OA10716A - Ligands for flt3 receptors - Google Patents
Ligands for flt3 receptors Download PDFInfo
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- OA10716A OA10716A OA60744A OA60744A OA10716A OA 10716 A OA10716 A OA 10716A OA 60744 A OA60744 A OA 60744A OA 60744 A OA60744 A OA 60744A OA 10716 A OA10716 A OA 10716A
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- flt3
- cells
- polypeptide
- csf
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Applications Claiming Priority (5)
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US6839493A | 1993-05-24 | 1993-05-24 | |
US10646393A | 1993-08-12 | 1993-08-12 | |
US11175893A | 1993-08-25 | 1993-08-25 | |
US16240793A | 1993-12-03 | 1993-12-03 | |
US20950294A | 1994-03-07 | 1994-03-07 |
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OA10716A true OA10716A (en) | 2002-12-09 |
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OA60744A OA10716A (en) | 1993-05-24 | 1995-11-21 | Ligands for flt3 receptors |
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US (3) | US5554512A (hu) |
JP (1) | JP4028594B2 (hu) |
KR (1) | KR100319359B1 (hu) |
CN (1) | CN1123574C (hu) |
AU (1) | AU683472B2 (hu) |
BR (1) | BR9407073A (hu) |
CA (1) | CA2162397C (hu) |
FI (1) | FI955646A (hu) |
HU (1) | HUT74831A (hu) |
MY (1) | MY148148A (hu) |
NO (1) | NO322373B1 (hu) |
NZ (1) | NZ267541A (hu) |
OA (1) | OA10716A (hu) |
PL (1) | PL311756A1 (hu) |
UA (1) | UA42726C2 (hu) |
WO (1) | WO1994028391A1 (hu) |
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AU7017494A (en) * | 1993-05-19 | 1994-12-12 | Institut National De La Sante Et De La Recherche Medicale | Purified mammalian flt3 ligands and agonists and antagonists thereof |
US7534867B1 (en) * | 1993-05-19 | 2009-05-19 | Schering Corporation | Purified mammalian Flt3 ligands; agonists; antagonists |
US5554512A (en) * | 1993-05-24 | 1996-09-10 | Immunex Corporation | Ligands for flt3 receptors |
NZ314644A (en) * | 1993-05-24 | 2000-11-24 | Immunex Corp | Use of flt3-ligands as a growth stimulator of stem cells in the transplantation of tissue |
US7294331B2 (en) * | 1994-03-07 | 2007-11-13 | Immunex Corporation | Methods of using flt3-ligand in hematopoietic cell transplantation |
US5525708A (en) * | 1994-03-28 | 1996-06-11 | Cytomed, Inc. | Covalent dimer of kit ligand |
US5789655A (en) | 1994-05-13 | 1998-08-04 | The Regents Of The University Of California | Transgenic animals expressing artificial epitope-tagged proteins |
WO1997003684A1 (en) * | 1995-07-21 | 1997-02-06 | THE GOVERNMENT OF THE UNITED STATES, represented by THE SECRETARY, DEPARTMENT OF HEALTH AND HUMAN SERVICES | Method of decreasing radiation or radio-mimetic chemotherapy for hematopoietic pluripotent cell engraftment |
US6117850A (en) * | 1995-08-28 | 2000-09-12 | The Collaborative Group, Ltd. | Mobilization of peripheral blood precursor cells by β(1,3)-glucan |
GB9519776D0 (en) * | 1995-09-28 | 1995-11-29 | Casimir Colin | Materials and methods relating to the transfer of nucleic acid into stem cells |
US7150992B1 (en) | 1995-10-04 | 2006-12-19 | Innunex Corporation | Methods of preparing dendritic cells with flt3-ligand and antigen |
US7361330B2 (en) * | 1995-10-04 | 2008-04-22 | Immunex Corporation | Methods of using flt3-ligand in the treatment of fibrosarcoma |
AU697539B2 (en) | 1995-10-04 | 1998-10-08 | Immunex Corporation | Dendritic cell stimulatory factor |
US20030103988A1 (en) * | 1995-10-26 | 2003-06-05 | Leonard Chess | Regulation of activated t cells by recognition of t cell receptor beta chains and major histocompatibility complex class ib molecules |
US5849999A (en) * | 1996-10-16 | 1998-12-15 | The Mclean Hospital Corporation | Transgenic non-human mice expressing Flag-APP-C100 protein develop alzheimer's disease brain morphology and behavior |
US6660257B1 (en) | 1996-10-25 | 2003-12-09 | Pharmacia Corporation | Circular permuteins of flt3 ligand |
US6967092B1 (en) | 1996-10-25 | 2005-11-22 | Mc Kearn John P | Multi-functional chimeric hematopoietic receptor agonists |
AU7835898A (en) * | 1997-06-17 | 1999-01-04 | Immunex Corporation | A method of enhancing antigen-specific peripheral immune tolerance |
WO1999026639A1 (en) * | 1997-11-26 | 1999-06-03 | Allegheny University Of The Health Sciences | Methods for mobilizing hematopoietic facilitating cells and hematopoietic stem cells into the peripheral blood |
DE69824039T2 (de) | 1997-12-08 | 2005-08-18 | Lexigen Pharmaceuticals Corp., Lexington | Heterodimäre fusionsproteine zur verwendung für gezielte immuntherapie und allgemeine immunerregung |
CA2316755C (en) * | 1998-01-23 | 2006-04-04 | Prolifaron, Inc. | Methods and compositions for the identification of growth factor mimetics, growth factors and inhibitors |
US6291661B1 (en) * | 1998-07-02 | 2001-09-18 | Immunex Corporation | flt3-L mutants and method of use |
US6376067B1 (en) * | 1998-12-21 | 2002-04-23 | Mitsubishi Polyester Film, Llc | Silicone coated film with back side slip control coating and method of controlling slip of such film |
US7112409B2 (en) * | 1999-01-29 | 2006-09-26 | Center For Molecular Medicine And Immunology | Method of determining cytokine dosage for myelosuppressive state |
US6649352B1 (en) * | 1999-01-29 | 2003-11-18 | Center For Molecular Medicine And Immunology | Method of evaluating myelosuppressive state |
JP2003530070A (ja) * | 1999-05-19 | 2003-10-14 | レキシジェン ファーマシューティカルズ コーポレイション | Fc融合タンパク質としてのインターフェロン−αタンパク質の発現および搬出 |
SK782002A3 (en) | 1999-07-21 | 2003-08-05 | Lexigen Pharm Corp | FC fusion proteins for enhancing the immunogenicity of protein and peptide antigens |
US7067110B1 (en) | 1999-07-21 | 2006-06-27 | Emd Lexigen Research Center Corp. | Fc fusion proteins for enhancing the immunogenicity of protein and peptide antigens |
US6617135B1 (en) | 1999-08-09 | 2003-09-09 | Emd Lexigen Research Center Corp. | Multiple cytokine protein complexes |
GB9924981D0 (en) * | 1999-10-21 | 1999-12-22 | Univ Manchester | Gene therapy |
AU2154401A (en) | 1999-11-12 | 2001-05-30 | Merck Patent Gmbh | Erythropoietin forms with improved properties |
EP2298334A3 (en) | 1999-12-20 | 2012-04-04 | Immunex Corporation | Tweak receptor |
WO2001058957A2 (en) | 2000-02-11 | 2001-08-16 | Lexigen Pharmaceuticals Corp. | Enhancing the circulating half-life of antibody-based fusion proteins |
US7572631B2 (en) | 2000-02-24 | 2009-08-11 | Invitrogen Corporation | Activation and expansion of T cells |
US7541184B2 (en) | 2000-02-24 | 2009-06-02 | Invitrogen Corporation | Activation and expansion of cells |
MXPA02012734A (es) | 2000-06-29 | 2003-04-25 | Merck Patent Gmbh | Mejoramiento de las respuestas inmunes mediadas por la proteina de fusion anticuerpo-citocina, mediante tratamiento combinado con agentes mejoradores de la captacion de inmunocitocina. |
US20020150552A1 (en) * | 2000-09-12 | 2002-10-17 | Lau Allan S. | Compositions comprising mixtures of therapeutic proteins and methods of producing the same |
US20030129162A1 (en) * | 2000-09-12 | 2003-07-10 | Lau Allan S. | Compositions comprising mixtures of therapeutic proteins and methods of producing the same |
US20020150541A1 (en) * | 2000-09-12 | 2002-10-17 | Gene Trol Biotherapeutics, Inc. | Compositions comprising mixtures of therapeutic proteins and methods of producing the same |
WO2002067760A2 (en) | 2001-01-09 | 2002-09-06 | Baylor Research Institute | Methods for treating autoimmune diseases in a subject and in vitro diagnostic assays |
MXPA03008031A (es) | 2001-03-07 | 2003-12-04 | Merck Patent Gmbh | Tecnologia de expresion para proteinas que contienen porcion de anticuerpo isotipo hibrida. |
US6992174B2 (en) | 2001-03-30 | 2006-01-31 | Emd Lexigen Research Center Corp. | Reducing the immunogenicity of fusion proteins |
EP1390076A4 (en) * | 2001-04-27 | 2004-12-15 | Xcyte Therapies Inc | Maturation of antigen-presenting cells with activated cells |
CN100503639C (zh) | 2001-05-03 | 2009-06-24 | 默克专利有限公司 | 重组肿瘤特异性抗体及其应用 |
US20030017529A1 (en) * | 2001-06-27 | 2003-01-23 | Applera Corporation | Isolated human secreted proteins, nucleic acid molecules encoding human secreted proteins, and uses thereof |
US7070996B2 (en) * | 2001-08-31 | 2006-07-04 | Rigel Pharmaceuticals, Inc. | Production of cultured human mast cells and basophils for high throughput small molecule drug discovery |
AU2002363322A1 (en) * | 2001-10-26 | 2003-05-19 | Large Scale Biology Corporation | Endothelial cell derived hemotopoietic growth factor |
WO2003048334A2 (en) | 2001-12-04 | 2003-06-12 | Merck Patent Gmbh | Immunocytokines with modulated selectivity |
EP1487477A4 (en) * | 2002-03-26 | 2006-07-19 | Immunex Corp | METHOD OF USE OF FLT3 LIGAND IN IMMUNIZATION PROTOCOLS |
ES2557741T3 (es) | 2002-03-27 | 2016-01-28 | Immunex Corporation | Procedimientos para incrementar la producción de polipéptidos |
US20050058622A1 (en) * | 2002-12-06 | 2005-03-17 | Lyman Stewart D. | Methods of using Flt3-Ligand in hematopoietic cell transplantation procedures incorporating nonmyeloablative conditioning regimens |
ATE471946T1 (de) | 2002-12-17 | 2010-07-15 | Merck Patent Gmbh | Humanisierter antikörper (h14.18) des maus antikörpers 14.18, der gd2 bindet und seine fusion mit il-2 |
US20050232926A1 (en) * | 2003-06-06 | 2005-10-20 | Oncomax Acquisition Corp. | Antibodies specific for cancer associated antigen SM5-1 and uses thereof |
US20040254108A1 (en) * | 2003-06-13 | 2004-12-16 | Jing Ma | Preparation and application of anti-tumor bifunctional fusion proteins |
US20050232931A1 (en) * | 2003-06-13 | 2005-10-20 | Oncomax Acquisition Corp. | Preparation and application of anti-tumor bifunctional fusion proteins |
CA2528595A1 (en) * | 2003-06-13 | 2005-01-06 | Oncomax Acquisition Corp. | Preparation and application of anti-tumor bifunctional fusion proteins |
EP1691852A2 (en) * | 2003-11-10 | 2006-08-23 | Angiotech International AG | Medical implants and fibrosis-inducing agents |
ES2616337T3 (es) | 2003-12-12 | 2017-06-12 | Government Of The United States Of America, As Repr. By The Secr. Of The Dept. Of Health And Human Services And His Successors | Un epítopo de linfocito T citotóxico humano y su epítopo agonista del número no variable de secuencias de repetición en tándem de MUC-1 |
CA2551189A1 (en) * | 2003-12-24 | 2005-07-07 | The Walter And Eliza Hall Institute Of Medical Research | Therapeutic agents and uses therefor |
JP2008502317A (ja) | 2003-12-30 | 2008-01-31 | メルク パテント ゲゼルシャフト ミット ベシュレンクテル ハフトング | Il−7融合タンパク質 |
WO2005063808A1 (en) | 2003-12-31 | 2005-07-14 | Merck Patent Gmbh | Fc-ERYTHROPOIETIN FUSION PROTEIN WITH IMPROVED PHARMACOKINETICS |
AU2005206277B2 (en) * | 2004-01-22 | 2011-06-23 | Merck Patent Gmbh | Anti-cancer antibodies with reduced complement fixation |
CN100404683C (zh) * | 2004-05-27 | 2008-07-23 | 中国医学科学院基础医学研究所 | 一种人fl多核苷酸及其与人gm-csf联合基因治疗恶性肿瘤的用途 |
US7670595B2 (en) * | 2004-06-28 | 2010-03-02 | Merck Patent Gmbh | Fc-interferon-beta fusion proteins |
CN1993460A (zh) * | 2004-07-12 | 2007-07-04 | 索林集团意大利有限公司 | 用于培养人细胞的装置和方法 |
EP1786474B1 (en) * | 2004-08-12 | 2011-06-01 | Cedars-Sinai Medical Center | Combined gene therapy for the treatment of macroscopic gliomas |
ES2342964T3 (es) * | 2004-12-09 | 2010-07-20 | Merck Patent Gmbh | Variantes de la interleucina-7 con inmunogenicidad reducida. |
WO2006090882A1 (ja) * | 2005-02-23 | 2006-08-31 | Foundation For Biomedical Research And Innovation | 血管内皮前駆細胞の生体外増幅方法 |
US20090050204A1 (en) * | 2007-08-03 | 2009-02-26 | Illuminex Corporation. | Photovoltaic device using nanostructured material |
US20070048254A1 (en) * | 2005-08-24 | 2007-03-01 | Mirus Bio Corporation | Generation of dendritic cells |
US7482165B2 (en) * | 2005-08-24 | 2009-01-27 | Beckman Coulter, Inc. | Method of preventing white blood cell interferences to red blood cell measurements of a blood sample |
ATE509954T1 (de) | 2005-12-30 | 2011-06-15 | Merck Patent Gmbh | Anti-cd19-antikörper mit reduzierter immunogenität |
ATE555125T1 (de) | 2005-12-30 | 2012-05-15 | Merck Patent Gmbh | Interleukin-12p40-varianten mit verbesserter stabilität |
MX2008011525A (es) * | 2006-03-09 | 2008-09-18 | Pharmacopeia Inc | Inhibidores de mnk2 de 8-heteroarilpurina para el tratamiento de trastornos metabolicos. |
US8921050B2 (en) | 2006-03-17 | 2014-12-30 | The United States Of America, As Represented By The Secretary, Department Of Health And Human Services | Methods of diagnosing renal cell carcinoma |
WO2008095027A2 (en) * | 2007-01-30 | 2008-08-07 | Cedars-Sinai Medical Center | Adenoviral vector comprising herpes simplex virus type 1 thymidine kinase and a transgene for increasing the expression of the transgene |
AR071891A1 (es) | 2008-05-30 | 2010-07-21 | Imclone Llc | Anticuerpos humanos anti-flt3 (receptor tirosina cinasa 3 tipo fms humano) |
US8834409B2 (en) | 2008-07-29 | 2014-09-16 | Covidien Lp | Method for ablation volume determination and geometric reconstruction |
WO2010047928A2 (en) * | 2008-10-24 | 2010-04-29 | Mount Sinai School Of Medicine Of New York University | Methods and compositions for treatment of fibrosis |
DE102008061522A1 (de) | 2008-12-10 | 2010-06-17 | Biontech Ag | Verwendung von Flt3-Ligand zur Verstärkung von Immunreaktionen bei RNA-Immunisierung |
KR101781966B1 (ko) | 2009-04-17 | 2017-09-27 | 글로브이뮨 | 암에 대한 병용 면역요법 조성물 및 방법 |
EP2421896A1 (en) | 2009-04-22 | 2012-02-29 | Merck Patent GmbH | Antibody fusion proteins with modified fcrn binding sites |
JP6073135B2 (ja) * | 2009-10-19 | 2017-02-01 | トライステム・トレイディング・(キプロス)・リミテッドTriStem Trading (Cyprus) Limited | 再プログラム化成熟成体細胞を用いる治療 |
DK2513311T4 (da) | 2009-12-18 | 2021-06-14 | Bavarian Nordic As | Produktion af ifn-lambda ved hjælp af traditionelle dendritceller og anvendelser deraf |
EP2601287B1 (en) | 2010-08-05 | 2015-01-07 | Amgen Inc. | Dipeptides to enhance yield and viability from cell cultures |
WO2012065755A1 (en) | 2010-11-19 | 2012-05-24 | Bavarian Nordic A/S | Production of ifn-lambda by b cells |
US9133493B2 (en) | 2011-04-21 | 2015-09-15 | Amgen Inc. | Method for culturing mammalian cells to improve recombinant protein production |
LT2837680T (lt) | 2011-07-01 | 2020-07-10 | Amgen Inc. | Žinduolių ląstelių kultūra |
BR112014004591A2 (pt) | 2011-09-02 | 2017-03-28 | Amgen Inc | produto farmacêutico de análise da exposição à luz de um produto farmacêutico |
AR089231A1 (es) | 2011-12-15 | 2014-08-06 | Amgen Inc | Metodo de floculacion |
EP2832851B1 (en) * | 2012-03-28 | 2019-04-17 | Quarrymen & Co. Inc. | Immortalized stem cells and medicinal composition and medicinal preparation comprising product thereof as active ingredient |
WO2014109858A1 (en) | 2013-01-14 | 2014-07-17 | Amgen Inc. | Methods of using cell-cycle inhibitors to modulate one or more properties of a cell culture |
US10023608B1 (en) | 2013-03-13 | 2018-07-17 | Amgen Inc. | Protein purification methods to remove impurities |
TWI625390B (zh) | 2013-03-14 | 2018-06-01 | 安美基公司 | 用於增加重組蛋白質之甘露糖含量之方法 |
JP6457479B2 (ja) | 2013-03-14 | 2019-01-23 | アムジエン・インコーポレーテツド | 漏出したアフィニティ精製リガンドの除去 |
US9481901B2 (en) | 2013-05-30 | 2016-11-01 | Amgen Inc. | Methods for increasing mannose content of recombinant proteins |
MX2016005572A (es) | 2013-10-31 | 2016-12-09 | Amgen Inc | Uso de monensina para regular la glicosilacion de proteinas recombinantes. |
BR122020004385B1 (pt) | 2014-01-13 | 2022-10-04 | Amgen Inc | Método para aumentar o teor de glicoforma de alta manose de uma glicoproteína recombinante e método de produção de uma glicoproteína recombinante |
US11384378B2 (en) | 2014-06-04 | 2022-07-12 | Amgen Inc. | Methods for harvesting mammalian cell cultures |
US11275090B2 (en) | 2014-11-19 | 2022-03-15 | Amgen Inc. | Quantitation of glycan moiety in recombinant glycoproteins |
SG11201704351WA (en) | 2014-12-01 | 2017-06-29 | Amgen Inc | Process for manipulating the level of glycan content of a glycoprotein |
WO2017218638A1 (en) * | 2016-06-14 | 2017-12-21 | Jianjun Chen | Methods for treating subjects suffering from acute myeloid leukemia with flt3 ligand-targeted mir-150 nanoparticles |
JP7146732B2 (ja) | 2016-07-13 | 2022-10-04 | オハイオ ステート イノベーション ファウンデーション | 宿主抗原提示並びに宿主抗腫瘍及び抗病原体免疫を最適化するためのプラットフォーム及び方法 |
SG10202111394XA (en) | 2017-04-13 | 2021-12-30 | Senti Biosciences Inc | Combinatorial cancer immunotherapy |
CN112218651A (zh) | 2018-01-08 | 2021-01-12 | 诺华公司 | 用于与嵌合抗原受体疗法组合的免疫增强rna |
EP3743095A1 (en) | 2018-01-26 | 2020-12-02 | Celldex Therapeutics, Inc. | Methods of treating cancer with dendritic cell mobilizing agents |
SG11202007702UA (en) * | 2018-02-14 | 2020-09-29 | Viela Bio Inc | Antibodies to feline mcdonough sarcoma (fms)-like tyrosine kinase 3 receptor ligand (flt3l) and uses thereof for treating autoimmune and inflammatory diseases |
MX2020011614A (es) | 2018-05-01 | 2020-12-09 | Amgen Inc | Anticuerpos con perfiles de glicanos modulados. |
KR20210094534A (ko) | 2018-10-17 | 2021-07-29 | 센티 바이오사이언시스, 인코포레이티드 | 병용 암 면역 요법 |
US11419898B2 (en) | 2018-10-17 | 2022-08-23 | Senti Biosciences, Inc. | Combinatorial cancer immunotherapy |
US20220177550A1 (en) * | 2019-03-28 | 2022-06-09 | Orionis Biosciences, Inc. | Chimeric proteins and chimeric protein complexes directed to fms-like tyrosine kinase 3 (flt3) |
CA3136626A1 (en) * | 2019-04-12 | 2020-10-15 | Emory University | Compositions and methods for promoting hematopoietic cell cytotoxicity |
CA3142513A1 (en) | 2019-06-25 | 2020-12-30 | Gilead Sciences, Inc. | Flt3l-fc fusion proteins and methods of use |
KR20230098201A (ko) * | 2020-10-26 | 2023-07-03 | 네오이뮨텍, 인코퍼레이티드 | 줄기 세포 동원의 유도 방법 |
TW202313094A (zh) | 2021-05-18 | 2023-04-01 | 美商基利科學股份有限公司 | 使用FLT3L—Fc融合蛋白之方法 |
WO2023129974A1 (en) | 2021-12-29 | 2023-07-06 | Bristol-Myers Squibb Company | Generation of landing pad cell lines |
Family Cites Families (22)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4745099A (en) * | 1985-02-06 | 1988-05-17 | Chugai Seiyaku Kabushiki Kaisha | Pharmaceutical composition for the treatment of the anemia of malignant tumors |
US5013824A (en) * | 1985-11-19 | 1991-05-07 | Schering Corporation | Human interleukin-4 peptides and conjugates thereof |
US5057420A (en) * | 1987-06-05 | 1991-10-15 | Granada Biosciences, Inc. | Bovine nuclear transplantation |
US5192553A (en) * | 1987-11-12 | 1993-03-09 | Biocyte Corporation | Isolation and preservation of fetal and neonatal hematopoietic stem and progenitor cells of the blood and methods of therapeutic use |
JPH0611705B2 (ja) * | 1988-02-10 | 1994-02-16 | 新技術事業団 | 血小板減少症治療剤 |
US5437994A (en) * | 1989-06-15 | 1995-08-01 | Regents Of The University Of Michigan | Method for the ex vivo replication of stem cells, for the optimization of hematopoietic progenitor cell cultures, and for increasing the metabolism, GM-CSF secretion and/or IL-6 secretion of human stromal cells |
US5635386A (en) * | 1989-06-15 | 1997-06-03 | The Regents Of The University Of Michigan | Methods for regulating the specific lineages of cells produced in a human hematopoietic cell culture |
US5399493A (en) * | 1989-06-15 | 1995-03-21 | The Regents Of The University Of Michigan | Methods and compositions for the optimization of human hematopoietic progenitor cell cultures |
US5763266A (en) * | 1989-06-15 | 1998-06-09 | The Regents Of The University Of Michigan | Methods, compositions and devices for maintaining and growing human stem and/or hematopoietics cells |
US5326558A (en) * | 1989-08-08 | 1994-07-05 | Genetics Institute, Inc. | Megakaryocytopoietic factor |
US5061620A (en) * | 1990-03-30 | 1991-10-29 | Systemix, Inc. | Human hematopoietic stem cell |
US5185438A (en) * | 1991-04-02 | 1993-02-09 | The Trustees Of Princeton University | Nucleic acids encoding hencatoporetic stem cell receptor flk-2 |
US5270458A (en) * | 1991-04-02 | 1993-12-14 | The Trustees Of Princeton University | Nucleic acids encoding fragments of hematopoietic stem cell receptor flk-2 |
US5367057A (en) * | 1991-04-02 | 1994-11-22 | The Trustees Of Princeton University | Tyrosine kinase receptor flk-2 and fragments thereof |
CA2107897A1 (en) * | 1991-04-09 | 1992-10-10 | Ronald Hoffman | System and process for supporting hematopoietic cells |
US5199942A (en) * | 1991-06-07 | 1993-04-06 | Immunex Corporation | Method for improving autologous transplantation |
DK0614485T3 (da) * | 1991-10-23 | 2002-10-28 | Nexell Therapeutics Inc | Fremgangsmåde til selektiv formering af CD34 positive celler |
CA2123094C (en) * | 1991-11-06 | 1999-08-10 | Paulo N. Correa | Cell culture medium |
US5453357A (en) * | 1992-10-08 | 1995-09-26 | Vanderbilt University | Pluripotential embryonic stem cells and methods of making same |
NZ314644A (en) * | 1993-05-24 | 2000-11-24 | Immunex Corp | Use of flt3-ligands as a growth stimulator of stem cells in the transplantation of tissue |
US5554512A (en) * | 1993-05-24 | 1996-09-10 | Immunex Corporation | Ligands for flt3 receptors |
US5525708A (en) * | 1994-03-28 | 1996-06-11 | Cytomed, Inc. | Covalent dimer of kit ligand |
-
1994
- 1994-05-11 US US08/243,545 patent/US5554512A/en not_active Expired - Lifetime
- 1994-05-12 BR BR9407073A patent/BR9407073A/pt not_active Application Discontinuation
- 1994-05-12 CA CA002162397A patent/CA2162397C/en not_active Expired - Fee Related
- 1994-05-12 NZ NZ267541A patent/NZ267541A/en not_active IP Right Cessation
- 1994-05-12 WO PCT/US1994/005365 patent/WO1994028391A1/en not_active Application Discontinuation
- 1994-05-12 JP JP50071595A patent/JP4028594B2/ja not_active Expired - Fee Related
- 1994-05-12 CN CN94192225A patent/CN1123574C/zh not_active Expired - Fee Related
- 1994-05-12 AU AU69877/94A patent/AU683472B2/en not_active Ceased
- 1994-05-12 KR KR1019950705236A patent/KR100319359B1/ko not_active IP Right Cessation
- 1994-05-12 HU HU9503341A patent/HUT74831A/hu unknown
- 1994-05-12 PL PL94311756A patent/PL311756A1/xx unknown
- 1994-05-12 UA UA95125567A patent/UA42726C2/uk unknown
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1995
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- 1995-11-23 FI FI955646A patent/FI955646A/fi not_active Application Discontinuation
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1997
- 1997-12-18 US US08/993,962 patent/US5843423A/en not_active Expired - Lifetime
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CA2162397A1 (en) | 1994-12-08 |
KR100319359B1 (ko) | 2002-07-31 |
JP4028594B2 (ja) | 2007-12-26 |
JPH08511251A (ja) | 1996-11-26 |
CN1123574C (zh) | 2003-10-08 |
NO322373B1 (no) | 2006-09-25 |
UA42726C2 (uk) | 2001-11-15 |
WO1994028391A1 (en) | 1994-12-08 |
NO954735D0 (no) | 1995-11-23 |
NZ267541A (en) | 1997-06-24 |
US5843423A (en) | 1998-12-01 |
PL311756A1 (en) | 1996-03-18 |
MY148148A (en) | 2013-03-15 |
US5554512A (en) | 1996-09-10 |
CA2162397C (en) | 2007-04-03 |
FI955646A (fi) | 1996-01-23 |
BR9407073A (pt) | 1996-08-27 |
FI955646A0 (fi) | 1995-11-23 |
CN1125479A (zh) | 1996-06-26 |
AU683472B2 (en) | 1997-11-13 |
HUT74831A (en) | 1997-02-28 |
US6919206B2 (en) | 2005-07-19 |
AU6987794A (en) | 1994-12-20 |
NO954735L (no) | 1996-01-23 |
HU9503341D0 (en) | 1996-01-29 |
US20030148516A1 (en) | 2003-08-07 |
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