JP2017514481A5 - - Google Patents
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- JP2017514481A5 JP2017514481A5 JP2016565162A JP2016565162A JP2017514481A5 JP 2017514481 A5 JP2017514481 A5 JP 2017514481A5 JP 2016565162 A JP2016565162 A JP 2016565162A JP 2016565162 A JP2016565162 A JP 2016565162A JP 2017514481 A5 JP2017514481 A5 JP 2017514481A5
- Authority
- JP
- Japan
- Prior art keywords
- binding
- reagent
- ligand
- receptor molecule
- target cell
- 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
- 230000027455 binding Effects 0.000 claims description 272
- 239000003153 chemical reaction reagent Substances 0.000 claims description 197
- 239000003446 ligand Substances 0.000 claims description 139
- 210000004027 cell Anatomy 0.000 claims description 118
- 238000000034 method Methods 0.000 claims description 101
- 230000009149 molecular binding Effects 0.000 claims description 94
- 239000007790 solid phase Substances 0.000 claims description 62
- 108010090804 Streptavidin Proteins 0.000 claims description 47
- 108090000765 processed proteins & peptides Proteins 0.000 claims description 33
- 230000005526 G1 to G0 transition Effects 0.000 claims description 30
- 150000001413 amino acids Chemical group 0.000 claims description 28
- 230000002441 reversible effect Effects 0.000 claims description 28
- 108090001008 Avidin Proteins 0.000 claims description 25
- YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical compound N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 claims description 24
- 239000000427 antigen Substances 0.000 claims description 21
- 102000036639 antigens Human genes 0.000 claims description 21
- 108091007433 antigens Proteins 0.000 claims description 21
- 150000001615 biotins Chemical class 0.000 claims description 15
- 238000010494 dissociation reaction Methods 0.000 claims description 15
- 230000005593 dissociations Effects 0.000 claims description 15
- 108010018381 streptavidin-binding peptide Proteins 0.000 claims description 15
- 229960002685 biotin Drugs 0.000 claims description 12
- 235000020958 biotin Nutrition 0.000 claims description 12
- 239000011616 biotin Substances 0.000 claims description 12
- 230000002860 competitive effect Effects 0.000 claims description 11
- 235000001014 amino acid Nutrition 0.000 claims description 10
- 229940024606 amino acid Drugs 0.000 claims description 10
- 230000003100 immobilizing effect Effects 0.000 claims description 10
- 102000004196 processed proteins & peptides Human genes 0.000 claims description 10
- 235000018102 proteins Nutrition 0.000 claims description 10
- 102000004169 proteins and genes Human genes 0.000 claims description 10
- 108090000623 proteins and genes Proteins 0.000 claims description 10
- 150000001768 cations Chemical class 0.000 claims description 9
- 101710175625 Maltose/maltodextrin-binding periplasmic protein Proteins 0.000 claims description 8
- 239000011324 bead Substances 0.000 claims description 7
- 102000000584 Calmodulin Human genes 0.000 claims description 6
- 108010041952 Calmodulin Proteins 0.000 claims description 6
- 102000008394 Immunoglobulin Fragments Human genes 0.000 claims description 6
- 108010021625 Immunoglobulin Fragments Proteins 0.000 claims description 6
- 230000009920 chelation Effects 0.000 claims description 6
- 102000005720 Glutathione transferase Human genes 0.000 claims description 5
- 108010070675 Glutathione transferase Proteins 0.000 claims description 5
- 229910001428 transition metal ion Inorganic materials 0.000 claims description 5
- 229920002101 Chitin Polymers 0.000 claims description 4
- 108010020195 FLAG peptide Proteins 0.000 claims description 4
- XZWYTXMRWQJBGX-VXBMVYAYSA-N FLAG peptide Chemical compound NCCCC[C@@H](C(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CC(O)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@@H](N)CC(O)=O)CC1=CC=C(O)C=C1 XZWYTXMRWQJBGX-VXBMVYAYSA-N 0.000 claims description 4
- 229920002678 cellulose Polymers 0.000 claims description 4
- 239000001913 cellulose Substances 0.000 claims description 4
- 102000021178 chitin binding proteins Human genes 0.000 claims description 4
- 108091011157 chitin binding proteins Proteins 0.000 claims description 4
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 claims description 4
- 239000011159 matrix material Substances 0.000 claims description 4
- KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 claims description 3
- 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 description 3
- 238000004587 chromatography analysis Methods 0.000 claims description 3
- DEFVIWRASFVYLL-UHFFFAOYSA-N ethylene glycol bis(2-aminoethyl)tetraacetic acid Chemical compound OC(=O)CN(CC(O)=O)CCOCCOCCN(CC(O)=O)CC(O)=O DEFVIWRASFVYLL-UHFFFAOYSA-N 0.000 claims description 3
- 229910052751 metal Inorganic materials 0.000 claims description 3
- 239000002184 metal Substances 0.000 claims description 3
- 229910021645 metal ion Inorganic materials 0.000 claims description 3
- 239000000203 mixture Substances 0.000 claims description 3
- OWEGMIWEEQEYGQ-UHFFFAOYSA-N 100676-05-9 Natural products OC1C(O)C(O)C(CO)OC1OCC1C(O)C(O)C(O)C(OC2C(OC(O)C(O)C2O)CO)O1 OWEGMIWEEQEYGQ-UHFFFAOYSA-N 0.000 claims description 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 description 2
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 claims description 2
- 108010024636 Glutathione Proteins 0.000 claims description 2
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 claims description 2
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 claims description 2
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims description 2
- GUBGYTABKSRVRQ-PICCSMPSSA-N Maltose Natural products O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-PICCSMPSSA-N 0.000 claims description 2
- 102000002933 Thioredoxin Human genes 0.000 claims description 2
- 101710120037 Toxin CcdB Proteins 0.000 claims description 2
- 238000001042 affinity chromatography Methods 0.000 claims description 2
- 229960001230 asparagine Drugs 0.000 claims description 2
- 235000009582 asparagine Nutrition 0.000 claims description 2
- GUBGYTABKSRVRQ-QUYVBRFLSA-N beta-maltose Chemical compound OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@@H]1O GUBGYTABKSRVRQ-QUYVBRFLSA-N 0.000 claims description 2
- 239000013522 chelant Substances 0.000 claims description 2
- 239000012504 chromatography matrix Substances 0.000 claims description 2
- 238000010828 elution Methods 0.000 claims description 2
- 238000002523 gelfiltration Methods 0.000 claims description 2
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims description 2
- 229960003180 glutathione Drugs 0.000 claims description 2
- 102000028557 immunoglobulin binding proteins Human genes 0.000 claims description 2
- 108091009323 immunoglobulin binding proteins Proteins 0.000 claims description 2
- 108010026228 mRNA guanylyltransferase Proteins 0.000 claims description 2
- 229930182817 methionine Natural products 0.000 claims description 2
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 claims description 2
- 238000000926 separation method Methods 0.000 claims description 2
- 108060008226 thioredoxin Proteins 0.000 claims description 2
- 229940094937 thioredoxin Drugs 0.000 claims description 2
- 229910052723 transition metal Inorganic materials 0.000 claims description 2
- 150000003624 transition metals Chemical class 0.000 claims description 2
- 238000011534 incubation Methods 0.000 claims 1
- AUTOLBMXDDTRRT-JGVFFNPUSA-N (4R,5S)-dethiobiotin Chemical compound C[C@@H]1NC(=O)N[C@@H]1CCCCCC(O)=O AUTOLBMXDDTRRT-JGVFFNPUSA-N 0.000 description 3
- DEQPBRIACBATHE-FXQIFTODSA-N 5-[(3as,4s,6ar)-2-oxo-1,3,3a,4,6,6a-hexahydrothieno[3,4-d]imidazol-4-yl]-2-iminopentanoic acid Chemical compound N1C(=O)N[C@@H]2[C@H](CCCC(=N)C(=O)O)SC[C@@H]21 DEQPBRIACBATHE-FXQIFTODSA-N 0.000 description 3
- 102000017727 Immunoglobulin Variable Region Human genes 0.000 description 3
- 108010067060 Immunoglobulin Variable Region Proteins 0.000 description 3
- 102000008102 Ankyrins Human genes 0.000 description 1
- 108010049777 Ankyrins Proteins 0.000 description 1
- 108091023037 Aptamer Proteins 0.000 description 1
- 102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 1
- 108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 1
- 102000019298 Lipocalin Human genes 0.000 description 1
- 108050006654 Lipocalin Proteins 0.000 description 1
- 238000010276 construction Methods 0.000 description 1
- 239000012634 fragment Substances 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP14166718 | 2014-04-30 | ||
| EP14166718.8 | 2014-04-30 | ||
| PCT/EP2015/059510 WO2015166049A1 (en) | 2014-04-30 | 2015-04-30 | Method of isolating a target cell |
Publications (3)
| Publication Number | Publication Date |
|---|---|
| JP2017514481A JP2017514481A (ja) | 2017-06-08 |
| JP2017514481A5 true JP2017514481A5 (enExample) | 2018-06-14 |
| JP6678593B2 JP6678593B2 (ja) | 2020-04-08 |
Family
ID=50693456
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP2016565162A Active JP6678593B2 (ja) | 2014-04-30 | 2015-04-30 | 標的細胞を単離する方法 |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US11150239B2 (enExample) |
| EP (1) | EP3137905B1 (enExample) |
| JP (1) | JP6678593B2 (enExample) |
| CN (1) | CN106662584B (enExample) |
| AU (1) | AU2015254588B2 (enExample) |
| CA (1) | CA2945414C (enExample) |
| WO (1) | WO2015166049A1 (enExample) |
Families Citing this family (16)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| AU2013224027B2 (en) | 2012-02-23 | 2019-01-24 | Juno Therapeutics Gmbh | Chromatographic isolation of cells and other complex biological materials |
| JP6696969B2 (ja) * | 2014-04-16 | 2020-05-20 | ユノ・セラピューティクス・ゲーエムベーハーＪｕｎｏ Ｔｈｅｒａｐｅｕｔｉｃｓ Ｇｍｂｈ | 細胞の集団を拡大する方法、キット、及び装置 |
| KR20180108567A (ko) | 2015-10-22 | 2018-10-04 | 주노 테라퓨틱스 게엠베하 | 형질도입을 위한 방법, 키트, 제제 및 장치 |
| MA45489A (fr) | 2015-10-22 | 2018-08-29 | Juno Therapeutics Gmbh | Procédés de culture de cellules, kits et appareil associés |
| MA45488A (fr) | 2015-10-22 | 2018-08-29 | Juno Therapeutics Gmbh | Procédés, kits et appareil de culture de cellules |
| WO2018197949A1 (en) | 2017-04-27 | 2018-11-01 | Juno Therapeutics Gmbh | Oligomeric particle reagents and methods of use thereof |
| KR102088277B1 (ko) * | 2018-04-27 | 2020-03-13 | 주식회사 유니언스진 | 면역 화학 진단법을 이용한 표적 항원 검출용 종이기반 3차원 구조의 미세칩과 이를 이용한 표적항원 검출 방법 |
| CN112912103B (zh) * | 2018-05-21 | 2025-08-29 | 广州邦定生物技术有限公司 | 多价蛋白质复合物 |
| WO2020018578A1 (en) * | 2018-07-17 | 2020-01-23 | University Of Washington | Compositions and methods related to aptamer-based reversible cell selection |
| EP3833742A2 (en) | 2018-08-09 | 2021-06-16 | Juno Therapeutics, Inc. | Processes for generating engineered cells and compositions thereof |
| US11604191B2 (en) * | 2018-08-31 | 2023-03-14 | Thermogenesis Corporation | Methods for isolating target cells from blood |
| MX2021005013A (es) | 2018-10-31 | 2021-07-21 | Juno Therapeutics Gmbh | Métodos para la selección y estimulación de células y aparatos para los mismos. |
| CA3163761C (en) | 2020-01-31 | 2023-07-11 | Herbert Stadler | Methods of isolating a biological entity |
| WO2023017115A1 (en) * | 2021-08-11 | 2023-02-16 | Iba Lifesciences Gmbh | Fractionation of cells based on a marker protein |
| EP4514944A1 (en) | 2022-04-28 | 2025-03-05 | Bio-ReCell Ltd. | Method for separating target cells |
| WO2025238197A1 (en) * | 2024-05-16 | 2025-11-20 | Iba Lifesciences Gmbh | Functionalized three-dimensional (3d) polymer scaffold for affinity chromatography |
Family Cites Families (19)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1986002077A1 (en) | 1984-10-02 | 1986-04-10 | Meade Harry M | Production of streptavidin-like polypeptides |
| US4851341A (en) | 1986-12-19 | 1989-07-25 | Immunex Corporation | Immunoaffinity purification system |
| DE4237113B4 (de) | 1992-11-03 | 2006-10-12 | "Iba Gmbh" | Peptide und deren Fusionsproteine, Expressionsvektor und Verfahren zur Herstellung eines Fusionsproteins |
| WO1996023879A1 (en) | 1995-01-30 | 1996-08-08 | Terrapin Technologies, Inc. | Glubodies - multiplicities of proteins capable of binding a variety of small molecules |
| JPH11501008A (ja) | 1995-02-09 | 1999-01-26 | ユニバーシティ オブ ワシントン | 改変−アフィニティーストレプトアビジン |
| US6022951A (en) | 1995-04-11 | 2000-02-08 | Univ Boston | Streptavidin mutants |
| DE19641876B4 (de) | 1996-10-10 | 2011-09-29 | Iba Gmbh | Streptavidinmuteine |
| WO1998040396A1 (en) | 1997-03-14 | 1998-09-17 | Trustees Of Boston University | Multiflavor streptavidin |
| US5985658A (en) | 1997-11-14 | 1999-11-16 | Health Research Incorporated | Calmodulin-based cell separation technique |
| DE19932688B4 (de) | 1999-07-13 | 2009-10-08 | Scil Proteins Gmbh | Design von Beta-Faltblatt-Proteinen des gamma-II-kristallins antikörperähnlichen |
| EP1227321A1 (en) | 2000-12-28 | 2002-07-31 | Institut für Bioanalytik GmbH | Reversible MHC multimer staining for functional purification of antigen-specific T cells |
| DE10113776B4 (de) | 2001-03-21 | 2012-08-09 | "Iba Gmbh" | Isoliertes streptavidinbindendes, kompetitiv eluierbares Peptid, dieses umfassendes Fusionspeptid, dafür codierende Nukleinsäure, Expressionsvektor, Verfahren zur Herstellung eines rekombinanten Fusionsproteins und Verfahren zum Nachweis und/oder zur Gewinnung des Fusionsproteins |
| WO2003029462A1 (en) | 2001-09-27 | 2003-04-10 | Pieris Proteolab Ag | Muteins of human neutrophil gelatinase-associated lipocalin and related proteins |
| JP4776619B2 (ja) | 2005-04-19 | 2011-09-21 | パナソニック株式会社 | 位置センサ、光ヘッド装置、ヘッド移動機構、情報記録再生装置、および位置制御システム |
| CA2671326A1 (en) * | 2006-11-15 | 2008-11-20 | Invitrogen Dynal As | Methods of reversibly binding a biotin compound to a support |
| US8008032B2 (en) * | 2008-02-25 | 2011-08-30 | Cellective Dx Corporation | Tagged ligands for enrichment of rare analytes from a mixed sample |
| US10023657B2 (en) * | 2010-10-01 | 2018-07-17 | Ludwig Institute For Cancer Research Ltd. | Reversible protein multimers, methods for their production and use |
| EP3418295B1 (en) * | 2011-07-18 | 2020-09-02 | IBA GmbH | Method of reversibly staining a target cell |
| AU2013224027B2 (en) * | 2012-02-23 | 2019-01-24 | Juno Therapeutics Gmbh | Chromatographic isolation of cells and other complex biological materials |
-
2015
- 2015-04-30 CA CA2945414A patent/CA2945414C/en active Active
- 2015-04-30 AU AU2015254588A patent/AU2015254588B2/en active Active
- 2015-04-30 EP EP15723655.5A patent/EP3137905B1/en active Active
- 2015-04-30 US US15/306,995 patent/US11150239B2/en active Active
- 2015-04-30 WO PCT/EP2015/059510 patent/WO2015166049A1/en not_active Ceased
- 2015-04-30 JP JP2016565162A patent/JP6678593B2/ja active Active
- 2015-04-30 CN CN201580035819.4A patent/CN106662584B/zh active Active
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