NO314151B1 - Pichia pastoris sur fosfatasegen - Google Patents
Pichia pastoris sur fosfatasegen Download PDFInfo
- Publication number
- NO314151B1 NO314151B1 NO19914935A NO914935A NO314151B1 NO 314151 B1 NO314151 B1 NO 314151B1 NO 19914935 A NO19914935 A NO 19914935A NO 914935 A NO914935 A NO 914935A NO 314151 B1 NO314151 B1 NO 314151B1
- Authority
- NO
- Norway
- Prior art keywords
- pichia pastoris
- seq
- acid phosphatase
- regulatory region
- dna
- Prior art date
Links
- 241000235058 Komagataella pastoris Species 0.000 title claims description 102
- 239000012634 fragment Substances 0.000 claims description 120
- 108020004414 DNA Proteins 0.000 claims description 92
- 108010051457 Acid Phosphatase Proteins 0.000 claims description 84
- 108090000623 proteins and genes Proteins 0.000 claims description 75
- 239000013612 plasmid Substances 0.000 claims description 70
- 102000013563 Acid Phosphatase Human genes 0.000 claims description 62
- 210000004027 cell Anatomy 0.000 claims description 59
- 108010076504 Protein Sorting Signals Proteins 0.000 claims description 58
- GZCWLCBFPRFLKL-UHFFFAOYSA-N 1-prop-2-ynoxypropan-2-ol Chemical compound CC(O)COCC#C GZCWLCBFPRFLKL-UHFFFAOYSA-N 0.000 claims description 56
- 230000001105 regulatory effect Effects 0.000 claims description 55
- 238000000034 method Methods 0.000 claims description 41
- 239000013598 vector Substances 0.000 claims description 36
- 108091028043 Nucleic acid sequence Proteins 0.000 claims description 33
- 230000014509 gene expression Effects 0.000 claims description 29
- 102000004169 proteins and genes Human genes 0.000 claims description 28
- 229910019142 PO4 Inorganic materials 0.000 claims description 22
- 239000010452 phosphate Substances 0.000 claims description 22
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 claims description 21
- 239000013604 expression vector Substances 0.000 claims description 19
- 101150023810 PHO1 gene Proteins 0.000 claims description 17
- 108010025188 Alcohol oxidase Proteins 0.000 claims description 15
- 229920001184 polypeptide Polymers 0.000 claims description 14
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 14
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 14
- 230000010354 integration Effects 0.000 claims description 13
- 238000004519 manufacturing process Methods 0.000 claims description 12
- 241000235648 Pichia Species 0.000 claims description 11
- 230000005030 transcription termination Effects 0.000 claims description 9
- 102100035703 Prostatic acid phosphatase Human genes 0.000 claims description 7
- 108010043671 prostatic acid phosphatase Proteins 0.000 claims description 7
- 210000005253 yeast cell Anatomy 0.000 claims description 6
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 claims description 5
- 102000003978 Tissue Plasminogen Activator Human genes 0.000 claims description 5
- 229960000187 tissue plasminogen activator Drugs 0.000 claims description 5
- 101100271429 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) ATP6 gene Proteins 0.000 claims 2
- 101100115751 Trypanosoma brucei brucei dnaaf11 gene Proteins 0.000 claims 2
- 108020005065 3' Flanking Region Proteins 0.000 claims 1
- 108020005029 5' Flanking Region Proteins 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- 102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 37
- 108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 37
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 24
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 22
- 239000000523 sample Substances 0.000 description 22
- 239000002609 medium Substances 0.000 description 20
- 108091034117 Oligonucleotide Proteins 0.000 description 19
- 239000002773 nucleotide Substances 0.000 description 18
- 125000003729 nucleotide group Chemical group 0.000 description 18
- 241000588724 Escherichia coli Species 0.000 description 17
- 239000002299 complementary DNA Substances 0.000 description 16
- 230000028327 secretion Effects 0.000 description 16
- OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 15
- 230000035897 transcription Effects 0.000 description 15
- 238000013518 transcription Methods 0.000 description 15
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 12
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 12
- 239000000499 gel Substances 0.000 description 12
- 230000029087 digestion Effects 0.000 description 11
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 11
- 239000000047 product Substances 0.000 description 11
- 230000009466 transformation Effects 0.000 description 11
- 238000010276 construction Methods 0.000 description 10
- 239000000243 solution Substances 0.000 description 10
- 108091032973 (ribonucleotides)n+m Proteins 0.000 description 9
- FBPFZTCFMRRESA-FSIIMWSLSA-N D-Glucitol Natural products OC[C@H](O)[C@H](O)[C@@H](O)[C@H](O)CO FBPFZTCFMRRESA-FSIIMWSLSA-N 0.000 description 9
- 239000007984 Tris EDTA buffer Substances 0.000 description 9
- 239000011543 agarose gel Substances 0.000 description 9
- 239000000600 sorbitol Substances 0.000 description 9
- 101150069554 HIS4 gene Proteins 0.000 description 8
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 8
- 108010051210 beta-Fructofuranosidase Proteins 0.000 description 8
- 239000000872 buffer Substances 0.000 description 8
- 238000009396 hybridization Methods 0.000 description 8
- 239000000203 mixture Substances 0.000 description 8
- 238000002703 mutagenesis Methods 0.000 description 8
- 231100000350 mutagenesis Toxicity 0.000 description 8
- 108091026890 Coding region Proteins 0.000 description 7
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 7
- 101150014136 SUC2 gene Proteins 0.000 description 7
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 7
- 230000000694 effects Effects 0.000 description 7
- 239000003550 marker Substances 0.000 description 7
- FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 description 6
- 150000001413 amino acids Chemical class 0.000 description 6
- 238000005119 centrifugation Methods 0.000 description 6
- 239000008121 dextrose Substances 0.000 description 6
- 239000001573 invertase Substances 0.000 description 6
- 235000011073 invertase Nutrition 0.000 description 6
- 238000002955 isolation Methods 0.000 description 6
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Chemical compound O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 6
- 229920001817 Agar Polymers 0.000 description 5
- 241001288713 Escherichia coli MC1061 Species 0.000 description 5
- 108020004511 Recombinant DNA Proteins 0.000 description 5
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 5
- 239000008272 agar Substances 0.000 description 5
- 101150073130 ampR gene Proteins 0.000 description 5
- 238000006243 chemical reaction Methods 0.000 description 5
- 238000002474 experimental method Methods 0.000 description 5
- 108020004999 messenger RNA Proteins 0.000 description 5
- 239000012071 phase Substances 0.000 description 5
- 238000002360 preparation method Methods 0.000 description 5
- 230000010076 replication Effects 0.000 description 5
- 238000012216 screening Methods 0.000 description 5
- 229930024421 Adenine Natural products 0.000 description 4
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 4
- 102000012410 DNA Ligases Human genes 0.000 description 4
- 108010061982 DNA Ligases Proteins 0.000 description 4
- 241001506991 Komagataella phaffii GS115 Species 0.000 description 4
- 101100173636 Rattus norvegicus Fhl2 gene Proteins 0.000 description 4
- 229960000643 adenine Drugs 0.000 description 4
- 230000006870 function Effects 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- 201000001441 melanoma Diseases 0.000 description 4
- 239000008188 pellet Substances 0.000 description 4
- 238000003259 recombinant expression Methods 0.000 description 4
- 238000012163 sequencing technique Methods 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 101150005709 ARG4 gene Proteins 0.000 description 3
- 102100038647 Fibroleukin Human genes 0.000 description 3
- 108010033128 Glucan Endo-1,3-beta-D-Glucosidase Proteins 0.000 description 3
- 101001031613 Homo sapiens Fibroleukin Proteins 0.000 description 3
- 108090000364 Ligases Proteins 0.000 description 3
- 239000000020 Nitrocellulose Substances 0.000 description 3
- 241000235070 Saccharomyces Species 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 102000005936 beta-Galactosidase Human genes 0.000 description 3
- 108010005774 beta-Galactosidase Proteins 0.000 description 3
- 230000033228 biological regulation Effects 0.000 description 3
- 230000015572 biosynthetic process Effects 0.000 description 3
- 238000011161 development Methods 0.000 description 3
- 230000018109 developmental process Effects 0.000 description 3
- 238000010790 dilution Methods 0.000 description 3
- 239000012895 dilution Substances 0.000 description 3
- 238000010362 genome editing Methods 0.000 description 3
- 230000012010 growth Effects 0.000 description 3
- 238000010438 heat treatment Methods 0.000 description 3
- 238000003780 insertion Methods 0.000 description 3
- 230000037431 insertion Effects 0.000 description 3
- 229920001220 nitrocellulos Polymers 0.000 description 3
- 238000007747 plating Methods 0.000 description 3
- 230000008929 regeneration Effects 0.000 description 3
- 238000011069 regeneration method Methods 0.000 description 3
- 230000004044 response Effects 0.000 description 3
- 238000002741 site-directed mutagenesis Methods 0.000 description 3
- 239000007222 ypd medium Substances 0.000 description 3
- SBKVPJHMSUXZTA-MEJXFZFPSA-N (2S)-2-[[(2S)-2-[[(2S)-1-[(2S)-5-amino-2-[[2-[[(2S)-1-[(2S)-6-amino-2-[[(2S)-2-[[(2S)-5-amino-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-[[(2S)-2-amino-3-(1H-indol-3-yl)propanoyl]amino]-3-(1H-imidazol-4-yl)propanoyl]amino]-3-(1H-indol-3-yl)propanoyl]amino]-4-methylpentanoyl]amino]-5-oxopentanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]pyrrolidine-2-carbonyl]amino]acetyl]amino]-5-oxopentanoyl]pyrrolidine-2-carbonyl]amino]-4-methylsulfanylbutanoyl]amino]-3-(4-hydroxyphenyl)propanoic acid Chemical compound C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 SBKVPJHMSUXZTA-MEJXFZFPSA-N 0.000 description 2
- 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
- 239000004475 Arginine Substances 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 2
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
- 101000801481 Homo sapiens Tissue-type plasminogen activator Proteins 0.000 description 2
- 102000008100 Human Serum Albumin Human genes 0.000 description 2
- 108091006905 Human Serum Albumin Proteins 0.000 description 2
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 description 2
- 102000003960 Ligases Human genes 0.000 description 2
- 108010038049 Mating Factor Proteins 0.000 description 2
- 108700026244 Open Reading Frames Proteins 0.000 description 2
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 2
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 2
- 208000037065 Subacute sclerosing leukoencephalitis Diseases 0.000 description 2
- 206010042297 Subacute sclerosing panencephalitis Diseases 0.000 description 2
- 239000008346 aqueous phase Substances 0.000 description 2
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 2
- 230000008901 benefit Effects 0.000 description 2
- 230000015556 catabolic process Effects 0.000 description 2
- 238000010367 cloning Methods 0.000 description 2
- 230000000295 complement effect Effects 0.000 description 2
- RXKJFZQQPQGTFL-UHFFFAOYSA-N dihydroxyacetone Chemical compound OCC(=O)CO RXKJFZQQPQGTFL-UHFFFAOYSA-N 0.000 description 2
- 238000005516 engineering process Methods 0.000 description 2
- 239000013613 expression plasmid Substances 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 238000000855 fermentation Methods 0.000 description 2
- 230000004151 fermentation Effects 0.000 description 2
- 239000001963 growth medium Substances 0.000 description 2
- 230000009931 harmful effect Effects 0.000 description 2
- 238000000338 in vitro Methods 0.000 description 2
- 229910052816 inorganic phosphate Inorganic materials 0.000 description 2
- 101150066555 lacZ gene Proteins 0.000 description 2
- KWGKDLIKAYFUFQ-UHFFFAOYSA-M lithium chloride Chemical group [Li+].[Cl-] KWGKDLIKAYFUFQ-UHFFFAOYSA-M 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 238000002156 mixing Methods 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 229920002401 polyacrylamide Polymers 0.000 description 2
- SCVFZCLFOSHCOH-UHFFFAOYSA-M potassium acetate Chemical compound [K+].CC([O-])=O SCVFZCLFOSHCOH-UHFFFAOYSA-M 0.000 description 2
- 239000002244 precipitate Substances 0.000 description 2
- 230000001737 promoting effect Effects 0.000 description 2
- 230000003362 replicative effect Effects 0.000 description 2
- 238000010561 standard procedure Methods 0.000 description 2
- 239000008223 sterile water Substances 0.000 description 2
- 239000000126 substance Substances 0.000 description 2
- 239000000758 substrate Substances 0.000 description 2
- 239000013589 supplement Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 241001515965 unidentified phage Species 0.000 description 2
- KMEMIMRPZGDOMG-UHFFFAOYSA-N 2-cyanoethoxyphosphonamidous acid Chemical compound NP(O)OCCC#N KMEMIMRPZGDOMG-UHFFFAOYSA-N 0.000 description 1
- OPIFSICVWOWJMJ-AEOCFKNESA-N 5-bromo-4-chloro-3-indolyl beta-D-galactoside Chemical compound O[C@@H]1[C@@H](O)[C@@H](O)[C@@H](CO)O[C@H]1OC1=CNC2=CC=C(Br)C(Cl)=C12 OPIFSICVWOWJMJ-AEOCFKNESA-N 0.000 description 1
- 101150061183 AOX1 gene Proteins 0.000 description 1
- 101710120911 Acid phosphatase PHO1 Proteins 0.000 description 1
- 244000144725 Amygdalus communis Species 0.000 description 1
- 108091033380 Coding strand Proteins 0.000 description 1
- 241001315286 Damon Species 0.000 description 1
- 101710088194 Dehydrogenase Proteins 0.000 description 1
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
- 108010067770 Endopeptidase K Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- VGGSQFUCUMXWEO-UHFFFAOYSA-N Ethene Chemical compound C=C VGGSQFUCUMXWEO-UHFFFAOYSA-N 0.000 description 1
- 101000976075 Homo sapiens Insulin Proteins 0.000 description 1
- 102000002265 Human Growth Hormone Human genes 0.000 description 1
- 108010000521 Human Growth Hormone Proteins 0.000 description 1
- 239000000854 Human Growth Hormone Substances 0.000 description 1
- 102000014150 Interferons Human genes 0.000 description 1
- 108010050904 Interferons Proteins 0.000 description 1
- 101710096444 Killer toxin Proteins 0.000 description 1
- 108091036060 Linker DNA Proteins 0.000 description 1
- 101001092933 Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) Phosphatidylinositol-3-phosphatase Proteins 0.000 description 1
- 125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
- 108020002230 Pancreatic Ribonuclease Proteins 0.000 description 1
- 102000005891 Pancreatic ribonuclease Human genes 0.000 description 1
- 102000013566 Plasminogen Human genes 0.000 description 1
- 108010051456 Plasminogen Proteins 0.000 description 1
- 239000004743 Polypropylene Substances 0.000 description 1
- 108010076181 Proinsulin Proteins 0.000 description 1
- 108091081024 Start codon Proteins 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 230000003321 amplification Effects 0.000 description 1
- 239000003242 anti bacterial agent Substances 0.000 description 1
- 230000000692 anti-sense effect Effects 0.000 description 1
- 229940088710 antibiotic agent Drugs 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- 239000011324 bead Substances 0.000 description 1
- 238000004166 bioassay Methods 0.000 description 1
- 230000006696 biosynthetic metabolic pathway Effects 0.000 description 1
- 238000009835 boiling Methods 0.000 description 1
- 230000003915 cell function Effects 0.000 description 1
- 230000010261 cell growth Effects 0.000 description 1
- 210000000170 cell membrane Anatomy 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 239000013599 cloning vector Substances 0.000 description 1
- 230000001276 controlling effect Effects 0.000 description 1
- 238000001816 cooling Methods 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 238000006731 degradation reaction Methods 0.000 description 1
- 238000013461 design Methods 0.000 description 1
- 229940120503 dihydroxyacetone Drugs 0.000 description 1
- 238000001962 electrophoresis Methods 0.000 description 1
- 230000002255 enzymatic effect Effects 0.000 description 1
- 238000011049 filling Methods 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 239000008103 glucose Substances 0.000 description 1
- 238000002744 homologous recombination Methods 0.000 description 1
- 230000006801 homologous recombination Effects 0.000 description 1
- 101150085823 hsdR gene Proteins 0.000 description 1
- 235000003642 hunger Nutrition 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 230000001939 inductive effect Effects 0.000 description 1
- PBGKTOXHQIOBKM-FHFVDXKLSA-N insulin (human) Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 PBGKTOXHQIOBKM-FHFVDXKLSA-N 0.000 description 1
- 229940047124 interferons Drugs 0.000 description 1
- 238000011835 investigation Methods 0.000 description 1
- 229960000318 kanamycin Drugs 0.000 description 1
- 229930027917 kanamycin Natural products 0.000 description 1
- SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
- 229930182823 kanamycin A Natural products 0.000 description 1
- 210000000265 leukocyte Anatomy 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 239000012139 lysis buffer Substances 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000013011 mating Effects 0.000 description 1
- 230000037353 metabolic pathway Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 231100000219 mutagenic Toxicity 0.000 description 1
- 230000003505 mutagenic effect Effects 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 238000003199 nucleic acid amplification method Methods 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 230000037361 pathway Effects 0.000 description 1
- OJMIONKXNSYLSR-UHFFFAOYSA-N phosphorous acid Chemical compound OP(O)O OJMIONKXNSYLSR-UHFFFAOYSA-N 0.000 description 1
- 239000013600 plasmid vector Substances 0.000 description 1
- 229920003023 plastic Polymers 0.000 description 1
- 239000004033 plastic Substances 0.000 description 1
- 230000008488 polyadenylation Effects 0.000 description 1
- -1 polypropylene Polymers 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 235000011056 potassium acetate Nutrition 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 230000008569 process Effects 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 101150072534 sbcB gene Proteins 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 230000009962 secretion pathway Effects 0.000 description 1
- 238000011218 seed culture Methods 0.000 description 1
- 230000013278 single fertilization Effects 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 230000028070 sporulation Effects 0.000 description 1
- 230000037351 starvation Effects 0.000 description 1
- 239000006228 supernatant Substances 0.000 description 1
- 230000004083 survival effect Effects 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- 238000011426 transformation method Methods 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
- 238000013519 translation Methods 0.000 description 1
- 230000032258 transport Effects 0.000 description 1
- 108010087967 type I signal peptidase Proteins 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
- C12N15/09—Recombinant DNA-technology
- C12N15/63—Introduction of foreign genetic material using vectors; Vectors; Use of hosts therefor; Regulation of expression
- C12N15/79—Vectors or expression systems specially adapted for eukaryotic hosts
- C12N15/80—Vectors or expression systems specially adapted for eukaryotic hosts for fungi
- C12N15/81—Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts
- C12N15/815—Vectors or expression systems specially adapted for eukaryotic hosts for fungi for yeasts for yeasts other than Saccharomyces
-
- 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
- C12N9/14—Hydrolases (3)
- C12N9/16—Hydrolases (3) acting on ester bonds (3.1)
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/8215—Microorganisms
- Y10S435/911—Microorganisms using fungi
- Y10S435/938—Pichia
Landscapes
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- Chemical & Material Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Organic Chemistry (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Biomedical Technology (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Biochemistry (AREA)
- Microbiology (AREA)
- General Health & Medical Sciences (AREA)
- Mycology (AREA)
- Physics & Mathematics (AREA)
- Biophysics (AREA)
- Plant Pathology (AREA)
- Medicinal Chemistry (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US07/627,539 US5268273A (en) | 1990-12-14 | 1990-12-14 | Pichia pastoris acid phosphatase gene, gene regions, signal sequence and expression vectors comprising same |
Publications (3)
Publication Number | Publication Date |
---|---|
NO914935D0 NO914935D0 (no) | 1991-12-13 |
NO914935L NO914935L (no) | 1992-06-15 |
NO314151B1 true NO314151B1 (no) | 2003-02-03 |
Family
ID=24515081
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
NO19914935A NO314151B1 (no) | 1990-12-14 | 1991-12-13 | Pichia pastoris sur fosfatasegen |
Country Status (22)
Country | Link |
---|---|
US (1) | US5268273A (ja) |
EP (1) | EP0495208B1 (ja) |
JP (1) | JP3437850B2 (ja) |
KR (1) | KR0181179B1 (ja) |
CN (1) | CN1062169A (ja) |
AR (1) | AR245218A1 (ja) |
AT (1) | ATE208822T1 (ja) |
AU (1) | AU637734B2 (ja) |
CA (1) | CA2055542C (ja) |
CS (1) | CS378891A3 (ja) |
DE (1) | DE69132812T2 (ja) |
FI (2) | FI104493B (ja) |
HU (1) | HU913926D0 (ja) |
IE (1) | IE914354A1 (ja) |
IL (1) | IL100363A0 (ja) |
MX (1) | MX9102546A (ja) |
NO (1) | NO314151B1 (ja) |
PL (1) | PL292765A1 (ja) |
PT (1) | PT99802A (ja) |
TW (1) | TW201330B (ja) |
YU (1) | YU193591A (ja) |
ZA (1) | ZA919776B (ja) |
Families Citing this family (51)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US5612198A (en) * | 1990-09-04 | 1997-03-18 | The Salk Institute | Production of insulin-like growth factor-1 in methylotrophic yeast cells |
GB9307371D0 (en) * | 1993-04-08 | 1993-06-02 | Walls Alan J | Fusion proteins |
US5521086A (en) * | 1993-09-16 | 1996-05-28 | Cephalon, Inc. | Secretion sequence for the production of a heterologous protein in yeast |
IT1266740B1 (it) * | 1994-07-01 | 1997-01-14 | Maria Paola Landini | Materiale proteico ricombinante legante anticorpi contro il citomegalovirus umano, reagenti diagnostici derivati da tale |
CA2202351A1 (en) * | 1994-10-18 | 1996-04-25 | George Phillip Vlasuk | Nematode-extracted serine protease inhibitors and anticoagulant proteins |
US5945275A (en) * | 1994-10-18 | 1999-08-31 | Corvas International, Inc. | Nematode-extracted anticoagulant protein |
US5872098A (en) * | 1995-06-05 | 1999-02-16 | Corvas International, Inc. | Nematode-extracted anticoagulant protein |
HU225126B1 (en) * | 1994-10-18 | 2006-06-28 | Dendreon Corp | Nematode-extracted serine protease inhibitors and anticoagulant proteins |
US5863894A (en) * | 1995-06-05 | 1999-01-26 | Corvas International, Inc. | Nematode-extracted anticoagulant protein |
US5866543A (en) * | 1995-06-05 | 1999-02-02 | Corvas International, Inc. | Nematode-extracted anticoagulant protein |
US5866542A (en) * | 1994-10-18 | 1999-02-02 | Corvas International, Inc. | Nematode-extracted anticoagulant protein |
EP0877816A1 (en) * | 1996-02-01 | 1998-11-18 | North American Vaccine, Inc. | Expression of group b neisseria meningitidis outer membrane (mb3) protein from yeast and vaccines |
MX9605082A (es) | 1996-10-24 | 1998-04-30 | Univ Autonoma De Nuevo Leon | Levaduras metilotroficas modificadas geneticamente para la produccion y secrecion de hormona de crecimiento humano. |
WO1999007862A1 (en) * | 1997-08-05 | 1999-02-18 | Chiron Corporation | Novel pichia pastoris gene sequences and methods for their use |
US6451572B1 (en) | 1998-06-25 | 2002-09-17 | Cornell Research Foundation, Inc. | Overexpression of phytase genes in yeast systems |
AU2614500A (en) * | 1999-01-14 | 2000-08-01 | Novozymes Biotech, Inc. | Polypeptides having acid phosphatase activity and nucleic acids encoding same |
ES2248067T3 (es) | 1999-03-31 | 2006-03-16 | Cornell Research Foundation, Inc. | Fosfatasas con actividad de fitasa mejorada. |
US6841370B1 (en) * | 1999-11-18 | 2005-01-11 | Cornell Research Foundation, Inc. | Site-directed mutagenesis of Escherichia coli phytase |
CN1320699A (zh) * | 2000-04-27 | 2001-11-07 | 上海博德基因开发有限公司 | 一种新的多肽——人磷脂酶9和编码这种多肽的多核苷酸 |
CN1324948A (zh) * | 2000-05-24 | 2001-12-05 | 上海博德基因开发有限公司 | 一种新的多肽——酸性磷酸酶14和编码这种多肽的多核苷酸 |
US6605450B1 (en) | 2000-05-25 | 2003-08-12 | Chiron Corporation | Iron regulation of the PpSEC10 transcriptional regulatory region of Pichia pastoris and methods of use |
CN1329020A (zh) * | 2000-06-21 | 2002-01-02 | 上海博德基因开发有限公司 | 一种新的多肽——酸性磷酸酶家族蛋白11和编码这种多肽的多核苷酸 |
US7009045B2 (en) * | 2000-07-14 | 2006-03-07 | Archer-Daniels-Midland Company | Transformation systems for flavinogenic yeast |
AU2002356880A1 (en) | 2001-10-31 | 2003-05-12 | Phytex, Llc | Phytase-containing animal food and method |
CA2498017C (en) * | 2002-09-13 | 2016-06-14 | Cornell Research Foundation, Inc. | Using mutations to improve aspergillus phytases |
JP2007519392A (ja) * | 2003-07-30 | 2007-07-19 | ザイモジェネティクス, インコーポレイテッド | ピキアメタノリカ分泌シグナル |
US7919297B2 (en) | 2006-02-21 | 2011-04-05 | Cornell Research Foundation, Inc. | Mutants of Aspergillus niger PhyA phytase and Aspergillus fumigatus phytase |
US20100196336A1 (en) | 2006-05-23 | 2010-08-05 | Dongsu Park | Modified dendritic cells having enhanced survival and immunogenicity and related compositions and methods |
WO2008017066A2 (en) | 2006-08-03 | 2008-02-07 | Cornell Research Foundation, Inc. | Phytases with improved thermal stability |
US8097422B2 (en) | 2007-06-20 | 2012-01-17 | Salk Institute For Biological Studies | Kir channel modulators |
US8192734B2 (en) | 2007-07-09 | 2012-06-05 | Cornell University | Compositions and methods for bone strengthening |
AU2009223846B2 (en) | 2008-03-03 | 2014-11-20 | Abbvie Inc. | Methods for transforming yeast |
US20090280103A1 (en) * | 2008-04-04 | 2009-11-12 | Martin Flueck | Regulation of muscle repair |
BRPI1011936A2 (pt) | 2009-07-02 | 2016-05-03 | Verdezyne Inc | métodos biológicos para a preparação de ácido adípico |
US20120184020A1 (en) * | 2009-07-09 | 2012-07-19 | Verdezyne, Inc. | Engineered microorganisms with enhanced fermentation activity |
US8889394B2 (en) * | 2009-09-07 | 2014-11-18 | Empire Technology Development Llc | Multiple domain proteins |
US8343752B2 (en) | 2011-05-03 | 2013-01-01 | Verdezyne, Inc. | Biological methods for preparing adipic acid |
US8728798B2 (en) | 2011-05-03 | 2014-05-20 | Verdezyne, Inc. | Biological methods for preparing adipic acid |
WO2013006730A2 (en) | 2011-07-06 | 2013-01-10 | Verdezyne, Inc. | Biological methods for preparing a fatty dicarboxylic acid |
IN2015DN02771A (ja) | 2012-10-29 | 2015-09-04 | Lonza Ag | |
HUE052914T2 (hu) | 2012-12-19 | 2021-05-28 | Corvay Bioproducts Gmbh | Biológiai eljárások zsírdikarbonsav elõállítására |
SG11201504838YA (en) | 2012-12-19 | 2015-07-30 | Verdezyne Inc | Biological methods for preparing a fatty dicarboxylic acid |
DK3129493T3 (da) | 2014-04-09 | 2021-09-27 | Scripps Research Inst | Import af unaturlige eller modificerede nukleosidtriphosphater ind i celler via nukleinsyre-triphosphat-transportører |
CN104195059B (zh) * | 2014-08-15 | 2016-08-24 | 陕西科技大学 | 多形汉逊酵母突变菌株及多形汉逊酵母生产d-阿拉伯糖醇的方法 |
US20180148744A1 (en) | 2015-03-20 | 2018-05-31 | Verdezyne, Inc. | Biological methods for preparing 3-hydroxypropionic acid |
EP3568408A4 (en) | 2017-01-13 | 2020-12-16 | Bolt Threads, Inc. | ELASTOMER PROTEINS |
CA3069321A1 (en) | 2017-07-11 | 2019-01-17 | Synthorx, Inc. | Incorporation of unnatural nucleotides and methods thereof |
CA3069697A1 (en) | 2017-07-13 | 2019-01-17 | Radici Chimica S.P.A. | Biological methods for modifying cellular carbon flux |
AU2018309166B2 (en) | 2017-08-03 | 2022-12-08 | Synthorx, Inc. | Cytokine conjugates for the treatment of proliferative and infectious diseases |
WO2020060948A1 (en) | 2018-09-17 | 2020-03-26 | Levadura Biotechnology, Inc. | Production of cannabinoids in yeast using a fatty acid feedstock |
SG11202107354WA (en) | 2019-02-06 | 2021-08-30 | Synthorx Inc | Il-2 conjugates and methods of use thereof |
Family Cites Families (16)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
JPS5974988A (ja) * | 1982-10-20 | 1984-04-27 | Suntory Ltd | 酵母の誘導発現型プラスミドベクタ−およびその利用方法 |
US4876197A (en) * | 1983-02-22 | 1989-10-24 | Chiron Corporation | Eukaryotic regulatable transcription |
US4753879A (en) * | 1984-08-27 | 1988-06-28 | Biogen N.V. | Modified tissue plasminogen activators |
ES8702945A1 (es) * | 1984-10-01 | 1987-01-16 | Integrated Genetics Inc | Un metodo de producir activador de plasminogeno de tejido uterino humano |
US4885242A (en) * | 1984-10-30 | 1989-12-05 | Phillips Petroleum Company | Genes from pichia histidine pathway and uses thereof |
US4808537A (en) * | 1984-10-30 | 1989-02-28 | Phillips Petroleum Company | Methanol inducible genes obtained from pichia and methods of use |
US4855231A (en) * | 1984-10-30 | 1989-08-08 | Phillips Petroleum Company | Regulatory region for heterologous gene expression in yeast |
US4882279A (en) * | 1985-10-25 | 1989-11-21 | Phillips Petroleum Company | Site selective genomic modification of yeast of the genus pichia |
US4895800A (en) * | 1985-11-26 | 1990-01-23 | Phillips Petroleum Company | Yeast production of hepatitis B surface antigen |
JPH0655146B2 (ja) * | 1985-12-27 | 1994-07-27 | 財団法人化学及血清療法研究所 | シヤトルベクタ− |
IL82935A0 (en) * | 1986-08-12 | 1987-12-20 | Phillips Petroleum Co | Secretion of heterologous proteins from yeast |
US5002876A (en) * | 1986-09-22 | 1991-03-26 | Phillips Petroleum Company | Yeast production of human tumor necrosis factor |
MY103358A (en) * | 1987-04-15 | 1993-06-30 | Novartis Ag | Process for the production of protiens. |
US5102789A (en) * | 1989-03-15 | 1992-04-07 | The Salk Institute Biotechnology/Industrial Associates, Inc. | Production of epideramal growth factor in pichia pastoris yeast cells |
CA2000101A1 (en) * | 1988-12-22 | 1990-06-22 | Mary E. Digan | Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase gene |
JPH0671434B2 (ja) * | 1989-09-18 | 1994-09-14 | 株式会社ミドリ十字 | ヒト血清アルブミンの製造方法 |
-
1990
- 1990-12-14 US US07/627,539 patent/US5268273A/en not_active Expired - Lifetime
-
1991
- 1991-11-14 CA CA002055542A patent/CA2055542C/en not_active Expired - Fee Related
- 1991-12-05 AU AU88823/91A patent/AU637734B2/en not_active Ceased
- 1991-12-11 ZA ZA919776A patent/ZA919776B/xx unknown
- 1991-12-12 HU HU913926A patent/HU913926D0/hu unknown
- 1991-12-13 NO NO19914935A patent/NO314151B1/no not_active IP Right Cessation
- 1991-12-13 IL IL100363A patent/IL100363A0/xx unknown
- 1991-12-13 AT AT91121452T patent/ATE208822T1/de not_active IP Right Cessation
- 1991-12-13 IE IE435491A patent/IE914354A1/en not_active IP Right Cessation
- 1991-12-13 KR KR1019910023053A patent/KR0181179B1/ko not_active IP Right Cessation
- 1991-12-13 FI FI915893A patent/FI104493B/fi active
- 1991-12-13 CN CN91111394A patent/CN1062169A/zh active Pending
- 1991-12-13 YU YU193591A patent/YU193591A/sh unknown
- 1991-12-13 MX MX9102546A patent/MX9102546A/es active IP Right Grant
- 1991-12-13 EP EP91121452A patent/EP0495208B1/en not_active Expired - Lifetime
- 1991-12-13 PT PT99802A patent/PT99802A/pt not_active Application Discontinuation
- 1991-12-13 DE DE69132812T patent/DE69132812T2/de not_active Expired - Fee Related
- 1991-12-13 PL PL29276591A patent/PL292765A1/xx unknown
- 1991-12-13 CS CS913788A patent/CS378891A3/cs unknown
- 1991-12-16 AR AR91321400A patent/AR245218A1/es active
- 1991-12-16 JP JP33233391A patent/JP3437850B2/ja not_active Expired - Lifetime
-
1992
- 1992-01-07 TW TW081100084A patent/TW201330B/zh not_active IP Right Cessation
-
1999
- 1999-11-24 FI FI992503A patent/FI113474B/fi active
Also Published As
Publication number | Publication date |
---|---|
FI19992503A (fi) | 1999-11-24 |
ZA919776B (en) | 1992-09-30 |
AR245218A1 (es) | 1993-12-30 |
AU637734B2 (en) | 1993-06-03 |
NO914935L (no) | 1992-06-15 |
KR920012442A (ko) | 1992-07-27 |
PL292765A1 (en) | 1992-08-24 |
FI915893A0 (fi) | 1991-12-13 |
TW201330B (ja) | 1993-03-01 |
NO914935D0 (no) | 1991-12-13 |
MX9102546A (es) | 1992-07-01 |
CA2055542A1 (en) | 1992-06-15 |
FI113474B (fi) | 2004-04-30 |
CA2055542C (en) | 1999-08-31 |
AU8882391A (en) | 1992-06-25 |
EP0495208B1 (en) | 2001-11-14 |
KR0181179B1 (ko) | 1999-04-01 |
IE914354A1 (en) | 1992-06-17 |
JPH0576371A (ja) | 1993-03-30 |
FI104493B (fi) | 2000-02-15 |
YU193591A (sh) | 1994-06-10 |
IL100363A0 (en) | 1992-09-06 |
EP0495208A3 (en) | 1994-05-18 |
US5268273A (en) | 1993-12-07 |
FI915893A (fi) | 1992-06-15 |
EP0495208A2 (en) | 1992-07-22 |
JP3437850B2 (ja) | 2003-08-18 |
CS378891A3 (en) | 1992-06-17 |
CN1062169A (zh) | 1992-06-24 |
PT99802A (pt) | 1992-12-31 |
ATE208822T1 (de) | 2001-11-15 |
DE69132812D1 (de) | 2001-12-20 |
HU913926D0 (en) | 1992-02-28 |
DE69132812T2 (de) | 2002-06-20 |
Similar Documents
Publication | Publication Date | Title |
---|---|---|
NO314151B1 (no) | Pichia pastoris sur fosfatasegen | |
IE83566B1 (en) | Pichia pastoris acid phosphatase gene | |
US5102789A (en) | Production of epideramal growth factor in pichia pastoris yeast cells | |
US5324639A (en) | Production of insulin-like growth factor-1 in methylotrophic yeast cells | |
US7517668B1 (en) | Process for the production of protein products in aspergillus | |
CA2168037C (en) | Transformation systems for the yeast candida utilis and the expression of heterologous genes therewith | |
EP0341215B1 (en) | Improvements in the production of polypeptides | |
EP0096430A1 (en) | Cloning system for Kluyveromyces species | |
NO180381B (no) | DNA-konstruksjoner inneholdende en Kluyveromyces alfa-faktor ledersekvens for utskillelse av heterologe polypeptider, ekspresjonsvektor og fremgangsmåte til fremstilling av et heterologt polypeptid i gjær | |
NO854333L (no) | Isolering av gener fra gjaerarter av slekten pichia. | |
CA2105064A1 (en) | Genes which influence pichia proteolytic activity, and uses therefor | |
NO179078B (no) | Replikerbar ekspresjonsvektor, anvendelse derav og transformert vert | |
NO302899B1 (no) | Rekombinant DNA-molekyl, transformert vertscelle, anvendelse av rekombinant DNA-molekyl og hybridvektor, og pektinlyasene PLA, PLB, PLC, PLE eller PLF i ren form | |
US5679544A (en) | Modified Kluyveromyces yeasts, their preparation and use | |
EP0592358B1 (en) | Process for the production of protease inhibitors | |
JP3140488B2 (ja) | 融合タンパク質の試験管内プロセシング | |
US5312735A (en) | Supersecreting mutants of saccharomyces cerevisiae | |
KR970005584B1 (ko) | 폴리 펩타이드의 개선된 제조방법 | |
NO894916L (no) | Pichia pastoris glyceraldehyd-3-fosfatdehydrogenasegen. |
Legal Events
Date | Code | Title | Description |
---|---|---|---|
MK1K | Patent expired |