IL84852A - Molecular cloning and expression of human IL-3 - Google Patents
Molecular cloning and expression of human IL-3Info
- Publication number
- IL84852A IL84852A IL8485287A IL8485287A IL84852A IL 84852 A IL84852 A IL 84852A IL 8485287 A IL8485287 A IL 8485287A IL 8485287 A IL8485287 A IL 8485287A IL 84852 A IL84852 A IL 84852A
- Authority
- IL
- Israel
- Prior art keywords
- human
- pgb
- protein
- obtainable
- dna
- Prior art date
Links
- 101001033279 Homo sapiens Interleukin-3 Proteins 0.000 title claims abstract description 103
- 230000014509 gene expression Effects 0.000 title claims abstract description 45
- 102000055276 human IL3 Human genes 0.000 title claims description 71
- 238000010369 molecular cloning Methods 0.000 title description 2
- 108090000623 proteins and genes Proteins 0.000 claims abstract description 134
- 102000004169 proteins and genes Human genes 0.000 claims abstract description 114
- 239000002299 complementary DNA Substances 0.000 claims abstract description 73
- 108010002386 Interleukin-3 Proteins 0.000 claims description 49
- 238000000034 method Methods 0.000 claims description 48
- 108020004414 DNA Proteins 0.000 claims description 37
- 230000000694 effects Effects 0.000 claims description 29
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 22
- 239000013604 expression vector Substances 0.000 claims description 22
- 239000002773 nucleotide Substances 0.000 claims description 22
- 125000003729 nucleotide group Chemical group 0.000 claims description 22
- 150000001413 amino acids Chemical class 0.000 claims description 21
- 238000004519 manufacturing process Methods 0.000 claims description 20
- 238000002360 preparation method Methods 0.000 claims description 17
- 241000894006 Bacteria Species 0.000 claims description 14
- 240000004808 Saccharomyces cerevisiae Species 0.000 claims description 14
- 102000004139 alpha-Amylases Human genes 0.000 claims description 10
- 108090000637 alpha-Amylases Proteins 0.000 claims description 10
- 229940024171 alpha-amylase Drugs 0.000 claims description 10
- 241000193830 Bacillus <bacterium> Species 0.000 claims description 8
- 241000894007 species Species 0.000 claims description 8
- 238000013518 transcription Methods 0.000 claims description 8
- 230000035897 transcription Effects 0.000 claims description 8
- 230000001105 regulatory effect Effects 0.000 claims description 6
- 241000233866 Fungi Species 0.000 claims description 5
- 238000006243 chemical reaction Methods 0.000 claims description 5
- 239000000523 sample Substances 0.000 claims description 5
- 108091092195 Intron Proteins 0.000 claims description 4
- 241000235070 Saccharomyces Species 0.000 claims description 4
- 239000000463 material Substances 0.000 claims description 4
- 108091036066 Three prime untranslated region Proteins 0.000 claims description 3
- 238000012216 screening Methods 0.000 claims description 3
- 230000002103 transcriptional effect Effects 0.000 claims description 3
- 230000000977 initiatory effect Effects 0.000 claims description 2
- 235000015097 nutrients Nutrition 0.000 claims description 2
- 241000251539 Vertebrata <Metazoa> Species 0.000 claims 1
- IBIKHMZPHNKTHM-RDTXWAMCSA-N merck compound 25 Chemical compound C1C[C@@H](C(O)=O)[C@H](O)CN1C(C1=C(F)C=CC=C11)=NN1C(=O)C1=C(Cl)C=CC=C1C1CC1 IBIKHMZPHNKTHM-RDTXWAMCSA-N 0.000 claims 1
- 238000003259 recombinant expression Methods 0.000 claims 1
- 230000001225 therapeutic effect Effects 0.000 abstract description 9
- 101100069853 Caenorhabditis elegans hil-3 gene Proteins 0.000 abstract description 4
- 239000012535 impurity Substances 0.000 abstract description 2
- 210000005105 peripheral blood lymphocyte Anatomy 0.000 abstract description 2
- 235000018102 proteins Nutrition 0.000 description 100
- 210000004027 cell Anatomy 0.000 description 67
- 239000013612 plasmid Substances 0.000 description 67
- 102000000646 Interleukin-3 Human genes 0.000 description 46
- 239000012634 fragment Substances 0.000 description 39
- 208000031261 Acute myeloid leukaemia Diseases 0.000 description 27
- 208000033776 Myeloid Acute Leukemia Diseases 0.000 description 27
- 238000010276 construction Methods 0.000 description 27
- 108010076504 Protein Sorting Signals Proteins 0.000 description 26
- 241000588724 Escherichia coli Species 0.000 description 25
- 102000037865 fusion proteins Human genes 0.000 description 24
- 108020001507 fusion proteins Proteins 0.000 description 24
- 235000001014 amino acid Nutrition 0.000 description 21
- 239000003636 conditioned culture medium Substances 0.000 description 21
- 108091026890 Coding region Proteins 0.000 description 17
- 238000003556 assay Methods 0.000 description 16
- 239000013598 vector Substances 0.000 description 15
- 101150066555 lacZ gene Proteins 0.000 description 14
- 238000004458 analytical method Methods 0.000 description 13
- 230000004071 biological effect Effects 0.000 description 13
- 239000002609 medium Substances 0.000 description 13
- 108010059881 Lactase Proteins 0.000 description 12
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 12
- 108010005774 beta-Galactosidase Proteins 0.000 description 12
- 102100026189 Beta-galactosidase Human genes 0.000 description 11
- 238000010367 cloning Methods 0.000 description 11
- 230000002607 hemopoietic effect Effects 0.000 description 11
- 238000000338 in vitro Methods 0.000 description 11
- 229940116108 lactase Drugs 0.000 description 11
- 239000000047 product Substances 0.000 description 11
- 230000035755 proliferation Effects 0.000 description 11
- 241001138401 Kluyveromyces lactis Species 0.000 description 10
- 241001529936 Murinae Species 0.000 description 10
- 230000001580 bacterial effect Effects 0.000 description 10
- 239000008188 pellet Substances 0.000 description 10
- 125000003275 alpha amino acid group Chemical group 0.000 description 9
- 210000000130 stem cell Anatomy 0.000 description 9
- 230000000638 stimulation Effects 0.000 description 9
- 239000006228 supernatant Substances 0.000 description 9
- 235000014469 Bacillus subtilis Nutrition 0.000 description 8
- 108091034117 Oligonucleotide Proteins 0.000 description 8
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 8
- IXKSXJFAGXLQOQ-XISFHERQSA-N WHWLQLKPGQPMY Chemical group C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 IXKSXJFAGXLQOQ-XISFHERQSA-N 0.000 description 8
- 239000000499 gel Substances 0.000 description 8
- 241000194108 Bacillus licheniformis Species 0.000 description 7
- 230000005757 colony formation Effects 0.000 description 7
- 108020004999 messenger RNA Proteins 0.000 description 7
- 239000000203 mixture Substances 0.000 description 7
- 230000035772 mutation Effects 0.000 description 7
- 229920002401 polyacrylamide Polymers 0.000 description 7
- 230000009466 transformation Effects 0.000 description 7
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical compound O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 6
- 238000001516 cell proliferation assay Methods 0.000 description 6
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 6
- 230000029087 digestion Effects 0.000 description 6
- 230000004927 fusion Effects 0.000 description 6
- 210000003714 granulocyte Anatomy 0.000 description 6
- 239000003102 growth factor Substances 0.000 description 6
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 6
- 230000006820 DNA synthesis Effects 0.000 description 5
- 241000699666 Mus <mouse, genus> Species 0.000 description 5
- 241000283973 Oryctolagus cuniculus Species 0.000 description 5
- 108091081024 Start codon Proteins 0.000 description 5
- 125000003295 alanine group Chemical group N[C@@H](C)C(=O)* 0.000 description 5
- 230000015572 biosynthetic process Effects 0.000 description 5
- AIYUHDOJVYHVIT-UHFFFAOYSA-M caesium chloride Chemical compound [Cl-].[Cs+] AIYUHDOJVYHVIT-UHFFFAOYSA-M 0.000 description 5
- 238000001514 detection method Methods 0.000 description 5
- 239000013613 expression plasmid Substances 0.000 description 5
- 230000013595 glycosylation Effects 0.000 description 5
- 238000006206 glycosylation reaction Methods 0.000 description 5
- 238000009396 hybridization Methods 0.000 description 5
- 238000002955 isolation Methods 0.000 description 5
- 210000000265 leukocyte Anatomy 0.000 description 5
- 210000002540 macrophage Anatomy 0.000 description 5
- 239000002243 precursor Substances 0.000 description 5
- 230000010076 replication Effects 0.000 description 5
- 230000004044 response Effects 0.000 description 5
- 230000014616 translation Effects 0.000 description 5
- 238000001262 western blot Methods 0.000 description 5
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 4
- 108700039691 Genetic Promoter Regions Proteins 0.000 description 4
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 4
- 108010017213 Granulocyte-Macrophage Colony-Stimulating Factor Proteins 0.000 description 4
- 102100039620 Granulocyte-macrophage colony-stimulating factor Human genes 0.000 description 4
- 108091092724 Noncoding DNA Proteins 0.000 description 4
- 108700026244 Open Reading Frames Proteins 0.000 description 4
- 210000001744 T-lymphocyte Anatomy 0.000 description 4
- 125000000539 amino acid group Chemical group 0.000 description 4
- 210000001185 bone marrow Anatomy 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 239000004202 carbamide Substances 0.000 description 4
- 230000001419 dependent effect Effects 0.000 description 4
- 230000004069 differentiation Effects 0.000 description 4
- 230000000925 erythroid effect Effects 0.000 description 4
- 238000002474 experimental method Methods 0.000 description 4
- 230000012010 growth Effects 0.000 description 4
- 239000001963 growth medium Substances 0.000 description 4
- 230000001939 inductive effect Effects 0.000 description 4
- 239000006166 lysate Substances 0.000 description 4
- YBYRMVIVWMBXKQ-UHFFFAOYSA-N phenylmethanesulfonyl fluoride Chemical compound FS(=O)(=O)CC1=CC=CC=C1 YBYRMVIVWMBXKQ-UHFFFAOYSA-N 0.000 description 4
- 238000012545 processing Methods 0.000 description 4
- 230000028327 secretion Effects 0.000 description 4
- 239000000243 solution Substances 0.000 description 4
- 229940104230 thymidine Drugs 0.000 description 4
- 210000001519 tissue Anatomy 0.000 description 4
- 238000013519 translation Methods 0.000 description 4
- BHNQPLPANNDEGL-UHFFFAOYSA-N 2-(4-octylphenoxy)ethanol Chemical compound CCCCCCCCC1=CC=C(OCCO)C=C1 BHNQPLPANNDEGL-UHFFFAOYSA-N 0.000 description 3
- 102000007469 Actins Human genes 0.000 description 3
- 108010085238 Actins Proteins 0.000 description 3
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 3
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 3
- DWRXFEITVBNRMK-UHFFFAOYSA-N Beta-D-1-Arabinofuranosylthymine Natural products O=C1NC(=O)C(C)=CN1C1C(O)C(O)C(CO)O1 DWRXFEITVBNRMK-UHFFFAOYSA-N 0.000 description 3
- 241000388186 Deltapapillomavirus 4 Species 0.000 description 3
- 241000196324 Embryophyta Species 0.000 description 3
- 241000206602 Eukaryota Species 0.000 description 3
- 239000012981 Hank's balanced salt solution Substances 0.000 description 3
- 101000898034 Homo sapiens Hepatocyte growth factor Proteins 0.000 description 3
- 241000235649 Kluyveromyces Species 0.000 description 3
- 108091005804 Peptidases Proteins 0.000 description 3
- 239000004365 Protease Substances 0.000 description 3
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 3
- 239000007983 Tris buffer Substances 0.000 description 3
- 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 3
- 239000002671 adjuvant Substances 0.000 description 3
- 235000004279 alanine Nutrition 0.000 description 3
- 229960000723 ampicillin Drugs 0.000 description 3
- 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 3
- IQFYYKKMVGJFEH-UHFFFAOYSA-N beta-L-thymidine Natural products O=C1NC(=O)C(C)=CN1C1OC(CO)C(O)C1 IQFYYKKMVGJFEH-UHFFFAOYSA-N 0.000 description 3
- 210000002960 bfu-e Anatomy 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 239000012228 culture supernatant Substances 0.000 description 3
- 231100000673 dose–response relationship Toxicity 0.000 description 3
- 238000011049 filling Methods 0.000 description 3
- 238000009472 formulation Methods 0.000 description 3
- 230000002068 genetic effect Effects 0.000 description 3
- 230000011132 hemopoiesis Effects 0.000 description 3
- 238000001727 in vivo Methods 0.000 description 3
- 238000011534 incubation Methods 0.000 description 3
- 208000015181 infectious disease Diseases 0.000 description 3
- 230000003834 intracellular effect Effects 0.000 description 3
- 208000032839 leukemia Diseases 0.000 description 3
- 210000004698 lymphocyte Anatomy 0.000 description 3
- 230000003211 malignant effect Effects 0.000 description 3
- 210000003643 myeloid progenitor cell Anatomy 0.000 description 3
- 108090000765 processed proteins & peptides Proteins 0.000 description 3
- 210000002966 serum Anatomy 0.000 description 3
- 238000010561 standard procedure Methods 0.000 description 3
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 3
- 238000011144 upstream manufacturing Methods 0.000 description 3
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 2
- 241000228212 Aspergillus Species 0.000 description 2
- 108010077805 Bacterial Proteins Proteins 0.000 description 2
- 108010062580 Concanavalin A Proteins 0.000 description 2
- 102000012410 DNA Ligases Human genes 0.000 description 2
- 108010061982 DNA Ligases Proteins 0.000 description 2
- 108090000204 Dipeptidase 1 Proteins 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- ULGZDMOVFRHVEP-RWJQBGPGSA-N Erythromycin Chemical compound O([C@@H]1[C@@H](C)C(=O)O[C@@H]([C@@]([C@H](O)[C@@H](C)C(=O)[C@H](C)C[C@@](C)(O)[C@H](O[C@H]2[C@@H]([C@H](C[C@@H](C)O2)N(C)C)O)[C@H]1C)(C)O)CC)[C@H]1C[C@@](C)(OC)[C@@H](O)[C@H](C)O1 ULGZDMOVFRHVEP-RWJQBGPGSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 102000003839 Human Proteins Human genes 0.000 description 2
- 108090000144 Human Proteins Proteins 0.000 description 2
- 239000007760 Iscove's Modified Dulbecco's Medium Substances 0.000 description 2
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical group OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- 101150068888 MET3 gene Proteins 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- 241001465754 Metazoa Species 0.000 description 2
- 229930193140 Neomycin Natural products 0.000 description 2
- 101100109292 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) arg-13 gene Proteins 0.000 description 2
- 101100022915 Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) cys-11 gene Proteins 0.000 description 2
- 239000000020 Nitrocellulose Substances 0.000 description 2
- 206010033661 Pancytopenia Diseases 0.000 description 2
- 102000002508 Peptide Elongation Factors Human genes 0.000 description 2
- 108010068204 Peptide Elongation Factors Proteins 0.000 description 2
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Chemical group OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 101100022918 Schizosaccharomyces pombe (strain 972 / ATCC 24843) sua1 gene Proteins 0.000 description 2
- 241000187747 Streptomyces Species 0.000 description 2
- 108020005038 Terminator Codon Proteins 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 239000011543 agarose gel Substances 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 230000008827 biological function Effects 0.000 description 2
- 230000033228 biological regulation Effects 0.000 description 2
- 210000003969 blast cell Anatomy 0.000 description 2
- 210000000601 blood cell Anatomy 0.000 description 2
- 238000010322 bone marrow transplantation Methods 0.000 description 2
- 239000001506 calcium phosphate Substances 0.000 description 2
- 229910000389 calcium phosphate Inorganic materials 0.000 description 2
- 235000011010 calcium phosphates Nutrition 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 210000002791 cfu-m Anatomy 0.000 description 2
- 230000008859 change Effects 0.000 description 2
- 230000002759 chromosomal effect Effects 0.000 description 2
- 238000012411 cloning technique Methods 0.000 description 2
- 208000024389 cytopenia Diseases 0.000 description 2
- 230000002950 deficient Effects 0.000 description 2
- 239000007857 degradation product Substances 0.000 description 2
- 238000012217 deletion Methods 0.000 description 2
- 230000037430 deletion Effects 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 2
- 239000000839 emulsion Substances 0.000 description 2
- 229940088598 enzyme Drugs 0.000 description 2
- 210000000751 eop Anatomy 0.000 description 2
- 210000003979 eosinophil Anatomy 0.000 description 2
- 239000000284 extract Substances 0.000 description 2
- 239000012894 fetal calf serum Substances 0.000 description 2
- 230000006870 function Effects 0.000 description 2
- 238000001415 gene therapy Methods 0.000 description 2
- 101150106093 gpt gene Proteins 0.000 description 2
- ZJYYHGLJYGJLLN-UHFFFAOYSA-N guanidinium thiocyanate Chemical compound SC#N.NC(N)=N ZJYYHGLJYGJLLN-UHFFFAOYSA-N 0.000 description 2
- 210000004524 haematopoietic cell Anatomy 0.000 description 2
- 210000001357 hemopoietic progenitor cell Anatomy 0.000 description 2
- 101150069378 hil-3 gene Proteins 0.000 description 2
- 102000057308 human HGF Human genes 0.000 description 2
- 210000004408 hybridoma Anatomy 0.000 description 2
- 238000010348 incorporation Methods 0.000 description 2
- 230000006698 induction Effects 0.000 description 2
- 239000007924 injection Substances 0.000 description 2
- 238000002347 injection Methods 0.000 description 2
- 230000010354 integration Effects 0.000 description 2
- BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 2
- 238000011031 large-scale manufacturing process Methods 0.000 description 2
- 239000007788 liquid Substances 0.000 description 2
- 210000004962 mammalian cell Anatomy 0.000 description 2
- 230000035800 maturation Effects 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 229960004927 neomycin Drugs 0.000 description 2
- 229920001220 nitrocellulos Polymers 0.000 description 2
- 210000000287 oocyte Anatomy 0.000 description 2
- 230000008488 polyadenylation Effects 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 102000004196 processed proteins & peptides Human genes 0.000 description 2
- 230000012846 protein folding Effects 0.000 description 2
- 238000001742 protein purification Methods 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 238000011084 recovery Methods 0.000 description 2
- 108091008146 restriction endonucleases Proteins 0.000 description 2
- 239000012723 sample buffer Substances 0.000 description 2
- 238000004062 sedimentation Methods 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 210000000952 spleen Anatomy 0.000 description 2
- 230000004936 stimulating effect Effects 0.000 description 2
- 230000008093 supporting effect Effects 0.000 description 2
- 238000003786 synthesis reaction Methods 0.000 description 2
- 238000004448 titration Methods 0.000 description 2
- 230000009261 transgenic effect Effects 0.000 description 2
- QORWJWZARLRLPR-UHFFFAOYSA-H tricalcium bis(phosphate) Chemical compound [Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O QORWJWZARLRLPR-UHFFFAOYSA-H 0.000 description 2
- DIGQNXIGRZPYDK-WKSCXVIASA-N (2R)-6-amino-2-[[2-[[(2S)-2-[[2-[[(2R)-2-[[(2S)-2-[[(2R,3S)-2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-[[(2R)-2-[[(2S,3S)-2-[[(2R)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2R)-2-[[2-[[2-[[2-[(2-amino-1-hydroxyethylidene)amino]-3-carboxy-1-hydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxypropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1,5-dihydroxy-5-iminopentylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxybutylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1,3-dihydroxypropylidene]amino]-1-hydroxyethylidene]amino]-1-hydroxy-3-sulfanylpropylidene]amino]-1-hydroxyethylidene]amino]hexanoic acid Chemical compound C[C@@H]([C@@H](C(=N[C@@H](CS)C(=N[C@@H](C)C(=N[C@@H](CO)C(=NCC(=N[C@@H](CCC(=N)O)C(=NC(CS)C(=N[C@H]([C@H](C)O)C(=N[C@H](CS)C(=N[C@H](CO)C(=NCC(=N[C@H](CS)C(=NCC(=N[C@H](CCCCN)C(=O)O)O)O)O)O)O)O)O)O)O)O)O)O)O)N=C([C@H](CS)N=C([C@H](CO)N=C([C@H](CO)N=C([C@H](C)N=C(CN=C([C@H](CO)N=C([C@H](CS)N=C(CN=C(C(CS)N=C(C(CC(=O)O)N=C(CN)O)O)O)O)O)O)O)O)O)O)O)O DIGQNXIGRZPYDK-WKSCXVIASA-N 0.000 description 1
- JUSMHIGDXPKSID-PHYPRBDBSA-N (2r,3r,4s,5r,6s)-2-(hydroxymethyl)-6-sulfanyloxane-3,4,5-triol Chemical compound OC[C@H]1O[C@@H](S)[C@H](O)[C@@H](O)[C@H]1O JUSMHIGDXPKSID-PHYPRBDBSA-N 0.000 description 1
- OSJPPGNTCRNQQC-UWTATZPHSA-N 3-phospho-D-glyceric acid Chemical compound OC(=O)[C@H](O)COP(O)(O)=O OSJPPGNTCRNQQC-UWTATZPHSA-N 0.000 description 1
- 208000030507 AIDS Diseases 0.000 description 1
- QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 description 1
- 206010000830 Acute leukaemia Diseases 0.000 description 1
- WPWUFUBLGADILS-WDSKDSINSA-N Ala-Pro Chemical compound C[C@H](N)C(=O)N1CCC[C@H]1C(O)=O WPWUFUBLGADILS-WDSKDSINSA-N 0.000 description 1
- BHTBAVZSZCQZPT-GUBZILKMSA-N Ala-Pro-Met Chemical compound CSCC[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@H](C)N BHTBAVZSZCQZPT-GUBZILKMSA-N 0.000 description 1
- 206010005089 Blast cell proliferation Diseases 0.000 description 1
- 208000010392 Bone Fractures Diseases 0.000 description 1
- 208000020084 Bone disease Diseases 0.000 description 1
- 108010035563 Chloramphenicol O-acetyltransferase Proteins 0.000 description 1
- 108020004705 Codon Proteins 0.000 description 1
- 102000004594 DNA Polymerase I Human genes 0.000 description 1
- 108010017826 DNA Polymerase I Proteins 0.000 description 1
- 108010076804 DNA Restriction Enzymes Proteins 0.000 description 1
- 108010066072 DNA modification methylase EcoRI 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
- 108010053770 Deoxyribonucleases Proteins 0.000 description 1
- 102000016911 Deoxyribonucleases Human genes 0.000 description 1
- 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 1
- 238000002965 ELISA Methods 0.000 description 1
- 241000702374 Enterobacteria phage fd Species 0.000 description 1
- 102000003951 Erythropoietin Human genes 0.000 description 1
- 108090000394 Erythropoietin Proteins 0.000 description 1
- 241000282326 Felis catus Species 0.000 description 1
- 229920001917 Ficoll Polymers 0.000 description 1
- 108010058643 Fungal Proteins Proteins 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- 229930182566 Gentamicin Natural products 0.000 description 1
- CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 0.000 description 1
- 101000930822 Giardia intestinalis Dipeptidyl-peptidase 4 Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 241000238631 Hexapoda Species 0.000 description 1
- 101100340751 Homo sapiens IL3 gene Proteins 0.000 description 1
- 241000282620 Hylobates sp. Species 0.000 description 1
- 206010062016 Immunosuppression Diseases 0.000 description 1
- 102100034343 Integrase Human genes 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 102000000589 Interleukin-1 Human genes 0.000 description 1
- 108010002352 Interleukin-1 Proteins 0.000 description 1
- 102000000588 Interleukin-2 Human genes 0.000 description 1
- 108010002350 Interleukin-2 Proteins 0.000 description 1
- 102100039064 Interleukin-3 Human genes 0.000 description 1
- 244000199866 Lactobacillus casei Species 0.000 description 1
- 235000013958 Lactobacillus casei Nutrition 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 102000003960 Ligases Human genes 0.000 description 1
- 108090000364 Ligases Proteins 0.000 description 1
- 102000008072 Lymphokines Human genes 0.000 description 1
- 108010074338 Lymphokines Proteins 0.000 description 1
- 102000003792 Metallothionein Human genes 0.000 description 1
- 108090000157 Metallothionein Proteins 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 101001033276 Mus musculus Interleukin-3 Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 241001049988 Mycobacterium tuberculosis H37Ra Species 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 238000000636 Northern blotting Methods 0.000 description 1
- 208000001132 Osteoporosis Diseases 0.000 description 1
- 241001494479 Pecora Species 0.000 description 1
- 108010087702 Penicillinase Proteins 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 206010035226 Plasma cell myeloma Diseases 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 101710135670 Putative Xaa-Pro dipeptidyl-peptidase Proteins 0.000 description 1
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 229920002684 Sepharose Polymers 0.000 description 1
- 238000012300 Sequence Analysis Methods 0.000 description 1
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 1
- 238000002105 Southern blotting Methods 0.000 description 1
- 241000256248 Spodoptera Species 0.000 description 1
- 241000256251 Spodoptera frugiperda Species 0.000 description 1
- 108010039445 Stem Cell Factor Proteins 0.000 description 1
- 101000895926 Streptomyces plicatus Endo-beta-N-acetylglucosaminidase H Proteins 0.000 description 1
- 229930006000 Sucrose Natural products 0.000 description 1
- 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 1
- 108091023045 Untranslated Region Proteins 0.000 description 1
- 241000700605 Viruses Species 0.000 description 1
- 101710143531 Xaa-Pro dipeptidyl-peptidase Proteins 0.000 description 1
- 241000269368 Xenopus laevis Species 0.000 description 1
- 230000005856 abnormality Effects 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000003213 activating effect Effects 0.000 description 1
- 230000001154 acute effect Effects 0.000 description 1
- 230000006978 adaptation Effects 0.000 description 1
- 238000011360 adjunctive therapy Methods 0.000 description 1
- 108010087924 alanylproline Proteins 0.000 description 1
- 150000001447 alkali salts Chemical group 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 230000003444 anaesthetic effect Effects 0.000 description 1
- 230000009286 beneficial effect Effects 0.000 description 1
- 230000008901 benefit Effects 0.000 description 1
- 102000006635 beta-lactamase Human genes 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000003995 blood forming stem cell Anatomy 0.000 description 1
- 210000002798 bone marrow cell Anatomy 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 238000010804 cDNA synthesis Methods 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000011712 cell development Effects 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 230000004663 cell proliferation Effects 0.000 description 1
- 210000002421 cell wall Anatomy 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
- 238000007385 chemical modification Methods 0.000 description 1
- 238000002512 chemotherapy Methods 0.000 description 1
- 210000004978 chinese hamster ovary cell Anatomy 0.000 description 1
- 239000013611 chromosomal DNA Substances 0.000 description 1
- 238000000975 co-precipitation Methods 0.000 description 1
- 230000002281 colonystimulating effect Effects 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000004590 computer program Methods 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- NKLPQNGYXWVELD-UHFFFAOYSA-M coomassie brilliant blue Chemical compound [Na+].C1=CC(OCC)=CC=C1NC1=CC=C(C(=C2C=CC(C=C2)=[N+](CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=2C=CC(=CC=2)N(CC)CC=2C=C(C=CC=2)S([O-])(=O)=O)C=C1 NKLPQNGYXWVELD-UHFFFAOYSA-M 0.000 description 1
- 238000007821 culture assay Methods 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 238000000432 density-gradient centrifugation Methods 0.000 description 1
- 238000001212 derivatisation Methods 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 239000012470 diluted sample Substances 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- 208000035475 disorder Diseases 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 239000003814 drug Substances 0.000 description 1
- 238000009585 enzyme analysis Methods 0.000 description 1
- 210000000222 eosinocyte Anatomy 0.000 description 1
- 210000000267 erythroid cell Anatomy 0.000 description 1
- 229960003276 erythromycin Drugs 0.000 description 1
- 229940105423 erythropoietin Drugs 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 150000002256 galaktoses Chemical class 0.000 description 1
- 201000011243 gastrointestinal stromal tumor Diseases 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 239000003862 glucocorticoid Substances 0.000 description 1
- 230000002414 glycolytic effect Effects 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 230000001506 immunosuppresive effect Effects 0.000 description 1
- 210000003000 inclusion body Anatomy 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 238000003780 insertion Methods 0.000 description 1
- 230000037431 insertion Effects 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 229940076264 interleukin-3 Drugs 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 230000036210 malignancy Effects 0.000 description 1
- 239000003550 marker Substances 0.000 description 1
- 210000001501 megacaryocyte Anatomy 0.000 description 1
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 1
- 210000002864 mononuclear phagocyte Anatomy 0.000 description 1
- 239000004570 mortar (masonry) Substances 0.000 description 1
- 210000002894 multi-fate stem cell Anatomy 0.000 description 1
- 210000000066 myeloid cell Anatomy 0.000 description 1
- 201000000050 myeloid neoplasm Diseases 0.000 description 1
- 239000013642 negative control Substances 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 230000003448 neutrophilic effect Effects 0.000 description 1
- 108091027963 non-coding RNA Proteins 0.000 description 1
- 102000042567 non-coding RNA Human genes 0.000 description 1
- 231100001160 nonlethal Toxicity 0.000 description 1
- 150000007523 nucleic acids Chemical group 0.000 description 1
- QYSGYZVSCZSLHT-UHFFFAOYSA-N octafluoropropane Chemical compound FC(F)(F)C(F)(F)C(F)(F)F QYSGYZVSCZSLHT-UHFFFAOYSA-N 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 210000000963 osteoblast Anatomy 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- 229950009506 penicillinase Drugs 0.000 description 1
- 239000008194 pharmaceutical composition Substances 0.000 description 1
- 239000000546 pharmaceutical excipient Substances 0.000 description 1
- 150000004633 phorbol derivatives Chemical class 0.000 description 1
- 239000002644 phorbol ester Substances 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 239000002504 physiological saline solution Substances 0.000 description 1
- 210000001778 pluripotent stem cell Anatomy 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 239000013641 positive control Substances 0.000 description 1
- OXCMYAYHXIHQOA-UHFFFAOYSA-N potassium;[2-butyl-5-chloro-3-[[4-[2-(1,2,4-triaza-3-azanidacyclopenta-1,4-dien-5-yl)phenyl]phenyl]methyl]imidazol-4-yl]methanol Chemical compound [K+].CCCCC1=NC(Cl)=C(CO)N1CC1=CC=C(C=2C(=CC=CC=2)C2=N[N-]N=N2)C=C1 OXCMYAYHXIHQOA-UHFFFAOYSA-N 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 230000002062 proliferating effect Effects 0.000 description 1
- 230000000644 propagated effect Effects 0.000 description 1
- 108010064037 prorennin Proteins 0.000 description 1
- 230000005664 protein glycosylation in endoplasmic reticulum Effects 0.000 description 1
- 230000008707 rearrangement Effects 0.000 description 1
- 102000005962 receptors Human genes 0.000 description 1
- 108020003175 receptors Proteins 0.000 description 1
- 230000003252 repetitive effect Effects 0.000 description 1
- 238000007894 restriction fragment length polymorphism technique Methods 0.000 description 1
- 150000003839 salts Chemical class 0.000 description 1
- 238000009738 saturating Methods 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 238000002741 site-directed mutagenesis Methods 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 239000005720 sucrose Substances 0.000 description 1
- 239000012134 supernatant fraction Substances 0.000 description 1
- 238000004114 suspension culture Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229940124597 therapeutic agent Drugs 0.000 description 1
- 238000000954 titration curve Methods 0.000 description 1
- 230000005029 transcription elongation Effects 0.000 description 1
- 230000001052 transient effect Effects 0.000 description 1
- 230000010474 transient expression Effects 0.000 description 1
- 230000014621 translational initiation Effects 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 238000011282 treatment Methods 0.000 description 1
- 238000000539 two dimensional gel electrophoresis Methods 0.000 description 1
- 239000007160 ty medium Substances 0.000 description 1
- 241000701161 unidentified adenovirus Species 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 241001430294 unidentified retrovirus Species 0.000 description 1
- 210000000689 upper leg Anatomy 0.000 description 1
- 238000002255 vaccination Methods 0.000 description 1
- 230000003612 virological effect Effects 0.000 description 1
- 239000011800 void material Substances 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
- 210000005253 yeast cell Anatomy 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K16/00—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies
- C07K16/18—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans
- C07K16/24—Immunoglobulins [IGs], e.g. monoclonal or polyclonal antibodies against material from animals or humans against cytokines, lymphokines or interferons
- C07K16/244—Interleukins [IL]
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
- C07K14/5403—IL-3
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Animal Behavior & Ethology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- General Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Immunology (AREA)
- Pharmacology & Pharmacy (AREA)
- Hematology (AREA)
- Diabetes (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP86202285 | 1986-12-16 | ||
EP87201322 | 1987-07-13 |
Publications (2)
Publication Number | Publication Date |
---|---|
IL84852A0 IL84852A0 (en) | 1988-06-30 |
IL84852A true IL84852A (en) | 1994-06-24 |
Family
ID=26103432
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
IL8485287A IL84852A (en) | 1986-12-16 | 1987-12-16 | Molecular cloning and expression of human IL-3 |
Country Status (14)
Country | Link |
---|---|
JP (2) | JPH01502157A (fi) |
AT (1) | ATE161882T1 (fi) |
AU (1) | AU617095B2 (fi) |
CA (1) | CA1341503C (fi) |
DE (1) | DE3752158T2 (fi) |
ES (1) | ES2113338T3 (fi) |
FI (1) | FI102293B1 (fi) |
GR (1) | GR3025857T3 (fi) |
IE (1) | IE81129B1 (fi) |
IL (1) | IL84852A (fi) |
NO (1) | NO180544C (fi) |
NZ (1) | NZ222939A (fi) |
PT (1) | PT86381B (fi) |
WO (1) | WO1988004691A1 (fi) |
Families Citing this family (19)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
GR871029B (en) * | 1986-07-14 | 1987-11-02 | Genetics Inst | Novel osteoinductive factors |
US6238889B1 (en) | 1986-12-16 | 2001-05-29 | Dsm N.V. | Molecular cloning and expression of the Pro8 isoform of human IL-3 |
OA09736A (en) * | 1987-02-18 | 1993-11-30 | Schering Biotech Corp | "Human interleukin-3 and muteins thereof". |
US5304637A (en) * | 1987-07-13 | 1994-04-19 | Gist-Brocades N.V. | Expression and purification of human interleukin-3 and muteins thereof |
GB2210883B (en) * | 1987-10-08 | 1992-01-02 | British Bio Technology | Synthetic interleukin-3 gene |
US6384194B1 (en) | 1987-12-16 | 2002-05-07 | Dsm N.V. | Expression and purification of human interleukin-3 and muteins thereof |
AU3864089A (en) * | 1988-07-20 | 1990-02-19 | Immunex Corporation | Nonglycosylated human interleukin-3 compositions |
NZ232913A (en) * | 1989-03-15 | 1992-08-26 | Gist Brocades Nv | Il-3 produced recombinantly and purified to homogeneity; vectors and pharmaceutical preparations |
US5128450A (en) * | 1989-06-30 | 1992-07-07 | Urdal David L | Nonglycosylated human interleukin-3 analog proteins |
DK0413383T3 (da) | 1989-08-14 | 1997-07-07 | Gist Brocades Nv | Mutanter af humant interleukin-3. |
US5516512A (en) | 1989-08-14 | 1996-05-14 | Gist-Brocades, N.V. | N- and C-terminal truncation and deletion mutants of human interleukin-3 |
DK0596881T3 (da) * | 1991-08-01 | 1997-10-13 | Fond Nat Transfusion Sanguine | Ekspression i ikke-tumurale humane lymofoblastoider med en integrativ vektor |
US5738849A (en) * | 1992-11-24 | 1998-04-14 | G. D. Searle & Co. | Interleukin-3 (IL-3) variant fusion proteins, their recombinant production, and therapeutic compositions comprising them |
ATE251669T1 (de) * | 1992-11-24 | 2003-10-15 | Searle & Co | Mutierte polypeptide des interleukin-3(il-3) |
US5501962A (en) * | 1993-06-21 | 1996-03-26 | G. D. Searle & Co. | Interleuken-3 (IL-3) human/murine hybrid polypeptides and recombinant production of the same |
US6017523A (en) * | 1995-06-06 | 2000-01-25 | G.D. Searle & Co. | Therapeutic methods employing mutant human interleukin-3 (IL-3) polypeptides |
WO1999041382A2 (en) * | 1998-02-17 | 1999-08-19 | Hyseq, Inc. | A novel interleukin-3 and uses thereof |
WO2006079169A1 (en) * | 2005-01-25 | 2006-08-03 | Apollo Life Sciences Limited | Parameter selected gm-csf, il-3, il-4, il-5 and chimeras thereof for therapeutic and diagnostic purposes |
JP2009532061A (ja) * | 2006-04-03 | 2009-09-10 | ニユー・イングランド・バイオレイブス・インコーポレイテツド | 組換えウシ血清アルブミン(rBSA)の発現、分泌及び精製、並びにその使用 |
Family Cites Families (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4695542A (en) * | 1983-10-04 | 1987-09-22 | Dnax Research Institute Of Molecular And Cellular Biology, Inc. | cDNA clones coding for polypeptides exhibiting multi-lineage cellular growth factor activity |
AU570762B2 (en) * | 1983-12-23 | 1988-03-24 | Australian National University, The | Cloning of cdna for il-3 |
GR871029B (en) * | 1986-07-14 | 1987-11-02 | Genetics Inst | Novel osteoinductive factors |
-
1987
- 1987-12-16 IL IL8485287A patent/IL84852A/en not_active IP Right Cessation
- 1987-12-16 PT PT86381A patent/PT86381B/pt not_active IP Right Cessation
- 1987-12-16 WO PCT/NL1987/000037 patent/WO1988004691A1/en active IP Right Grant
- 1987-12-16 JP JP63500606A patent/JPH01502157A/ja active Pending
- 1987-12-16 DE DE3752158T patent/DE3752158T2/de not_active Expired - Fee Related
- 1987-12-16 ES ES87202566T patent/ES2113338T3/es not_active Expired - Lifetime
- 1987-12-16 AU AU10577/88A patent/AU617095B2/en not_active Ceased
- 1987-12-16 IE IE340987A patent/IE81129B1/en not_active IP Right Cessation
- 1987-12-16 AT AT87202566T patent/ATE161882T1/de not_active IP Right Cessation
- 1987-12-16 NZ NZ222939A patent/NZ222939A/en unknown
-
1988
- 1988-08-08 FI FI883688A patent/FI102293B1/fi not_active IP Right Cessation
- 1988-08-12 NO NO883614A patent/NO180544C/no not_active IP Right Cessation
-
1997
- 1997-05-28 JP JP9154513A patent/JPH1080286A/ja active Pending
- 1997-12-16 CA CA000554561A patent/CA1341503C/en not_active Expired - Fee Related
-
1998
- 1998-01-08 GR GR980400027T patent/GR3025857T3/el unknown
Also Published As
Publication number | Publication date |
---|---|
ATE161882T1 (de) | 1998-01-15 |
IL84852A0 (en) | 1988-06-30 |
GR3025857T3 (en) | 1998-04-30 |
NO180544C (no) | 1997-05-07 |
AU617095B2 (en) | 1991-11-21 |
DE3752158T2 (de) | 1998-05-20 |
FI102293B (fi) | 1998-11-13 |
ES2113338T3 (es) | 1998-05-01 |
FI883688A0 (fi) | 1988-08-08 |
CA1341503C (en) | 2006-04-04 |
NO180544B (no) | 1997-01-27 |
FI102293B1 (fi) | 1998-11-13 |
NO883614D0 (no) | 1988-08-12 |
PT86381B (pt) | 1990-11-20 |
NO883614L (no) | 1988-08-12 |
WO1988004691A1 (en) | 1988-06-30 |
NZ222939A (en) | 1991-03-26 |
AU1057788A (en) | 1988-07-15 |
JPH1080286A (ja) | 1998-03-31 |
IE81129B1 (en) | 2000-03-22 |
PT86381A (en) | 1988-01-01 |
DE3752158D1 (de) | 1998-02-12 |
JPH01502157A (ja) | 1989-08-03 |
FI883688A (fi) | 1988-08-08 |
IE873409L (en) | 1988-06-12 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
IL84852A (en) | Molecular cloning and expression of human IL-3 | |
EP0275598B1 (en) | Molecular cloning and expression of human IL-3 | |
US5081228A (en) | Interleukin-1 receptors | |
US5319071A (en) | Soluble interleukin-1 receptors | |
EP0318296B1 (en) | DNA encoding proteins which bind to human IL-1 | |
CA1341611C (en) | Interleukin-1 receptors | |
JP2952203B2 (ja) | タンパク質の製造方法 | |
US4965195A (en) | Interleukin-7 | |
FI106044B (fi) | Menetelmä nisäkkään interleukiini-4-reseptorin (IL-4R) ja sen vasta-aineen tuottamiseksi ja IL-4R:ä koodaava DNA, vektori ja isäntäsolu | |
IE890207L (en) | Amphiregulin: a novel bifunctional growth modulating glycoprotein | |
US5115096A (en) | Amphiregulin: a bifunctional growth modulating glycoprotein | |
JP2749838B2 (ja) | インターロイキン−7 | |
Sherr et al. | Colony-stimulating factor 1 (macrophage colony-stimulating-factor) | |
IE912135A1 (en) | Mast cell growth factor | |
US5296592A (en) | Process for purifying interleukin-1 receptors | |
US5304637A (en) | Expression and purification of human interleukin-3 and muteins thereof | |
US5328988A (en) | Interleukin-7 | |
US6384194B1 (en) | Expression and purification of human interleukin-3 and muteins thereof | |
AU625534B2 (en) | Interleukin-1 receptors | |
US6238889B1 (en) | Molecular cloning and expression of the Pro8 isoform of human IL-3 | |
DD296691A5 (de) | Verfahren zur herstellung von antikoerpern gegen ein epitop von amphiregulin |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
KB | Patent renewed | ||
RH | Patent void | ||
HP | Change in proprietorship | ||
KB | Patent renewed | ||
MM9K | Patent not in force due to non-payment of renewal fees |