JP2017536835A5 - - Google Patents
Download PDFInfo
- Publication number
- JP2017536835A5 JP2017536835A5 JP2017530121A JP2017530121A JP2017536835A5 JP 2017536835 A5 JP2017536835 A5 JP 2017536835A5 JP 2017530121 A JP2017530121 A JP 2017530121A JP 2017530121 A JP2017530121 A JP 2017530121A JP 2017536835 A5 JP2017536835 A5 JP 2017536835A5
- Authority
- JP
- Japan
- Prior art keywords
- seq
- recombinant fusion
- fusion protein
- protein
- polypeptide
- 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
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 claims 27
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 claims 27
- 108090000765 processed proteins & peptides Proteins 0.000 claims 22
- 229920001184 polypeptide Polymers 0.000 claims 17
- 102000004196 processed proteins & peptides Human genes 0.000 claims 17
- 102000004169 proteins and genes Human genes 0.000 claims 17
- 108090000623 proteins and genes Proteins 0.000 claims 17
- 150000001413 amino acids Chemical class 0.000 claims 10
- 238000003776 cleavage reaction Methods 0.000 claims 10
- 230000007017 scission Effects 0.000 claims 10
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 claims 9
- 230000004927 fusion Effects 0.000 claims 7
- 210000004899 c-terminal region Anatomy 0.000 claims 6
- 108091005804 Peptidases Proteins 0.000 claims 5
- 241000982698 Prorodonopsis coli Species 0.000 claims 5
- 239000004365 Protease Substances 0.000 claims 5
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims 5
- 238000000034 method Methods 0.000 claims 5
- 125000006850 spacer group Chemical group 0.000 claims 5
- 108010093488 His-His-His-His-His-His Proteins 0.000 claims 4
- 108090001061 Insulin Proteins 0.000 claims 3
- 102000004877 Insulin Human genes 0.000 claims 3
- 241000589540 Pseudomonas fluorescens Species 0.000 claims 3
- 210000004027 cell Anatomy 0.000 claims 3
- 230000000593 degrading effect Effects 0.000 claims 3
- 229940125396 insulin Drugs 0.000 claims 3
- 239000004026 insulin derivative Substances 0.000 claims 3
- 108010013369 Enteropeptidase Proteins 0.000 claims 2
- 102100029727 Enteropeptidase Human genes 0.000 claims 2
- 102000004190 Enzymes Human genes 0.000 claims 2
- 108090000790 Enzymes Proteins 0.000 claims 2
- 108010074860 Factor Xa Proteins 0.000 claims 2
- 102000004961 Furin Human genes 0.000 claims 2
- 108090001126 Furin Proteins 0.000 claims 2
- -1 Glp2 Proteins 0.000 claims 2
- 108010076181 Proinsulin Proteins 0.000 claims 2
- 108090000631 Trypsin Proteins 0.000 claims 2
- 102000004142 Trypsin Human genes 0.000 claims 2
- 230000001580 bacterial effect Effects 0.000 claims 2
- 229940088598 enzyme Drugs 0.000 claims 2
- 239000013604 expression vector Substances 0.000 claims 2
- 239000002773 nucleotide Substances 0.000 claims 2
- 125000003729 nucleotide group Chemical group 0.000 claims 2
- 239000012588 trypsin Substances 0.000 claims 2
- 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 claims 1
- 101800000407 Brain natriuretic peptide 32 Proteins 0.000 claims 1
- 108010075254 C-Peptide Proteins 0.000 claims 1
- 108090000317 Chymotrypsin Proteins 0.000 claims 1
- 101100192865 Drosophila melanogaster GlyP gene Proteins 0.000 claims 1
- 108010032976 Enfuvirtide Proteins 0.000 claims 1
- 108010011459 Exenatide Proteins 0.000 claims 1
- HTQBXNHDCUEHJF-XWLPCZSASA-N Exenatide Chemical compound C([C@@H](C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)NCC(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CO)C(N)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@@H](NC(=O)CNC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)O)C(C)C)C1=CC=CC=C1 HTQBXNHDCUEHJF-XWLPCZSASA-N 0.000 claims 1
- 102100039619 Granulocyte colony-stimulating factor Human genes 0.000 claims 1
- HVLSXIKZNLPZJJ-TXZCQADKSA-N HA peptide Chemical compound C([C@@H](C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](C(C)C)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](C)C(O)=O)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CC=1C=CC(O)=CC=1)C1=CC=C(O)C=C1 HVLSXIKZNLPZJJ-TXZCQADKSA-N 0.000 claims 1
- 101000746367 Homo sapiens Granulocyte colony-stimulating factor Proteins 0.000 claims 1
- 108010073961 Insulin Aspart Proteins 0.000 claims 1
- 108010057186 Insulin Glargine Proteins 0.000 claims 1
- 108010065920 Insulin Lispro Proteins 0.000 claims 1
- FYZPCMFQCNBYCY-WIWKJPBBSA-N Insulin degludec Chemical compound CC[C@H](C)[C@H](NC(=O)CN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@H]1CSSC[C@@H]2NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CSSC[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc3c[nH]cn3)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)Cc3ccccc3)C(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](Cc3c[nH]cn3)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc3ccc(O)cc3)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](Cc3ccc(O)cc3)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc3ccc(O)cc3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC2=O)C(=O)N[C@@H](CC(N)=O)C(O)=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](Cc2ccccc2)C(=O)N[C@@H](Cc2ccccc2)C(=O)N[C@@H](Cc2ccc(O)cc2)C(=O)N[C@@H]([C@@H](C)O)C(=O)N2CCC[C@H]2C(=O)N[C@@H](CCCCNC(=O)CC[C@H](NC(=O)CCCCCCCCCCCCCCC(O)=O)C(O)=O)C(O)=O)NC1=O)[C@@H](C)O)[C@@H](C)CC FYZPCMFQCNBYCY-WIWKJPBBSA-N 0.000 claims 1
- COCFEDIXXNGUNL-RFKWWTKHSA-N Insulin glargine Chemical group 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)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O)C(=O)NCC(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 COCFEDIXXNGUNL-RFKWWTKHSA-N 0.000 claims 1
- 108090000723 Insulin-Like Growth Factor I Proteins 0.000 claims 1
- 102000004218 Insulin-Like Growth Factor I Human genes 0.000 claims 1
- 102100026720 Interferon beta Human genes 0.000 claims 1
- 108090000467 Interferon-beta Proteins 0.000 claims 1
- 101710175625 Maltose/maltodextrin-binding periplasmic protein Proteins 0.000 claims 1
- 229960002376 chymotrypsin Drugs 0.000 claims 1
- 238000012258 culturing Methods 0.000 claims 1
- PEASPLKKXBYDKL-FXEVSJAOSA-N enfuvirtide Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC(O)=CC=1)NC(C)=O)[C@@H](C)O)[C@@H](C)CC)C1=CN=CN1 PEASPLKKXBYDKL-FXEVSJAOSA-N 0.000 claims 1
- 229960002062 enfuvirtide Drugs 0.000 claims 1
- 229960001519 exenatide Drugs 0.000 claims 1
- WNRQPCUGRUFHED-DETKDSODSA-N humalog Chemical compound C([C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CS)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CO)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CS)NC(=O)[C@H](CS)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(=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=1C=CC(O)=CC=1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(O)=O)C1=CC=C(O)C=C1.C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CS)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)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CS)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1NC=NC=1)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 WNRQPCUGRUFHED-DETKDSODSA-N 0.000 claims 1
- 238000011534 incubation Methods 0.000 claims 1
- 230000001939 inductive effect Effects 0.000 claims 1
- 229960004717 insulin aspart Drugs 0.000 claims 1
- 108010050259 insulin degludec Proteins 0.000 claims 1
- 229960003948 insulin detemir Drugs 0.000 claims 1
- 229960002869 insulin glargine Drugs 0.000 claims 1
- 229960002068 insulin lispro Drugs 0.000 claims 1
- UGOZVNFCFYTPAZ-IOXYNQHNSA-N levemir Chemical compound CCCCCCCCCCCCCC(=O)NCCCC[C@@H](C(O)=O)NC(=O)[C@@H]1CCCN1C(=O)[C@H]([C@@H](C)O)NC(=O)[C@@H](NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)CNC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(O)=O)NC(=O)CNC(=O)[C@H]1NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=2C=CC(O)=CC=2)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=2N=CNC=2)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=2N=CNC=2)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=2C=CC=CC=2)C(C)C)CSSC[C@@H]2NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)C(C)C)CSSC[C@H](NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CO)NC(=O)[C@H]([C@@H](C)O)NC2=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=2C=CC(O)=CC=2)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=2C=CC(O)=CC=2)C(=O)N[C@@H](CSSC1)C(=O)N[C@@H](CC(N)=O)C(O)=O)CC1=CC=C(O)C=C1 UGOZVNFCFYTPAZ-IOXYNQHNSA-N 0.000 claims 1
- 238000004519 manufacturing process Methods 0.000 claims 1
- 244000005700 microbiome Species 0.000 claims 1
- HPNRHPKXQZSDFX-OAQDCNSJSA-N nesiritide Chemical compound C([C@H]1C(=O)NCC(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)NCC(=O)N[C@@H](CSSC[C@@H](C(=O)N1)NC(=O)CNC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CCSC)NC(=O)[C@H](CCCCN)NC(=O)[C@H]1N(CCC1)C(=O)[C@@H](N)CO)C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1N=CNC=1)C(O)=O)=O)[C@@H](C)CC)C1=CC=CC=C1 HPNRHPKXQZSDFX-OAQDCNSJSA-N 0.000 claims 1
- 229960001267 nesiritide Drugs 0.000 claims 1
- VOMXSOIBEJBQNF-UTTRGDHVSA-N novorapid Chemical compound C([C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CS)NC(=O)[C@H]([C@@H](C)CC)NC(=O)[C@H](CO)NC(=O)[C@H]([C@@H](C)O)NC(=O)[C@H](CS)NC(=O)[C@H](CS)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(=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=1C=CC(O)=CC=1)C(=O)N[C@@H](CS)C(=O)N[C@@H](CC(N)=O)C(O)=O)C1=CC=C(O)C=C1.C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CS)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)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(O)=O)C(C)C)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CS)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1NC=NC=1)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 VOMXSOIBEJBQNF-UTTRGDHVSA-N 0.000 claims 1
- 229920002704 polyhistidine Polymers 0.000 claims 1
- 229960003611 pramlintide Drugs 0.000 claims 1
- 108010029667 pramlintide Proteins 0.000 claims 1
- NRKVKVQDUCJPIZ-MKAGXXMWSA-N pramlintide acetate Chemical compound C([C@@H](C(=O)NCC(=O)N1CCC[C@H]1C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N1[C@@H](CCC1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1NC=NC=1)NC(=O)[C@@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CS)NC(=O)[C@@H](N)CCCCN)[C@@H](C)O)[C@@H](C)O)[C@@H](C)O)C(C)C)C1=CC=CC=C1 NRKVKVQDUCJPIZ-MKAGXXMWSA-N 0.000 claims 1
- 210000003046 sporozoite Anatomy 0.000 claims 1
- 108010073046 teduglutide Proteins 0.000 claims 1
- CILIXQOJUNDIDU-ASQIGDHWSA-N teduglutide Chemical compound C([C@@H](C(=O)N[C@H](C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(O)=O)C(O)=O)[C@@H](C)CC)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCCNC(N)=N)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCSC)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CC=1C=CC=CC=1)NC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(O)=O)NC(=O)CNC(=O)[C@@H](N)CC=1NC=NC=1)[C@@H](C)O)[C@@H](C)CC)C1=CC=CC=C1 CILIXQOJUNDIDU-ASQIGDHWSA-N 0.000 claims 1
- 229960002444 teduglutide Drugs 0.000 claims 1
- BPKIMPVREBSLAJ-QTBYCLKRSA-N ziconotide Chemical compound C([C@H]1C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H]2C(=O)N[C@@H]3C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CO)C(=O)N[C@H](C(N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CSSC2)C(N)=O)=O)CSSC[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@H](CCCCN)NC(=O)[C@@H](N)CSSC3)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(N1)=O)CCSC)[C@@H](C)O)C1=CC=C(O)C=C1 BPKIMPVREBSLAJ-QTBYCLKRSA-N 0.000 claims 1
- 229960002811 ziconotide Drugs 0.000 claims 1
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201462086119P | 2014-12-01 | 2014-12-01 | |
| US62/086,119 | 2014-12-01 | ||
| PCT/US2015/063027 WO2016089782A1 (en) | 2014-12-01 | 2015-11-30 | Fusion partners for peptide production |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2020148237A Division JP7148579B2 (ja) | 2014-12-01 | 2020-09-03 | ペプチド産生のための融合パートナー |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2017536835A JP2017536835A (ja) | 2017-12-14 |
| JP2017536835A5 true JP2017536835A5 (enExample) | 2019-01-10 |
| JP6817939B2 JP6817939B2 (ja) | 2021-01-20 |
Family
ID=56092296
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2017530121A Active JP6817939B2 (ja) | 2014-12-01 | 2015-11-30 | ペプチド産生のための融合パートナー |
| JP2020148237A Active JP7148579B2 (ja) | 2014-12-01 | 2020-09-03 | ペプチド産生のための融合パートナー |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2020148237A Active JP7148579B2 (ja) | 2014-12-01 | 2020-09-03 | ペプチド産生のための融合パートナー |
Country Status (16)
| Country | Link |
|---|---|
| US (2) | US10118956B2 (enExample) |
| EP (1) | EP3227455B1 (enExample) |
| JP (2) | JP6817939B2 (enExample) |
| KR (1) | KR102353262B1 (enExample) |
| CN (2) | CN113444183B (enExample) |
| AR (1) | AR102865A1 (enExample) |
| AU (1) | AU2015355242B2 (enExample) |
| CA (1) | CA2966358C (enExample) |
| DK (1) | DK3227455T3 (enExample) |
| ES (1) | ES2952405T3 (enExample) |
| MX (1) | MX386884B (enExample) |
| NZ (1) | NZ732400A (enExample) |
| RU (1) | RU2017123283A (enExample) |
| SG (1) | SG11201704362VA (enExample) |
| TW (1) | TWI702289B (enExample) |
| WO (1) | WO2016089782A1 (enExample) |
Families Citing this family (29)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| CN113444183B (zh) | 2014-12-01 | 2025-06-17 | 佩利肯科技控股公司 | 用于肽生产的融合伴侣 |
| US20160357801A1 (en) | 2015-05-15 | 2016-12-08 | Foogal Incorporated | Consumption notification from personal food inventory |
| EP3700921A4 (en) | 2017-10-27 | 2021-12-15 | Pfenex Inc. | Method for production of recombinant erwinia asparaginase |
| JP7358347B2 (ja) | 2017-10-27 | 2023-10-10 | フェネックス インク． | 組み換えＥ．ｃｏｌｉアスパラギナーゼの製造のための方法 |
| US11267863B2 (en) | 2018-01-19 | 2022-03-08 | Pepgene Inc. | N-terminal fusion partner for producing recombinant polypeptide, and method for producing recombinant polypeptide using same |
| CN108191981B (zh) * | 2018-02-06 | 2020-11-03 | 美药星（南京）制药有限公司 | 一种利拉鲁肽中间体多肽的制备方法 |
| KR102017542B1 (ko) * | 2018-02-14 | 2019-09-03 | 주식회사 펩진 | 융합 폴리펩타이드를 이용하여 글루카곤 유사 펩타이드-2 또는 이의 유사체를 생산하는 방법 |
| KR102017540B1 (ko) * | 2018-02-14 | 2019-09-03 | 주식회사 펩진 | 융합 폴리펩타이드를 이용하여 글루카곤 유사 펩타이드-1 또는 이의 유사체를 생산하는 방법 |
| KR102009709B1 (ko) * | 2018-02-14 | 2019-08-12 | 주식회사 펩진 | 융합 폴리펩타이드를 이용하여 인간 부갑상선 호르몬 1-84를 생산하는 방법 |
| CN108977423A (zh) * | 2018-08-17 | 2018-12-11 | 集美大学 | 一种从猪肺中分离提纯血管紧张素转化酶的方法 |
| KR102011291B1 (ko) * | 2018-12-05 | 2019-10-21 | 주식회사 펩진 | 신규한 융합 폴리펩타이드 및 이를 이용하여 인간 부갑상선 호르몬 1-34를 생산하는 방법 |
| EP3893870A1 (en) | 2018-12-13 | 2021-10-20 | Huya Bioscience International LLC | Sulcardine administration for treatment of acute atrial fibrillation |
| CN110305223B (zh) * | 2019-06-26 | 2022-05-13 | 重庆派金生物科技有限公司 | 重组串联融合蛋白制备目标多肽的方法 |
| KR20210010367A (ko) * | 2019-07-19 | 2021-01-27 | 주식회사 펩진 | 인간부갑상선호르몬1-34 생산용 융합태그 |
| KR20210010366A (ko) * | 2019-07-19 | 2021-01-27 | 주식회사 펩진 | 글루카곤 유사 펩타이드-1 또는 이의 유사체 생산용 융합태그 |
| KR20210010368A (ko) * | 2019-07-19 | 2021-01-27 | 주식회사 펩진 | 글루카곤 유사 펩타이드-2 또는 이의 유사체 생산용 융합태그 |
| EP4056584A4 (en) * | 2019-11-08 | 2024-06-05 | Korea Institute of Ocean Science & Technology | NOVEL HUMAN EPIDERMAL GROWTH FACTOR-TF FUSION PROTEIN AND USE THEREOF |
| CN113773400B (zh) * | 2020-06-09 | 2023-08-18 | 宁波鲲鹏生物科技有限公司 | 一种门冬胰岛素衍生物及其应用 |
| WO2022016118A2 (en) * | 2020-07-17 | 2022-01-20 | Cb Therapeutics, Inc. | Prenyltransferase enzymes |
| CN113151296B (zh) * | 2021-03-22 | 2022-09-13 | 云南中烟工业有限责任公司 | 一种烟草热激蛋白相关的基因及其应用 |
| CN112941058B (zh) * | 2021-04-02 | 2023-12-05 | 重庆科润生物医药研发有限公司 | 一种重组溶组织梭菌ii型胶原酶及其制备方法和应用 |
| CN113025599B (zh) * | 2021-04-02 | 2023-09-12 | 重庆科润生物医药研发有限公司 | 一种重组溶组织梭菌i型胶原酶及其制备方法和应用 |
| US20230100757A1 (en) * | 2021-06-10 | 2023-03-30 | Pfenex Inc. | Bacterial hosts for recombinant protein expression |
| EP4380955A1 (en) * | 2021-08-06 | 2024-06-12 | Roche Diagnostics GmbH | Chimeric igg-fc-binding ligand polypeptide and uses thereof for igg affinity purification |
| US20240383959A1 (en) * | 2021-09-09 | 2024-11-21 | Northwestern University | Cell-free methods and compositions comprising tagless therapeutic hormones |
| CN114350587B (zh) * | 2022-01-24 | 2023-10-31 | 修实生物医药(南通)有限公司 | 一种基因重组串联表达利那洛肽的工程菌 |
| CN115109766A (zh) * | 2022-02-14 | 2022-09-27 | 上海理工大学 | 一种耐高温金属蛋白酶及其编码基因和应用 |
| WO2024035782A1 (en) * | 2022-08-10 | 2024-02-15 | Aav Gene Therapeutics, Inc. | Aav-mediated intramuscular delivery of insulin |
| WO2025081111A1 (en) * | 2023-10-12 | 2025-04-17 | The University Of Chicago | Methods and compositions for characterizing rna-binding protein binding sites by in-situ reverse transcription-based sequencing |
Family Cites Families (58)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4769326A (en) | 1980-02-29 | 1988-09-06 | The Regents Of The University Of California | Expression linkers |
| US4551433A (en) | 1981-05-18 | 1985-11-05 | Genentech, Inc. | Microbial hybrid promoters |
| US4755465A (en) | 1983-04-25 | 1988-07-05 | Genentech, Inc. | Secretion of correctly processed human growth hormone in E. coli and Pseudomonas |
| US5281532A (en) | 1983-07-27 | 1994-01-25 | Mycogen Corporation | Pseudomas hosts transformed with bacillus endotoxin genes |
| US4695455A (en) | 1985-01-22 | 1987-09-22 | Mycogen Corporation | Cellular encapsulation of pesticides produced by expression of heterologous genes |
| US4695462A (en) | 1985-06-28 | 1987-09-22 | Mycogen Corporation | Cellular encapsulation of biological pesticides |
| GB8517071D0 (en) | 1985-07-05 | 1985-08-14 | Hoffmann La Roche | Gram-positive expression control sequence |
| US5013653A (en) | 1987-03-20 | 1991-05-07 | Creative Biomolecules, Inc. | Product and process for introduction of a hinge region into a fusion protein to facilitate cleavage |
| US5128130A (en) | 1988-01-22 | 1992-07-07 | Mycogen Corporation | Hybrid Bacillus thuringiensis gene, plasmid and transformed Pseudomonas fluorescens |
| US5055294A (en) | 1988-03-03 | 1991-10-08 | Mycogen Corporation | Chimeric bacillus thuringiensis crystal protein gene comprising hd-73 and berliner 1715 toxin genes, transformed and expressed in pseudomonas fluorescens |
| US5169760A (en) | 1989-07-27 | 1992-12-08 | Mycogen Corporation | Method, vectors, and host cells for the control of expression of heterologous genes from lac operated promoters |
| US7150974B1 (en) | 1991-04-05 | 2006-12-19 | The General Hospital Corporation | Parathyroid hormone receptor binding method |
| EP0604580A1 (en) | 1991-09-19 | 1994-07-06 | Genentech, Inc. | EXPRESSION IN E. COLI OF ANTIBODY FRAGMENTS HAVING AT LEAST A CYSTEINE PRESENT AS A FREE THIOL, USE FOR THE PRODUCTION OF BIFUNCTIONAL F(ab') 2? ANTIBODIES |
| CA2125467C (en) | 1993-07-06 | 2001-02-06 | Heinz Dobeli | Process for producing hydrophobic polypeptides, proteins or peptides |
| US5935824A (en) | 1996-01-31 | 1999-08-10 | Technologene, Inc. | Protein expression system |
| CA2198966C (en) | 1996-03-04 | 2011-06-21 | Yuji Suzuki | Method for cleaving chimeric protein using processing enzyme |
| JPH1175879A (ja) * | 1997-07-08 | 1999-03-23 | Toyota Central Res & Dev Lab Inc | プロテインジスルフィドイソメラーゼを含有する融合タンパク質をコードするｄｎａ |
| US5989868A (en) | 1997-09-12 | 1999-11-23 | The Board Of Regents Of The University Of Oklahoma | Fusion protein systems designed to increase soluble cytoplasmic expression of heterologous proteins in esherichia coli |
| KR100627590B1 (ko) | 1998-01-30 | 2006-09-25 | 다이이치 아스비오파마 가부시키가이샤 | 보조 펩타이드를 사용하는 펩타이드의 제조방법 |
| US6242219B1 (en) | 1999-03-18 | 2001-06-05 | Xoma (Us) Llc | Methods for recombinant peptide production |
| WO2001098366A2 (en) | 2000-06-19 | 2001-12-27 | Dyax Corp. | Enterokinase cleavage sequences and their use |
| JP2002262873A (ja) | 2001-03-06 | 2002-09-17 | Inst Of Physical & Chemical Res | タンパク質ドメインの製造方法及びその方法により得られたドメインを用いるタンパク質の立体構造解析方法 |
| JP4262594B2 (ja) | 2001-06-22 | 2009-05-13 | エフ．ホフマン−ラ ロシュ アーゲー | レトロウイルス表面糖タンパク質を含む可溶性複合体 |
| JP4088584B2 (ja) | 2001-07-26 | 2008-05-21 | アドバンスド プロテイン テクノロジーズ コーポレイション | 融合タンパク質から目的タンパク質を分離する方法。 |
| ATE419265T1 (de) | 2002-07-03 | 2009-01-15 | Dow Global Technologies Inc | Benzoat- und antranilatinduzierbare promotoren |
| CA2495145A1 (en) | 2002-08-09 | 2004-02-19 | National Research Council Of Canada | Staphylococcal nuclease fusion proteins for the production of recombinant peptides |
| US7208585B2 (en) | 2002-09-18 | 2007-04-24 | Genencor International, Inc. | Protein purification |
| US9453251B2 (en) | 2002-10-08 | 2016-09-27 | Pfenex Inc. | Expression of mammalian proteins in Pseudomonas fluorescens |
| US20070026501A1 (en) | 2003-04-18 | 2007-02-01 | Joe Chiba | Immunogen, composition for immulogical use and process for producing antibody using the same |
| JP2005110591A (ja) | 2003-10-08 | 2005-04-28 | Sekisui Chem Co Ltd | 蛋白質の分離方法 |
| WO2005052151A1 (en) | 2003-11-19 | 2005-06-09 | Dow Global Technologies Inc. | Improved protein expression systems |
| EP2327718B1 (en) | 2003-11-21 | 2016-03-23 | Pfenex, Inc. | Improved expression systems with SEC-system secretion |
| EP1689877A1 (en) | 2003-11-24 | 2006-08-16 | Novo Nordisk A/S | Fusion proteins and methods of cleavage of such proteins |
| KR20120076377A (ko) | 2004-01-16 | 2012-07-09 | 다우 글로벌 테크놀로지스 엘엘씨 | 슈도모나스 플루오레센스에서의 포유류 단백질의 발현 |
| WO2006078273A2 (en) | 2004-04-26 | 2006-07-27 | The United States Of America As Represented By Teh Secretary Of Health And Human Services, Nih | Methods and compositions for producing recombinant proteins |
| EP1748071A4 (en) | 2004-05-21 | 2009-01-07 | Takara Bio Inc | PROCESS FOR PRODUCTION OF POLYPEPTIDE |
| EP2412816B1 (en) * | 2004-07-26 | 2014-12-03 | Pfenex Inc. | Process for improved protein expression by strain engineering |
| WO2006016370A2 (en) | 2004-08-11 | 2006-02-16 | Ramot At Tel Aviv University Ltd. | Soluble fusion proteins comprising heterologous polypeptides |
| US7585943B2 (en) | 2005-04-20 | 2009-09-08 | Viromed Co., Ltd. | Compositions and methods for fusion protein separation |
| CN101193906B (zh) | 2005-06-06 | 2012-09-05 | 陶氏环球技术公司 | 细菌宿主细胞中甘露糖醇诱导的启动子系统 |
| BRPI0711878A2 (pt) | 2006-05-30 | 2012-01-10 | Dow Global Technologies Inc | método de otimização do códon |
| EP2363495B1 (en) | 2006-05-30 | 2019-07-24 | Pfenex Inc. | Anthrax vaccine |
| EP1873251A1 (en) | 2006-06-29 | 2008-01-02 | Chemotherapeutisches Forschungsinstitut Georg-Speyer-Haus | Expression vector(s) for enhanced expression of a protein of interest in eukaryotic or prokaryotic host cells |
| CA2677179C (en) | 2007-01-31 | 2016-02-16 | Dow Global Technologies Inc. | Bacterial leader sequences for increased expression |
| CA2685326A1 (en) | 2007-04-27 | 2008-11-06 | Dow Global Technologies Inc. | Method for rapidly screening microbial hosts to identify certain strains with improved yield and/or quality in the expression of heterologous proteins |
| US9580719B2 (en) | 2007-04-27 | 2017-02-28 | Pfenex, Inc. | Method for rapidly screening microbial hosts to identify certain strains with improved yield and/or quality in the expression of heterologous proteins |
| WO2009019715A1 (en) | 2007-08-09 | 2009-02-12 | Usv Limited | Novel orthogonal process for purification of recombinant human parathyroid hormone (rhpth) (1-34) |
| EP2594646A3 (en) * | 2007-09-21 | 2013-11-06 | BASF Plant Science GmbH | Plant with increased yield |
| WO2009086132A2 (en) | 2007-12-20 | 2009-07-09 | University Of Southern California | Design of spacers to increase the expression of recombinant fusion proteins |
| EP2127678A1 (en) | 2008-05-26 | 2009-12-02 | Roche Diagnostics GmbH | SlpA as a tool for recombinant protein and enzyme technology |
| JP2010006745A (ja) * | 2008-06-27 | 2010-01-14 | Sekisui Chem Co Ltd | 融合タンパク質、融合タンパク質固定化担体、化合物のスクリーニング方法、スクリーニング用組成物、並びに、スクリーニング用キット |
| CN102239183B (zh) | 2008-12-04 | 2017-06-30 | 韩国生命工学研究院 | 大量分泌的蛋白的筛选和它们作为融合配偶体在重组蛋白制备中应用 |
| US8455218B2 (en) | 2010-04-01 | 2013-06-04 | Pfenex, Inc. | Methods for G-CSF production in a Pseudomonas host cell |
| WO2011151714A1 (en) | 2010-06-04 | 2011-12-08 | Lupin Limited | Modified sak gene for the production of recombinant proteins |
| AR086250A1 (es) | 2011-05-05 | 2013-11-27 | Hoffmann La Roche | Polipeptido de fusion presentador de una secuencia de aminoacidos y utilizacion del mismo |
| US9169304B2 (en) | 2012-05-01 | 2015-10-27 | Pfenex Inc. | Process for purifying recombinant Plasmodium falciparum circumsporozoite protein |
| CN113444183B (zh) | 2014-12-01 | 2025-06-17 | 佩利肯科技控股公司 | 用于肽生产的融合伴侣 |
| CA2974343A1 (en) | 2015-02-13 | 2016-08-18 | Sekisui Chemical Co., Ltd. | Nucleic acid, fusion protein, recombined cell, and isoprene or cyclic terpene production method |
-
2015
- 2015-11-30 CN CN202110725675.2A patent/CN113444183B/zh active Active
- 2015-11-30 JP JP2017530121A patent/JP6817939B2/ja active Active
- 2015-11-30 WO PCT/US2015/063027 patent/WO2016089782A1/en not_active Ceased
- 2015-11-30 CA CA2966358A patent/CA2966358C/en active Active
- 2015-11-30 NZ NZ732400A patent/NZ732400A/en unknown
- 2015-11-30 RU RU2017123283A patent/RU2017123283A/ru not_active Application Discontinuation
- 2015-11-30 AU AU2015355242A patent/AU2015355242B2/en active Active
- 2015-11-30 MX MX2017006866A patent/MX386884B/es unknown
- 2015-11-30 CN CN201580064973.4A patent/CN107532190B/zh active Active
- 2015-11-30 US US14/954,766 patent/US10118956B2/en active Active
- 2015-11-30 SG SG11201704362VA patent/SG11201704362VA/en unknown
- 2015-11-30 KR KR1020177017007A patent/KR102353262B1/ko active Active
- 2015-11-30 DK DK15866061.3T patent/DK3227455T3/da active
- 2015-11-30 ES ES15866061T patent/ES2952405T3/es active Active
- 2015-11-30 EP EP15866061.3A patent/EP3227455B1/en active Active
- 2015-12-01 AR ARP150103916A patent/AR102865A1/es unknown
- 2015-12-01 TW TW104140109A patent/TWI702289B/zh active
-
2018
- 2018-09-19 US US16/135,875 patent/US10981968B2/en active Active
-
2020
- 2020-09-03 JP JP2020148237A patent/JP7148579B2/ja active Active
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2017536835A5 (enExample) | ||
| RU2017123283A (ru) | Партнеры по слиянию для получения пептидов | |
| CN104619726B (zh) | 由超折叠绿色荧光蛋白构成的融合蛋白及其用途 | |
| HRP20200871T1 (hr) | Izmjenjeni rsv f proteini i postupci njihove uporabe | |
| EP2280066A2 (en) | Recombinant Clostridium neurotoxin fragments | |
| CA2443365A1 (en) | Methods for the recombinant production of antifusogenic peptides | |
| JP2004532033A5 (enExample) | ||
| NZ597685A (en) | Proteins and nucleic acids from meningitis/sepsis-associated escherichia coli | |
| Yang et al. | Expression and purification of the antimicrobial peptide cecropin AD by fusion with cationic elastin-like polypeptides | |
| JP2020529221A5 (enExample) | ||
| CN101967493A (zh) | 一种原核表达载体及其应用 | |
| CA2636075A1 (en) | Chimaeric fusion protein with superior chaperone and folding activities | |
| US7575920B2 (en) | Yeast expression vectors for production of ITF | |
| US11267863B2 (en) | N-terminal fusion partner for producing recombinant polypeptide, and method for producing recombinant polypeptide using same | |
| CN110835366B (zh) | 促进蛋白质可溶性表达的标签多肽及其用途 | |
| ES2525317T3 (es) | Producción recombinante de inhibidores de la fusión antivirales peptídicos | |
| WO2016161983A1 (zh) | 一种融合载体蛋白及其在促进目的蛋白或多肽表达中的应用 | |
| WO2022194375A1 (en) | Fusion proteins comprising gg repeat sequences | |
| JP2015510770A (ja) | 組換えペプチドの産生方法 | |
| CN105255932B (zh) | 一种芋螺毒素变异体gmviia及其制备方法和应用 | |
| EP4587452A1 (en) | Fusion proteins comprising gg repeat sequences iii | |
| WO2023143563A1 (zh) | IgA蛋白酶截短体、包含IgA蛋白酶截短体的融合蛋白及其用途 | |
| KR101830792B1 (ko) | 항균 펩타이드를 포함하는 불용성 융합단백질 및 이를 이용한 항균 펩타이드의 제조 방법 | |
| KR102064810B1 (ko) | 재조합 폴리펩타이드 생산용 n-말단 융합 파트너 및 이를 이용하여 재조합 폴리펩타이드를 생산하는 방법 | |
| JP2004529601A5 (enExample) |