JP2016518833A5 - - Google Patents
Download PDFInfo
- Publication number
- JP2016518833A5 JP2016518833A5 JP2016509127A JP2016509127A JP2016518833A5 JP 2016518833 A5 JP2016518833 A5 JP 2016518833A5 JP 2016509127 A JP2016509127 A JP 2016509127A JP 2016509127 A JP2016509127 A JP 2016509127A JP 2016518833 A5 JP2016518833 A5 JP 2016518833A5
- Authority
- JP
- Japan
- Prior art keywords
- protein
- isomerase
- extract
- exogenous
- interest
- 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
- 108090000623 proteins and genes Proteins 0.000 claims description 80
- 239000000284 extract Substances 0.000 claims description 73
- 102000004169 proteins and genes Human genes 0.000 claims description 63
- 102000006010 Protein Disulfide-Isomerase Human genes 0.000 claims description 62
- 108020003519 protein disulfide isomerase Proteins 0.000 claims description 62
- 238000000034 method Methods 0.000 claims description 57
- 241000894006 Bacteria Species 0.000 claims description 44
- 230000001580 bacterial effect Effects 0.000 claims description 39
- 101000878213 Homo sapiens Inactive peptidyl-prolyl cis-trans isomerase FKBP6 Proteins 0.000 claims description 29
- 102100036984 Inactive peptidyl-prolyl cis-trans isomerase FKBP6 Human genes 0.000 claims description 29
- 108010020062 Peptidylprolyl Isomerase Proteins 0.000 claims description 22
- 102000009658 Peptidylprolyl Isomerase Human genes 0.000 claims description 22
- 230000015572 biosynthetic process Effects 0.000 claims description 18
- 238000003786 synthesis reaction Methods 0.000 claims description 18
- 241000588724 Escherichia coli Species 0.000 claims description 15
- 230000014509 gene expression Effects 0.000 claims description 15
- 150000001413 amino acids Chemical class 0.000 claims description 12
- 238000011534 incubation Methods 0.000 claims description 12
- 238000001243 protein synthesis Methods 0.000 claims description 12
- 210000003705 ribosome Anatomy 0.000 claims description 12
- 230000014616 translation Effects 0.000 claims description 12
- 102000039446 nucleic acids Human genes 0.000 claims description 11
- 108020004707 nucleic acids Proteins 0.000 claims description 11
- 150000007523 nucleic acids Chemical class 0.000 claims description 11
- 230000010627 oxidative phosphorylation Effects 0.000 claims description 10
- 102000004195 Isomerases Human genes 0.000 claims description 9
- 108090000769 Isomerases Proteins 0.000 claims description 9
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 claims description 7
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims description 6
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims description 6
- 230000000975 bioactive effect Effects 0.000 claims description 6
- 210000004027 cell Anatomy 0.000 claims description 5
- 238000012258 culturing Methods 0.000 claims description 2
- 230000002045 lasting effect Effects 0.000 claims description 2
- 102000035195 Peptidases Human genes 0.000 claims 4
- 108091005804 Peptidases Proteins 0.000 claims 4
- 235000019833 protease Nutrition 0.000 claims 4
- 101001065501 Escherichia phage MS2 Lysis protein Proteins 0.000 claims 1
- 230000008827 biological function Effects 0.000 claims 1
- 125000001151 peptidyl group Chemical group 0.000 claims 1
- 108090000175 Cis-trans-isomerases Proteins 0.000 description 1
- 102000003813 Cis-trans-isomerases Human genes 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000003834 intracellular effect Effects 0.000 description 1
- 230000002018 overexpression Effects 0.000 description 1
- 230000001131 transforming effect Effects 0.000 description 1
Applications Claiming Priority (5)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US201361813914P | 2013-04-19 | 2013-04-19 | |
| US61/813,914 | 2013-04-19 | ||
| US201461937069P | 2014-02-07 | 2014-02-07 | |
| US61/937,069 | 2014-02-07 | ||
| PCT/US2014/034643 WO2014172631A2 (en) | 2013-04-19 | 2014-04-18 | Expression of biologically active proteins in a bacterial cell-free synthesis system using bacterial cells transformed to exhibit elevated levels of chaperone expression |
Related Child Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2018136909A Division JP2018157837A (ja) | 2013-04-19 | 2018-07-20 | 上昇したレベルの外因性シャペロンを有する細胞抽出物を用いる細菌無細胞合成系における生物活性のあるタンパク質の発現 |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2016518833A JP2016518833A (ja) | 2016-06-30 |
| JP2016518833A5 true JP2016518833A5 (enExample) | 2017-07-20 |
| JP6463732B2 JP6463732B2 (ja) | 2019-02-06 |
Family
ID=50733442
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2016509127A Active JP6463732B2 (ja) | 2013-04-19 | 2014-04-18 | 上昇したレベルの外因性シャペロンを有する細胞抽出物を用いる細菌無細胞合成系における生物活性のあるタンパク質の発現 |
| JP2018136909A Withdrawn JP2018157837A (ja) | 2013-04-19 | 2018-07-20 | 上昇したレベルの外因性シャペロンを有する細胞抽出物を用いる細菌無細胞合成系における生物活性のあるタンパク質の発現 |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2018136909A Withdrawn JP2018157837A (ja) | 2013-04-19 | 2018-07-20 | 上昇したレベルの外因性シャペロンを有する細胞抽出物を用いる細菌無細胞合成系における生物活性のあるタンパク質の発現 |
Country Status (13)
| Country | Link |
|---|---|
| US (3) | US10190145B2 (enExample) |
| EP (1) | EP2986731B1 (enExample) |
| JP (2) | JP6463732B2 (enExample) |
| KR (1) | KR102289258B1 (enExample) |
| CN (1) | CN105283556B (enExample) |
| AU (1) | AU2014253785B2 (enExample) |
| CA (1) | CA2909516C (enExample) |
| DK (1) | DK2986731T3 (enExample) |
| ES (1) | ES2922358T3 (enExample) |
| HU (1) | HUE059565T2 (enExample) |
| IL (1) | IL242148B (enExample) |
| SG (2) | SG11201508642WA (enExample) |
| WO (1) | WO2014172631A2 (enExample) |
Families Citing this family (51)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| SG11201508642WA (en) | 2013-04-19 | 2015-11-27 | Sutro Biopharma Inc | Expression of biologically active proteins in a bacterial cell-free synthesis system using cell extracts with elevated levels of exogenous chaperones |
| US10316322B2 (en) * | 2014-07-02 | 2019-06-11 | Sutro Biopharma, Inc. | High growth capacity auxotrophic Escherichia coli and methods of use |
| ES2819256T3 (es) | 2014-11-05 | 2021-04-15 | Genentech Inc | Métodos para producir proteínas bicatenarias en bacterias |
| US10112994B2 (en) | 2014-11-05 | 2018-10-30 | Genentech, Inc. | Methods of producing two chain proteins in bacteria |
| EP3234170A4 (en) * | 2014-12-19 | 2018-07-25 | Sutro Biopharma, Inc. | Codon optimization for titer and fidelity improvement |
| EA037654B1 (ru) | 2014-12-30 | 2021-04-27 | Селджин Корпорейшн | Анти-cd47-антитела и их применения |
| EP3265557B1 (en) * | 2015-03-06 | 2019-10-16 | F. Hoffmann-La Roche AG | Ultrapurified dsba and dsbc and methods of making and using the same |
| US20170029798A1 (en) * | 2015-07-27 | 2017-02-02 | Cellivery Therapeutics, Inc. | Development of Improved Cell-Permeable (iCP) Parkin Recombinant Protein as a Protein-Based Anti-Neurodegenerative Agent for the Treatment of Parkinson's Disease-Associated Phenotypes by Utilizing BBB-Penetrating Protein Delivery System MITT, Enabled by Advanced Macromolecule Transduction Domain (aMTD) |
| BR112018003127A2 (pt) * | 2015-08-20 | 2018-09-25 | Genentech Inc | purificação de fkpa e usos do mesmo para produzir polipeptídeos recombinantes |
| CN105198983B (zh) * | 2015-09-11 | 2018-11-06 | 中国石油大学(华东) | 一种利于七次跨膜蛋白ccr5功能性表达的方法 |
| CN106190940B (zh) * | 2016-07-19 | 2019-06-14 | 北京三元基因药业股份有限公司 | 表达抗TNF抗体Fab片段的重组大肠杆菌工程菌 |
| CN106399352B (zh) * | 2016-11-09 | 2020-04-17 | 华东理工大学 | 调节目标蛋白表达的折叠因子及其应用 |
| JP7015836B2 (ja) * | 2016-12-30 | 2022-02-03 | エヌティーエックスバイオ，エルエルシー | 新規無機リン酸ベースエネルギー再生機能を備えた無細胞発現系 |
| US12227778B2 (en) | 2016-12-30 | 2025-02-18 | Nature's Toolbox, Inc. | Cell-free expression system having novel inorganic polyphosphate-based energy regeneration |
| US11951165B2 (en) | 2016-12-30 | 2024-04-09 | Vaxcyte, Inc. | Conjugated vaccine carrier proteins |
| WO2018126229A2 (en) | 2016-12-30 | 2018-07-05 | Sutrovax, Inc. | Polypeptide-antigen conjugates with non-natural amino acids |
| AU2018300069C1 (en) | 2017-07-11 | 2025-11-20 | Synthorx, Inc. | Incorporation of unnatural nucleotides and methods thereof |
| MX2020001332A (es) | 2017-08-03 | 2020-09-09 | Synthorx Inc | Conjugados de citoquina para el tratamiento de enfermedades proliferativas e infecciosas. |
| WO2019033095A1 (en) * | 2017-08-11 | 2019-02-14 | Synvitrobio, Inc. | ENHANCED IN VITRO TRANSCRIPTION / TRANSLATION (TXTL) SYSTEM AND USE THEREOF |
| WO2019127469A1 (zh) * | 2017-12-29 | 2019-07-04 | 康码（上海）生物科技有限公司 | 一种高效的能源再生体系(bes)、试剂盒及其制备方法 |
| MY203509A (en) | 2018-02-26 | 2024-06-30 | Synthorx Inc | Il-15 conjugates and uses thereof |
| AU2019301699C1 (en) | 2018-07-11 | 2024-10-10 | Actym Therapeutics, Inc. | Engineered immunostimulatory bacterial strains and uses thereof |
| AU2019375413A1 (en) * | 2018-11-05 | 2021-05-27 | Genentech, Inc. | Methods of producing two chain proteins in prokaryotic host cells |
| BR112021005401A2 (pt) | 2018-11-08 | 2021-06-29 | Synthorx, Inc. | conjugados de interleucina 10 e usos dos mesmos |
| DK3877552T3 (en) * | 2018-11-08 | 2023-05-15 | Sutro Biopharma Inc | E coli-stammer med oxidativt cytoplasma |
| CN109371049A (zh) * | 2018-11-14 | 2019-02-22 | 天津大学 | 分子伴侣在促进单克隆抗体的形成和/或提高单克隆抗体的表达量中的应用 |
| BR112021014415A2 (pt) | 2019-02-06 | 2021-09-21 | Synthorx, Inc. | Conjugados de il-2 e métodos de uso dos mesmos |
| US12024709B2 (en) | 2019-02-27 | 2024-07-02 | Actym Therapeutics, Inc. | Immunostimulatory bacteria engineered to colonize tumors, tumor-resident immune cells, and the tumor microenvironment |
| TWI873169B (zh) | 2019-08-15 | 2025-02-21 | 美商欣爍克斯公司 | 使用il-2接合物之免疫腫瘤學組合療法 |
| JP7758662B2 (ja) | 2019-09-10 | 2025-10-22 | シンソークス， インコーポレイテッド | Ｉｌ－２コンジュゲートおよび自己免疫疾患を治療するための使用方法 |
| IL291786A (en) | 2019-11-04 | 2022-06-01 | Synthorx Inc | Interleukin 10 conjugates and their use |
| WO2021091304A1 (ko) * | 2019-11-08 | 2021-05-14 | 한국해양과학기술원 | 신규한 인간 상피세포성장인자-tf 융합 단백질 및 이의 용도 |
| EP4114931A4 (en) * | 2020-03-05 | 2024-05-01 | Curie Co. Inc. | METHODS FOR CELL PROTEIN EXPRESSION OF MATURE POLYPEPTIDES DERIVED FROM ZYMOGENS AND PROPROTEINS |
| EP4142711A1 (en) * | 2020-04-29 | 2023-03-08 | Willow Biosciences Inc. | Compositions and methods for enhancing recombinant biosynthesis of cannabinoids |
| KR20230027235A (ko) | 2020-06-25 | 2023-02-27 | 신톡스, 인크. | Il-2 콘쥬게이트 및 항-egfr 항체를 사용한 면역 종양학 병용 요법 |
| KR20220000028U (ko) | 2020-06-29 | 2022-01-05 | 채인자 | 농작물용 농약 간편 분무장치 |
| EP4211156A1 (en) | 2020-09-14 | 2023-07-19 | Sutro Biopharma, Inc. | Method for large scale production of antibodies using a cell-free protein synthesis system |
| WO2022076853A1 (en) | 2020-10-09 | 2022-04-14 | Synthorx, Inc. | Immuno oncology combination therapy with il-2 conjugates and pembrolizumab |
| TW202228786A (zh) | 2020-10-09 | 2022-08-01 | 美商欣爍克斯公司 | Il-2接合物的免疫腫瘤學療法 |
| TW202245843A (zh) | 2021-02-12 | 2022-12-01 | 美商欣爍克斯公司 | Ｉｌ－２接合物及西米普利單抗（ｃｅｍｉｐｌｉｍａｂ）之皮膚癌組合療法 |
| TW202302148A (zh) | 2021-02-12 | 2023-01-16 | 美商欣爍克斯公司 | 使用ｉｌ－２接合物和抗ｐｄ－１抗體或其抗原結合片段的肺癌組合療法 |
| EP4346903A1 (en) | 2021-06-03 | 2024-04-10 | Synthorx, Inc. | Head and neck cancer combination therapy comprising an il-2 conjugate and pembrolizumab |
| WO2023122573A1 (en) | 2021-12-20 | 2023-06-29 | Synthorx, Inc. | Head and neck cancer combination therapy comprising an il-2 conjugate and pembrolizumab |
| WO2023122750A1 (en) | 2021-12-23 | 2023-06-29 | Synthorx, Inc. | Cancer combination therapy with il-2 conjugates and cetuximab |
| AU2023295552A1 (en) * | 2022-06-17 | 2024-12-12 | Insitro, Inc. | In situ sequencing of rna transcripts with non-uniform 5' ends |
| CN115028691B (zh) * | 2022-06-29 | 2024-09-10 | 青岛硕景生物科技有限公司 | 一种检测试纸用的独立质控系统、杂交瘤细胞株、质控线用包被单克隆抗体及其应用 |
| WO2024136899A1 (en) | 2022-12-21 | 2024-06-27 | Synthorx, Inc. | Cancer therapy with il-2 conjugates and chimeric antigen receptor therapies |
| TW202444349A (zh) | 2023-03-20 | 2024-11-16 | 美商欣爍克斯公司 | 使用ｉｌ－２綴合物之癌症療法 |
| CN116925196B (zh) * | 2023-06-08 | 2025-04-18 | 齐鲁工业大学(山东省科学院) | 小分子热休克蛋白rsp_1572在提高宿主菌环境耐受性中的应用 |
| WO2025158385A1 (en) | 2024-01-25 | 2025-07-31 | Genzyme Corporation | Pegylated il-2 for suppressing adaptive immune response to gene therapy |
| CN118048325B (zh) * | 2024-04-16 | 2024-07-16 | 天津凯莱英生物科技有限公司 | 酶的高通量筛选方法及酶库的构建方法 |
Family Cites Families (10)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE10145694A1 (de) * | 2001-09-17 | 2003-04-03 | Roche Diagnostics Gmbh | Verfahren zur Erhöhung der Löslichkeit, der Expressionsrate und der Aktivität von Proteinen während der rekombinanten Herstellung |
| US20060134739A1 (en) * | 2003-03-11 | 2006-06-22 | Chatterjee Deb K | Synthesis of proteins by cell-free protein expression |
| JP2005253432A (ja) * | 2004-03-15 | 2005-09-22 | Sekisui Chem Co Ltd | タンパク質の生産方法、並びにそれに使用するための組成物、試薬及びキット |
| JP4561243B2 (ja) * | 2004-08-27 | 2010-10-13 | 株式会社豊田中央研究所 | 無細胞タンパク質合成系のための媒体 |
| EP2035554B1 (en) * | 2006-06-29 | 2013-04-24 | The Board of Trustees of The Leland Stanford Junior University | Cell-free synthesis of proteins containing unnatural amino acids |
| CA2673765A1 (en) * | 2007-01-18 | 2008-07-24 | The Board Of Trustees Of The Leland Stanford Junior University | Enhanced cell-free synthesis of active proteins containing disulfide bonds |
| JP5798489B2 (ja) * | 2009-01-12 | 2015-10-21 | ストロ バイオファーマ， インコーポレイテッド | インビトロタンパク質合成システムを用いて非天然アミノ酸をタンパク質に選択的に導入するためのモノチャージシステム |
| CN102732548A (zh) * | 2012-05-16 | 2012-10-17 | 中国农业大学 | 一种表达蛇毒激肽原酶的高效麦胚无细胞蛋白合成系统的建立及应用 |
| KR102018863B1 (ko) * | 2012-10-12 | 2019-09-05 | 서트로 바이오파마, 인크. | 개선된 발현을 위해 박테리아 추출물 중 선택 단백질의 단백질분해 불활성화 |
| SG11201508642WA (en) * | 2013-04-19 | 2015-11-27 | Sutro Biopharma Inc | Expression of biologically active proteins in a bacterial cell-free synthesis system using cell extracts with elevated levels of exogenous chaperones |
-
2014
- 2014-04-18 SG SG11201508642WA patent/SG11201508642WA/en unknown
- 2014-04-18 CA CA2909516A patent/CA2909516C/en active Active
- 2014-04-18 ES ES14724974T patent/ES2922358T3/es active Active
- 2014-04-18 SG SG10202108497TA patent/SG10202108497TA/en unknown
- 2014-04-18 US US14/256,324 patent/US10190145B2/en active Active
- 2014-04-18 AU AU2014253785A patent/AU2014253785B2/en active Active
- 2014-04-18 WO PCT/US2014/034643 patent/WO2014172631A2/en not_active Ceased
- 2014-04-18 KR KR1020157032515A patent/KR102289258B1/ko active Active
- 2014-04-18 EP EP14724974.2A patent/EP2986731B1/en active Active
- 2014-04-18 DK DK14724974.2T patent/DK2986731T3/da active
- 2014-04-18 CN CN201480032258.8A patent/CN105283556B/zh active Active
- 2014-04-18 JP JP2016509127A patent/JP6463732B2/ja active Active
- 2014-04-18 HU HUE14724974A patent/HUE059565T2/hu unknown
-
2015
- 2015-10-18 IL IL242148A patent/IL242148B/en active IP Right Grant
-
2018
- 2018-07-20 JP JP2018136909A patent/JP2018157837A/ja not_active Withdrawn
- 2018-12-03 US US16/208,245 patent/US10774354B2/en active Active
-
2020
- 2020-08-12 US US16/991,607 patent/US20210054429A1/en active Pending
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| JP2016518833A5 (enExample) | ||
| WO2014172631A4 (en) | Expression of biologically active proteins in a bacterial cell-free synthesis system using cell extracts with elevated levels of exogenous chaperones | |
| Bhatwa et al. | Challenges associated with the formation of recombinant protein inclusion bodies in Escherichia coli and strategies to address them for industrial applications | |
| Song et al. | Cultivation at 6–10 C is an effective strategy to overcome the insolubility of recombinant proteins in Escherichia coli | |
| Kinney et al. | Elucidating essential role of conserved carboxysomal protein CcmN reveals common feature of bacterial microcompartment assembly | |
| Ferrer-Miralles et al. | General introduction: recombinant protein production and purification of insoluble proteins | |
| Gasser et al. | Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview | |
| Oganesyan et al. | Effect of osmotic stress and heat shock in recombinant protein overexpression and crystallization | |
| Sarkari et al. | Improved expression of single-chain antibodies in Ustilago maydis | |
| WO2011075686A3 (en) | Methods & compositions comprising heat shock proteins | |
| JP2021506328A (ja) | 発酵プロセス | |
| Sun et al. | Enhanced production of recombinant proteins in Corynebacterium glutamicum by constructing a bicistronic gene expression system | |
| Ukkonen et al. | Use of slow glucose feeding as supporting carbon source in lactose autoinduction medium improves the robustness of protein expression at different aeration conditions | |
| WO2011091350A3 (en) | Methods & compositions for improving protein production | |
| CN104611396B (zh) | 一种生产谷胱甘肽的方法 | |
| JP2017517257A5 (enExample) | ||
| Samant et al. | Effect of codon-optimized E. coli signal peptides on recombinant Bacillus stearothermophilus maltogenic amylase periplasmic localization, yield and activity | |
| Skretas et al. | Multi-copy genes that enhance the yield of mammalian G protein-coupled receptors in Escherichia coli | |
| Liu et al. | Efficient extracellular production of κ-carrageenase in Escherichia coli: Effects of wild-type signal sequence and process conditions on extracellular secretion | |
| Ahn et al. | Improved recombinant protein production using heat shock proteins in Escherichia coli | |
| Tan et al. | The role of lac operon and lac repressor in the induction using lactose for the expression of periplasmic human interferon-α2b by Escherichia coli | |
| Mohammadinezhad et al. | Efficient osmolyte-based procedure to increase expression level and solubility of infectious hematopoietic necrosis virus (IHNV) nucleoprotein in E. coli | |
| KR20170105079A (ko) | 천연 또는 가공된 진핵 세포의 생리에 긍정적으로 영향을 미치는 박테리아 샤페론의 조합물 | |
| JP2014512814A (ja) | 大腸菌での異種タンパク質生成のための新規発現および分泌ベクター系 | |
| Cho et al. | Maltose binding protein facilitates high-level expression and functional purification of the chemokines RANTES and SDF-1α from Escherichia coli |