IL286671B2 - Methods for the analysis of the promoter region and cells for their practice - Google Patents
Methods for the analysis of the promoter region and cells for their practiceInfo
- Publication number
- IL286671B2 IL286671B2 IL286671A IL28667121A IL286671B2 IL 286671 B2 IL286671 B2 IL 286671B2 IL 286671 A IL286671 A IL 286671A IL 28667121 A IL28667121 A IL 28667121A IL 286671 B2 IL286671 B2 IL 286671B2
- Authority
- IL
- Israel
- Prior art keywords
- cell
- activity
- promoter region
- carrier protein
- level
- Prior art date
Links
- 108700039691 Genetic Promoter Regions Proteins 0.000 title claims description 207
- 238000004458 analytical method Methods 0.000 title description 3
- 230000000694 effects Effects 0.000 claims description 186
- 238000000034 method Methods 0.000 claims description 155
- 239000003795 chemical substances by application Substances 0.000 claims description 124
- 102000040945 Transcription factor Human genes 0.000 claims description 120
- 108091023040 Transcription factor Proteins 0.000 claims description 120
- 230000037361 pathway Effects 0.000 claims description 111
- 102000004190 Enzymes Human genes 0.000 claims description 108
- 108090000790 Enzymes Proteins 0.000 claims description 108
- 102000014914 Carrier Proteins Human genes 0.000 claims description 106
- 108010078791 Carrier Proteins Proteins 0.000 claims description 106
- 230000002255 enzymatic effect Effects 0.000 claims description 104
- 102000039446 nucleic acids Human genes 0.000 claims description 85
- 108020004707 nucleic acids Proteins 0.000 claims description 85
- 150000007523 nucleic acids Chemical class 0.000 claims description 85
- 108090000623 proteins and genes Proteins 0.000 claims description 63
- 238000012360 testing method Methods 0.000 claims description 62
- 108091027981 Response element Proteins 0.000 claims description 57
- 230000004913 activation Effects 0.000 claims description 51
- 230000005754 cellular signaling Effects 0.000 claims description 51
- 235000018102 proteins Nutrition 0.000 claims description 49
- 102000004169 proteins and genes Human genes 0.000 claims description 49
- 230000012743 protein tagging Effects 0.000 claims description 42
- 238000012258 culturing Methods 0.000 claims description 29
- 230000004044 response Effects 0.000 claims description 28
- 239000000758 substrate Substances 0.000 claims description 26
- 230000015556 catabolic process Effects 0.000 claims description 13
- 238000006731 degradation reaction Methods 0.000 claims description 13
- 150000003384 small molecules Chemical group 0.000 claims description 13
- 230000002934 lysing effect Effects 0.000 claims description 12
- 241000607479 Yersinia pestis Species 0.000 claims description 11
- 150000001413 amino acids Chemical group 0.000 claims description 7
- 230000003213 activating effect Effects 0.000 claims description 6
- 239000013604 expression vector Substances 0.000 claims description 5
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims description 4
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 claims description 4
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 claims description 4
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 claims description 4
- 239000004473 Threonine Substances 0.000 claims description 4
- 235000013922 glutamic acid Nutrition 0.000 claims description 4
- 239000004220 glutamic acid Substances 0.000 claims description 4
- 230000007062 hydrolysis Effects 0.000 claims description 3
- 238000006460 hydrolysis reaction Methods 0.000 claims description 3
- 210000004027 cell Anatomy 0.000 description 392
- 238000003556 assay Methods 0.000 description 119
- 239000012634 fragment Substances 0.000 description 102
- 238000003174 enzyme fragment complementation Methods 0.000 description 55
- 230000014509 gene expression Effects 0.000 description 48
- 108010057466 NF-kappa B Proteins 0.000 description 46
- 102000003945 NF-kappa B Human genes 0.000 description 46
- 230000019491 signal transduction Effects 0.000 description 45
- 239000000556 agonist Substances 0.000 description 41
- 239000000203 mixture Substances 0.000 description 31
- 239000013612 plasmid Substances 0.000 description 30
- 230000000638 stimulation Effects 0.000 description 30
- 238000001514 detection method Methods 0.000 description 27
- 239000003446 ligand Substances 0.000 description 27
- 108010002350 Interleukin-2 Proteins 0.000 description 24
- 102000000588 Interleukin-2 Human genes 0.000 description 23
- 108010018525 NFATC Transcription Factors Proteins 0.000 description 23
- 102000002673 NFATC Transcription Factors Human genes 0.000 description 23
- 108700012920 TNF Proteins 0.000 description 23
- 230000002103 transcriptional effect Effects 0.000 description 23
- 125000003275 alpha amino acid group Chemical group 0.000 description 22
- 108090000765 processed proteins & peptides Proteins 0.000 description 20
- 238000011534 incubation Methods 0.000 description 19
- 231100000491 EC50 Toxicity 0.000 description 18
- 108060001084 Luciferase Proteins 0.000 description 17
- 108010029697 CD40 Ligand Proteins 0.000 description 16
- 102100032937 CD40 ligand Human genes 0.000 description 16
- 239000005089 Luciferase Substances 0.000 description 16
- 230000027455 binding Effects 0.000 description 16
- 102100040678 Programmed cell death protein 1 Human genes 0.000 description 15
- 101710089372 Programmed cell death protein 1 Proteins 0.000 description 15
- 108091008874 T cell receptors Proteins 0.000 description 15
- 102000016266 T-Cell Antigen Receptors Human genes 0.000 description 15
- PHEDXBVPIONUQT-RGYGYFBISA-N phorbol 13-acetate 12-myristate Chemical compound C([C@]1(O)C(=O)C(C)=C[C@H]1[C@@]1(O)[C@H](C)[C@H]2OC(=O)CCCCCCCCCCCCC)C(CO)=C[C@H]1[C@H]1[C@]2(OC(C)=O)C1(C)C PHEDXBVPIONUQT-RGYGYFBISA-N 0.000 description 15
- 102000005962 receptors Human genes 0.000 description 15
- 108020003175 receptors Proteins 0.000 description 15
- 239000000872 buffer Substances 0.000 description 14
- 210000000349 chromosome Anatomy 0.000 description 14
- 239000002773 nucleotide Substances 0.000 description 14
- 125000003729 nucleotide group Chemical group 0.000 description 14
- PHEDXBVPIONUQT-UHFFFAOYSA-N Cocarcinogen A1 Natural products CCCCCCCCCCCCCC(=O)OC1C(C)C2(O)C3C=C(C)C(=O)C3(O)CC(CO)=CC2C2C1(OC(C)=O)C2(C)C PHEDXBVPIONUQT-UHFFFAOYSA-N 0.000 description 13
- 108010017324 STAT3 Transcription Factor Proteins 0.000 description 13
- 102100024040 Signal transducer and activator of transcription 3 Human genes 0.000 description 13
- 239000003153 chemical reaction reagent Substances 0.000 description 12
- PGHMRUGBZOYCAA-UHFFFAOYSA-N ionomycin Natural products O1C(CC(O)C(C)C(O)C(C)C=CCC(C)CC(C)C(O)=CC(=O)C(C)CC(C)CC(CCC(O)=O)C)CCC1(C)C1OC(C)(C(C)O)CC1 PGHMRUGBZOYCAA-UHFFFAOYSA-N 0.000 description 12
- 102000004196 processed proteins & peptides Human genes 0.000 description 12
- 206010028980 Neoplasm Diseases 0.000 description 11
- 210000001744 T-lymphocyte Anatomy 0.000 description 11
- 230000015572 biosynthetic process Effects 0.000 description 11
- 230000005764 inhibitory process Effects 0.000 description 11
- PGHMRUGBZOYCAA-ADZNBVRBSA-N ionomycin Chemical compound O1[C@H](C[C@H](O)[C@H](C)[C@H](O)[C@H](C)/C=C/C[C@@H](C)C[C@@H](C)C(/O)=C/C(=O)[C@@H](C)C[C@@H](C)C[C@@H](CCC(O)=O)C)CC[C@@]1(C)[C@@H]1O[C@](C)([C@@H](C)O)CC1 PGHMRUGBZOYCAA-ADZNBVRBSA-N 0.000 description 11
- 239000012139 lysis buffer Substances 0.000 description 11
- 229920001184 polypeptide Polymers 0.000 description 11
- 239000003112 inhibitor Substances 0.000 description 10
- 230000035945 sensitivity Effects 0.000 description 10
- -1 P-lactamase Proteins 0.000 description 9
- 150000001875 compounds Chemical class 0.000 description 9
- 229940048921 humira Drugs 0.000 description 9
- 239000002609 medium Substances 0.000 description 9
- 238000007747 plating Methods 0.000 description 9
- 102000018697 Membrane Proteins Human genes 0.000 description 8
- 108010052285 Membrane Proteins Proteins 0.000 description 8
- 239000005557 antagonist Substances 0.000 description 8
- 201000011510 cancer Diseases 0.000 description 8
- 229940125425 inverse agonist Drugs 0.000 description 8
- 238000004020 luminiscence type Methods 0.000 description 8
- 238000010899 nucleation Methods 0.000 description 8
- 102000008096 B7-H1 Antigen Human genes 0.000 description 7
- 108010074708 B7-H1 Antigen Proteins 0.000 description 7
- 108091034117 Oligonucleotide Proteins 0.000 description 7
- 239000008186 active pharmaceutical agent Substances 0.000 description 7
- 235000001014 amino acid Nutrition 0.000 description 7
- 230000011664 signaling Effects 0.000 description 7
- 101150013553 CD40 gene Proteins 0.000 description 6
- 108010035563 Chloramphenicol O-acetyltransferase Proteins 0.000 description 6
- 108020004414 DNA Proteins 0.000 description 6
- 102000005744 Glycoside Hydrolases Human genes 0.000 description 6
- 108010031186 Glycoside Hydrolases Proteins 0.000 description 6
- 230000006037 cell lysis Effects 0.000 description 6
- 238000011198 co-culture assay Methods 0.000 description 6
- 230000007423 decrease Effects 0.000 description 6
- 230000000368 destabilizing effect Effects 0.000 description 6
- 239000007788 liquid Substances 0.000 description 6
- 210000001519 tissue Anatomy 0.000 description 6
- 230000004568 DNA-binding Effects 0.000 description 5
- 239000006144 Dulbecco’s modified Eagle's medium Substances 0.000 description 5
- 102000002464 Galactosidases Human genes 0.000 description 5
- 108010093031 Galactosidases Proteins 0.000 description 5
- 102100039556 Galectin-4 Human genes 0.000 description 5
- 101000608765 Homo sapiens Galectin-4 Proteins 0.000 description 5
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 5
- 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 5
- 239000012190 activator Substances 0.000 description 5
- 230000033228 biological regulation Effects 0.000 description 5
- 230000008859 change Effects 0.000 description 5
- 108091006047 fluorescent proteins Proteins 0.000 description 5
- 102000034287 fluorescent proteins Human genes 0.000 description 5
- 238000012494 forced degradation Methods 0.000 description 5
- 230000002401 inhibitory effect Effects 0.000 description 5
- 230000001404 mediated effect Effects 0.000 description 5
- 230000035772 mutation Effects 0.000 description 5
- 230000004063 proteosomal degradation Effects 0.000 description 5
- 108091028043 Nucleic acid sequence Proteins 0.000 description 4
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
- 108060008683 Tumor Necrosis Factor Receptor Proteins 0.000 description 4
- 238000004113 cell culture Methods 0.000 description 4
- 230000001413 cellular effect Effects 0.000 description 4
- 231100000673 dose–response relationship Toxicity 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 230000006870 function Effects 0.000 description 4
- 210000002865 immune cell Anatomy 0.000 description 4
- 230000002779 inactivation Effects 0.000 description 4
- 230000003993 interaction Effects 0.000 description 4
- 230000003834 intracellular effect Effects 0.000 description 4
- 230000000670 limiting effect Effects 0.000 description 4
- 239000000463 material Substances 0.000 description 4
- 210000003071 memory t lymphocyte Anatomy 0.000 description 4
- 239000002679 microRNA Substances 0.000 description 4
- 125000004573 morpholin-4-yl group Chemical group N1(CCOCC1)* 0.000 description 4
- CEICQMBWAQAIQX-UHFFFAOYSA-N n-[3,5-dichloro-4-[2-(trifluoromethoxy)phenyl]phenyl]-2-(4-ethylsulfonylphenyl)acetamide Chemical compound C1=CC(S(=O)(=O)CC)=CC=C1CC(=O)NC1=CC(Cl)=C(C=2C(=CC=CC=2)OC(F)(F)F)C(Cl)=C1 CEICQMBWAQAIQX-UHFFFAOYSA-N 0.000 description 4
- 230000004936 stimulating effect Effects 0.000 description 4
- 102000003298 tumor necrosis factor receptor Human genes 0.000 description 4
- 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
- 201000009030 Carcinoma Diseases 0.000 description 3
- 102000004127 Cytokines Human genes 0.000 description 3
- 108090000695 Cytokines Proteins 0.000 description 3
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
- 108700011259 MicroRNAs Proteins 0.000 description 3
- 239000006146 Roswell Park Memorial Institute medium Substances 0.000 description 3
- 206010039491 Sarcoma Diseases 0.000 description 3
- 229960002964 adalimumab Drugs 0.000 description 3
- 239000006143 cell culture medium Substances 0.000 description 3
- 230000009849 deactivation Effects 0.000 description 3
- 230000003247 decreasing effect Effects 0.000 description 3
- 239000003599 detergent Substances 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 230000003828 downregulation Effects 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 239000003623 enhancer Substances 0.000 description 3
- 238000003173 enzyme complementation Methods 0.000 description 3
- 230000001747 exhibiting effect Effects 0.000 description 3
- 238000001727 in vivo Methods 0.000 description 3
- 230000006698 induction Effects 0.000 description 3
- 239000007758 minimum essential medium Substances 0.000 description 3
- 239000002547 new drug Substances 0.000 description 3
- 230000003389 potentiating effect Effects 0.000 description 3
- 238000012216 screening Methods 0.000 description 3
- 230000008685 targeting Effects 0.000 description 3
- 238000011144 upstream manufacturing Methods 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- 108010011376 AMP-Activated Protein Kinases Proteins 0.000 description 2
- 102000014156 AMP-Activated Protein Kinases Human genes 0.000 description 2
- 102000001301 EGF receptor Human genes 0.000 description 2
- 108060006698 EGF receptor Proteins 0.000 description 2
- 108091008794 FGF receptors Proteins 0.000 description 2
- 102000044168 Fibroblast Growth Factor Receptor Human genes 0.000 description 2
- 102000004889 Interleukin-6 Human genes 0.000 description 2
- 108090001005 Interleukin-6 Proteins 0.000 description 2
- 241000254158 Lampyridae Species 0.000 description 2
- 108091054455 MAP kinase family Proteins 0.000 description 2
- 102000043136 MAP kinase family Human genes 0.000 description 2
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 2
- YNLCVAQJIKOXER-UHFFFAOYSA-N N-[tris(hydroxymethyl)methyl]-3-aminopropanesulfonic acid Chemical compound OCC(CO)(CO)NCCCS(O)(=O)=O YNLCVAQJIKOXER-UHFFFAOYSA-N 0.000 description 2
- 108091007494 Nucleic acid- binding domains Proteins 0.000 description 2
- 108091034057 RNA (poly(A)) Proteins 0.000 description 2
- 108020004459 Small interfering RNA Proteins 0.000 description 2
- 238000010459 TALEN Methods 0.000 description 2
- 108700026226 TATA Box Proteins 0.000 description 2
- 108010065917 TOR Serine-Threonine Kinases Proteins 0.000 description 2
- 102000013530 TOR Serine-Threonine Kinases Human genes 0.000 description 2
- 102000002689 Toll-like receptor Human genes 0.000 description 2
- 108020000411 Toll-like receptor Proteins 0.000 description 2
- 108010043645 Transcription Activator-Like Effector Nucleases Proteins 0.000 description 2
- 108010073929 Vascular Endothelial Growth Factor A Proteins 0.000 description 2
- 102000005789 Vascular Endothelial Growth Factors Human genes 0.000 description 2
- 108010019530 Vascular Endothelial Growth Factors Proteins 0.000 description 2
- PVNJLUVGTFULAE-UHFFFAOYSA-N [NH4+].[Cl-].[K] Chemical compound [NH4+].[Cl-].[K] PVNJLUVGTFULAE-UHFFFAOYSA-N 0.000 description 2
- 230000002159 abnormal effect Effects 0.000 description 2
- 239000000654 additive Substances 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 238000003149 assay kit Methods 0.000 description 2
- 230000003115 biocidal effect Effects 0.000 description 2
- 238000000423 cell based assay Methods 0.000 description 2
- 210000000170 cell membrane Anatomy 0.000 description 2
- 230000004640 cellular pathway Effects 0.000 description 2
- 239000013611 chromosomal DNA Substances 0.000 description 2
- 230000001419 dependent effect Effects 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 229940000406 drug candidate Drugs 0.000 description 2
- 238000004520 electroporation Methods 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 238000000684 flow cytometry Methods 0.000 description 2
- 238000001943 fluorescence-activated cell sorting Methods 0.000 description 2
- 230000004927 fusion Effects 0.000 description 2
- 230000012010 growth Effects 0.000 description 2
- 230000008611 intercellular interaction Effects 0.000 description 2
- 108020004999 messenger RNA Proteins 0.000 description 2
- 108091070501 miRNA Proteins 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 239000000178 monomer Substances 0.000 description 2
- 229930014626 natural product Natural products 0.000 description 2
- 210000003463 organelle Anatomy 0.000 description 2
- 238000004806 packaging method and process Methods 0.000 description 2
- 239000004031 partial agonist Substances 0.000 description 2
- 239000000137 peptide hydrolase inhibitor Substances 0.000 description 2
- 239000002644 phorbol ester Substances 0.000 description 2
- 230000029279 positive regulation of transcription, DNA-dependent Effects 0.000 description 2
- 238000001556 precipitation Methods 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 150000003839 salts Chemical class 0.000 description 2
- 230000028327 secretion Effects 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 238000006467 substitution reaction Methods 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
- 230000003827 upregulation Effects 0.000 description 2
- WQZGKKKJIJFFOK-SVZMEOIVSA-N (+)-Galactose Chemical compound OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@H]1O WQZGKKKJIJFFOK-SVZMEOIVSA-N 0.000 description 1
- SXGZJKUKBWWHRA-UHFFFAOYSA-N 2-(N-morpholiniumyl)ethanesulfonate Chemical compound [O-]S(=O)(=O)CC[NH+]1CCOCC1 SXGZJKUKBWWHRA-UHFFFAOYSA-N 0.000 description 1
- 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 1
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- OPIFSICVWOWJMJ-AEOCFKNESA-N 5-bromo-4-chloro-3-indolyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-AEOCFKNESA-N 0.000 description 1
- 241000023308 Acca Species 0.000 description 1
- 230000007730 Akt signaling Effects 0.000 description 1
- 102000002260 Alkaline Phosphatase Human genes 0.000 description 1
- 108020004774 Alkaline Phosphatase Proteins 0.000 description 1
- 102100027207 CD27 antigen Human genes 0.000 description 1
- 102000017420 CD3 protein, epsilon/gamma/delta subunit Human genes 0.000 description 1
- 108050005493 CD3 protein, epsilon/gamma/delta subunit Proteins 0.000 description 1
- 210000001266 CD8-positive T-lymphocyte Anatomy 0.000 description 1
- 238000010356 CRISPR-Cas9 genome editing Methods 0.000 description 1
- 102000000844 Cell Surface Receptors Human genes 0.000 description 1
- 108010001857 Cell Surface Receptors Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 230000022963 DNA damage response, signal transduction by p53 class mediator Effects 0.000 description 1
- YQYJSBFKSSDGFO-UHFFFAOYSA-N Epihygromycin Natural products OC1C(O)C(C(=O)C)OC1OC(C(=C1)O)=CC=C1C=C(C)C(=O)NC1C(O)C(O)C2OCOC2C1O YQYJSBFKSSDGFO-UHFFFAOYSA-N 0.000 description 1
- 102000009465 Growth Factor Receptors Human genes 0.000 description 1
- 108010009202 Growth Factor Receptors Proteins 0.000 description 1
- 101000914511 Homo sapiens CD27 antigen Proteins 0.000 description 1
- 101000946889 Homo sapiens Monocyte differentiation antigen CD14 Proteins 0.000 description 1
- 101000914514 Homo sapiens T-cell-specific surface glycoprotein CD28 Proteins 0.000 description 1
- 101150083678 IL2 gene Proteins 0.000 description 1
- 206010061598 Immunodeficiency Diseases 0.000 description 1
- 102000008394 Immunoglobulin Fragments Human genes 0.000 description 1
- 108010021625 Immunoglobulin Fragments Proteins 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 102000010781 Interleukin-6 Receptors Human genes 0.000 description 1
- 108010038501 Interleukin-6 Receptors Proteins 0.000 description 1
- 239000007993 MOPS buffer Substances 0.000 description 1
- 241001529936 Murinae Species 0.000 description 1
- 230000005913 Notch signaling pathway Effects 0.000 description 1
- 102000017954 Nuclear factor of activated T cells (NFAT) Human genes 0.000 description 1
- 108050007058 Nuclear factor of activated T cells (NFAT) Proteins 0.000 description 1
- 229940122426 Nuclease inhibitor Drugs 0.000 description 1
- 229940124060 PD-1 antagonist Drugs 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 229920001213 Polysorbate 20 Polymers 0.000 description 1
- 229940124158 Protease/peptidase inhibitor Drugs 0.000 description 1
- 102000004245 Proteasome Endopeptidase Complex Human genes 0.000 description 1
- 108090000708 Proteasome Endopeptidase Complex Proteins 0.000 description 1
- 102000001253 Protein Kinase Human genes 0.000 description 1
- 108010076504 Protein Sorting Signals Proteins 0.000 description 1
- 108091030071 RNAI Proteins 0.000 description 1
- 108091028664 Ribonucleotide Proteins 0.000 description 1
- 241000283984 Rodentia Species 0.000 description 1
- 230000006044 T cell activation Effects 0.000 description 1
- 102100027213 T-cell-specific surface glycoprotein CD28 Human genes 0.000 description 1
- 108010009583 Transforming Growth Factors Proteins 0.000 description 1
- 102000009618 Transforming Growth Factors Human genes 0.000 description 1
- 239000007983 Tris buffer Substances 0.000 description 1
- 102100040245 Tumor necrosis factor receptor superfamily member 5 Human genes 0.000 description 1
- 102000044159 Ubiquitin Human genes 0.000 description 1
- 108090000848 Ubiquitin Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 230000004156 Wnt signaling pathway Effects 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 230000009824 affinity maturation Effects 0.000 description 1
- 210000002203 alpha-beta t lymphocyte Anatomy 0.000 description 1
- 125000000539 amino acid group Chemical class 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
- 239000003708 ampul Substances 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 210000003651 basophil Anatomy 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000004071 biological effect Effects 0.000 description 1
- 230000031018 biological processes and functions Effects 0.000 description 1
- 238000001574 biopsy Methods 0.000 description 1
- 239000008366 buffered solution Substances 0.000 description 1
- 239000006172 buffering agent Substances 0.000 description 1
- 235000019846 buffering salt Nutrition 0.000 description 1
- 244000309464 bull Species 0.000 description 1
- 125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 210000002390 cell membrane structure Anatomy 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 239000002738 chelating agent Substances 0.000 description 1
- 239000013000 chemical inhibitor Substances 0.000 description 1
- 239000003593 chromogenic compound Substances 0.000 description 1
- 238000003501 co-culture Methods 0.000 description 1
- 230000004186 co-expression Effects 0.000 description 1
- 230000000536 complexating effect Effects 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 239000003431 cross linking reagent Substances 0.000 description 1
- 230000009089 cytolysis Effects 0.000 description 1
- 238000004163 cytometry Methods 0.000 description 1
- 108091007930 cytoplasmic receptors Proteins 0.000 description 1
- 210000000172 cytosol Anatomy 0.000 description 1
- 210000001151 cytotoxic T lymphocyte Anatomy 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- 210000004443 dendritic cell Anatomy 0.000 description 1
- 239000005547 deoxyribonucleotide Substances 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 229940042399 direct acting antivirals protease inhibitors Drugs 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 1
- 230000007783 downstream signaling Effects 0.000 description 1
- 238000007876 drug discovery Methods 0.000 description 1
- 239000012636 effector Substances 0.000 description 1
- 210000003162 effector t lymphocyte Anatomy 0.000 description 1
- 210000002889 endothelial cell Anatomy 0.000 description 1
- 210000003979 eosinophil Anatomy 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 229940011871 estrogen Drugs 0.000 description 1
- 239000000262 estrogen Substances 0.000 description 1
- 238000002474 experimental method Methods 0.000 description 1
- GNBHRKFJIUUOQI-UHFFFAOYSA-N fluorescein Chemical compound O1C(=O)C2=CC=CC=C2C21C1=CC=C(O)C=C1OC1=CC(O)=CC=C21 GNBHRKFJIUUOQI-UHFFFAOYSA-N 0.000 description 1
- 239000007850 fluorescent dye Substances 0.000 description 1
- 210000004475 gamma-delta t lymphocyte Anatomy 0.000 description 1
- 210000003976 gap junction Anatomy 0.000 description 1
- 230000009368 gene silencing by RNA Effects 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 238000010362 genome editing Methods 0.000 description 1
- 230000009036 growth inhibition Effects 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 210000002443 helper t lymphocyte Anatomy 0.000 description 1
- 210000003630 histaminocyte Anatomy 0.000 description 1
- 230000001744 histochemical effect Effects 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 102000046699 human CD14 Human genes 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 230000006882 induction of apoptosis Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000004155 insulin signaling pathway Effects 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 229940079322 interferon Drugs 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- 238000002372 labelling Methods 0.000 description 1
- 238000011068 loading method Methods 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 238000003670 luciferase enzyme activity assay Methods 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 235000019341 magnesium sulphate Nutrition 0.000 description 1
- 230000003211 malignant effect Effects 0.000 description 1
- 210000004962 mammalian cell Anatomy 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 210000005033 mesothelial cell Anatomy 0.000 description 1
- 206010061289 metastatic neoplasm Diseases 0.000 description 1
- 238000000520 microinjection Methods 0.000 description 1
- 230000003278 mimic effect Effects 0.000 description 1
- 230000002438 mitochondrial effect Effects 0.000 description 1
- 210000001616 monocyte Anatomy 0.000 description 1
- UPSFMJHZUCSEHU-JYGUBCOQSA-N n-[(2s,3r,4r,5s,6r)-2-[(2r,3s,4r,5r,6s)-5-acetamido-4-hydroxy-2-(hydroxymethyl)-6-(4-methyl-2-oxochromen-7-yl)oxyoxan-3-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide Chemical compound CC(=O)N[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@H]1[C@H](O)[C@@H](NC(C)=O)[C@H](OC=2C=C3OC(=O)C=C(C)C3=CC=2)O[C@@H]1CO UPSFMJHZUCSEHU-JYGUBCOQSA-N 0.000 description 1
- 230000001613 neoplastic effect Effects 0.000 description 1
- 210000000440 neutrophil Anatomy 0.000 description 1
- 229940124276 oligodeoxyribonucleotide Drugs 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 201000008968 osteosarcoma Diseases 0.000 description 1
- 210000003819 peripheral blood mononuclear cell Anatomy 0.000 description 1
- 108040007629 peroxidase activity proteins Proteins 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 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
- 229920001223 polyethylene glycol Polymers 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 102000040430 polynucleotide Human genes 0.000 description 1
- 108091033319 polynucleotide Proteins 0.000 description 1
- 239000002157 polynucleotide Substances 0.000 description 1
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- KCXFHTAICRTXLI-UHFFFAOYSA-N propane-1-sulfonic acid Chemical compound CCCS(O)(=O)=O KCXFHTAICRTXLI-UHFFFAOYSA-N 0.000 description 1
- 108060006633 protein kinase Proteins 0.000 description 1
- 108091006084 receptor activators Proteins 0.000 description 1
- 230000002829 reductive effect Effects 0.000 description 1
- 210000003289 regulatory T cell Anatomy 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- HSSLDCABUXLXKM-UHFFFAOYSA-N resorufin Chemical compound C1=CC(=O)C=C2OC3=CC(O)=CC=C3N=C21 HSSLDCABUXLXKM-UHFFFAOYSA-N 0.000 description 1
- 230000002441 reversible effect Effects 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 125000002652 ribonucleotide group Chemical group 0.000 description 1
- 238000007423 screening assay Methods 0.000 description 1
- KQFAFFYKLIBKDE-UHFFFAOYSA-M sodium;ethanesulfonate Chemical compound [Na+].CCS([O-])(=O)=O KQFAFFYKLIBKDE-UHFFFAOYSA-M 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 238000010186 staining Methods 0.000 description 1
- 230000002195 synergetic effect Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 210000004881 tumor cell Anatomy 0.000 description 1
- 230000005748 tumor development Effects 0.000 description 1
- 230000004614 tumor growth Effects 0.000 description 1
- 230000007306 turnover Effects 0.000 description 1
- 238000010798 ubiquitination Methods 0.000 description 1
- 239000013603 viral vector Substances 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/54—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving glucose or galactose
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/34—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving hydrolase
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/53—Immunoassay; Biospecific binding assay; Materials therefor
- G01N33/536—Immunoassay; Biospecific binding assay; Materials therefor with immune complex formed in liquid phase
- G01N33/542—Immunoassay; Biospecific binding assay; Materials therefor with immune complex formed in liquid phase with steric inhibition or signal modification, e.g. fluorescent quenching
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y302/00—Hydrolases acting on glycosyl compounds, i.e. glycosylases (3.2)
- C12Y302/01—Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds (3.2.1)
- C12Y302/01023—Beta-galactosidase (3.2.1.23), i.e. exo-(1-->4)-beta-D-galactanase
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
- G01N2333/924—Hydrolases (3) acting on glycosyl compounds (3.2)
- G01N2333/938—Hydrolases (3) acting on glycosyl compounds (3.2) acting on beta-galactose-glycoside bonds, e.g. beta-galactosidase
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Microbiology (AREA)
- Biomedical Technology (AREA)
- Physics & Mathematics (AREA)
- Biophysics (AREA)
- Immunology (AREA)
- Analytical Chemistry (AREA)
- Plant Pathology (AREA)
- Emergency Medicine (AREA)
- Urology & Nephrology (AREA)
- Hematology (AREA)
- Food Science & Technology (AREA)
- Cell Biology (AREA)
- Medicinal Chemistry (AREA)
- General Physics & Mathematics (AREA)
- Pathology (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Apparatus Associated With Microorganisms And Enzymes (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201962825559P | 2019-03-28 | 2019-03-28 | |
| PCT/US2020/025055 WO2020198525A1 (en) | 2019-03-28 | 2020-03-26 | Promoter region analysis methods and cells for practicing same |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| IL286671A IL286671A (en) | 2021-10-31 |
| IL286671B1 IL286671B1 (en) | 2023-09-01 |
| IL286671B2 true IL286671B2 (en) | 2024-01-01 |
Family
ID=72607352
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IL286671A IL286671B2 (en) | 2019-03-28 | 2020-03-26 | Methods for the analysis of the promoter region and cells for their practice |
Country Status (9)
| Country | Link |
|---|---|
| US (1) | US20200308591A1 (https=) |
| EP (1) | EP3947714A4 (https=) |
| JP (1) | JP2022528270A (https=) |
| KR (1) | KR20210138766A (https=) |
| CN (1) | CN113785072A (https=) |
| AU (1) | AU2020248020A1 (https=) |
| CA (1) | CA3116068A1 (https=) |
| IL (1) | IL286671B2 (https=) |
| WO (1) | WO2020198525A1 (https=) |
Families Citing this family (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| TW202328452A (zh) * | 2021-09-07 | 2023-07-16 | 俄羅斯聯邦商拜奧卡德聯合股份公司 | 誘導型啟動子、基於其的載體和宿主細胞 |
| CN115786340B (zh) * | 2022-11-04 | 2023-12-05 | 江南大学 | 一种提高leaderless启动子活性的方法及其应用 |
Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1999002719A1 (en) * | 1997-07-11 | 1999-01-21 | The University Of British Columbia | Complementation trap |
Family Cites Families (11)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0338045B1 (en) * | 1987-09-21 | 1994-08-24 | Microgenics Corporation | Solid-phase non-separation enzyme assay |
| US5223393A (en) * | 1990-06-12 | 1993-06-29 | Microgenics Corporation | Detection of analytes having binding sites for at least two binding moieties |
| US7062219B2 (en) * | 1997-01-31 | 2006-06-13 | Odyssey Thera Inc. | Protein fragment complementation assays for high-throughput and high-content screening |
| AU2217800A (en) * | 1998-12-24 | 2000-07-31 | Small Molecule Therapeutics, Inc. | Methods and compositions for identifying protease modulators |
| WO2003065004A2 (en) * | 2002-01-29 | 2003-08-07 | Discoverx, Inc. | Enzyme activation protease assay |
| JP4796059B2 (ja) * | 2004-06-30 | 2011-10-19 | ディスカヴァーエックス コーポレイション | 細胞内修飾の分析 |
| JP5303448B2 (ja) * | 2006-03-13 | 2013-10-02 | ボード オブ トラスティーズ オブ ザ レランド スタンフォード ジュニア ユニバーシティ | 親和性が減少した酵素の相補性レポーター系を用いた分子相互作用の検出 |
| US8865421B2 (en) * | 2008-07-02 | 2014-10-21 | Discoverx Corporation | Assays for nuclear hormone receptor binding |
| WO2013119579A1 (en) * | 2012-02-06 | 2013-08-15 | Discoveryx Corporation | Detection of intracellular binding events by measuring protein abundance |
| JP2016523088A (ja) * | 2013-06-26 | 2016-08-08 | フィロジカ リミテッドＰｈｙｌｏｇｉｃａ Ｌｉｍｉｔｅｄ | ペプチドの細胞輸送をモニタリングする方法 |
| EP3183580B1 (en) * | 2014-08-21 | 2025-03-26 | Eurofins DiscoverX Corporation | Homogenous thermal shift ligand binding assay |
-
2020
- 2020-03-26 CN CN202080025188.9A patent/CN113785072A/zh active Pending
- 2020-03-26 US US16/831,586 patent/US20200308591A1/en not_active Abandoned
- 2020-03-26 AU AU2020248020A patent/AU2020248020A1/en not_active Abandoned
- 2020-03-26 EP EP20778747.4A patent/EP3947714A4/en active Pending
- 2020-03-26 WO PCT/US2020/025055 patent/WO2020198525A1/en not_active Ceased
- 2020-03-26 CA CA3116068A patent/CA3116068A1/en active Pending
- 2020-03-26 KR KR1020217034926A patent/KR20210138766A/ko not_active Ceased
- 2020-03-26 JP JP2021560297A patent/JP2022528270A/ja active Pending
- 2020-03-26 IL IL286671A patent/IL286671B2/en unknown
Patent Citations (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1999002719A1 (en) * | 1997-07-11 | 1999-01-21 | The University Of British Columbia | Complementation trap |
Non-Patent Citations (2)
| Title |
|---|
| ANONYMOUS,, PROMOTER ACTIVITY REPORTER (LACZ-ALPHA AND RFP) (6VDC5L0) | DOULIX, 24 July 2018 (2018-07-24) * |
| IZUMO, MARIKO, ET AL., QUANTITATIVE ANALYSES OF CIRCADIAN GENE EXPRESSION IN MAMMALIAN CELL CULTURES., 13 October 2006 (2006-10-13) * |
Also Published As
| Publication number | Publication date |
|---|---|
| WO2020198525A1 (en) | 2020-10-01 |
| KR20210138766A (ko) | 2021-11-19 |
| US20200308591A1 (en) | 2020-10-01 |
| JP2022528270A (ja) | 2022-06-09 |
| IL286671A (en) | 2021-10-31 |
| AU2020248020A1 (en) | 2021-10-28 |
| EP3947714A4 (en) | 2022-12-14 |
| CN113785072A (zh) | 2021-12-10 |
| IL286671B1 (en) | 2023-09-01 |
| EP3947714A1 (en) | 2022-02-09 |
| CA3116068A1 (en) | 2020-10-01 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| Yogev et al. | Fumarase: a paradigm of dual targeting and dual localized functions | |
| Powell et al. | TRMT2B is responsible for both tRNA and rRNA m5U-methylation in human mitochondria | |
| Boyle et al. | ROCK-mediated selective activation of PERK signalling causes fibroblast reprogramming and tumour progression through a CRELD2-dependent mechanism | |
| Bryans et al. | Absence of DNA ligase IV protein in XR-1 cells: evidence for stabilization by XRCC4 | |
| Kong et al. | α4 is an essential regulator of PP2A phosphatase activity | |
| Lesnik et al. | Localized translation near the mitochondrial outer membrane: An update | |
| Shi et al. | tRNA synthetase counteracts c-Myc to develop functional vasculature | |
| Michlewski et al. | The splicing factor SF2/ASF regulates translation initiation by enhancing phosphorylation of 4E-BP1 | |
| US8426194B2 (en) | Methods and agents for screening for compounds capable of modulating VEGF expression | |
| Shiwarski et al. | PI3K class II α regulates δ-opioid receptor export from the trans-Golgi network | |
| Fritsch et al. | Cell fate decisions regulated by K63 ubiquitination of tumor necrosis factor receptor 1 | |
| Goodchild et al. | Access of torsinA to the inner nuclear membrane is activity dependent and regulated in the endoplasmic reticulum | |
| Wu et al. | Nuclear localization signal deletion mutants of lamin A and progerin reveal insights into lamin A processing and emerin targeting | |
| Kim et al. | Deletion of BRCA2 exon 27 causes defects in response to both stalled and collapsed replication forks | |
| Heyza et al. | Systematic analysis of the molecular and biophysical properties of key DNA damage response factors | |
| IL286671B2 (en) | Methods for the analysis of the promoter region and cells for their practice | |
| Stelter et al. | Monitoring spatiotemporal biogenesis of macromolecular assemblies by pulse-chase epitope labeling | |
| Griffiths et al. | Bit‐1 is an essential regulator of myogenic differentiation | |
| Bate et al. | Intrinsic differences in the mechanisms of Tie2 binding to angiopoietins exploited by directed evolution to create an Ang2-selective ligand trap | |
| Lee et al. | Ring finger protein 126 (RNF126) suppresses ionizing radiation–induced p53-binding protein 1 (53BP1) focus formation | |
| Ma et al. | The nuclear localization of ACLY guards early embryo development through recruiting P300 and HAT1 to promote histone acetylation and transcription | |
| Liao et al. | Mis-localization of Arp2 mRNA impairs persistence of directional cell migration | |
| Gonzaga-Saavedra et al. | Nucleation-dependent propagation of Polycomb modifications emerges during the Drosophila maternal to zygotic transition | |
| EP2810064B1 (en) | Cell based sensor | |
| Bowman et al. | Posttranslational modification of HOIP blocks toll-like receptor 4-mediated linear-ubiquitin-chain formation |