monoclonal antibodies |
Country Status (12)
| Country | Link |
|---|---|
| US (2) | US9920110B2 (cg-RX-API-DMAC7.html) |
| EP (2) | EP3345922A1 (cg-RX-API-DMAC7.html) |
| JP (3) | JP6211931B2 (cg-RX-API-DMAC7.html) |
| KR (3) | KR101938343B1 (cg-RX-API-DMAC7.html) |
| CN (2) | CN108220297A (cg-RX-API-DMAC7.html) |
| AU (3) | AU2012225310B2 (cg-RX-API-DMAC7.html) |
| CA (1) | CA2829606C (cg-RX-API-DMAC7.html) |
| DK (1) | DK2683736T3 (cg-RX-API-DMAC7.html) |
| ES (1) | ES2666301T3 (cg-RX-API-DMAC7.html) |
| HK (1) | HK1256304A1 (cg-RX-API-DMAC7.html) |
| HU (1) | HUE037095T2 (cg-RX-API-DMAC7.html) |
| WO (1) | WO2012122484A1 (cg-RX-API-DMAC7.html) |
Families Citing this family (53)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| PT2387627E (pt) | 2009-01-15 | 2016-06-03 | Adaptive Biotechnologies Corp | Determinação do perfil de imunidade adaptativa e métodos de geração de anticorpos monoclonais |
| EP2783214A2 (en) | 2011-11-23 | 2014-10-01 | The Board of Regents of The University of Texas System | Proteomic identification of antibodies |
| US10077478B2 (en) | 2012-03-05 | 2018-09-18 | Adaptive Biotechnologies Corp. | Determining paired immune receptor chains from frequency matched subunits |
| EP2831276B1 (en) | 2012-05-08 | 2016-04-20 | Adaptive Biotechnologies Corporation | Compositions and method for measuring and calibrating amplification bias in multiplexed pcr reactions |
| AU2013273953B2 (en) | 2012-06-15 | 2018-12-13 | The Board Of Regents Of The University Of Texas System | High throughput sequencing of multiple transcripts of a single cell |
| WO2015160439A2 (en) | 2014-04-17 | 2015-10-22 | Adaptive Biotechnologies Corporation | Quantification of adaptive immune cell genomes in a complex mixture of cells |
| US20160024493A1 (en) * | 2013-03-15 | 2016-01-28 | Adaptive Biotechnologies Corporation | Uniquely tagged rearranged adaptive immune receptor genes in a complex gene set |
| US9708657B2 (en) | 2013-07-01 | 2017-07-18 | Adaptive Biotechnologies Corp. | Method for generating clonotype profiles using sequence tags |
| US10208125B2 (en) | 2013-07-15 | 2019-02-19 | University of Pittsburgh—of the Commonwealth System of Higher Education | Anti-mucin 1 binding agents and uses thereof |
| ES2649147T3 (es) * | 2013-09-09 | 2018-01-10 | Shimadzu Corporation | Método para preparar fragmentos de péptidos, kit para preparar fragmentos de péptidos que se van a emplear en el mismo y método de análisis |
| GB201316644D0 (en) * | 2013-09-19 | 2013-11-06 | Kymab Ltd | Expression vector production & High-Throughput cell screening |
| US10066265B2 (en) | 2014-04-01 | 2018-09-04 | Adaptive Biotechnologies Corp. | Determining antigen-specific t-cells |
| EP3399052A3 (en) * | 2014-06-25 | 2018-12-26 | The Rockefeller University | Compositions and methods for rapid production of versatile nanobody repertoires |
| CN105277638A (zh) * | 2014-07-22 | 2016-01-27 | 沈鹤霄 | 一种单克隆抗体IgG质谱测序方法 |
| EP3212790B1 (en) | 2014-10-29 | 2020-03-25 | Adaptive Biotechnologies Corp. | Highly-multiplexed simultaneous detection of nucleic acids encoding paired adaptive immune receptor heterodimers from many samples |
| US10246701B2 (en) | 2014-11-14 | 2019-04-02 | Adaptive Biotechnologies Corp. | Multiplexed digital quantitation of rearranged lymphoid receptors in a complex mixture |
| CN104560979B (zh) * | 2015-01-20 | 2017-04-05 | 中国人民解放军第三军医大学 | 基于高通量测序构建鼠bcr重链文库的多重pcr引物和方法 |
| CN104560980B (zh) * | 2015-01-20 | 2017-04-05 | 中国人民解放军第三军医大学 | 基于高通量测序构建鼠BCR轻链Lamda文库的多重PCR引物和方法 |
| WO2016138122A1 (en) | 2015-02-24 | 2016-09-01 | Adaptive Biotechnologies Corp. | Methods for diagnosing infectious disease and determining hla status using immune repertoire sequencing |
| CN112557490B (zh) * | 2015-03-06 | 2025-05-23 | 英国质谱公司 | 拭子和活检样品的快速蒸发电离质谱和解吸电喷雾电离质谱分析 |
| GB2553918B (en) | 2015-03-06 | 2022-10-12 | Micromass Ltd | Ambient ionization mass spectrometry imaging platform for direct mapping from bulk tissue |
| EP3264989B1 (en) | 2015-03-06 | 2023-12-20 | Micromass UK Limited | Spectrometric analysis |
| WO2016142681A1 (en) | 2015-03-06 | 2016-09-15 | Micromass Uk Limited | Spectrometric analysis of microbes |
| GB2556436B (en) | 2015-03-06 | 2022-01-26 | Micromass Ltd | Cell population analysis |
| GB2555921B (en) | 2015-03-06 | 2021-09-15 | Micromass Ltd | Endoscopic tissue identification tool |
| WO2016142689A1 (en) | 2015-03-06 | 2016-09-15 | Micromass Uk Limited | Tissue analysis by mass spectrometry or ion mobility spectrometry |
| US10513733B2 (en) | 2015-03-23 | 2019-12-24 | Board Of Regents, The University Of Texas System | High throughout sequencing of paired VH and VL transcripts from B cells secreting antigen-specific antibodies |
| EP3277294B1 (en) | 2015-04-01 | 2024-05-15 | Adaptive Biotechnologies Corp. | Method of identifying human compatible t cell receptors specific for an antigenic target |
| EP3346912A4 (en) * | 2015-09-09 | 2019-08-21 | Ubiome Inc. | METHOD AND SYSTEM FOR MICROBIAL-DERIVED DIAGNOSTICS AND THERAPEUTIC FOR DISEASES RELATED TO CEREBRO-KRANIOFAZIAL HEALTH |
| US11454611B2 (en) | 2016-04-14 | 2022-09-27 | Micromass Uk Limited | Spectrometric analysis of plants |
| CN106047857B (zh) * | 2016-06-01 | 2020-04-03 | 苏州金唯智生物科技有限公司 | 一种发掘特异性功能抗体的方法 |
| CN107525934A (zh) * | 2016-06-21 | 2017-12-29 | 张效龙 | 一种测定血液中抗体氨基酸序列的方法 |
| US10428325B1 (en) | 2016-09-21 | 2019-10-01 | Adaptive Biotechnologies Corporation | Identification of antigen-specific B cell receptors |
| CN118497192A (zh) * | 2017-03-07 | 2024-08-16 | 豪夫迈·罗氏有限公司 | 发现替代性抗原特异性抗体变体的方法 |
| AU2018303254B2 (en) * | 2017-07-21 | 2025-05-29 | Novimmune Sa | Generating multispecific antibody mixtures and methods of uses thereof |
| CN109425662A (zh) * | 2017-08-23 | 2019-03-05 | 深圳华大基因研究院 | 一种鉴定蛋白的方法及系统 |
| WO2019084538A1 (en) | 2017-10-27 | 2019-05-02 | Board Of Regents, The University Of Texas System | TUMOR SPECIFIC ANTIBODIES, T CELL RECEPTORS AND METHODS OF IDENTIFICATION THEREOF |
| US11254980B1 (en) | 2017-11-29 | 2022-02-22 | Adaptive Biotechnologies Corporation | Methods of profiling targeted polynucleotides while mitigating sequencing depth requirements |
| CN119881293A (zh) | 2018-03-21 | 2025-04-25 | 沃特世科技公司 | 基于非抗体高亲和力的样品制备、吸附剂、装置和方法 |
| WO2019183882A1 (zh) * | 2018-03-29 | 2019-10-03 | 深圳达闼科技控股有限公司 | 物质检测方法、装置、电子设备及计算机可读存储介质 |
| CN108530533B (zh) * | 2018-04-13 | 2020-09-04 | 吉林大学 | 猪瘟病毒单克隆抗体hk24及医用用途 |
| EP3894867A4 (en) * | 2018-12-11 | 2022-09-28 | Merck Sharp & Dohme Corp. | PROCEDURE FOR IDENTIFICATION OF HIGH-AFFINITY MONOCLONAL ANTIBODIES OF HEAVY AND LIGHT CHAIN FROM HIGH-THROUGHPUT SCREENS OF B-CELL AND HYBRIDOME LIBRARIES |
| EP3982369A4 (en) * | 2019-06-07 | 2023-06-14 | Chugai Seiyaku Kabushiki Kaisha | INFORMATION PROCESSING SYSTEM, INFORMATION PROCESSING PROCESS, PROGRAM AND METHOD FOR PRODUCTION OF AN ANTIGEN-BINDING MOLECULE OR PROTEIN |
| CN110452296A (zh) * | 2019-07-16 | 2019-11-15 | 福州精锐生物技术有限公司 | 一种兔单克隆抗体制备方法 |
| MX2022003244A (es) * | 2019-09-16 | 2022-04-26 | Regeneron Pharma | Metodos de lc-ms para la isotipificacion y cuantificacion de anticuerpos. |
| CN115175919A (zh) * | 2019-12-09 | 2022-10-11 | 光行科技株式会社 | 转换结合剂、其制备方法、和各自使用该转换结合剂的药物组合物、测定试剂盒、以及抗原和抗体测定方法 |
| WO2021222546A1 (en) * | 2020-05-01 | 2021-11-04 | University Of Pittsburgh-Of The Commonwealth System Of Higher Education | Compositions and methods for identifying nanobodies and nanobody affinities |
| EP4320148A4 (en) * | 2021-04-09 | 2025-05-14 | Abterra Biosciences, Inc. | METHOD FOR IDENTIFYING ANTIBODIES FROM PROTEIN MIXTURES |
| IT202100019334A1 (it) * | 2021-07-21 | 2023-01-21 | Univ Degli Studi Di Pavia | Metodo per l’identificazione dell’intera sequenza della regione variabile delle catene pesanti e leggere di immunoglobuline |
| CN115894687B (zh) * | 2022-03-31 | 2024-06-07 | 台州恩泽医疗中心(集团) | 一种抗hla-g1，-g2，-g5及hla-g6异构体分子的单克隆抗体及其用途 |
| CN116779037B (zh) * | 2022-07-27 | 2025-08-05 | 北京理工大学 | 一种基于从头测序和同源标签图论的抗体序列鉴定方法 |
| CN117849159B (zh) * | 2024-01-09 | 2025-01-07 | 融智生物科技（青岛）有限公司 | M蛋白的检测方法、电子设备及存储介质 |
| CN120214310B (zh) * | 2025-05-20 | 2025-08-19 | 中国农业大学 | 一种禽白血病抗原检测试剂盒及其制备方法 |
Family Cites Families (63)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4485045A (en) | 1981-07-06 | 1984-11-27 | Research Corporation | Synthetic phosphatidyl cholines useful in forming liposomes |
| GB8308235D0 (en) | 1983-03-25 | 1983-05-05 | Celltech Ltd | Polypeptides |
| US4816567A (en) | 1983-04-08 | 1989-03-28 | Genentech, Inc. | Recombinant immunoglobin preparations |
| US4544545A (en) | 1983-06-20 | 1985-10-01 | Trustees University Of Massachusetts | Liposomes containing modified cholesterol for organ targeting |
| US6548640B1 (en) | 1986-03-27 | 2003-04-15 | Btg International Limited | Altered antibodies |
| US5075109A (en) | 1986-10-24 | 1991-12-24 | Southern Research Institute | Method of potentiating an immune response |
| US4897268A (en) | 1987-08-03 | 1990-01-30 | Southern Research Institute | Drug delivery system and method of making the same |
| US5530101A (en) | 1988-12-28 | 1996-06-25 | Protein Design Labs, Inc. | Humanized immunoglobulins |
| US6673776B1 (en) | 1989-03-21 | 2004-01-06 | Vical Incorporated | Expression of exogenous polynucleotide sequences in a vertebrate, mammal, fish, bird or human |
| US5013556A (en) | 1989-10-20 | 1991-05-07 | Liposome Technology, Inc. | Liposomes with enhanced circulation time |
| ATE139258T1 (de) | 1990-01-12 | 1996-06-15 | Cell Genesys Inc | Erzeugung xenogener antikörper |
| US6150584A (en) | 1990-01-12 | 2000-11-21 | Abgenix, Inc. | Human antibodies derived from immunized xenomice |
| US5427908A (en) | 1990-05-01 | 1995-06-27 | Affymax Technologies N.V. | Recombinant library screening methods |
| GB9015198D0 (en) | 1990-07-10 | 1990-08-29 | Brien Caroline J O | Binding substance |
| US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
| EP0746609A4 (en) | 1991-12-17 | 1997-12-17 | Genpharm Int | NON-HUMAN TRANSGENIC ANIMALS CAPABLE OF PRODUCING HETEROLOGOUS ANTIBODIES |
| ATE182625T1 (de) | 1993-01-12 | 1999-08-15 | Biogen Inc | Rekombinante anti-vla4 antikörpermoleküle |
| US6436908B1 (en) | 1995-05-30 | 2002-08-20 | Duke University | Use of exogenous β-adrenergic receptor and β-adrenergic receptor kinase gene constructs to enhance myocardial function |
| US5641870A (en) | 1995-04-20 | 1997-06-24 | Genentech, Inc. | Low pH hydrophobic interaction chromatography for antibody purification |
| US5739277A (en) | 1995-04-14 | 1998-04-14 | Genentech Inc. | Altered polypeptides with increased half-life |
| US5750341A (en) | 1995-04-17 | 1998-05-12 | Lynx Therapeutics, Inc. | DNA sequencing by parallel oligonucleotide extensions |
| AU9692198A (en) | 1997-10-10 | 1999-05-03 | Kevin J. Donahue | Gene delivery compositions and methods |
| US6780591B2 (en) | 1998-05-01 | 2004-08-24 | Arizona Board Of Regents | Method of determining the nucleotide sequence of oligonucleotides and DNA molecules |
| WO1999057321A1 (en) | 1998-05-01 | 1999-11-11 | Arizona Board Of Regents | Method of determining the nucleotide sequence of oligonucleotides and dna molecules |
| US7300753B2 (en) | 1998-09-04 | 2007-11-27 | John Rush | Immunoaffinity isolation of modified peptides from complex mixtures |
| AR021833A1 (es) | 1998-09-30 | 2002-08-07 | Applied Research Systems | Metodos de amplificacion y secuenciacion de acido nucleico |
| US7211390B2 (en) | 1999-09-16 | 2007-05-01 | 454 Life Sciences Corporation | Method of sequencing a nucleic acid |
| US7244559B2 (en) | 1999-09-16 | 2007-07-17 | 454 Life Sciences Corporation | Method of sequencing a nucleic acid |
| WO2003016861A2 (en) | 2001-08-14 | 2003-02-27 | President And Fellows Of Harvard College | Absolute quantification of proteins and modified forms thereof by multistage mass spectrometry |
| WO2003052059A2 (en) * | 2001-12-14 | 2003-06-26 | Eli Lilly And Company | Recombinant bovine thrombin |
| GB0130267D0 (en) | 2001-12-19 | 2002-02-06 | Neutec Pharma Plc | Focussed antibody technology |
| US7485291B2 (en) | 2003-06-03 | 2009-02-03 | Cell Genesys, Inc. | Compositions and methods for generating multiple polypeptides from a single vector using a virus derived peptide cleavage site, and uses thereof |
| JP4644663B2 (ja) | 2003-06-03 | 2011-03-02 | セル ジェネシス インコーポレイテッド | ペプチド開裂部位を用いた単一ベクターからの組換えポリペプチドの高められた発現のための構成と方法 |
| US7169560B2 (en) | 2003-11-12 | 2007-01-30 | Helicos Biosciences Corporation | Short cycle methods for sequencing polynucleotides |
| CA2555699C (en) | 2004-02-09 | 2013-10-15 | Northeastern University | Monoclonal antibody based biomarker discovery and development platform |
| WO2005082098A2 (en) | 2004-02-27 | 2005-09-09 | President And Fellows Of Harvard College | Polony fluorescent in situ sequencing beads |
| WO2005084134A2 (en) | 2004-03-04 | 2005-09-15 | Dena Leshkowitz | Quantifying and profiling antibody and t cell receptor gene expression |
| PA8672101A1 (es) | 2005-04-29 | 2006-12-07 | Centocor Inc | Anticuerpos anti-il-6, composiciones, métodos y usos |
| PT1891088E (pt) * | 2005-06-10 | 2011-12-19 | Ares Trading Sa | Processo para a purificação da proteína de ligação il-18 |
| EP1989230B1 (en) | 2006-02-10 | 2016-06-01 | Genentech, Inc. | Anti-fgf19 antibodies and methods using same |
| GB0612928D0 (en) | 2006-06-29 | 2006-08-09 | Ucb Sa | Biological products |
| US20090209737A1 (en) * | 2006-07-07 | 2009-08-20 | Pall Corporation | Use of denaturing agents during affinity capture |
| ATE529752T1 (de) | 2006-12-21 | 2011-11-15 | Novartis Ag | Antikörperquantifizierung |
| AU2008221118B2 (en) | 2007-03-01 | 2013-10-03 | Les Laboratoires Servier | Recombinant anti-epidermal growth factor receptor antibody compositions |
| AU2008224259A1 (en) | 2007-03-06 | 2008-09-12 | Symphogen A/S | Recombinant antibodies for treatment of respiratory syncytial virus infections |
| JP5721951B2 (ja) | 2007-03-22 | 2015-05-20 | バイオジェン アイデック マサチューセッツ インコーポレイテッド | 抗体、抗体誘導体、および抗体断片を含む、ｃｄ１５４に特異的に結合する結合タンパク質ならびにその使用 |
| SI2602323T1 (en) | 2007-06-01 | 2018-05-31 | Open Monoclonal Technology, Inc. | Compositions and procedures for inhibiting endogenous immunoglobin gene and the formation of transgenic human idiopathic antibodies |
| US7887801B2 (en) | 2007-07-13 | 2011-02-15 | Topotarget Germany Ag | Optimized DNA and protein sequence of an antibody to improve quality and yield of bacterially expressed antibody fusion proteins |
| US8057796B2 (en) * | 2007-11-12 | 2011-11-15 | Theraclone Sciences, Inc. | Compositions and methods for the therapy and diagnosis of influenza |
| JP2011522213A (ja) | 2007-11-22 | 2011-07-28 | シムフォゲン・アクティーゼルスカブ | 組み換えポリクローナルタンパク質の特徴づけに関する方法 |
| EP2088432A1 (en) | 2008-02-11 | 2009-08-12 | MorphoSys AG | Methods for identification of an antibody or a target |
| US20110151494A1 (en) | 2008-06-30 | 2011-06-23 | H. Lee Moffit Cancer & Research Institute | Methods and materials for monitoring myeloma using quantitative mass spectrometry |
| DK2346994T3 (da) | 2008-09-30 | 2022-02-28 | Ablexis Llc | Knock-in-mus til fremstilling af kimære antistoffer |
| RU2011129459A (ru) | 2008-12-18 | 2013-01-27 | Эрасмус Юниверсити Медикал Сентр Роттердам | Трансгенные животные (не человек), экспрессирующие гуманизированные антитела, и их применение |
| PT2387627E (pt) | 2009-01-15 | 2016-06-03 | Adaptive Biotechnologies Corp | Determinação do perfil de imunidade adaptativa e métodos de geração de anticorpos monoclonais |
| TR201818431T4 (tr) | 2009-02-25 | 2019-01-21 | Ucb Biopharma Sprl | Antikorlar Üretmek İçin Usul |
| EP2517556B2 (en) | 2009-07-08 | 2023-03-22 | Kymab Limited | Site-Specific Recombination Method, Rodents & Rodent Cells capable of Expressing Chimaeric Antibodies or Chains |
| US20110045534A1 (en) | 2009-08-20 | 2011-02-24 | Cell Signaling Technology, Inc. | Nucleic Acid Cassette For Producing Recombinant Antibodies |
| US8293483B2 (en) | 2009-09-11 | 2012-10-23 | Epitomics, Inc. | Method for identifying lineage-related antibodies |
| KR102004106B1 (ko) | 2010-03-31 | 2019-07-25 | 아블렉시스, 엘엘씨 | 키메라 항체의 제조를 위한 비-인간 동물의 유전적 조작 |
| CA2796822C (en) | 2010-05-07 | 2021-10-05 | The Board Of Trustees Of The Leland Standford Junior University | Measurement and comparison of immune diversity by high-throughput sequencing |
| WO2011146514A2 (en) | 2010-05-17 | 2011-11-24 | The Board Of Regents Of The University Of Texas System | Rapid isolation of monoclonal antibodies from animals |
| SG186238A1 (en) | 2010-06-17 | 2013-01-30 | Kymab Ltd | Animal models and therapeutic molecules |
-
2012
- 2012-03-09 KR KR1020137026647A patent/KR101938343B1/ko active Active
- 2012-03-09 EP EP17196465.3A patent/EP3345922A1/en not_active Withdrawn
- 2012-03-09 AU AU2012225310A patent/AU2012225310B2/en active Active
- 2012-03-09 KR KR1020197026655A patent/KR20190107761A/ko not_active Ceased
- 2012-03-09 CN CN201810154961.6A patent/CN108220297A/zh active Pending
- 2012-03-09 JP JP2013557906A patent/JP6211931B2/ja active Active
- 2012-03-09 EP EP12711501.2A patent/EP2683736B1/en active Active
- 2012-03-09 DK DK12711501.2T patent/DK2683736T3/en active
- 2012-03-09 HU HUE12711501A patent/HUE037095T2/hu unknown
- 2012-03-09 US US13/416,582 patent/US9920110B2/en active Active
- 2012-03-09 CN CN201280021326.1A patent/CN103842379A/zh active Pending
- 2012-03-09 WO PCT/US2012/028501 patent/WO2012122484A1/en not_active Ceased
- 2012-03-09 ES ES12711501.2T patent/ES2666301T3/es active Active
- 2012-03-09 KR KR1020197000660A patent/KR20190006083A/ko not_active Ceased
- 2012-03-09 CA CA2829606A patent/CA2829606C/en active Active
-
2017
- 2017-09-13 JP JP2017175320A patent/JP6557709B2/ja not_active Expired - Fee Related
- 2017-10-12 AU AU2017245395A patent/AU2017245395B2/en active Active
-
2018
- 2018-01-19 US US15/875,615 patent/US20190002532A1/en not_active Abandoned
- 2018-11-30 HK HK18115369.1A patent/HK1256304A1/en unknown
-
2019
- 2019-07-11 JP JP2019128863A patent/JP2019195335A/ja active Pending
- 2019-08-14 AU AU2019216660A patent/AU2019216660A1/en not_active Abandoned
Also Published As
| Publication number | Publication date |
|---|---|
| CN108220297A (zh) | 2018-06-29 |
| ES2666301T3 (es) | 2018-05-03 |
| US20120308555A1 (en) | 2012-12-06 |
| US9920110B2 (en) | 2018-03-20 |
| US20190002532A1 (en) | 2019-01-03 |
| AU2019216660A1 (en) | 2019-09-05 |
| AU2012225310B2 (en) | 2017-08-03 |
| HUE037095T2 (hu) | 2018-08-28 |
| AU2012225310A1 (en) | 2013-09-26 |
| EP2683736B1 (en) | 2018-01-17 |
| KR20140010436A (ko) | 2014-01-24 |
| DK2683736T3 (en) | 2018-04-23 |
| AU2017245395A1 (en) | 2017-11-02 |
| JP2014509853A (ja) | 2014-04-24 |
| AU2017245395A2 (en) | 2017-11-23 |
| EP3345922A1 (en) | 2018-07-11 |
| CN103842379A (zh) | 2014-06-04 |
| KR20190107761A (ko) | 2019-09-20 |
| JP6211931B2 (ja) | 2017-10-11 |
| WO2012122484A1 (en) | 2012-09-13 |
| CA2829606A1 (en) | 2012-09-13 |
| JP2019195335A (ja) | 2019-11-14 |
| AU2017245395B2 (en) | 2019-05-16 |
| HK1256304A1 (en) | 2019-09-20 |
| KR20190006083A (ko) | 2019-01-16 |
| EP2683736A1 (en) | 2014-01-15 |
| JP2018027090A (ja) | 2018-02-22 |
| KR101938343B1 (ko) | 2019-01-14 |
| JP6557709B2 (ja) | 2019-08-07 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| CA2829606C (en) | Methods and reagents for creating monoclonal antibodies | |
| Nguyen et al. | Functional heavy-chain antibodies in Camelidae | |
| CN114126646B (zh) | 基于序列的高通量方法产生骆驼抗体以高分辨率覆盖广泛表位 | |
| EP3421592A1 (en) | Identification of polynucleotides associated with a sample | |
| CN102216328A (zh) | 骆驼科动物来源的抗原结合多肽 | |
| JP2018148915A (ja) | 抗ｖａｓａ抗体、ならびにその産生法および使用法 | |
| Chassagne et al. | A high-affinity macaque antibody Fab with human-like framework regions obtained from a small phage display immune library | |
| CN111788223A (zh) | 抗IL-5Rα的单克隆抗体 | |
| HK1193825A (en) | Methods and reagents for creating monoclonal antibodies | |
| HK1193825B (en) | Methods and reagents for creating monoclonal antibodies | |
| CN111201239A (zh) | 用于开发特异于表位翻译后修饰状态的抗体的方法和组合物 | |
| TW202229328A (zh) | 抗原特異性抗體之鑑定及產生 | |
| US20130109586A1 (en) | Generation of antibodies to an epitope of interest that contains a phosphomimetic amino acid | |
| WO2021258114A1 (en) | Process for direct readout of immunoglobulins | |
| US12331133B2 (en) | Therapeutic antibodies for treating lung cancer | |
| CN117015302A (zh) | 抗原特异性抗体的鉴定和产生 | |
| WO2025238133A1 (en) | Multispecific antibody with binding specificity for il-11 and il-17 | |
| Almagro et al. | Novel approaches in discovery and design of antibody-based therapeutics |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request |
Effective date: 20161212 |