CN1498269A - 用改变程序的供体染色质或供体细胞克隆哺乳动物的方法 - Google Patents
用改变程序的供体染色质或供体细胞克隆哺乳动物的方法 Download PDFInfo
- Publication number
- CN1498269A CN1498269A CNA01820967XA CN01820967A CN1498269A CN 1498269 A CN1498269 A CN 1498269A CN A01820967X A CNA01820967X A CN A01820967XA CN 01820967 A CN01820967 A CN 01820967A CN 1498269 A CN1498269 A CN 1498269A
- Authority
- CN
- China
- Prior art keywords
- cell
- embryo
- ovocyte
- reprogramming
- described method
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Granted
Links
- 238000000034 method Methods 0.000 title claims abstract description 198
- 241000124008 Mammalia Species 0.000 title claims abstract description 77
- 238000010367 cloning Methods 0.000 title claims abstract description 34
- 210000004027 cell Anatomy 0.000 claims abstract description 561
- 210000000287 oocyte Anatomy 0.000 claims abstract description 188
- 210000004940 nucleus Anatomy 0.000 claims abstract description 180
- 210000000349 chromosome Anatomy 0.000 claims abstract description 13
- 238000003780 insertion Methods 0.000 claims abstract description 4
- 230000037431 insertion Effects 0.000 claims abstract description 4
- 210000001161 mammalian embryo Anatomy 0.000 claims description 373
- 210000003483 chromatin Anatomy 0.000 claims description 181
- 108010077544 Chromatin Proteins 0.000 claims description 180
- 239000000284 extract Substances 0.000 claims description 136
- 230000008672 reprogramming Effects 0.000 claims description 136
- 238000011534 incubation Methods 0.000 claims description 101
- 238000012546 transfer Methods 0.000 claims description 67
- 210000003754 fetus Anatomy 0.000 claims description 53
- 230000000394 mitotic effect Effects 0.000 claims description 52
- 108090000623 proteins and genes Proteins 0.000 claims description 50
- 230000004720 fertilization Effects 0.000 claims description 48
- 238000000338 in vitro Methods 0.000 claims description 36
- 210000002257 embryonic structure Anatomy 0.000 claims description 32
- 102000004169 proteins and genes Human genes 0.000 claims description 32
- 230000004083 survival effect Effects 0.000 claims description 30
- 230000002269 spontaneous effect Effects 0.000 claims description 24
- 102000001253 Protein Kinase Human genes 0.000 claims description 22
- 108060006633 protein kinase Proteins 0.000 claims description 22
- 210000004291 uterus Anatomy 0.000 claims description 18
- 150000003839 salts Chemical class 0.000 claims description 17
- 230000001605 fetal effect Effects 0.000 claims description 16
- 241000894007 species Species 0.000 claims description 15
- 210000000130 stem cell Anatomy 0.000 claims description 15
- 210000004340 zona pellucida Anatomy 0.000 claims description 11
- 210000002353 nuclear lamina Anatomy 0.000 claims description 10
- 230000004543 DNA replication Effects 0.000 claims description 9
- 210000002826 placenta Anatomy 0.000 claims description 9
- 241000699666 Mus <mouse, genus> Species 0.000 claims description 8
- 210000002308 embryonic cell Anatomy 0.000 claims description 7
- 241000283973 Oryctolagus cuniculus Species 0.000 claims description 6
- 241001494479 Pecora Species 0.000 claims description 5
- 210000003101 oviduct Anatomy 0.000 claims description 5
- 241000283707 Capra Species 0.000 claims description 4
- 241000700159 Rattus Species 0.000 claims description 4
- 241000282898 Sus scrofa Species 0.000 claims description 4
- 239000003599 detergent Substances 0.000 claims description 4
- 210000004996 female reproductive system Anatomy 0.000 claims description 4
- 210000001744 T-lymphocyte Anatomy 0.000 claims description 3
- 210000001612 chondrocyte Anatomy 0.000 claims description 3
- 210000002919 epithelial cell Anatomy 0.000 claims description 3
- 210000003958 hematopoietic stem cell Anatomy 0.000 claims description 3
- 210000002510 keratinocyte Anatomy 0.000 claims description 3
- 210000005075 mammary gland Anatomy 0.000 claims description 3
- 210000002752 melanocyte Anatomy 0.000 claims description 3
- 210000001616 monocyte Anatomy 0.000 claims description 3
- 230000002611 ovarian Effects 0.000 claims description 3
- 239000002516 radical scavenger Substances 0.000 claims description 3
- 108010025821 lamin C Proteins 0.000 claims 3
- 210000001185 bone marrow Anatomy 0.000 claims 2
- 210000004698 lymphocyte Anatomy 0.000 claims 2
- 210000003098 myoblast Anatomy 0.000 claims 2
- 239000000835 fiber Substances 0.000 claims 1
- 239000000243 solution Substances 0.000 description 60
- 238000010449 nuclear transplantation Methods 0.000 description 51
- 108020004414 DNA Proteins 0.000 description 47
- 108010035916 Nuclear Matrix-Associated Proteins Proteins 0.000 description 47
- 102000008297 Nuclear Matrix-Associated Proteins Human genes 0.000 description 44
- 239000012530 fluid Substances 0.000 description 43
- 210000000299 nuclear matrix Anatomy 0.000 description 43
- 238000013016 damping Methods 0.000 description 42
- 230000008859 change Effects 0.000 description 39
- 102100040086 A-kinase anchor protein 8 Human genes 0.000 description 36
- 101000890594 Homo sapiens A-kinase anchor protein 8 Proteins 0.000 description 36
- 239000000203 mixture Substances 0.000 description 36
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 34
- 101001003584 Homo sapiens Prelamin-A/C Proteins 0.000 description 32
- 210000000633 nuclear envelope Anatomy 0.000 description 32
- 102100026531 Prelamin-A/C Human genes 0.000 description 31
- YPHMISFOHDHNIV-FSZOTQKASA-N cycloheximide Chemical compound C1[C@@H](C)C[C@H](C)C(=O)[C@@H]1[C@H](O)CC1CC(=O)NC(=O)C1 YPHMISFOHDHNIV-FSZOTQKASA-N 0.000 description 30
- 238000002347 injection Methods 0.000 description 26
- 239000007924 injection Substances 0.000 description 26
- 108010075210 streptolysin O Proteins 0.000 description 23
- 238000005406 washing Methods 0.000 description 23
- 239000007788 liquid Substances 0.000 description 22
- 239000006228 supernatant Substances 0.000 description 22
- 230000012010 growth Effects 0.000 description 21
- 210000005053 lamin Anatomy 0.000 description 21
- 238000001556 precipitation Methods 0.000 description 21
- 230000004913 activation Effects 0.000 description 20
- LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 20
- 239000002953 phosphate buffered saline Substances 0.000 description 20
- 108010047294 Lamins Proteins 0.000 description 19
- 102000006835 Lamins Human genes 0.000 description 19
- 150000001875 compounds Chemical class 0.000 description 19
- 235000018102 proteins Nutrition 0.000 description 19
- 230000015572 biosynthetic process Effects 0.000 description 17
- 230000004927 fusion Effects 0.000 description 17
- 230000008569 process Effects 0.000 description 17
- 239000011780 sodium chloride Substances 0.000 description 17
- -1 cell lamin Proteins 0.000 description 16
- 239000007995 HEPES buffer Substances 0.000 description 15
- 210000002459 blastocyst Anatomy 0.000 description 15
- 238000002360 preparation method Methods 0.000 description 15
- 239000010410 layer Substances 0.000 description 14
- 210000001519 tissue Anatomy 0.000 description 14
- 108091023040 Transcription factor Proteins 0.000 description 13
- 102000040945 Transcription factor Human genes 0.000 description 13
- 210000005059 placental tissue Anatomy 0.000 description 13
- 108010021101 Lamin Type B Proteins 0.000 description 12
- 229930006000 Sucrose Natural products 0.000 description 12
- 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 12
- 230000002759 chromosomal effect Effects 0.000 description 12
- 238000005336 cracking Methods 0.000 description 12
- 108020004999 messenger RNA Proteins 0.000 description 12
- 150000007523 nucleic acids Chemical class 0.000 description 12
- 238000003860 storage Methods 0.000 description 12
- 239000005720 sucrose Substances 0.000 description 12
- 238000005516 engineering process Methods 0.000 description 11
- 230000035800 maturation Effects 0.000 description 11
- 102000039446 nucleic acids Human genes 0.000 description 11
- 108020004707 nucleic acids Proteins 0.000 description 11
- 238000010561 standard procedure Methods 0.000 description 11
- 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 10
- 241001550206 Colla Species 0.000 description 10
- RJURFGZVJUQBHK-UHFFFAOYSA-N actinomycin D Natural products CC1OC(=O)C(C(C)C)N(C)C(=O)CN(C)C(=O)C2CCCN2C(=O)C(C(C)C)NC(=O)C1NC(=O)C1=C(N)C(=O)C(C)=C2OC(C(C)=CC=C3C(=O)NC4C(=O)NC(C(N5CCCC5C(=O)N(C)CC(=O)N(C)C(C(C)C)C(=O)OC4C)=O)C(C)C)=C3N=C21 RJURFGZVJUQBHK-UHFFFAOYSA-N 0.000 description 10
- 229910052757 nitrogen Inorganic materials 0.000 description 10
- 230000008521 reorganization Effects 0.000 description 10
- 238000012360 testing method Methods 0.000 description 10
- CWHJIJJSDGEHNS-MYLFLSLOSA-N Senegenin Chemical group C1[C@H](O)[C@H](O)[C@@](C)(C(O)=O)[C@@H]2CC[C@@]3(C)C(CC[C@]4(CCC(C[C@H]44)(C)C)C(O)=O)=C4[C@@H](CCl)C[C@@H]3[C@]21C CWHJIJJSDGEHNS-MYLFLSLOSA-N 0.000 description 9
- 210000001109 blastomere Anatomy 0.000 description 9
- 239000011575 calcium Substances 0.000 description 9
- 210000000170 cell membrane Anatomy 0.000 description 9
- 238000000280 densification Methods 0.000 description 9
- 239000002480 mineral oil Substances 0.000 description 9
- 235000010446 mineral oil Nutrition 0.000 description 9
- 238000002156 mixing Methods 0.000 description 9
- 230000001568 sexual effect Effects 0.000 description 9
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 8
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 8
- 241000283690 Bos taurus Species 0.000 description 8
- LCTONWCANYUPML-UHFFFAOYSA-N Pyruvic acid Chemical compound CC(=O)C(O)=O LCTONWCANYUPML-UHFFFAOYSA-N 0.000 description 8
- 235000001014 amino acid Nutrition 0.000 description 8
- SDZRWUKZFQQKKV-JHADDHBZSA-N cytochalasin D Chemical compound C([C@H]1[C@@H]2[C@@H](C([C@@H](O)[C@H]\3[C@]2([C@@H](/C=C/[C@@](C)(O)C(=O)[C@@H](C)C/C=C/3)OC(C)=O)C(=O)N1)=C)C)C1=CC=CC=C1 SDZRWUKZFQQKKV-JHADDHBZSA-N 0.000 description 8
- 230000009089 cytolysis Effects 0.000 description 8
- 230000004992 fission Effects 0.000 description 8
- 230000008014 freezing Effects 0.000 description 8
- 238000007710 freezing Methods 0.000 description 8
- 230000001976 improved effect Effects 0.000 description 8
- 239000000463 material Substances 0.000 description 8
- 239000009871 tenuigenin Substances 0.000 description 8
- 238000013518 transcription Methods 0.000 description 8
- 230000035897 transcription Effects 0.000 description 8
- 102000000905 Cadherin Human genes 0.000 description 7
- 108050007957 Cadherin Proteins 0.000 description 7
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 7
- 102000008130 Cyclic AMP-Dependent Protein Kinases Human genes 0.000 description 7
- 108010049894 Cyclic AMP-Dependent Protein Kinases Proteins 0.000 description 7
- 102000002322 Egg Proteins Human genes 0.000 description 7
- 108010000912 Egg Proteins Proteins 0.000 description 7
- 108091000080 Phosphotransferase Proteins 0.000 description 7
- 108010007568 Protamines Proteins 0.000 description 7
- 102000007327 Protamines Human genes 0.000 description 7
- RJURFGZVJUQBHK-IIXSONLDSA-N actinomycin D Chemical compound C[C@H]1OC(=O)[C@H](C(C)C)N(C)C(=O)CN(C)C(=O)[C@@H]2CCCN2C(=O)[C@@H](C(C)C)NC(=O)[C@H]1NC(=O)C1=C(N)C(=O)C(C)=C2OC(C(C)=CC=C3C(=O)N[C@@H]4C(=O)N[C@@H](C(N5CCC[C@H]5C(=O)N(C)CC(=O)N(C)[C@@H](C(C)C)C(=O)O[C@@H]4C)=O)C(C)C)=C3N=C21 RJURFGZVJUQBHK-IIXSONLDSA-N 0.000 description 7
- 150000001413 amino acids Chemical group 0.000 description 7
- 238000004458 analytical method Methods 0.000 description 7
- 229910052791 calcium Inorganic materials 0.000 description 7
- 239000006059 cover glass Substances 0.000 description 7
- 230000001086 cytosolic effect Effects 0.000 description 7
- 239000006166 lysate Substances 0.000 description 7
- 239000003550 marker Substances 0.000 description 7
- 210000000056 organ Anatomy 0.000 description 7
- 210000004681 ovum Anatomy 0.000 description 7
- 102000020233 phosphotransferase Human genes 0.000 description 7
- 230000035935 pregnancy Effects 0.000 description 7
- 229940048914 protamine Drugs 0.000 description 7
- 230000001360 synchronised effect Effects 0.000 description 7
- 108010092160 Dactinomycin Proteins 0.000 description 6
- 108090000353 Histone deacetylase Proteins 0.000 description 6
- 102000003964 Histone deacetylase Human genes 0.000 description 6
- 108010033040 Histones Proteins 0.000 description 6
- GBOGMAARMMDZGR-UHFFFAOYSA-N UNPD149280 Natural products N1C(=O)C23OC(=O)C=CC(O)CCCC(C)CC=CC3C(O)C(=C)C(C)C2C1CC1=CC=CC=C1 GBOGMAARMMDZGR-UHFFFAOYSA-N 0.000 description 6
- 239000002253 acid Substances 0.000 description 6
- 239000012190 activator Substances 0.000 description 6
- HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol Chemical compound C1C=C2C[C@@H](O)CC[C@]2(C)[C@@H]2[C@@H]1[C@@H]1CC[C@H]([C@H](C)CCCC(C)C)[C@@]1(C)CC2 HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 6
- 230000010428 chromatin condensation Effects 0.000 description 6
- GBOGMAARMMDZGR-JREHFAHYSA-N cytochalasin B Natural products C[C@H]1CCC[C@@H](O)C=CC(=O)O[C@@]23[C@H](C=CC1)[C@H](O)C(=C)[C@@H](C)[C@@H]2[C@H](Cc4ccccc4)NC3=O GBOGMAARMMDZGR-JREHFAHYSA-N 0.000 description 6
- GBOGMAARMMDZGR-TYHYBEHESA-N cytochalasin B Chemical compound C([C@H]1[C@@H]2[C@@H](C([C@@H](O)[C@@H]3/C=C/C[C@H](C)CCC[C@@H](O)/C=C/C(=O)O[C@@]23C(=O)N1)=C)C)C1=CC=CC=C1 GBOGMAARMMDZGR-TYHYBEHESA-N 0.000 description 6
- 239000000975 dye Substances 0.000 description 6
- 210000002950 fibroblast Anatomy 0.000 description 6
- 239000011521 glass Substances 0.000 description 6
- 238000010166 immunofluorescence Methods 0.000 description 6
- 239000003112 inhibitor Substances 0.000 description 6
- 239000012528 membrane Substances 0.000 description 6
- 230000004048 modification Effects 0.000 description 6
- 238000012986 modification Methods 0.000 description 6
- 230000026731 phosphorylation Effects 0.000 description 6
- 238000006366 phosphorylation reaction Methods 0.000 description 6
- 239000000126 substance Substances 0.000 description 6
- PRDFBSVERLRRMY-UHFFFAOYSA-N 2'-(4-ethoxyphenyl)-5-(4-methylpiperazin-1-yl)-2,5'-bibenzimidazole Chemical compound C1=CC(OCC)=CC=C1C1=NC2=CC=C(C=3NC4=CC(=CC=C4N=3)N3CCN(C)CC3)C=C2N1 PRDFBSVERLRRMY-UHFFFAOYSA-N 0.000 description 5
- BMGMINKVTPDDRZ-UHFFFAOYSA-N 2-acetamido-n-[1-[[5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]-4-methylpentanamide;n-[1-[[5-(diaminomethylideneamino)-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]-4-methyl-2-(propanoylamino)pentanamide Chemical compound CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N.CCC(=O)NC(CC(C)C)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N BMGMINKVTPDDRZ-UHFFFAOYSA-N 0.000 description 5
- QRLVDLBMBULFAL-UHFFFAOYSA-N Digitonin Natural products CC1CCC2(OC1)OC3C(O)C4C5CCC6CC(OC7OC(CO)C(OC8OC(CO)C(O)C(OC9OCC(O)C(O)C9OC%10OC(CO)C(O)C(OC%11OC(CO)C(O)C(O)C%11O)C%10O)C8O)C(O)C7O)C(O)CC6(C)C5CCC4(C)C3C2C QRLVDLBMBULFAL-UHFFFAOYSA-N 0.000 description 5
- 108010011078 Leupeptins Proteins 0.000 description 5
- 241001465754 Metazoa Species 0.000 description 5
- 229930040373 Paraformaldehyde Natural products 0.000 description 5
- 102000003923 Protein Kinase C Human genes 0.000 description 5
- 108090000315 Protein Kinase C Proteins 0.000 description 5
- 229920004890 Triton X-100 Polymers 0.000 description 5
- 239000013504 Triton X-100 Substances 0.000 description 5
- 101710162629 Trypsin inhibitor Proteins 0.000 description 5
- 229940122618 Trypsin inhibitor Drugs 0.000 description 5
- 229910052799 carbon Inorganic materials 0.000 description 5
- 239000011248 coating agent Substances 0.000 description 5
- 238000000576 coating method Methods 0.000 description 5
- 229960000640 dactinomycin Drugs 0.000 description 5
- UVYVLBIGDKGWPX-KUAJCENISA-N digitonin Chemical compound O([C@@H]1[C@@H]([C@]2(CC[C@@H]3[C@@]4(C)C[C@@H](O)[C@H](O[C@H]5[C@@H]([C@@H](O)[C@@H](O[C@H]6[C@@H]([C@@H](O[C@H]7[C@@H]([C@@H](O)[C@H](O)CO7)O)[C@H](O)[C@@H](CO)O6)O[C@H]6[C@@H]([C@@H](O[C@H]7[C@@H]([C@@H](O)[C@H](O)[C@@H](CO)O7)O)[C@@H](O)[C@@H](CO)O6)O)[C@@H](CO)O5)O)C[C@@H]4CC[C@H]3[C@@H]2[C@@H]1O)C)[C@@H]1C)[C@]11CC[C@@H](C)CO1 UVYVLBIGDKGWPX-KUAJCENISA-N 0.000 description 5
- UVYVLBIGDKGWPX-UHFFFAOYSA-N digitonine Natural products CC1C(C2(CCC3C4(C)CC(O)C(OC5C(C(O)C(OC6C(C(OC7C(C(O)C(O)CO7)O)C(O)C(CO)O6)OC6C(C(OC7C(C(O)C(O)C(CO)O7)O)C(O)C(CO)O6)O)C(CO)O5)O)CC4CCC3C2C2O)C)C2OC11CCC(C)CO1 UVYVLBIGDKGWPX-UHFFFAOYSA-N 0.000 description 5
- 230000005611 electricity Effects 0.000 description 5
- 230000007159 enucleation Effects 0.000 description 5
- 238000011156 evaluation Methods 0.000 description 5
- 230000008175 fetal development Effects 0.000 description 5
- 239000001963 growth medium Substances 0.000 description 5
- 238000010185 immunofluorescence analysis Methods 0.000 description 5
- 150000002632 lipids Chemical class 0.000 description 5
- 238000012544 monitoring process Methods 0.000 description 5
- 230000035772 mutation Effects 0.000 description 5
- 229920002866 paraformaldehyde Polymers 0.000 description 5
- 230000008823 permeabilization Effects 0.000 description 5
- 238000000746 purification Methods 0.000 description 5
- 238000007634 remodeling Methods 0.000 description 5
- 238000007789 sealing Methods 0.000 description 5
- 238000010186 staining Methods 0.000 description 5
- 239000002753 trypsin inhibitor Substances 0.000 description 5
- KSXTUUUQYQYKCR-LQDDAWAPSA-M 2,3-bis[[(z)-octadec-9-enoyl]oxy]propyl-trimethylazanium;chloride Chemical compound [Cl-].CCCCCCCC\C=C/CCCCCCCC(=O)OCC(C[N+](C)(C)C)OC(=O)CCCCCCC\C=C/CCCCCCCC KSXTUUUQYQYKCR-LQDDAWAPSA-M 0.000 description 4
- QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 4
- 102000004127 Cytokines Human genes 0.000 description 4
- 108090000695 Cytokines Proteins 0.000 description 4
- 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 4
- LYCAIKOWRPUZTN-UHFFFAOYSA-N Ethylene glycol Chemical compound OCCO LYCAIKOWRPUZTN-UHFFFAOYSA-N 0.000 description 4
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 4
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 description 4
- 102000015696 Interleukins Human genes 0.000 description 4
- 108010063738 Interleukins Proteins 0.000 description 4
- DRBBFCLWYRJSJZ-UHFFFAOYSA-N N-phosphocreatine Chemical compound OC(=O)CN(C)C(=N)NP(O)(O)=O DRBBFCLWYRJSJZ-UHFFFAOYSA-N 0.000 description 4
- 108091028043 Nucleic acid sequence Proteins 0.000 description 4
- 102000013275 Somatomedins Human genes 0.000 description 4
- 241000251539 Vertebrata <Metazoa> Species 0.000 description 4
- 230000003213 activating effect Effects 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 239000008004 cell lysis buffer Substances 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 239000003153 chemical reaction reagent Substances 0.000 description 4
- 238000012258 culturing Methods 0.000 description 4
- 210000000172 cytosol Anatomy 0.000 description 4
- 238000000354 decomposition reaction Methods 0.000 description 4
- 230000000694 effects Effects 0.000 description 4
- 238000000605 extraction Methods 0.000 description 4
- 239000012091 fetal bovine serum Substances 0.000 description 4
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 4
- 229940088597 hormone Drugs 0.000 description 4
- 239000005556 hormone Substances 0.000 description 4
- 238000000520 microinjection Methods 0.000 description 4
- 239000012452 mother liquor Substances 0.000 description 4
- 210000002220 organoid Anatomy 0.000 description 4
- 238000007500 overflow downdraw method Methods 0.000 description 4
- 108010091212 pepstatin Proteins 0.000 description 4
- FAXGPCHRFPCXOO-LXTPJMTPSA-N pepstatin A Chemical compound OC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)C[C@H](O)[C@H](CC(C)C)NC(=O)[C@H](C(C)C)NC(=O)[C@H](C(C)C)NC(=O)CC(C)C FAXGPCHRFPCXOO-LXTPJMTPSA-N 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
- 229940107700 pyruvic acid Drugs 0.000 description 4
- 210000003370 receptor cell Anatomy 0.000 description 4
- 238000000926 separation method Methods 0.000 description 4
- 210000002966 serum Anatomy 0.000 description 4
- NGSFWBMYFKHRBD-UHFFFAOYSA-N sodium;2-hydroxypropanoic acid Chemical compound [Na+].CC(O)C(O)=O NGSFWBMYFKHRBD-UHFFFAOYSA-N 0.000 description 4
- 239000000725 suspension Substances 0.000 description 4
- 230000009261 transgenic effect Effects 0.000 description 4
- 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 3
- XULFJDKZVHTRLG-JDVCJPALSA-N DOSPA trifluoroacetate Chemical compound [O-]C(=O)C(F)(F)F.CCCCCCCC\C=C/CCCCCCCCOCC(C[N+](C)(C)CCNC(=O)C(CCCNCCCN)NCCCN)OCCCCCCCC\C=C/CCCCCCCC XULFJDKZVHTRLG-JDVCJPALSA-N 0.000 description 3
- IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 3
- 241000257465 Echinoidea Species 0.000 description 3
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
- 239000012981 Hank's balanced salt solution Substances 0.000 description 3
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
- 229920001213 Polysorbate 20 Polymers 0.000 description 3
- 239000012980 RPMI-1640 medium Substances 0.000 description 3
- PFNFFQXMRSDOHW-UHFFFAOYSA-N Spermine Natural products NCCCNCCCCNCCCN PFNFFQXMRSDOHW-UHFFFAOYSA-N 0.000 description 3
- 108010011834 Streptolysins Proteins 0.000 description 3
- HMNZFMSWFCAGGW-XPWSMXQVSA-N [3-[hydroxy(2-hydroxyethoxy)phosphoryl]oxy-2-[(e)-octadec-9-enoyl]oxypropyl] (e)-octadec-9-enoate Chemical compound CCCCCCCC\C=C\CCCCCCCC(=O)OCC(COP(O)(=O)OCCO)OC(=O)CCCCCCC\C=C\CCCCCCCC HMNZFMSWFCAGGW-XPWSMXQVSA-N 0.000 description 3
- 238000001261 affinity purification Methods 0.000 description 3
- 230000006907 apoptotic process Effects 0.000 description 3
- 239000012298 atmosphere Substances 0.000 description 3
- 210000004369 blood Anatomy 0.000 description 3
- 239000008280 blood Substances 0.000 description 3
- 244000309464 bull Species 0.000 description 3
- 239000003710 calcium ionophore Substances 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 235000012000 cholesterol Nutrition 0.000 description 3
- 230000001186 cumulative effect Effects 0.000 description 3
- 230000006378 damage Effects 0.000 description 3
- 230000004069 differentiation Effects 0.000 description 3
- 201000010099 disease Diseases 0.000 description 3
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 3
- 238000009826 distribution Methods 0.000 description 3
- CJAONIOAQZUHPN-KKLWWLSJSA-N ethyl 12-[[2-[(2r,3r)-3-[2-[(12-ethoxy-12-oxododecyl)-methylamino]-2-oxoethoxy]butan-2-yl]oxyacetyl]-methylamino]dodecanoate Chemical compound CCOC(=O)CCCCCCCCCCCN(C)C(=O)CO[C@H](C)[C@@H](C)OCC(=O)N(C)CCCCCCCCCCCC(=O)OCC CJAONIOAQZUHPN-KKLWWLSJSA-N 0.000 description 3
- 230000003328 fibroblastic effect Effects 0.000 description 3
- 230000002068 genetic effect Effects 0.000 description 3
- 230000002779 inactivation Effects 0.000 description 3
- 230000010354 integration Effects 0.000 description 3
- 230000014759 maintenance of location Effects 0.000 description 3
- 230000007935 neutral effect Effects 0.000 description 3
- 239000003921 oil Substances 0.000 description 3
- 235000010486 polyoxyethylene sorbitan monolaurate Nutrition 0.000 description 3
- 239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 3
- 230000001105 regulatory effect Effects 0.000 description 3
- 239000000523 sample Substances 0.000 description 3
- 210000001082 somatic cell Anatomy 0.000 description 3
- 238000003756 stirring Methods 0.000 description 3
- 210000003932 urinary bladder Anatomy 0.000 description 3
- 210000002700 urine Anatomy 0.000 description 3
- ASWBNKHCZGQVJV-UHFFFAOYSA-N (3-hexadecanoyloxy-2-hydroxypropyl) 2-(trimethylazaniumyl)ethyl phosphate Chemical compound CCCCCCCCCCCCCCCC(=O)OCC(O)COP([O-])(=O)OCC[N+](C)(C)C ASWBNKHCZGQVJV-UHFFFAOYSA-N 0.000 description 2
- 241000251468 Actinopterygii Species 0.000 description 2
- 102000000584 Calmodulin Human genes 0.000 description 2
- 108010041952 Calmodulin Proteins 0.000 description 2
- 241000282836 Camelus dromedarius Species 0.000 description 2
- CURLTUGMZLYLDI-UHFFFAOYSA-N Carbon dioxide Chemical compound O=C=O CURLTUGMZLYLDI-UHFFFAOYSA-N 0.000 description 2
- 102000005403 Casein Kinases Human genes 0.000 description 2
- 108010031425 Casein Kinases Proteins 0.000 description 2
- 241000282994 Cervidae Species 0.000 description 2
- 108091060290 Chromatid Proteins 0.000 description 2
- 102000004420 Creatine Kinase Human genes 0.000 description 2
- 108010042126 Creatine kinase Proteins 0.000 description 2
- 102000004190 Enzymes Human genes 0.000 description 2
- 108090000790 Enzymes Proteins 0.000 description 2
- 102000030902 Galactosyltransferase Human genes 0.000 description 2
- 108060003306 Galactosyltransferase Proteins 0.000 description 2
- DHCLVCXQIBBOPH-UHFFFAOYSA-N Glycerol 2-phosphate Chemical compound OCC(CO)OP(O)(O)=O DHCLVCXQIBBOPH-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 108010001336 Horseradish Peroxidase Proteins 0.000 description 2
- 101150077556 LMNA gene Proteins 0.000 description 2
- XUYPXLNMDZIRQH-LURJTMIESA-N N-acetyl-L-methionine Chemical compound CSCC[C@@H](C(O)=O)NC(C)=O XUYPXLNMDZIRQH-LURJTMIESA-N 0.000 description 2
- 229920003171 Poly (ethylene oxide) Polymers 0.000 description 2
- 229940123573 Protein synthesis inhibitor Drugs 0.000 description 2
- 230000018199 S phase Effects 0.000 description 2
- 239000006180 TBST buffer Substances 0.000 description 2
- 208000035199 Tetraploidy Diseases 0.000 description 2
- 231100000768 Toxicity label Toxicity 0.000 description 2
- DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 230000005856 abnormality Effects 0.000 description 2
- 229910021529 ammonia Inorganic materials 0.000 description 2
- 238000013459 approach Methods 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 230000033228 biological regulation Effects 0.000 description 2
- 210000001124 body fluid Anatomy 0.000 description 2
- 239000010839 body fluid Substances 0.000 description 2
- 210000004556 brain Anatomy 0.000 description 2
- 210000000481 breast Anatomy 0.000 description 2
- 244000309466 calf Species 0.000 description 2
- 125000004432 carbon atom Chemical group C* 0.000 description 2
- 235000011089 carbon dioxide Nutrition 0.000 description 2
- 230000022131 cell cycle Effects 0.000 description 2
- 239000013592 cell lysate Substances 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 210000004756 chromatid Anatomy 0.000 description 2
- 230000001112 coagulating effect Effects 0.000 description 2
- 238000004440 column chromatography Methods 0.000 description 2
- 238000005056 compaction Methods 0.000 description 2
- JVHIPYJQMFNCEK-UHFFFAOYSA-N cytochalasin Natural products N1C(=O)C2(C(C=CC(C)CC(C)CC=C3)OC(C)=O)C3C(O)C(=C)C(C)C2C1CC1=CC=CC=C1 JVHIPYJQMFNCEK-UHFFFAOYSA-N 0.000 description 2
- ZMAODHOXRBLOQO-UHFFFAOYSA-N cytochalasin-A Natural products N1C(=O)C23OC(=O)C=CC(=O)CCCC(C)CC=CC3C(O)C(=C)C(C)C2C1CC1=CC=CC=C1 ZMAODHOXRBLOQO-UHFFFAOYSA-N 0.000 description 2
- 238000001514 detection method Methods 0.000 description 2
- 238000010790 dilution Methods 0.000 description 2
- 239000012895 dilution Substances 0.000 description 2
- 230000008034 disappearance Effects 0.000 description 2
- 238000004043 dyeing Methods 0.000 description 2
- 210000001671 embryonic stem cell Anatomy 0.000 description 2
- 238000012407 engineering method Methods 0.000 description 2
- 229940088598 enzyme Drugs 0.000 description 2
- 230000012173 estrus Effects 0.000 description 2
- 238000012239 gene modification Methods 0.000 description 2
- 230000005017 genetic modification Effects 0.000 description 2
- 235000013617 genetically modified food Nutrition 0.000 description 2
- 235000011187 glycerol Nutrition 0.000 description 2
- 210000003783 haploid cell Anatomy 0.000 description 2
- 230000006801 homologous recombination Effects 0.000 description 2
- 238000002744 homologous recombination Methods 0.000 description 2
- WGCNASOHLSPBMP-UHFFFAOYSA-N hydroxyacetaldehyde Natural products OCC=O WGCNASOHLSPBMP-UHFFFAOYSA-N 0.000 description 2
- 238000002513 implantation Methods 0.000 description 2
- 230000003993 interaction Effects 0.000 description 2
- ICIWUVCWSCSTAQ-UHFFFAOYSA-M iodate Chemical compound [O-]I(=O)=O ICIWUVCWSCSTAQ-UHFFFAOYSA-M 0.000 description 2
- 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 2
- 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 2
- 210000004185 liver Anatomy 0.000 description 2
- 239000011159 matrix material Substances 0.000 description 2
- 239000002609 medium Substances 0.000 description 2
- 238000002844 melting Methods 0.000 description 2
- 230000008018 melting Effects 0.000 description 2
- 229930182817 methionine Natural products 0.000 description 2
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 2
- UHOVQNZJYSORNB-UHFFFAOYSA-N monobenzene Natural products C1=CC=CC=C1 UHOVQNZJYSORNB-UHFFFAOYSA-N 0.000 description 2
- 239000004570 mortar (masonry) Substances 0.000 description 2
- 239000002773 nucleotide Substances 0.000 description 2
- 125000003729 nucleotide group Chemical group 0.000 description 2
- 210000001672 ovary Anatomy 0.000 description 2
- 210000000496 pancreas Anatomy 0.000 description 2
- 150000008106 phosphatidylserines Chemical class 0.000 description 2
- 229950007002 phosphocreatine Drugs 0.000 description 2
- 230000003169 placental effect Effects 0.000 description 2
- 210000004508 polar body Anatomy 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 239000000007 protein synthesis inhibitor Substances 0.000 description 2
- 125000001453 quaternary ammonium group Chemical group 0.000 description 2
- 230000004044 response Effects 0.000 description 2
- 229920006395 saturated elastomer Polymers 0.000 description 2
- 210000003491 skin Anatomy 0.000 description 2
- PUZPDOWCWNUUKD-UHFFFAOYSA-M sodium fluoride Chemical compound [F-].[Na+] PUZPDOWCWNUUKD-UHFFFAOYSA-M 0.000 description 2
- 239000007787 solid Substances 0.000 description 2
- 230000000392 somatic effect Effects 0.000 description 2
- 210000004336 spermatogonium Anatomy 0.000 description 2
- ATHGHQPFGPMSJY-UHFFFAOYSA-N spermidine Chemical compound NCCCCNCCCN ATHGHQPFGPMSJY-UHFFFAOYSA-N 0.000 description 2
- 229940063675 spermine Drugs 0.000 description 2
- 230000008093 supporting effect Effects 0.000 description 2
- 210000001550 testis Anatomy 0.000 description 2
- JGVWCANSWKRBCS-UHFFFAOYSA-N tetramethylrhodamine thiocyanate Chemical compound [Cl-].C=12C=CC(N(C)C)=CC2=[O+]C2=CC(N(C)C)=CC=C2C=1C1=CC=C(SC#N)C=C1C(O)=O JGVWCANSWKRBCS-UHFFFAOYSA-N 0.000 description 2
- 238000009210 therapy by ultrasound Methods 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- 238000010361 transduction Methods 0.000 description 2
- 230000026683 transduction Effects 0.000 description 2
- 230000014616 translation Effects 0.000 description 2
- 238000013519 translation Methods 0.000 description 2
- 238000002054 transplantation Methods 0.000 description 2
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 2
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 2
- 238000005199 ultracentrifugation Methods 0.000 description 2
- 238000009281 ultraviolet germicidal irradiation Methods 0.000 description 2
- 238000002255 vaccination Methods 0.000 description 2
- WKVZMKDXJFCMMD-UVWUDEKDSA-L (5ar,8ar,9r)-5-[[(2r,4ar,6r,7r,8r,8as)-7,8-dihydroxy-2-methyl-4,4a,6,7,8,8a-hexahydropyrano[3,2-d][1,3]dioxin-6-yl]oxy]-9-(4-hydroxy-3,5-dimethoxyphenyl)-5a,6,8a,9-tetrahydro-5h-[2]benzofuro[6,5-f][1,3]benzodioxol-8-one;azanide;n,3-bis(2-chloroethyl)-2-ox Chemical compound [NH2-].[NH2-].Cl[Pt+2]Cl.ClCCNP1(=O)OCCCN1CCCl.COC1=C(O)C(OC)=CC([C@@H]2C3=CC=4OCOC=4C=C3C(O[C@H]3[C@@H]([C@@H](O)[C@@H]4O[C@H](C)OC[C@H]4O3)O)[C@@H]3[C@@H]2C(OC3)=O)=C1 WKVZMKDXJFCMMD-UVWUDEKDSA-L 0.000 description 1
- PXGPLTODNUVGFL-BRIYLRKRSA-N (E,Z)-(1R,2R,3R,5S)-7-(3,5-Dihydroxy-2-((3S)-(3-hydroxy-1-octenyl))cyclopentyl)-5-heptenoic acid Chemical compound CCCCC[C@H](O)C=C[C@H]1[C@H](O)C[C@H](O)[C@@H]1CC=CCCCC(O)=O PXGPLTODNUVGFL-BRIYLRKRSA-N 0.000 description 1
- UCTWMZQNUQWSLP-VIFPVBQESA-N (R)-adrenaline Chemical compound CNC[C@H](O)C1=CC=C(O)C(O)=C1 UCTWMZQNUQWSLP-VIFPVBQESA-N 0.000 description 1
- MMWCIQZXVOZEGG-UHFFFAOYSA-N 1,4,5-IP3 Natural products OC1C(O)C(OP(O)(O)=O)C(OP(O)(O)=O)C(O)C1OP(O)(O)=O MMWCIQZXVOZEGG-UHFFFAOYSA-N 0.000 description 1
- IDOQDZANRZQBTP-UHFFFAOYSA-N 2-[2-(2,4,4-trimethylpentan-2-yl)phenoxy]ethanol Chemical compound CC(C)(C)CC(C)(C)C1=CC=CC=C1OCCO IDOQDZANRZQBTP-UHFFFAOYSA-N 0.000 description 1
- UMCMPZBLKLEWAF-BCTGSCMUSA-N 3-[(3-cholamidopropyl)dimethylammonio]propane-1-sulfonate Chemical compound C([C@H]1C[C@H]2O)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC(=O)NCCC[N+](C)(C)CCCS([O-])(=O)=O)C)[C@@]2(C)[C@@H](O)C1 UMCMPZBLKLEWAF-BCTGSCMUSA-N 0.000 description 1
- 102100031912 A-kinase anchor protein 1, mitochondrial Human genes 0.000 description 1
- 206010000234 Abortion spontaneous Diseases 0.000 description 1
- 241000282979 Alces alces Species 0.000 description 1
- 208000024827 Alzheimer disease Diseases 0.000 description 1
- QGZKDVFQNNGYKY-UHFFFAOYSA-O Ammonium Chemical compound [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
- 102100021569 Apoptosis regulator Bcl-2 Human genes 0.000 description 1
- 208000023275 Autoimmune disease Diseases 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 241000283725 Bos Species 0.000 description 1
- 241000283730 Bos primigenius Species 0.000 description 1
- 241000282817 Bovidae Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 108010009575 CD55 Antigens Proteins 0.000 description 1
- 102100022002 CD59 glycoprotein Human genes 0.000 description 1
- 108091007914 CDKs Proteins 0.000 description 1
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 1
- 241000282693 Cercopithecidae Species 0.000 description 1
- 206010053567 Coagulopathies Diseases 0.000 description 1
- 229940124073 Complement inhibitor Drugs 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 102000016736 Cyclin Human genes 0.000 description 1
- 108050006400 Cyclin Proteins 0.000 description 1
- 102000003903 Cyclin-dependent kinases Human genes 0.000 description 1
- 108090000266 Cyclin-dependent kinases Proteins 0.000 description 1
- MMWCIQZXVOZEGG-XJTPDSDZSA-N D-myo-Inositol 1,4,5-trisphosphate Chemical compound O[C@@H]1[C@H](O)[C@@H](OP(O)(O)=O)[C@H](OP(O)(O)=O)[C@@H](O)[C@@H]1OP(O)(O)=O MMWCIQZXVOZEGG-XJTPDSDZSA-N 0.000 description 1
- 102000007260 Deoxyribonuclease I Human genes 0.000 description 1
- 108010008532 Deoxyribonuclease I Proteins 0.000 description 1
- 208000035240 Disease Resistance Diseases 0.000 description 1
- 101100136092 Drosophila melanogaster peng gene Proteins 0.000 description 1
- 241000196324 Embryophyta Species 0.000 description 1
- 241000283074 Equus asinus Species 0.000 description 1
- 241001331845 Equus asinus x caballus Species 0.000 description 1
- 241000283073 Equus caballus Species 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 108010043121 Green Fluorescent Proteins Proteins 0.000 description 1
- 102000004144 Green Fluorescent Proteins Human genes 0.000 description 1
- HTTJABKRGRZYRN-UHFFFAOYSA-N Heparin Chemical compound OC1C(NC(=O)C)C(O)OC(COS(O)(=O)=O)C1OC1C(OS(O)(=O)=O)C(O)C(OC2C(C(OS(O)(=O)=O)C(OC3C(C(O)C(O)C(O3)C(O)=O)OS(O)(=O)=O)C(CO)O2)NS(O)(=O)=O)C(C(O)=O)O1 HTTJABKRGRZYRN-UHFFFAOYSA-N 0.000 description 1
- 101000774717 Homo sapiens A-kinase anchor protein 1, mitochondrial Proteins 0.000 description 1
- 101000971171 Homo sapiens Apoptosis regulator Bcl-2 Proteins 0.000 description 1
- 101000897400 Homo sapiens CD59 glycoprotein Proteins 0.000 description 1
- 101000741910 Homo sapiens Protein phosphatase 1 regulatory subunit 7 Proteins 0.000 description 1
- 101000741917 Homo sapiens Serine/threonine-protein phosphatase 1 regulatory subunit 10 Proteins 0.000 description 1
- 241000701044 Human gammaherpesvirus 4 Species 0.000 description 1
- DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
- 239000000232 Lipid Bilayer Substances 0.000 description 1
- 101100496858 Mus musculus Colec12 gene Proteins 0.000 description 1
- 241000699670 Mus sp. Species 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 208000012902 Nervous system disease Diseases 0.000 description 1
- 239000000020 Nitrocellulose Substances 0.000 description 1
- 108020004485 Nonsense Codon Proteins 0.000 description 1
- 102000003789 Nuclear pore complex proteins Human genes 0.000 description 1
- 108090000163 Nuclear pore complex proteins Proteins 0.000 description 1
- 102000011931 Nucleoproteins Human genes 0.000 description 1
- 108010061100 Nucleoproteins Proteins 0.000 description 1
- 108700020796 Oncogene Proteins 0.000 description 1
- 208000018737 Parkinson disease Diseases 0.000 description 1
- 241000721454 Pemphigus Species 0.000 description 1
- 102000057297 Pepsin A Human genes 0.000 description 1
- 108090000284 Pepsin A Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 1
- 208000005155 Picornaviridae Infections Diseases 0.000 description 1
- 241000288906 Primates Species 0.000 description 1
- 102000003946 Prolactin Human genes 0.000 description 1
- 108010057464 Prolactin Proteins 0.000 description 1
- 102100038755 Protein phosphatase 1 regulatory subunit 7 Human genes 0.000 description 1
- 102000004097 Protein phosphatase inhibitor 1 Human genes 0.000 description 1
- 108090000506 Protein phosphatase inhibitor 1 Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 108700008625 Reporter Genes Proteins 0.000 description 1
- 102100038743 Serine/threonine-protein phosphatase 1 regulatory subunit 10 Human genes 0.000 description 1
- 241001665167 Solter Species 0.000 description 1
- 208000020339 Spinal injury Diseases 0.000 description 1
- 101710172711 Structural protein Proteins 0.000 description 1
- 108010017842 Telomerase Proteins 0.000 description 1
- HATRDXDCPOXQJX-UHFFFAOYSA-N Thapsigargin Natural products CCCCCCCC(=O)OC1C(OC(O)C(=C/C)C)C(=C2C3OC(=O)C(C)(O)C3(O)C(CC(C)(OC(=O)C)C12)OC(=O)CCC)C HATRDXDCPOXQJX-UHFFFAOYSA-N 0.000 description 1
- 229920004929 Triton X-114 Polymers 0.000 description 1
- 206010067584 Type 1 diabetes mellitus Diseases 0.000 description 1
- 241001416177 Vicugna pacos Species 0.000 description 1
- 241000269368 Xenopus laevis Species 0.000 description 1
- 229930183665 actinomycin Natural products 0.000 description 1
- 238000005054 agglomeration Methods 0.000 description 1
- 230000002776 aggregation Effects 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 239000005557 antagonist Substances 0.000 description 1
- 230000001857 anti-mycotic effect Effects 0.000 description 1
- 239000002543 antimycotic Substances 0.000 description 1
- 230000001640 apoptogenic effect Effects 0.000 description 1
- 239000007864 aqueous solution Substances 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 210000003719 b-lymphocyte Anatomy 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 238000010352 biotechnological method Methods 0.000 description 1
- 230000017531 blood circulation Effects 0.000 description 1
- 230000023555 blood coagulation Effects 0.000 description 1
- 230000003139 buffering effect Effects 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 150000001720 carbohydrates Chemical class 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 239000006143 cell culture medium Substances 0.000 description 1
- 238000003163 cell fusion method Methods 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 210000003855 cell nucleus Anatomy 0.000 description 1
- 230000001413 cellular effect Effects 0.000 description 1
- 230000008668 cellular reprogramming Effects 0.000 description 1
- 238000004587 chromatography analysis Methods 0.000 description 1
- 238000005352 clarification Methods 0.000 description 1
- 230000035602 clotting Effects 0.000 description 1
- 230000024203 complement activation Effects 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 239000004074 complement inhibitor Substances 0.000 description 1
- 235000020247 cow milk Nutrition 0.000 description 1
- 210000004748 cultured cell Anatomy 0.000 description 1
- 230000024835 cytogamy Effects 0.000 description 1
- 210000004292 cytoskeleton Anatomy 0.000 description 1
- 230000007850 degeneration Effects 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 230000008021 deposition Effects 0.000 description 1
- 238000011161 development Methods 0.000 description 1
- 230000018109 developmental process Effects 0.000 description 1
- 238000010586 diagram Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 238000001085 differential centrifugation Methods 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 238000007865 diluting Methods 0.000 description 1
- 238000010291 electrical method Methods 0.000 description 1
- 238000004520 electroporation Methods 0.000 description 1
- 238000005538 encapsulation Methods 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 229960005139 epinephrine Drugs 0.000 description 1
- 210000003238 esophagus Anatomy 0.000 description 1
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 description 1
- DEFVIWRASFVYLL-UHFFFAOYSA-N ethylene glycol bis(2-aminoethyl)tetraacetic acid Chemical compound OC(=O)CN(CC(O)=O)CCOCCOCCN(CC(O)=O)CC(O)=O DEFVIWRASFVYLL-UHFFFAOYSA-N 0.000 description 1
- 239000004744 fabric Substances 0.000 description 1
- 230000002349 favourable effect Effects 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 210000000232 gallbladder Anatomy 0.000 description 1
- 238000010363 gene targeting Methods 0.000 description 1
- 102000034356 gene-regulatory proteins Human genes 0.000 description 1
- 108091006104 gene-regulatory proteins Proteins 0.000 description 1
- 239000003292 glue Substances 0.000 description 1
- 239000005090 green fluorescent protein Substances 0.000 description 1
- 238000003306 harvesting Methods 0.000 description 1
- 210000002216 heart Anatomy 0.000 description 1
- 244000309465 heifer Species 0.000 description 1
- 230000002949 hemolytic effect Effects 0.000 description 1
- 229960002897 heparin Drugs 0.000 description 1
- 229920000669 heparin Polymers 0.000 description 1
- 238000004128 high performance liquid chromatography Methods 0.000 description 1
- 125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
- VVIUBCNYACGLLV-UHFFFAOYSA-N hypotaurine Chemical class [NH3+]CCS([O-])=O VVIUBCNYACGLLV-UHFFFAOYSA-N 0.000 description 1
- 230000036039 immunity Effects 0.000 description 1
- 230000003053 immunization Effects 0.000 description 1
- 238000002649 immunization Methods 0.000 description 1
- 238000003119 immunoblot Methods 0.000 description 1
- 238000001114 immunoprecipitation Methods 0.000 description 1
- 239000007943 implant Substances 0.000 description 1
- 230000008676 import Effects 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000007901 in situ hybridization Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000011065 in-situ storage Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 239000003999 initiator Substances 0.000 description 1
- 238000011081 inoculation Methods 0.000 description 1
- 238000009413 insulation Methods 0.000 description 1
- 210000000936 intestine Anatomy 0.000 description 1
- 239000002555 ionophore Substances 0.000 description 1
- 230000000236 ionophoric effect Effects 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 230000001788 irregular Effects 0.000 description 1
- 210000003734 kidney Anatomy 0.000 description 1
- YDTFRJLNMPSCFM-YDALLXLXSA-M levothyroxine sodium anhydrous Chemical compound [Na+].IC1=CC(C[C@H](N)C([O-])=O)=CC(I)=C1OC1=CC(I)=C(O)C(I)=C1 YDTFRJLNMPSCFM-YDALLXLXSA-M 0.000 description 1
- 150000002634 lipophilic molecules Chemical class 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 229940090213 lutalyse Drugs 0.000 description 1
- 230000002934 lysing effect Effects 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 229940074869 marquis Drugs 0.000 description 1
- 230000008774 maternal effect Effects 0.000 description 1
- 239000000155 melt Substances 0.000 description 1
- JZMJDSHXVKJFKW-UHFFFAOYSA-M methyl sulfate(1-) Chemical compound COS([O-])(=O)=O JZMJDSHXVKJFKW-UHFFFAOYSA-M 0.000 description 1
- 239000000178 monomer Substances 0.000 description 1
- 230000004660 morphological change Effects 0.000 description 1
- 210000000472 morula Anatomy 0.000 description 1
- 201000006417 multiple sclerosis Diseases 0.000 description 1
- 210000000663 muscle cell Anatomy 0.000 description 1
- 206010028417 myasthenia gravis Diseases 0.000 description 1
- 210000000653 nervous system Anatomy 0.000 description 1
- 230000001537 neural effect Effects 0.000 description 1
- 210000002569 neuron Anatomy 0.000 description 1
- 229920001220 nitrocellulos Polymers 0.000 description 1
- 230000037434 nonsense mutation Effects 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 239000002777 nucleoside Substances 0.000 description 1
- 150000003833 nucleoside derivatives Chemical class 0.000 description 1
- VEFJHAYOIAAXEU-UHFFFAOYSA-N okadaic acid Natural products CC(CC(O)C1OC2CCC3(CCC(O3)C=CC(C)C4CC(=CC5(OC(CC(C)(O)C(=O)O)CCC5O)O4)C)OC2C(O)C1C)C6OC7(CCCCO7)CCC6C VEFJHAYOIAAXEU-UHFFFAOYSA-N 0.000 description 1
- 125000002811 oleoyl group Chemical group O=C([*])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])/C([H])=C([H])\C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 238000005457 optimization Methods 0.000 description 1
- 229910052958 orpiment Inorganic materials 0.000 description 1
- 230000003204 osmotic effect Effects 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 238000002559 palpation Methods 0.000 description 1
- 230000003071 parasitic effect Effects 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 230000000737 periodic effect Effects 0.000 description 1
- 230000010363 phase shift Effects 0.000 description 1
- 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 1
- 239000002644 phorbol ester Substances 0.000 description 1
- 238000000053 physical method Methods 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 229920000768 polyamine Polymers 0.000 description 1
- 235000010482 polyoxyethylene sorbitan monooleate Nutrition 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 229920000053 polysorbate 80 Polymers 0.000 description 1
- VBUNOIXRZNJNAD-UHFFFAOYSA-N ponazuril Chemical compound CC1=CC(N2C(N(C)C(=O)NC2=O)=O)=CC=C1OC1=CC=C(S(=O)(=O)C(F)(F)F)C=C1 VBUNOIXRZNJNAD-UHFFFAOYSA-N 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 230000002265 prevention Effects 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 229940097325 prolactin Drugs 0.000 description 1
- 125000001436 propyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])[H] 0.000 description 1
- 210000002307 prostate Anatomy 0.000 description 1
- 238000000197 pyrolysis Methods 0.000 description 1
- 150000004728 pyruvic acid derivatives Chemical class 0.000 description 1
- 238000012797 qualification Methods 0.000 description 1
- 238000011002 quantification Methods 0.000 description 1
- 238000010791 quenching Methods 0.000 description 1
- 230000000171 quenching effect Effects 0.000 description 1
- 238000007348 radical reaction Methods 0.000 description 1
- 210000000664 rectum Anatomy 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 230000007363 regulatory process Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 230000000717 retained effect Effects 0.000 description 1
- 230000001177 retroviral effect Effects 0.000 description 1
- 201000003068 rheumatic fever Diseases 0.000 description 1
- 238000009666 routine test Methods 0.000 description 1
- 239000012266 salt solution Substances 0.000 description 1
- 238000004062 sedimentation Methods 0.000 description 1
- 238000005204 segregation Methods 0.000 description 1
- 238000013207 serial dilution Methods 0.000 description 1
- 230000035939 shock Effects 0.000 description 1
- 238000004904 shortening Methods 0.000 description 1
- 230000037432 silent mutation Effects 0.000 description 1
- 239000002356 single layer Substances 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- FHHPUSMSKHSNKW-SMOYURAASA-M sodium deoxycholate Chemical compound [Na+].C([C@H]1CC2)[C@H](O)CC[C@]1(C)[C@@H]1[C@@H]2[C@@H]2CC[C@H]([C@@H](CCC([O-])=O)C)[C@@]2(C)[C@@H](O)C1 FHHPUSMSKHSNKW-SMOYURAASA-M 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 239000011775 sodium fluoride Substances 0.000 description 1
- 235000013024 sodium fluoride Nutrition 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229940063673 spermidine Drugs 0.000 description 1
- 210000000278 spinal cord Anatomy 0.000 description 1
- 210000000952 spleen Anatomy 0.000 description 1
- 208000000995 spontaneous abortion Diseases 0.000 description 1
- 210000002784 stomach Anatomy 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- IXFPJGBNCFXKPI-FSIHEZPISA-N thapsigargin Chemical compound CCCC(=O)O[C@H]1C[C@](C)(OC(C)=O)[C@H]2[C@H](OC(=O)CCCCCCC)[C@@H](OC(=O)C(\C)=C/C)C(C)=C2[C@@H]2OC(=O)[C@@](C)(O)[C@]21O IXFPJGBNCFXKPI-FSIHEZPISA-N 0.000 description 1
- 210000001541 thymus gland Anatomy 0.000 description 1
- 238000004448 titration Methods 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 229910000406 trisodium phosphate Inorganic materials 0.000 description 1
- 235000019801 trisodium phosphate Nutrition 0.000 description 1
- IHIXIJGXTJIKRB-UHFFFAOYSA-N trisodium vanadate Chemical compound [Na+].[Na+].[Na+].[O-][V]([O-])([O-])=O IHIXIJGXTJIKRB-UHFFFAOYSA-N 0.000 description 1
- 210000000626 ureter Anatomy 0.000 description 1
- 210000003708 urethra Anatomy 0.000 description 1
- 239000002966 varnish Substances 0.000 description 1
- 230000035899 viability Effects 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Images
Classifications
-
- 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
-
- 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
- C12N15/87—Introduction of foreign genetic material using processes not otherwise provided for, e.g. co-transformation
- C12N15/873—Techniques for producing new embryos, e.g. nuclear transfer, manipulation of totipotent cells or production of chimeric embryos
- C12N15/877—Techniques for producing new mammalian cloned embryos
- C12N15/8771—Bovine embryos
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K67/00—Rearing or breeding animals, not otherwise provided for; New or modified breeds of animals
- A01K67/027—New or modified breeds of vertebrates
- A01K67/0273—Cloned vertebrates
-
- 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
- C12N15/87—Introduction of foreign genetic material using processes not otherwise provided for, e.g. co-transformation
- C12N15/873—Techniques for producing new embryos, e.g. nuclear transfer, manipulation of totipotent cells or production of chimeric embryos
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2227/00—Animals characterised by species
- A01K2227/10—Mammal
- A01K2227/101—Bovine
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2227/00—Animals characterised by species
- A01K2227/10—Mammal
- A01K2227/102—Caprine
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2227/00—Animals characterised by species
- A01K2227/10—Mammal
- A01K2227/103—Ovine
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2227/00—Animals characterised by species
- A01K2227/10—Mammal
- A01K2227/105—Murine
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2227/00—Animals characterised by species
- A01K2227/10—Mammal
- A01K2227/107—Rabbit
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2227/00—Animals characterised by species
- A01K2227/10—Mammal
- A01K2227/108—Swine
-
- A—HUMAN NECESSITIES
- A01—AGRICULTURE; FORESTRY; ANIMAL HUSBANDRY; HUNTING; TRAPPING; FISHING
- A01K—ANIMAL HUSBANDRY; AVICULTURE; APICULTURE; PISCICULTURE; FISHING; REARING OR BREEDING ANIMALS, NOT OTHERWISE PROVIDED FOR; NEW BREEDS OF ANIMALS
- A01K2267/00—Animals characterised by purpose
- A01K2267/02—Animal zootechnically ameliorated
-
- 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
- C12N2501/00—Active agents used in cell culture processes, e.g. differentation
- C12N2501/999—Small molecules not provided for elsewhere
-
- 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
- C12N2517/00—Cells related to new breeds of animals
- C12N2517/10—Conditioning of cells for in vitro fecondation or nuclear transfer
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Biomedical Technology (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Health & Medical Sciences (AREA)
- Developmental Biology & Embryology (AREA)
- Biophysics (AREA)
- Microbiology (AREA)
- Plant Pathology (AREA)
- Biochemistry (AREA)
- Molecular Biology (AREA)
- Physics & Mathematics (AREA)
- Environmental Sciences (AREA)
- Animal Behavior & Ethology (AREA)
- Animal Husbandry (AREA)
- Biodiversity & Conservation Biology (AREA)
- Veterinary Medicine (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
Description
植入 | 对照核转移 | 嵌合的核转移 | ||
受体数 | 40天妊娠 | 受体数 | 40天妊娠 | |
第1次 | 2 | 1 | 2 | 1 |
第2次 | 6 | 1 | 4 | 3 |
合计 | 8 | 2(25%) | 6 | 4(67%) |
Claims (42)
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US25815100P | 2000-12-22 | 2000-12-22 | |
US60/258,151 | 2000-12-22 |
Publications (2)
Publication Number | Publication Date |
---|---|
CN1498269A true CN1498269A (zh) | 2004-05-19 |
CN100448991C CN100448991C (zh) | 2009-01-07 |
Family
ID=22979301
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
CNB01820967XA Expired - Lifetime CN100448991C (zh) | 2000-12-22 | 2001-12-21 | 用改变程序的供体染色质或供体细胞克隆哺乳动物的方法 |
Country Status (13)
Country | Link |
---|---|
US (2) | US7253334B2 (zh) |
EP (1) | EP1356035B1 (zh) |
JP (1) | JP4420604B2 (zh) |
KR (1) | KR100832943B1 (zh) |
CN (1) | CN100448991C (zh) |
AT (1) | ATE502106T1 (zh) |
AU (1) | AU2002232858B2 (zh) |
CA (1) | CA2427322C (zh) |
DE (1) | DE60144248D1 (zh) |
HK (1) | HK1066028A1 (zh) |
MX (1) | MXPA03005624A (zh) |
NZ (1) | NZ525607A (zh) |
WO (1) | WO2002051997A1 (zh) |
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN109988745A (zh) * | 2018-01-03 | 2019-07-09 | 复旦大学 | 一种细胞核的提取方法 |
Families Citing this family (43)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US7621606B2 (en) * | 2001-08-27 | 2009-11-24 | Advanced Cell Technology, Inc. | Trans-differentiation and re-differentiation of somatic cells and production of cells for cell therapies |
US20110171185A1 (en) * | 1999-06-30 | 2011-07-14 | Klimanskaya Irina V | Genetically intact induced pluripotent cells or transdifferentiated cells and methods for the production thereof |
US20030027331A1 (en) * | 2000-11-30 | 2003-02-06 | Yan Wen Liang | Isolated homozygous stem cells, differentiated cells derived therefrom, and materials and methods for making and using same |
US20020142397A1 (en) * | 2000-12-22 | 2002-10-03 | Philippe Collas | Methods for altering cell fate |
DE60144248D1 (de) * | 2000-12-22 | 2011-04-28 | Kyowa Hakko Kirin Co Ltd | Verfahren zur klonierung von nichtmenschliche säugern unter verwendung von reprogrammiertem donorchromatin oder donorzellen |
US7491534B2 (en) * | 2000-12-22 | 2009-02-17 | Kirin Holdings Kabushiki Kaisha | Methods for altering cell fate to generate T-cells specific for an antigen of interest |
NZ568250A (en) * | 2001-01-02 | 2009-07-31 | Stemron Inc | A method for producing a population of homozygous stem cells having a pre-selected immunotype and/or genotype, cells suitable for transplant derived therefrom, and materials and methods using same |
CA2450652A1 (en) * | 2001-06-14 | 2002-12-27 | Infigen, Inc. | Methods for cloning mammals using remodeling factors |
US20030044976A1 (en) * | 2001-08-27 | 2003-03-06 | Advanced Cell Technology | De-differentiation and re-differentiation of somatic cells and production of cells for cell therapies |
US20050090004A1 (en) * | 2003-01-16 | 2005-04-28 | Sayre Chauncey B. | Stem cell maturation for all tissue lines |
US20030134422A1 (en) * | 2002-01-16 | 2003-07-17 | Sayre Chauncey Bigelow | Stem cell maturation for all tissue lines |
US20050170506A1 (en) * | 2002-01-16 | 2005-08-04 | Primegen Biotech Llc | Therapeutic reprogramming, hybrid stem cells and maturation |
EP1563084A4 (en) | 2002-11-08 | 2006-03-01 | Hematech Llc | TRANSGENE UNGULATES WITH REDUCED PRION PROTEIN ACTIVITY AND USES THEREOF |
US20060037086A1 (en) * | 2003-04-09 | 2006-02-16 | Schatten Gerald P | Methods for correcting mitotic spindle defects and optimizing preimplantation embryonic developmental rates associated with somatic cell nuclear transfer in animals |
KR20060057528A (ko) * | 2003-04-09 | 2006-05-26 | 마제-위민스 헬스 코퍼레이션 | 동물에서 체세포 핵 전이와 연관된 유사분열 방추 결함을교정하는 방법 |
FR2855183B1 (fr) * | 2003-05-23 | 2005-08-12 | Agronomique Inst Nat Rech | Procede de clonage du rat par transfert nucleaire |
EP1749102A4 (en) | 2004-04-22 | 2009-02-25 | Kirin Pharma Kk | TRANSGENIC ANIMALS AND USES THEREOF |
FR2885368A1 (fr) * | 2005-05-04 | 2006-11-10 | Fred Zacouto | Systemes et procedes de regeneration cellulaire et utilisations de telles cellules regenerees |
EP1984487B1 (en) | 2005-08-03 | 2022-10-12 | Astellas Institute for Regenerative Medicine | Improved methods of reprogramming animal somatic cells |
WO2007058401A1 (en) * | 2005-11-18 | 2007-05-24 | Imgen Co., Ltd. | Composition comprising okadaic acid for undifferentiated proliferation of embryonic stem cells |
KR100710008B1 (ko) * | 2006-02-02 | 2007-04-23 | 충남대학교산학협력단 | Streptolysin O의 체세포 처리에 의한 복제효율 증진 방법 |
EP2101724B1 (en) * | 2006-05-11 | 2020-12-02 | Regenics AS | Administration of cellular extracts for rejuvenation |
EP2049677B1 (en) * | 2006-08-10 | 2011-07-20 | Merck Patent GmbH | Method for isolating cells |
US20090111184A1 (en) * | 2007-10-24 | 2009-04-30 | Searete Llc, A Limited Liability Corporation Of The State Of Delaware | Chromosome selection |
US20090111764A1 (en) * | 2007-10-25 | 2009-04-30 | Searete Llc, A Limited Liability Corporation Of The State Of Delaware | Mitochondrial selection |
US20090111185A1 (en) * | 2007-10-26 | 2009-04-30 | Searete Llc, A Limited Liability Corporation Of The State Of Delaware | Female genome selection |
DK2296676T3 (en) | 2008-05-09 | 2016-12-19 | Regenics As | cellular extracts |
WO2011062207A1 (ja) | 2009-11-17 | 2011-05-26 | 協和発酵キリン株式会社 | ヒト人工染色体ベクター |
US9420770B2 (en) | 2009-12-01 | 2016-08-23 | Indiana University Research & Technology Corporation | Methods of modulating thrombocytopenia and modified transgenic pigs |
EP2566583B1 (en) | 2010-05-06 | 2018-07-11 | Regenics AS | Process for preparing fish egg cellular extract |
EP2630232A4 (en) | 2010-10-22 | 2014-04-02 | Biotime Inc | METHOD FOR MODIFYING TRANSCRIPTIONAL REGULATORY NETWORKS IN STEM CELLS |
EP2701727B1 (en) | 2011-03-04 | 2019-05-08 | The Regents of The University of California | Locally released growth factors to mediate motor recovery after stroke |
US10865383B2 (en) | 2011-07-12 | 2020-12-15 | Lineage Cell Therapeutics, Inc. | Methods and formulations for orthopedic cell therapy |
EP2716751A1 (en) | 2012-10-08 | 2014-04-09 | BioTime, Inc. | Differentiated progeny of clonal progenitor cell lines |
KR101662734B1 (ko) * | 2012-11-08 | 2016-10-06 | 한국생명공학연구원 | 스트렙토라이신 o의 처리에 의한 형질전환 동물의 생산성 향상 방법 |
CA2894448C (en) | 2012-12-10 | 2019-09-17 | Regenics As | Use of cellular extracts for skin rejuvenation |
EP3003290B1 (en) | 2013-06-05 | 2021-03-10 | AgeX Therapeutics, Inc. | Compositions for use in the treatment of wounds in mammalian species |
US11078462B2 (en) | 2014-02-18 | 2021-08-03 | ReCyte Therapeutics, Inc. | Perivascular stromal cells from primate pluripotent stem cells |
US10240127B2 (en) | 2014-07-03 | 2019-03-26 | ReCyte Therapeutics, Inc. | Exosomes from clonal progenitor cells |
US11072649B2 (en) | 2015-11-25 | 2021-07-27 | Sab, Llc | Systems and methods for the production of human polyclonal antibodies |
AU2016366158B2 (en) | 2015-12-07 | 2023-02-23 | Agex Therapeutics, Inc. | Methods for the re-derivation of diverse pluripotent stem cell-derived brown fat cells |
CN106489843A (zh) * | 2016-11-14 | 2017-03-15 | 深圳职业技术学院 | 一种可无需解剖判断黄喉拟水龟胚胎发育时相的方法 |
EP4204005A1 (en) | 2020-08-31 | 2023-07-05 | Sab, Llc | Ungulate-derived polyclonal immunoglobulin specific for coronavirus protein and uses thereof |
Family Cites Families (100)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CA1293460C (en) | 1985-10-07 | 1991-12-24 | Brian Lee Sauer | Site-specific recombination of dna in yeast |
US4994384A (en) | 1986-12-31 | 1991-02-19 | W. R. Grace & Co.-Conn. | Multiplying bovine embryos |
US5470560A (en) | 1987-01-20 | 1995-11-28 | Genentech, Inc. | Method for evaluating immunogenicity |
EP0832981A1 (en) | 1987-02-17 | 1998-04-01 | Pharming B.V. | DNA sequences to target proteins to the mammary gland for efficient secretion |
US5057420A (en) | 1987-06-05 | 1991-10-15 | Granada Biosciences, Inc. | Bovine nuclear transplantation |
US4873316A (en) | 1987-06-23 | 1989-10-10 | Biogen, Inc. | Isolation of exogenous recombinant proteins from the milk of transgenic mammals |
US5750172A (en) | 1987-06-23 | 1998-05-12 | Pharming B.V. | Transgenic non human mammal milk |
US5202238A (en) | 1987-10-27 | 1993-04-13 | Oncogen | Production of chimeric antibodies by homologous recombination |
US5213979A (en) | 1987-12-30 | 1993-05-25 | W. R. Grace & Co.-Conn. | In vitro culture of bovine embryos |
GB8823869D0 (en) | 1988-10-12 | 1988-11-16 | Medical Res Council | Production of antibodies |
US5175384A (en) | 1988-12-05 | 1992-12-29 | Genpharm International | Transgenic mice depleted in mature t-cells and methods for making transgenic mice |
US5464764A (en) | 1989-08-22 | 1995-11-07 | University Of Utah Research Foundation | Positive-negative selection methods and vectors |
US5633076A (en) | 1989-12-01 | 1997-05-27 | Pharming Bv | Method of producing a transgenic bovine or transgenic bovine embryo |
DE4000939A1 (de) | 1990-01-15 | 1991-07-18 | Brem Gottfried Prof Dr Dr | Verfahren zur antikoerpergewinnung |
US5160312A (en) | 1990-02-09 | 1992-11-03 | W. R. Grace & Co.-Conn. | Cryopreservation process for direct transfer of embryos |
US5614396A (en) | 1990-06-14 | 1997-03-25 | Baylor College Of Medicine | Methods for the genetic modification of endogenous genes in animal cells by homologous recombination |
US5096822A (en) * | 1990-07-26 | 1992-03-17 | W. R. Grace & Co.- Conn. | Bovine embryo medium |
US5453366A (en) | 1990-07-26 | 1995-09-26 | Sims; Michele M. | Method of cloning bovine embryos |
KR100272077B1 (ko) | 1990-08-29 | 2000-11-15 | 젠팜인터내셔날,인코포레이티드 | 이종 항체를 생산할 수 있는 전이유전자를 가진 인간이외의 동물 |
US5661016A (en) | 1990-08-29 | 1997-08-26 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
US6300129B1 (en) | 1990-08-29 | 2001-10-09 | Genpharm International | Transgenic non-human animals for producing heterologous antibodies |
DE69133557D1 (de) | 1990-08-29 | 2007-03-15 | Pharming Intellectual Pty Bv | Homologe rekombination in säugetier-zellen |
US5633425A (en) | 1990-08-29 | 1997-05-27 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
US5625126A (en) | 1990-08-29 | 1997-04-29 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
US5545806A (en) | 1990-08-29 | 1996-08-13 | Genpharm International, Inc. | Ransgenic non-human animals for producing heterologous antibodies |
US5770429A (en) | 1990-08-29 | 1998-06-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
US5814318A (en) | 1990-08-29 | 1998-09-29 | Genpharm International Inc. | Transgenic non-human animals for producing heterologous antibodies |
US5874299A (en) | 1990-08-29 | 1999-02-23 | Genpharm International, Inc. | Transgenic non-human animals capable of producing heterologous antibodies |
US5789650A (en) | 1990-08-29 | 1998-08-04 | Genpharm International, Inc. | Transgenic non-human animals for producing heterologous antibodies |
US5877397A (en) | 1990-08-29 | 1999-03-02 | Genpharm International Inc. | Transgenic non-human animals capable of producing heterologous antibodies of various isotypes |
WO1992015694A1 (en) | 1991-03-08 | 1992-09-17 | The Salk Institute For Biological Studies | Flp-mediated gene modification in mammalian cells, and compositions and cells useful therefor |
US5240840A (en) | 1991-04-05 | 1993-08-31 | Regents Of The University Of Michigan | Dna superfragment cloning |
WO1993004169A1 (en) | 1991-08-20 | 1993-03-04 | Genpharm International, Inc. | Gene targeting in animal cells using isogenic dna constructs |
WO1993007266A1 (en) | 1991-10-07 | 1993-04-15 | Idaho Research Foundation, Inc. | Genetic construct for selection of homologous recombinants on a single selective medium |
ATE288484T1 (de) | 1991-11-14 | 2005-02-15 | Charles Weissmann | Transgene nicht-menschliche tiere ohne prionprotein |
WO1993015191A1 (en) | 1992-01-24 | 1993-08-05 | Life Technologies, Inc. | Modulation of enzyme activities in the in vivo cloning of dna |
US5843643A (en) | 1992-02-21 | 1998-12-01 | Ratner; Paul L. | Site-specific transfection of eukaryotic cells using polypeptide-linked recombinant nucleic acid |
US5763240A (en) | 1992-04-24 | 1998-06-09 | Sri International | In vivo homologous sequence targeting in eukaryotic cells |
US5654183A (en) | 1992-07-27 | 1997-08-05 | California Institute Of Technology | Genetically engineered mammalian neural crest stem cells |
US6107543A (en) | 1992-08-20 | 2000-08-22 | Infigen, Inc. | Culture of totipotent embryonic inner cells mass cells and production of bovine animals |
US5480772A (en) | 1993-02-03 | 1996-01-02 | Brandeis University | In vitro activation of a nucleus |
US5496720A (en) | 1993-02-10 | 1996-03-05 | Susko-Parrish; Joan L. | Parthenogenic oocyte activation |
JP4038236B2 (ja) | 1993-03-16 | 2008-01-23 | オースチン・リサーチ・インスティテュート | 異種移植治療におけるブタGa1α(1,3)ガラクトシルトランスフェラーゼの使用 |
EP0733059B1 (en) | 1993-12-09 | 2000-09-13 | Thomas Jefferson University | Compounds and methods for site-directed mutations in eukaryotic cells |
US5827690A (en) | 1993-12-20 | 1998-10-27 | Genzyme Transgenics Corporatiion | Transgenic production of antibodies in milk |
US6001654A (en) | 1994-01-28 | 1999-12-14 | California Institute Of Technology | Methods for differentiating neural stem cells to neurons or smooth muscle cells using TGT-β super family growth factors |
DE69535752D1 (de) | 1994-04-13 | 2008-06-26 | Biotransplant Inc | Alpha(1,3)galactosyltransferase-negatives schwein |
US5723331A (en) | 1994-05-05 | 1998-03-03 | Genzyme Corporation | Methods and compositions for the repair of articular cartilage defects in mammals |
US5583016A (en) | 1994-07-07 | 1996-12-10 | Geron Corporation | Mammalian telomerase |
US5876979A (en) | 1994-07-07 | 1999-03-02 | Cold Spring Harbor Laboratory | RNA component of mouse, rat, Chinese hamster and bovine telomerase |
US5780296A (en) | 1995-01-17 | 1998-07-14 | Thomas Jefferson University | Compositions and methods to promote homologous recombination in eukaryotic cells and organisms |
US5776744A (en) | 1995-06-07 | 1998-07-07 | Yale University | Methods and compositions for effecting homologous recombination |
US5952222A (en) | 1995-08-04 | 1999-09-14 | The Board Of Trustees Of The University Of Arkansas | Functional enucleation of bovine oocytes |
US5733730A (en) | 1995-08-25 | 1998-03-31 | The Rockefeller University | Telomere repeat binding factor and diagnostic and therapeutic use thereof |
US7307198B2 (en) * | 1995-08-31 | 2007-12-11 | Roslin Institute | Ungulates produced by nuclear transfer of G1 cells |
US5695977A (en) | 1995-08-31 | 1997-12-09 | Genetic Information Research Institute | Site directed recombination |
GB9517779D0 (en) * | 1995-08-31 | 1995-11-01 | Roslin Inst Edinburgh | Biological manipulation |
GB9517780D0 (en) * | 1995-08-31 | 1995-11-01 | Roslin Inst Edinburgh | Biological manipulation |
US5801030A (en) | 1995-09-01 | 1998-09-01 | Genvec, Inc. | Methods and vectors for site-specific recombination |
JP2848286B2 (ja) * | 1995-09-29 | 1999-01-20 | ヤマハ株式会社 | カラオケ装置 |
US5679523A (en) | 1995-11-16 | 1997-10-21 | The Board Of Trustees Of The Leland Stanford Junior University | Method for concurrent disruption of expression of multiple alleles of mammalian genes |
US20060021070A1 (en) * | 1996-04-01 | 2006-01-26 | University of Massachusetts, a Public Institution of Higher Education of the Commonwealth of MA | Production of chimeric bovine or porcine animals using cultured inner cell mass |
US5905042A (en) | 1996-04-01 | 1999-05-18 | University Of Massachusetts, A Public Institution Of Higher Education Of The Commonwealth Of Massachusetts, As Represented By Its Amherst Campus | Cultured inner cell mass cell lines derived from bovine or porcine embryos |
US5770422A (en) | 1996-07-08 | 1998-06-23 | The Regents Of The University Of California | Human telomerase |
US20020194637A1 (en) * | 2001-06-06 | 2002-12-19 | University Of Massachussetts | Embryonic or stem-like cell lines produced by cross species nuclear transplantation |
JP2002511732A (ja) * | 1996-10-11 | 2002-04-16 | ザ・テキサス・エイ・アンド・エム・ユニヴァーシティ・システム | トランスジェニック動物を発生させるための組成物および方法 |
US20010039667A1 (en) * | 1997-01-10 | 2001-11-08 | University Of Massachusetts | Cloned ungulate embryos and animals, use of cells, tissues and organs thereof for transplantation therapies including parkinson's disease |
US6215041B1 (en) * | 1997-01-10 | 2001-04-10 | University Of Mmassachusetts | Cloning using donor nuclei from a non-quiesecent somatic cells |
US5945577A (en) * | 1997-01-10 | 1999-08-31 | University Of Massachusetts As Represented By Its Amherst Campus | Cloning using donor nuclei from proliferating somatic cells |
US20020012655A1 (en) * | 1997-01-10 | 2002-01-31 | Steven L. Stice | Cloned ungulate embryos and animals, use of cells, tissues and organs thereof for transplantation therapies including parkinson's disease |
US6235969B1 (en) * | 1997-01-10 | 2001-05-22 | University Of Massachusetts | Cloning pigs using donor nuclei from non-quiescent differentiated cells |
US6011197A (en) * | 1997-03-06 | 2000-01-04 | Infigen, Inc. | Method of cloning bovines using reprogrammed non-embryonic bovine cells |
US5830698A (en) | 1997-03-14 | 1998-11-03 | Idec Pharmaceuticals Corporation | Method for integrating genes at specific sites in mammalian cells via homologous recombination and vectors for accomplishing the same |
AU7979098A (en) * | 1997-06-18 | 1999-01-04 | Curators Of The University Of Missouri, The | Complete activation of mammalian oocytes |
CN101003800A (zh) * | 1997-07-03 | 2007-07-25 | 马萨诸塞大学 | 使用来自无血清饥饿的分化细胞的供体细胞核进行克隆 |
US20020019993A1 (en) * | 1998-01-21 | 2002-02-14 | Teruhiko Wakayama | Full term development of animals from enucleated oocytes reconstituted with adult somatic cell nuclei |
WO1999041403A1 (en) * | 1998-02-12 | 1999-08-19 | The Regents Of The University Of California | Compositions for receptor/liposome mediated transfection and methods of using same |
US6258998B1 (en) | 1998-11-24 | 2001-07-10 | Infigen, Inc. | Method of cloning porcine animals |
US20020012660A1 (en) | 1999-03-04 | 2002-01-31 | Alan Colman | Method of preparing a somatic cells for nuclear transfer |
NZ515890A (en) * | 1999-05-06 | 2004-07-30 | Stem Cell Sciences Pty Ltd | Preparing a reprogrammed diploid cell by nuclear addition where the donor nucleus is placed into an intact cell and exposed to reprogramming factors |
AUPQ025999A0 (en) * | 1999-05-10 | 1999-06-03 | Garelag Pty Ltd | Non enucleation and enucleation post fusion of nuclear transfer embryos |
AU782286B2 (en) * | 1999-06-30 | 2005-07-14 | Advanced Cell Technology, Inc. | Cytoplasmic transfer to de-differentiate recipient cells |
US20030129745A1 (en) * | 1999-10-28 | 2003-07-10 | Robl James M. | Gynogenetic or androgenetic production of pluripotent cells and cell lines, and use thereof to produce differentiated cells and tissues |
CA2388510A1 (en) * | 1999-11-02 | 2001-05-10 | James M. Robl | Use of haploid genomes for genetic diagnosis, modification and multiplication |
US7414170B2 (en) * | 1999-11-19 | 2008-08-19 | Kirin Beer Kabushiki Kaisha | Transgenic bovines capable of human antibody production |
US7074983B2 (en) * | 1999-11-19 | 2006-07-11 | Kirin Beer Kabushiki Kaisha | Transgenic bovine comprising human immunoglobulin loci and producing human immunoglobulin |
AU2103601A (en) * | 1999-12-17 | 2001-06-25 | Oregon Health And Science University | Methods for producing transgenic animals |
CA2396210A1 (en) * | 2000-01-04 | 2001-07-12 | Chikara Kubota | Method for cloning animals with targetted genetic alterations by transfer_of long-term cultured male or female somatic cell nuclei, comprising artificially-induced genetic alterations, to enucleated recipient cells |
CA2403344C (en) * | 2000-03-15 | 2013-05-21 | The University Of Georgia Research Foundation, Inc. | Effective nuclear reprogramming in mammals |
BR0109521A (pt) * | 2000-03-24 | 2003-06-10 | Univ Massachusetts Public Inst | Ungulados transgênicos sem prìons |
AU2001294851B2 (en) * | 2000-09-28 | 2007-06-14 | Sangamo Biosciences, Inc. | Nuclear reprogramming using IWSI and related chromatin remodeling atpases |
US7491534B2 (en) * | 2000-12-22 | 2009-02-17 | Kirin Holdings Kabushiki Kaisha | Methods for altering cell fate to generate T-cells specific for an antigen of interest |
DE60144248D1 (de) * | 2000-12-22 | 2011-04-28 | Kyowa Hakko Kirin Co Ltd | Verfahren zur klonierung von nichtmenschliche säugern unter verwendung von reprogrammiertem donorchromatin oder donorzellen |
US20020142397A1 (en) * | 2000-12-22 | 2002-10-03 | Philippe Collas | Methods for altering cell fate |
JP2002262716A (ja) * | 2001-03-07 | 2002-09-17 | National Agricultural Research Organization | 株化細胞を用いて家畜個体を作出する方法 |
US20030027330A1 (en) * | 2001-04-02 | 2003-02-06 | Robert Lanza | Method for facilitating the production of differentiated cell types and tissues from embryonic and adult pluripotent and multipotent cells |
US20060083722A1 (en) * | 2001-07-18 | 2006-04-20 | Advanced Cell Technology, Inc | Methods and compositions for cell therapy |
US20040139489A1 (en) * | 2001-10-05 | 2004-07-15 | Robert Lanza | Method for generating cloned animals using chromosome shuffling |
WO2003100011A2 (en) * | 2002-05-23 | 2003-12-04 | Advanced Cell Technology, Inc. | Generation of histocompatible tissues using nuclear transplantation |
JP2004221836A (ja) * | 2003-01-14 | 2004-08-05 | Ricoh Co Ltd | 画像処理装置、プログラム、記憶媒体及び符号伸長方法 |
-
2001
- 2001-12-21 DE DE60144248T patent/DE60144248D1/de not_active Expired - Lifetime
- 2001-12-21 US US10/032,191 patent/US7253334B2/en not_active Expired - Lifetime
- 2001-12-21 KR KR1020037008319A patent/KR100832943B1/ko active IP Right Grant
- 2001-12-21 EP EP01992388A patent/EP1356035B1/en not_active Expired - Lifetime
- 2001-12-21 CA CA2427322A patent/CA2427322C/en not_active Expired - Lifetime
- 2001-12-21 AT AT01992388T patent/ATE502106T1/de not_active IP Right Cessation
- 2001-12-21 AU AU2002232858A patent/AU2002232858B2/en not_active Expired
- 2001-12-21 CN CNB01820967XA patent/CN100448991C/zh not_active Expired - Lifetime
- 2001-12-21 JP JP2002553478A patent/JP4420604B2/ja not_active Expired - Lifetime
- 2001-12-21 NZ NZ525607A patent/NZ525607A/en not_active IP Right Cessation
- 2001-12-21 MX MXPA03005624A patent/MXPA03005624A/es active IP Right Grant
- 2001-12-21 WO PCT/US2001/050406 patent/WO2002051997A1/en active IP Right Grant
-
2004
- 2004-11-15 HK HK04109008.7A patent/HK1066028A1/xx not_active IP Right Cessation
-
2006
- 2006-05-24 US US11/439,788 patent/US20060212952A1/en not_active Abandoned
Cited By (1)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
CN109988745A (zh) * | 2018-01-03 | 2019-07-09 | 复旦大学 | 一种细胞核的提取方法 |
Also Published As
Publication number | Publication date |
---|---|
JP2004516835A (ja) | 2004-06-10 |
KR20030082555A (ko) | 2003-10-22 |
WO2002051997A1 (en) | 2002-07-04 |
US7253334B2 (en) | 2007-08-07 |
ATE502106T1 (de) | 2011-04-15 |
US20030046722A1 (en) | 2003-03-06 |
MXPA03005624A (es) | 2004-12-03 |
EP1356035B1 (en) | 2011-03-16 |
CN100448991C (zh) | 2009-01-07 |
AU2002232858B2 (en) | 2007-01-11 |
NZ525607A (en) | 2005-05-27 |
EP1356035A1 (en) | 2003-10-29 |
KR100832943B1 (ko) | 2008-05-27 |
HK1066028A1 (en) | 2005-03-11 |
US20060212952A1 (en) | 2006-09-21 |
EP1356035A4 (en) | 2004-07-28 |
JP4420604B2 (ja) | 2010-02-24 |
CA2427322C (en) | 2012-03-06 |
CA2427322A1 (en) | 2002-07-04 |
DE60144248D1 (de) | 2011-04-28 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
CN1498269A (zh) | 用改变程序的供体染色质或供体细胞克隆哺乳动物的方法 | |
CN1200107C (zh) | 以成年体细胞胞核重建的去核卵母细胞足月发育成动物 | |
Galli et al. | Mammalian leukocytes contain all the genetic information necessary for the development of a new individual | |
Ogura et al. | Behaviour of hamster and mouse round spermatid nuclei incorporated into mature oocytes by electrofusion | |
CN1524121A (zh) | 一种核转移的方法 | |
AU2002232858A1 (en) | Methods for cloning mammals using reprogrammed donor chromatin or donor cells | |
CN1334870A (zh) | 通过胞质内精子注射进行哺乳动物基因转移 | |
Bui et al. | The cytoplasm of mouse germinal vesicle stage oocytes can enhance somatic cell nuclear reprogramming | |
Park et al. | Assisted reproductive techniques and genetic manipulation in the common marmoset | |
CN1280412C (zh) | 产生克隆胚胎和其子代的方法以及由所述方法生产的细胞 | |
CN1425064A (zh) | 通过交叉物种核移植制备的胚胎或干样细胞 | |
Ross et al. | Bovine somatic cell nuclear transfer | |
Sparman et al. | Cloning of non-human primates: the road “less traveled by” | |
CN1299408A (zh) | 通过异种间的核移植产生的胚细胞或干细胞样细胞系 | |
CN1298841C (zh) | 重建胚胎中核转移后融合和活化的方法和系统 | |
CN1447854A (zh) | 来自猿猴的胚胎干细胞 | |
CN1399513A (zh) | 用于核移植的供体细胞的制备和选择 | |
CN1293188C (zh) | 一种将长期培养的可包括人工诱导基因改变的雌或雄体细胞的细胞核转移到去核受体细胞中实现靶向基因改变的克隆动物的方法 | |
Navarro-Serna et al. | Generation of Calpain-3 knock-out porcine embryos by CRISPR-Cas9 electroporation and intracytoplasmic microinjection of oocytes before insemination | |
CN1735338A (zh) | 利用体细胞核转移胚胎作为细胞供体进行附加核转移的方法和系统 | |
CN1284851C (zh) | 体细胞起源的胚胎干细胞及其分化细胞 | |
CN1650003A (zh) | 选择用于哺乳动物种中核转移的细胞系的方法 | |
KR20060057528A (ko) | 동물에서 체세포 핵 전이와 연관된 유사분열 방추 결함을교정하는 방법 | |
CN1423565A (zh) | 精子因子oscillogenin | |
Evecen et al. | Somatic cloning in cats using MI or MII oocytes |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
C06 | Publication | ||
PB01 | Publication | ||
C10 | Entry into substantive examination | ||
SE01 | Entry into force of request for substantive examination | ||
REG | Reference to a national code |
Ref country code: HK Ref legal event code: DE Ref document number: 1066028 Country of ref document: HK |
|
ASS | Succession or assignment of patent right |
Owner name: KIRIN BEER K.K. Free format text: FORMER OWNER: HEMA TECHNOLOGY CO.,LTD. Effective date: 20070608 |
|
C41 | Transfer of patent application or patent right or utility model | ||
TA01 | Transfer of patent application right |
Effective date of registration: 20070608 Address after: Tokyo, Japan, Japan Applicant after: Kirin Beer Co., Ltd. Address before: American Connecticut Applicant before: Hemr technology company |
|
ASS | Succession or assignment of patent right |
Owner name: KIRIN MEDICINE CO., LTD. Free format text: FORMER OWNER: QILIN CO., LTD. Effective date: 20080201 |
|
C41 | Transfer of patent application or patent right or utility model | ||
TA01 | Transfer of patent application right |
Effective date of registration: 20080201 Address after: Tokyo, Japan, Japan Applicant after: Kirin Pharma Kabushiki Kaisha Address before: Tokyo, Japan, Japan Applicant before: Kirin Holdings Kabushiki Kaish (JP) |
|
C14 | Grant of patent or utility model | ||
GR01 | Patent grant | ||
REG | Reference to a national code |
Ref country code: HK Ref legal event code: GR Ref document number: 1066028 Country of ref document: HK |
|
C56 | Change in the name or address of the patentee |
Owner name: XIEHE FERMENTATION QILIN CO., LTD. Free format text: FORMER NAME: QILIN MEDICINE CO., LTD. |
|
CP01 | Change in the name or title of a patent holder |
Address after: Tokyo, Japan, Japan Patentee after: Kyowa Hakko Kirin Co., Ltd. Address before: Tokyo, Japan, Japan Patentee before: Kirin Pharma Kabushiki Kaisha |
|
ASS | Succession or assignment of patent right |
Owner name: XIEHE FERMENTATION QILIN CO., LTD. Free format text: FORMER OWNER: QILIN MEDICINE CO., LTD. Effective date: 20091127 |
|
C41 | Transfer of patent application or patent right or utility model | ||
TR01 | Transfer of patent right |
Effective date of registration: 20091127 Address after: Tokyo, Japan, Japan Patentee after: Kyowa Hakko Kirin Co., Ltd. Address before: Tokyo, Japan, Japan Patentee before: Kirin Pharma Kabushiki Kaisha |
|
ASS | Succession or assignment of patent right |
Owner name: SANFORD APPLIED BIOLOGICAL SCIENCES CO., LTD. Free format text: FORMER OWNER: KYOWA HAKKO KIRIN CO., LTD. Effective date: 20130515 |
|
C41 | Transfer of patent application or patent right or utility model | ||
TR01 | Transfer of patent right |
Effective date of registration: 20130515 Address after: South Dakota Patentee after: Sanford Applied Bioscience Ltd Address before: Tokyo, Japan, Japan Patentee before: Kyowa Hakko Kirin Co., Ltd. |
|
C56 | Change in the name or address of the patentee |
Owner name: SAB LLC Free format text: FORMER NAME: SANFORD APPLIED BIOLOGICAL SCIENCES CO., LTD. |
|
CP01 | Change in the name or title of a patent holder |
Address after: South Dakota Patentee after: SAB limited liability company Address before: South Dakota Patentee before: Sanford Applied Bioscience Ltd |
|
CX01 | Expiry of patent term | ||
CX01 | Expiry of patent term |
Granted publication date: 20090107 |