NO319706B1 - Protein med luciferaseaktivitet, DNA, vektor, celle, provekit samt analysemetode. - Google Patents
Protein med luciferaseaktivitet, DNA, vektor, celle, provekit samt analysemetode. Download PDFInfo
- Publication number
- NO319706B1 NO319706B1 NO19963983A NO963983A NO319706B1 NO 319706 B1 NO319706 B1 NO 319706B1 NO 19963983 A NO19963983 A NO 19963983A NO 963983 A NO963983 A NO 963983A NO 319706 B1 NO319706 B1 NO 319706B1
- Authority
- NO
- Norway
- Prior art keywords
- amino acid
- stated
- protein
- luciferase
- dna
- Prior art date
Links
- 108060001084 Luciferase Proteins 0.000 title claims abstract description 86
- 239000005089 Luciferase Substances 0.000 title claims abstract description 60
- 230000000694 effects Effects 0.000 title claims abstract description 37
- 108090000623 proteins and genes Proteins 0.000 title claims description 78
- 102000004169 proteins and genes Human genes 0.000 title claims description 51
- 239000013598 vector Substances 0.000 title claims description 24
- 238000003556 assay Methods 0.000 title abstract description 3
- 150000001413 amino acids Chemical group 0.000 claims description 48
- 235000018102 proteins Nutrition 0.000 claims description 48
- 235000001014 amino acid Nutrition 0.000 claims description 47
- 229940024606 amino acid Drugs 0.000 claims description 46
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims description 21
- 235000013922 glutamic acid Nutrition 0.000 claims description 21
- 239000004220 glutamic acid Substances 0.000 claims description 21
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 claims description 20
- 241000588724 Escherichia coli Species 0.000 claims description 17
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 claims description 16
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 16
- 239000004472 Lysine Substances 0.000 claims description 16
- 235000018977 lysine Nutrition 0.000 claims description 16
- 238000004458 analytical method Methods 0.000 claims description 15
- IGXWBGJHJZYPQS-SSDOTTSWSA-N D-Luciferin Chemical compound OC(=O)[C@H]1CSC(C=2SC3=CC=C(O)C=C3N=2)=N1 IGXWBGJHJZYPQS-SSDOTTSWSA-N 0.000 claims description 14
- 241000254064 Photinus pyralis Species 0.000 claims description 13
- CYCGRDQQIOGCKX-UHFFFAOYSA-N Dehydro-luciferin Natural products OC(=O)C1=CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 CYCGRDQQIOGCKX-UHFFFAOYSA-N 0.000 claims description 10
- BJGNCJDXODQBOB-UHFFFAOYSA-N Fivefly Luciferin Natural products OC(=O)C1CSC(C=2SC3=CC(O)=CC=C3N=2)=N1 BJGNCJDXODQBOB-UHFFFAOYSA-N 0.000 claims description 10
- DDWFXDSYGUXRAY-UHFFFAOYSA-N Luciferin Natural products CCc1c(C)c(CC2NC(=O)C(=C2C=C)C)[nH]c1Cc3[nH]c4C(=C5/NC(CC(=O)O)C(C)C5CC(=O)O)CC(=O)c4c3C DDWFXDSYGUXRAY-UHFFFAOYSA-N 0.000 claims description 10
- 241000254060 Aquatica lateralis Species 0.000 claims description 9
- 108020004705 Codon Proteins 0.000 claims description 9
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 claims description 9
- 229960003136 leucine Drugs 0.000 claims description 9
- 239000004471 Glycine Substances 0.000 claims description 8
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 claims description 8
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims description 8
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 claims description 8
- 241000254054 Luciola cruciata Species 0.000 claims description 8
- 241001124207 Luciola mingrelica Species 0.000 claims description 8
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 claims description 8
- 235000013930 proline Nutrition 0.000 claims description 8
- 101000622060 Photinus pyralis Luciferin 4-monooxygenase Proteins 0.000 claims description 7
- 235000003704 aspartic acid Nutrition 0.000 claims description 7
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims description 7
- 238000002741 site-directed mutagenesis Methods 0.000 claims description 6
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 claims description 5
- KZSNJWFQEVHDMF-BYPYZUCNSA-N L-valine Chemical compound CC(C)[C@H](N)C(O)=O KZSNJWFQEVHDMF-BYPYZUCNSA-N 0.000 claims description 5
- KZSNJWFQEVHDMF-UHFFFAOYSA-N Valine Natural products CC(C)C(N)C(O)=O KZSNJWFQEVHDMF-UHFFFAOYSA-N 0.000 claims description 5
- 125000000539 amino acid group Chemical group 0.000 claims description 5
- 230000002209 hydrophobic effect Effects 0.000 claims description 5
- 229960000310 isoleucine Drugs 0.000 claims description 5
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 claims description 5
- 229960004295 valine Drugs 0.000 claims description 5
- 239000004474 valine Substances 0.000 claims description 5
- 239000004475 Arginine Substances 0.000 claims description 4
- 235000009697 arginine Nutrition 0.000 claims description 4
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 4
- 239000003153 chemical reaction reagent Substances 0.000 claims description 4
- 125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 claims description 4
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 claims description 3
- 241000238631 Hexapoda Species 0.000 claims description 3
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 claims description 3
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 claims description 3
- 235000009582 asparagine Nutrition 0.000 claims description 3
- 229960001230 asparagine Drugs 0.000 claims description 3
- 238000005259 measurement Methods 0.000 claims description 3
- 239000002773 nucleotide Substances 0.000 claims description 3
- 125000003729 nucleotide group Chemical group 0.000 claims description 3
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 claims description 2
- 229930195712 glutamate Natural products 0.000 claims description 2
- 229960004799 tryptophan Drugs 0.000 claims description 2
- 238000002360 preparation method Methods 0.000 abstract description 8
- 238000000034 method Methods 0.000 abstract description 7
- 239000003795 chemical substances by application Substances 0.000 abstract description 2
- 210000004027 cell Anatomy 0.000 description 32
- 108020004414 DNA Proteins 0.000 description 22
- 230000014509 gene expression Effects 0.000 description 21
- 239000013612 plasmid Substances 0.000 description 19
- 125000003275 alpha amino acid group Chemical group 0.000 description 16
- 230000035772 mutation Effects 0.000 description 15
- 230000002779 inactivation Effects 0.000 description 13
- 239000000872 buffer Substances 0.000 description 10
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 9
- 229940098773 bovine serum albumin Drugs 0.000 description 9
- 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 8
- 230000001965 increasing effect Effects 0.000 description 8
- 108091034117 Oligonucleotide Proteins 0.000 description 7
- 239000000284 extract Substances 0.000 description 7
- 102000004190 Enzymes Human genes 0.000 description 6
- 108090000790 Enzymes Proteins 0.000 description 6
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
- 229940088598 enzyme Drugs 0.000 description 6
- 230000003647 oxidation Effects 0.000 description 6
- 238000007254 oxidation reaction Methods 0.000 description 6
- 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 5
- 108090000331 Firefly luciferases Proteins 0.000 description 5
- 239000007995 HEPES buffer Substances 0.000 description 5
- 150000001540 azides Chemical class 0.000 description 5
- 241001198387 Escherichia coli BL21(DE3) Species 0.000 description 4
- 241000254158 Lampyridae Species 0.000 description 4
- 101710137500 T7 RNA polymerase Proteins 0.000 description 4
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 4
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 4
- 235000011130 ammonium sulphate Nutrition 0.000 description 4
- 239000000287 crude extract Substances 0.000 description 4
- 230000000977 initiatory effect Effects 0.000 description 4
- 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 4
- 239000012139 lysis buffer 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
- 108091028043 Nucleic acid sequence Proteins 0.000 description 3
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 3
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 3
- 108091081024 Start codon Proteins 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 238000003780 insertion Methods 0.000 description 3
- 230000037431 insertion Effects 0.000 description 3
- 238000004519 manufacturing process Methods 0.000 description 3
- 231100000219 mutagenic Toxicity 0.000 description 3
- 230000003505 mutagenic effect Effects 0.000 description 3
- 239000008363 phosphate buffer Substances 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 238000012360 testing method Methods 0.000 description 3
- 230000009466 transformation Effects 0.000 description 3
- 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 2
- RGJOEKWQDUBAIZ-IBOSZNHHSA-N CoASH Chemical compound O[C@@H]1[C@H](OP(O)(O)=O)[C@@H](COP(O)(=O)OP(O)(=O)OCC(C)(C)[C@@H](O)C(=O)NCCC(=O)NCCS)O[C@H]1N1C2=NC=NC(N)=C2N=C1 RGJOEKWQDUBAIZ-IBOSZNHHSA-N 0.000 description 2
- AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 2
- 241000254056 Luciola Species 0.000 description 2
- 239000006137 Luria-Bertani broth Substances 0.000 description 2
- SEQKRHFRPICQDD-UHFFFAOYSA-N N-tris(hydroxymethyl)methylglycine Chemical compound OCC(CO)(CO)[NH2+]CC([O-])=O SEQKRHFRPICQDD-UHFFFAOYSA-N 0.000 description 2
- 241000254058 Photinus Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 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 2
- 229960000723 ampicillin Drugs 0.000 description 2
- 230000027455 binding Effects 0.000 description 2
- 238000006243 chemical reaction Methods 0.000 description 2
- 239000013599 cloning vector Substances 0.000 description 2
- RGJOEKWQDUBAIZ-UHFFFAOYSA-N coenzime A Natural products OC1C(OP(O)(O)=O)C(COP(O)(=O)OP(O)(=O)OCC(C)(C)C(O)C(=O)NCCC(=O)NCCS)OC1N1C2=NC=NC(N)=C2N=C1 RGJOEKWQDUBAIZ-UHFFFAOYSA-N 0.000 description 2
- 239000005516 coenzyme A Substances 0.000 description 2
- 229940093530 coenzyme a Drugs 0.000 description 2
- 230000009089 cytolysis Effects 0.000 description 2
- 230000007812 deficiency Effects 0.000 description 2
- KDTSHFARGAKYJN-UHFFFAOYSA-N dephosphocoenzyme A Natural products OC1C(O)C(COP(O)(=O)OP(O)(=O)OCC(C)(C)C(O)C(=O)NCCC(=O)NCCS)OC1N1C2=NC=NC(N)=C2N=C1 KDTSHFARGAKYJN-UHFFFAOYSA-N 0.000 description 2
- 239000012634 fragment Substances 0.000 description 2
- 108020001507 fusion proteins Proteins 0.000 description 2
- 102000037865 fusion proteins Human genes 0.000 description 2
- 238000011534 incubation Methods 0.000 description 2
- 238000004020 luminiscence type Methods 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 239000000203 mixture Substances 0.000 description 2
- 230000003287 optical effect Effects 0.000 description 2
- 239000007858 starting material Substances 0.000 description 2
- 238000006467 substitution reaction Methods 0.000 description 2
- 230000036962 time dependent Effects 0.000 description 2
- MTCFGRXMJLQNBG-REOHCLBHSA-N (2S)-2-Amino-3-hydroxypropansäure Chemical group OC[C@H](N)C(O)=O MTCFGRXMJLQNBG-REOHCLBHSA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- -1 Cat No L9009) Substances 0.000 description 1
- 241000254173 Coleoptera Species 0.000 description 1
- 102000053602 DNA Human genes 0.000 description 1
- 238000001712 DNA sequencing Methods 0.000 description 1
- MYMOFIZGZYHOMD-UHFFFAOYSA-N Dioxygen Chemical compound O=O MYMOFIZGZYHOMD-UHFFFAOYSA-N 0.000 description 1
- 101710202200 Endolysin A Proteins 0.000 description 1
- 241001522878 Escherichia coli B Species 0.000 description 1
- 101000578940 Homo sapiens PDZ domain-containing protein MAGIX Proteins 0.000 description 1
- 108010060231 Insect Proteins Proteins 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical group NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 description 1
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical group OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical group OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 1
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical group NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical group CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical group OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical group C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical group OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 241000131894 Lampyris noctiluca Species 0.000 description 1
- 102000015930 Lon proteases Human genes 0.000 description 1
- 101000622057 Luciola mingrelica Luciferin 4-monooxygenase Proteins 0.000 description 1
- 239000006142 Luria-Bertani Agar Substances 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010021466 Mutant Proteins Proteins 0.000 description 1
- 102000008300 Mutant Proteins Human genes 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
- 239000004677 Nylon Substances 0.000 description 1
- 102100028326 PDZ domain-containing protein MAGIX Human genes 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 108010030688 Photinus luciferase Proteins 0.000 description 1
- ZLMJMSJWJFRBEC-UHFFFAOYSA-N Potassium Chemical compound [K] ZLMJMSJWJFRBEC-UHFFFAOYSA-N 0.000 description 1
- 239000004365 Protease Substances 0.000 description 1
- 108010023294 Protease La Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 108700008625 Reporter Genes Proteins 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Chemical group OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- UZMAPBJVXOGOFT-UHFFFAOYSA-N Syringetin Natural products COC1=C(O)C(OC)=CC(C2=C(C(=O)C3=C(O)C=C(O)C=C3O2)O)=C1 UZMAPBJVXOGOFT-UHFFFAOYSA-N 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Chemical group CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Chemical group 0.000 description 1
- 239000007997 Tricine buffer Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- 238000009825 accumulation Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 230000000996 additive effect Effects 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 238000005349 anion exchange Methods 0.000 description 1
- 229940009098 aspartate Drugs 0.000 description 1
- 239000012131 assay buffer Substances 0.000 description 1
- 238000003149 assay kit Methods 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000011230 binding agent Substances 0.000 description 1
- 238000005415 bioluminescence Methods 0.000 description 1
- 230000029918 bioluminescence Effects 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 239000013592 cell lysate Substances 0.000 description 1
- 150000005829 chemical entities Chemical class 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 239000003086 colorant Substances 0.000 description 1
- 239000002299 complementary DNA Substances 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Chemical group SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 238000012217 deletion Methods 0.000 description 1
- 230000037430 deletion Effects 0.000 description 1
- KCFYHBSOLOXZIF-UHFFFAOYSA-N dihydrochrysin Natural products COC1=C(O)C(OC)=CC(C2OC3=CC(O)=CC(O)=C3C(=O)C2)=C1 KCFYHBSOLOXZIF-UHFFFAOYSA-N 0.000 description 1
- 229910001882 dioxygen Inorganic materials 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
- 230000002349 favourable effect Effects 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 238000005194 fractionation Methods 0.000 description 1
- 230000004927 fusion Effects 0.000 description 1
- 235000004554 glutamine Nutrition 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Chemical group OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 235000014304 histidine Nutrition 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Chemical group OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 239000000411 inducer Substances 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- 125000000741 isoleucyl group Chemical group [H]N([H])C(C(C([H])([H])[H])C([H])([H])C([H])([H])[H])C(=O)O* 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 125000001909 leucine group Chemical group [H]N(*)C(C(*)=O)C([H])([H])C(C([H])([H])[H])C([H])([H])[H] 0.000 description 1
- 238000009630 liquid culture Methods 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 238000003670 luciferase enzyme activity assay Methods 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
- 239000002609 medium Substances 0.000 description 1
- 239000012528 membrane Substances 0.000 description 1
- 235000006109 methionine Nutrition 0.000 description 1
- 229930182817 methionine Chemical group 0.000 description 1
- 238000001823 molecular biology technique Methods 0.000 description 1
- 238000002703 mutagenesis Methods 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 229920001778 nylon Polymers 0.000 description 1
- 101150093139 ompT gene Proteins 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Chemical group OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 229910052700 potassium Inorganic materials 0.000 description 1
- 239000011591 potassium Substances 0.000 description 1
- XAEFZNCEHLXOMS-UHFFFAOYSA-M potassium benzoate Chemical compound [K+].[O-]C(=O)C1=CC=CC=C1 XAEFZNCEHLXOMS-UHFFFAOYSA-M 0.000 description 1
- 239000008057 potassium phosphate buffer Substances 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 230000002335 preservative effect Effects 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 108090000765 processed proteins & peptides Proteins 0.000 description 1
- 239000000047 product Substances 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 238000006862 quantum yield reaction Methods 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 239000006152 selective media Substances 0.000 description 1
- 235000004400 serine Nutrition 0.000 description 1
- 238000002791 soaking Methods 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 239000001509 sodium citrate Substances 0.000 description 1
- NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
- 239000001488 sodium phosphate Substances 0.000 description 1
- 229910000162 sodium phosphate Inorganic materials 0.000 description 1
- 239000012064 sodium phosphate buffer Substances 0.000 description 1
- 239000000243 solution Substances 0.000 description 1
- 230000009870 specific binding Effects 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 238000003860 storage Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 235000008521 threonine Nutrition 0.000 description 1
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- JLEXUIVKURIPFI-UHFFFAOYSA-N tris phosphate Chemical compound OP(O)(O)=O.OCC(N)(CO)CO JLEXUIVKURIPFI-UHFFFAOYSA-N 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
- 125000000430 tryptophan group Chemical group [H]N([H])C(C(=O)O*)C([H])([H])C1=C([H])N([H])C2=C([H])C([H])=C([H])C([H])=C12 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 238000011144 upstream manufacturing Methods 0.000 description 1
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- 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
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0069—Oxidoreductases (1.) acting on single donors with incorporation of molecular oxygen, i.e. oxygenases (1.13)
-
- 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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/0004—Oxidoreductases (1.)
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y113/00—Oxidoreductases acting on single donors with incorporation of molecular oxygen (oxygenases) (1.13)
- C12Y113/12—Oxidoreductases acting on single donors with incorporation of molecular oxygen (oxygenases) (1.13) with incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases)(1.13.12)
- C12Y113/12007—Photinus-luciferin 4-monooxygenase (ATP-hydrolysing) (1.13.12.7), i.e. firefly-luciferase
-
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biomedical Technology (AREA)
- Molecular Biology (AREA)
- General Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Medicinal Chemistry (AREA)
- Immunology (AREA)
- Physics & Mathematics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Hematology (AREA)
- Urology & Nephrology (AREA)
- Biophysics (AREA)
- Analytical Chemistry (AREA)
- Pathology (AREA)
- General Physics & Mathematics (AREA)
- Food Science & Technology (AREA)
- Plant Pathology (AREA)
- Cell Biology (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Enzymes And Modification Thereof (AREA)
- Acyclic And Carbocyclic Compounds In Medicinal Compositions (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Peptides Or Proteins (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB9405750A GB9405750D0 (en) | 1994-03-23 | 1994-03-23 | Luciferases |
| GBGB9501170.6A GB9501170D0 (en) | 1994-03-23 | 1995-01-20 | Luciferases |
| PCT/GB1995/000629 WO1995025798A1 (fr) | 1994-03-23 | 1995-03-22 | Luciferases |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| NO963983D0 NO963983D0 (no) | 1996-09-23 |
| NO963983L NO963983L (no) | 1996-09-23 |
| NO319706B1 true NO319706B1 (no) | 2005-09-05 |
Family
ID=26304561
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NO19963983A NO319706B1 (no) | 1994-03-23 | 1996-09-23 | Protein med luciferaseaktivitet, DNA, vektor, celle, provekit samt analysemetode. |
Country Status (17)
| Country | Link |
|---|---|
| US (1) | US6132983A (fr) |
| EP (2) | EP1281762B1 (fr) |
| JP (3) | JP4490508B2 (fr) |
| KR (1) | KR100392020B1 (fr) |
| CN (1) | CN100387720C (fr) |
| AT (1) | ATE230800T1 (fr) |
| AU (1) | AU697883B2 (fr) |
| BR (1) | BR9507140A (fr) |
| CA (1) | CA2186144C (fr) |
| DE (1) | DE69529337T2 (fr) |
| DK (1) | DK0751996T3 (fr) |
| ES (1) | ES2185697T3 (fr) |
| FI (1) | FI120096B (fr) |
| GB (1) | GB9501170D0 (fr) |
| NO (1) | NO319706B1 (fr) |
| RU (1) | RU2192467C2 (fr) |
| WO (1) | WO1995025798A1 (fr) |
Families Citing this family (41)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB9501170D0 (en) * | 1994-03-23 | 1995-03-08 | Secr Defence | Luciferases |
| WO1996022376A1 (fr) * | 1995-01-20 | 1996-07-25 | The Secretary Of State For Defence | Luciferases mutantes |
| GB2311525B (en) * | 1995-01-20 | 1998-11-11 | Secr Defence | Mutant Luciferases |
| GB9707486D0 (en) * | 1997-04-11 | 1997-05-28 | Secr Defence | Enzyme assays |
| US6602677B1 (en) * | 1997-09-19 | 2003-08-05 | Promega Corporation | Thermostable luciferases and methods of production |
| JP4537573B2 (ja) * | 1997-09-19 | 2010-09-01 | プロメガ・コーポレイシヨン | 熱安定ルシフェラーゼと生産方法 |
| GB9722481D0 (en) * | 1997-10-25 | 1997-12-24 | Secr Defence | Expression system |
| US6117643A (en) * | 1997-11-25 | 2000-09-12 | Ut Battelle, Llc | Bioluminescent bioreporter integrated circuit |
| CA2324648C (fr) * | 1998-03-27 | 2013-02-26 | Prolume, Ltd. | Luciferases, proteines fluorescentes, acides nucleiques codant pour les luciferases et les proteines fluorescentes, et leur utilisation dans des diagnostics |
| EP1925320A3 (fr) | 1998-03-27 | 2008-09-03 | Prolume, Ltd. | Luciférases, protéines fluorescentes, acides nucléiques codant pour les luciférases et protéines fluorescentes et leur utilisation pour le diagnostic, le criblage à haut rendement et articles nouveaux |
| GB9823468D0 (en) * | 1998-10-28 | 1998-12-23 | Secr Defence | Novel enzyme |
| GB9925161D0 (en) * | 1999-10-26 | 1999-12-22 | Secr Defence | Novel enzyme |
| NZ518413A (en) * | 1999-10-26 | 2004-11-26 | Secr Defence | Novel enzyme |
| US7879540B1 (en) | 2000-08-24 | 2011-02-01 | Promega Corporation | Synthetic nucleic acid molecule compositions and methods of preparation |
| US20020073441A1 (en) | 2000-12-13 | 2002-06-13 | Ross Brian D. | Compositions and methods for detecting proteolytic activity |
| GB0111275D0 (en) | 2001-05-09 | 2001-06-27 | Secr Defence | Analytical method and kit |
| EP1485468A4 (fr) | 2002-02-21 | 2007-01-03 | Medimmune Vaccines Inc | Systemes d'expression de virus recombinant parainfluenza et vaccins comprenant des antigenes heterologues derives de metapneumovirus |
| US20040142356A1 (en) * | 2002-10-30 | 2004-07-22 | Stacey Patterson | Modified luciferase nucleic acids and methods of use |
| US7413874B2 (en) | 2002-12-09 | 2008-08-19 | University Of Miami | Nucleic acid encoding fluorescent proteins from aquatic species |
| EP1613158A4 (fr) | 2003-03-27 | 2007-08-22 | Ptc Therapeutics Inc | Procedes d'identification de composes ciblant une endonuclease d'epissage d'arnt et utilisations desdits composes comme agents anti-proliferatifs |
| JP2006521116A (ja) | 2003-03-27 | 2006-09-21 | ピーティーシー セラピューティクス，インコーポレーテッド | 抗真菌性および／または抗増殖性分子を同定するためのｔＲＮＡスプライシング経路の酵素の標的化 |
| JP4385135B2 (ja) * | 2003-05-06 | 2009-12-16 | 独立行政法人産業技術総合研究所 | マルチ遺伝子転写活性測定システム |
| US7728118B2 (en) | 2004-09-17 | 2010-06-01 | Promega Corporation | Synthetic nucleic acid molecule compositions and methods of preparation |
| GB0517005D0 (en) | 2005-08-19 | 2005-09-28 | Enigma Diagnostics Ltd | Analytical method and kit |
| US7807429B2 (en) * | 2006-02-13 | 2010-10-05 | Connecticut College | Isolated luciferase gene of L. italica |
| JP5188771B2 (ja) * | 2007-09-26 | 2013-04-24 | 株式会社日立製作所 | 変異型ホタルルシフェラーゼ |
| WO2010011607A1 (fr) | 2008-07-22 | 2010-01-28 | Promega Corporation | Dosage luminescent de la phosphotransférase ou de l’atp hydrolase basé sur la détection de l’adp |
| JP2010081908A (ja) * | 2008-10-02 | 2010-04-15 | Hitachi Ltd | 変異型のホタルルシフェラーゼ |
| JP2011120559A (ja) | 2008-12-26 | 2011-06-23 | Kikkoman Corp | ホタルルシフェラーゼ、その遺伝子、およびホタルルシフェラーゼの製造法 |
| US20110076706A1 (en) * | 2009-06-26 | 2011-03-31 | Genprime, Inc. | Methods and kits for the rapid detection of microorganisms |
| ES2543913T3 (es) | 2010-11-02 | 2015-08-25 | Promega Corporation | Derivados de coelenterazina y métodos de uso de los mismos |
| SG190104A1 (en) | 2010-11-02 | 2013-06-28 | Promega Corp | Oplophorus-derived luciferases, novel coelenterazine substrates, and methods of use |
| EP2959010B1 (fr) | 2013-02-22 | 2020-07-29 | Promega Corporation | Formulation stabilisée pour la détection de luminescence de la luciférase et de nucléosides phosphates |
| WO2015116806A1 (fr) | 2014-01-29 | 2015-08-06 | Promega Corporation | Pro-substrats pour applications se rapportant à des cellules vivantes |
| WO2015116867A1 (fr) | 2014-01-29 | 2015-08-06 | Promega Corporation | Sondes masquées par quinone utilisées comme réactifs de marquage pour mesurer l'absorption cellulaire |
| EP3191600A1 (fr) | 2014-09-11 | 2017-07-19 | Promega Corporation | Substrats émettant dans l'infrarouge utilisant des séquences de luciférase pour produire une luminescence augmentée |
| EP3204509B1 (fr) | 2014-10-08 | 2019-07-10 | Promega Corporation | Dosage de détection de succinate bioluminescente |
| CN105200022B (zh) * | 2015-11-03 | 2018-11-16 | 南京工业大学 | 萤火虫荧光素酶热稳定性改造的方法 |
| JP6349003B1 (ja) * | 2017-03-17 | 2018-06-27 | 東洋ビーネット株式会社 | 耐熱性ルシフェラーゼ |
| CN115087743A (zh) | 2020-02-14 | 2022-09-20 | 龟甲万株式会社 | 用于测定样本中的atp、以及amp和/或adp的液体组合物 |
| CN114015664B (zh) * | 2021-12-06 | 2023-07-21 | 郑州伊美诺生物技术有限公司 | 荧光素酶突变体及其应用 |
Family Cites Families (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JP3048466B2 (ja) * | 1991-06-27 | 2000-06-05 | キッコーマン株式会社 | 耐熱性ホタルルシフェラーゼ、耐熱性ホタルルシフェラーゼ遺伝子、新規な組み換え体ｄｎａ、及び耐熱性ホタルルシフェラーゼの製造法 |
| US5229285A (en) * | 1991-06-27 | 1993-07-20 | Kikkoman Corporation | Thermostable luciferase of firefly, thermostable luciferase gene of firefly, novel recombinant dna, and process for the preparation of thermostable luciferase of firefly |
| DE4124495A1 (de) * | 1991-07-24 | 1993-01-28 | Happich Gmbh Gebr | Fenstereinfassrahmen, insbesondere fuer fahrzeuge |
| GB9501170D0 (en) * | 1994-03-23 | 1995-03-08 | Secr Defence | Luciferases |
-
1995
- 1995-01-20 GB GBGB9501170.6A patent/GB9501170D0/en active Pending
- 1995-03-22 CN CNB951932594A patent/CN100387720C/zh not_active Expired - Fee Related
- 1995-03-22 EP EP02010994.8A patent/EP1281762B1/fr not_active Expired - Lifetime
- 1995-03-22 US US08/718,425 patent/US6132983A/en not_active Expired - Lifetime
- 1995-03-22 AT AT95912320T patent/ATE230800T1/de not_active IP Right Cessation
- 1995-03-22 BR BR9507140A patent/BR9507140A/pt not_active IP Right Cessation
- 1995-03-22 RU RU96119246/13A patent/RU2192467C2/ru active
- 1995-03-22 CA CA002186144A patent/CA2186144C/fr not_active Expired - Fee Related
- 1995-03-22 JP JP52448695A patent/JP4490508B2/ja not_active Expired - Lifetime
- 1995-03-22 AU AU19545/95A patent/AU697883B2/en not_active Ceased
- 1995-03-22 DE DE69529337T patent/DE69529337T2/de not_active Expired - Lifetime
- 1995-03-22 KR KR1019960705464A patent/KR100392020B1/ko not_active IP Right Cessation
- 1995-03-22 ES ES95912320T patent/ES2185697T3/es not_active Expired - Lifetime
- 1995-03-22 DK DK95912320T patent/DK0751996T3/da active
- 1995-03-22 WO PCT/GB1995/000629 patent/WO1995025798A1/fr active IP Right Grant
- 1995-03-22 EP EP95912320A patent/EP0751996B1/fr not_active Expired - Lifetime
-
1996
- 1996-09-20 FI FI963741A patent/FI120096B/fi active IP Right Grant
- 1996-09-23 NO NO19963983A patent/NO319706B1/no not_active IP Right Cessation
-
2006
- 2006-06-13 JP JP2006163388A patent/JP2006271393A/ja active Pending
-
2009
- 2009-12-03 JP JP2009275807A patent/JP2010088440A/ja not_active Withdrawn
Also Published As
| Publication number | Publication date |
|---|---|
| AU697883B2 (en) | 1998-10-22 |
| FI120096B (fi) | 2009-06-30 |
| ES2185697T3 (es) | 2003-05-01 |
| ATE230800T1 (de) | 2003-01-15 |
| JPH09510610A (ja) | 1997-10-28 |
| CA2186144C (fr) | 2009-12-22 |
| NO963983D0 (no) | 1996-09-23 |
| AU1954595A (en) | 1995-10-09 |
| JP4490508B2 (ja) | 2010-06-30 |
| GB9501170D0 (en) | 1995-03-08 |
| JP2006271393A (ja) | 2006-10-12 |
| CA2186144A1 (fr) | 1995-09-28 |
| EP0751996B1 (fr) | 2003-01-08 |
| US6132983A (en) | 2000-10-17 |
| JP2010088440A (ja) | 2010-04-22 |
| DK0751996T3 (da) | 2003-02-24 |
| NO963983L (no) | 1996-09-23 |
| KR100392020B1 (ko) | 2003-10-22 |
| FI963741A0 (fi) | 1996-09-20 |
| EP1281762A3 (fr) | 2003-11-05 |
| WO1995025798A1 (fr) | 1995-09-28 |
| FI963741A (fi) | 1996-11-20 |
| RU2192467C2 (ru) | 2002-11-10 |
| DE69529337T2 (de) | 2003-10-16 |
| EP1281762A2 (fr) | 2003-02-05 |
| EP1281762B1 (fr) | 2014-12-31 |
| DE69529337D1 (de) | 2003-02-13 |
| KR970702369A (ko) | 1997-05-13 |
| CN100387720C (zh) | 2008-05-14 |
| BR9507140A (pt) | 1997-09-30 |
| EP0751996A1 (fr) | 1997-01-08 |
| CN1149318A (zh) | 1997-05-07 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| NO319706B1 (no) | Protein med luciferaseaktivitet, DNA, vektor, celle, provekit samt analysemetode. | |
| JP4342608B2 (ja) | 突然変異体ルシフェラーゼ | |
| White et al. | Improved thermostability of the North American firefly luciferase: saturation mutagenesis at position 354 | |
| EP1479763B1 (fr) | Luciferase mutée ayant une thermostabilité améliorée | |
| US20140186918A1 (en) | Luciferase mutant | |
| JP2017225372A (ja) | 変異型甲虫ルシフェラーゼ、遺伝子、組換えベクター、形質転換体、及び変異型甲虫ルシフェラーゼの製造方法 | |
| RU2210594C2 (ru) | Мутантная люцифераза (варианты), днк, кодирующая указанную люциферазу, и вектор для экспрессии указанного белка | |
| MXPA96004194A (en) | Lucifera | |
| CN101173254A (zh) | 虫荧光素酶 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MM1K | Lapsed by not paying the annual fees |