Chemistry: molecular biology and microbiology – Animal cell – per se ; composition thereof; process of...
Reexamination Certificate
2009-06-19
2011-12-20
Joike, Michele K (Department: 1636)
Chemistry: molecular biology and microbiology
Animal cell, per se ; composition thereof; process of...
C435S070100, C435S455000
Reexamination Certificate
active
08080414
ABSTRACT:
Disclosed are a stable recombinant cell clones which are stable in serum- and protein-free medium for at least 40 generations, a biomass obtained by multiplying the stable cell clone under serum- and protein-free culturing conditions, and a method of preparing recombinant proteins by means of the biomass. Furthermore, the invention relates to a method of recovering stable recombinant cell clones.
REFERENCES:
patent: 4431629 (1984-02-01), Olsen
patent: 4443540 (1984-04-01), Chervan et al.
patent: 4767704 (1988-08-01), Cleveland et al.
patent: 4978616 (1990-12-01), Dean, Jr. et al.
patent: 5122469 (1992-06-01), Mather et al.
patent: 5316938 (1994-05-01), Keen et al.
patent: 5378612 (1995-01-01), Nakashima et al.
patent: 5393668 (1995-02-01), Cinatl et al.
patent: 5441868 (1995-08-01), Lin
patent: 5573937 (1996-11-01), Shinmoto et al.
patent: 5633162 (1997-05-01), Keen et al.
patent: 5719050 (1998-02-01), Hashimoto et al.
patent: 5741705 (1998-04-01), Blom et al.
patent: 5789247 (1998-08-01), Ballay et al.
patent: 5804420 (1998-09-01), Chan et al.
patent: 5811299 (1998-09-01), Renner et al.
patent: 5851800 (1998-12-01), Adamson et al.
patent: 5885835 (1999-03-01), Blom et al.
patent: 6048728 (2000-04-01), Inlow et al.
patent: 6100061 (2000-08-01), Reiter et al.
patent: 6114146 (2000-09-01), Herlitschka et al.
patent: 6475725 (2002-11-01), Reiter
patent: 2002/0182679 (2002-12-01), Reiter et al.
patent: 2003/0203448 (2003-10-01), Reiter et al.
patent: 2006/0148074 (2006-07-01), Gorfien et al.
patent: 1659/99 (1999-09-01), None
patent: 78958/98 (1998-10-01), None
patent: 199953636 (2001-03-01), None
patent: 2161517 (1994-11-01), None
patent: 0 160 457 (1985-11-01), None
patent: 0 481 791 (1992-04-01), None
patent: 0 485 689 (1992-05-01), None
patent: 0 631 731 (1995-01-01), None
patent: 0 666 312 (1995-08-01), None
patent: 0 711 835 (1996-05-01), None
patent: 0 872 487 (1998-10-01), None
patent: 00 120 896.6 (2000-09-01), None
patent: 1 200 561 (2006-06-01), None
patent: 2 196 386 (1974-03-01), None
patent: 3-244391 (1991-10-01), None
patent: 4-316484 (1992-11-01), None
patent: 5-123178 (1993-05-01), None
patent: 7-039386 (1995-02-01), None
patent: 2-859679 (1999-02-01), None
patent: H01-211488 (1999-08-01), None
patent: WO 85/02610 (1985-06-01), None
patent: WO 86/04920 (1986-08-01), None
patent: WO 88/00967 (1988-02-01), None
patent: WO 89/00192 (1989-01-01), None
patent: WO 91/09122 (1991-06-01), None
patent: WO 91/10726 (1991-07-01), None
patent: WO 94/25599 (1994-11-01), None
patent: WO 96/07730 (1996-03-01), None
patent: WO 96/07730 (1996-03-01), None
patent: WO 96/15231 (1996-05-01), None
patent: WO 96/18734 (1996-06-01), None
patent: WO 96/26266 (1996-08-01), None
patent: WO 96/40866 (1996-12-01), None
patent: WO 97/05240 (1997-02-01), None
patent: WO 98/08934 (1998-03-01), None
patent: WO 98/15614 (1998-04-01), None
patent: WO 98/54296 (1998-12-01), None
patent: WO 99/05268 (1999-02-01), None
patent: WO 99/57246 (1999-11-01), None
patent: WO 00/03000 (2000-01-01), None
patent: WO 01/11021 (2001-02-01), None
patent: WO 01/14529 (2001-03-01), None
patent: WO 01/23527 (2001-04-01), None
patent: WO 02/24876 (2002-03-01), None
patent: WO 02/24876 (2002-03-01), None
patent: WO 2004/005493 (2004-01-01), None
Berg, D.T. et al..; “High-Level Expression of Secreted Proteins from Cells Adapted to Serum-Free Suspension Culture”;BioTechniques; 1993 vol. 14(6); pp. 972-978.
Bielicki, J. et al.; “Recombinant Human Sulphamidase: Expression, Amplification, Purification and Characterization”; 1998;Biochem. J.; vol. 329; pp. 145-150.
Brown, M.E. et al.; “Process Development for the Production of Recombinant Antibodies Using the Glutamine Synthetase (GS) System”; 1992;Cytotechnology; vol. 9; pp. 231-236.
Burger, C. et al.; “An Integrated Strategy for the Process Development of a Recombinant Antibody-Cytokine Fusion Protein Expressed in BHK Cells”; 1999;Appl. Microbiol. Biotechnol.; vol. 52; pp. 345-353.
Cartier, M. and Stanners, C.P.; “Stable, High-Level Expression of a Carcinoembryonic Antigen-encoding cDNA After Transfection and Amplification with the Dominant and Selectable Asparagine Synthetase Marker”; 1990;Gene; vol. 95; pp. 223-230.
Cole, E.S. et al.; “Recombinant Human Thyroid Stimulating Hormone: Development of a Biotechnology Product for Detection of Metastatic Lesions of Thyroid Carcinoma”; Sep. 1993;Biotechnology; vol. 11; pp. 1014-1024.
Cruz, H.J. et al.; “Adaptation of BHK Cells Producing a Recombinant Protein to Serum-Free Media and Protein-Free Medium”; 1998;Cytotechnology; vol. 26; pp. 59-64.
Donaldson, M.S. and Sculer, M.L.; “Low-Cost Serum-Free Medium for the BTI-Tn5B1-4 Insect Cell Line”; 1998;Biotechnol. Prog.; vol. 14; pp. 573-579.
Doyle, A. et al. eds.; “Cloning”; Part 4D Module 4D1In Cell&Tissue Culture: Laboratory Procedures; 1998; John Wiley & Sons; London; Cloning Techniques (Non-hybridoma Related); pp. 4D:1.1-4D:1.9.
Eagle, H.; “Amino Acid Metabolism in Mammalian Cell Cultures”; Aug. 21, 1939;Science; vol. 130; pp. 432-437.
Farrell, P.J. et al.; “High-Level Expression of Secreted Glycoproteins in Transformed Lepidopteran Insect Cells Using a Novel Expression Vector”; Dec. 20, 1998;Biotechnology and Bioengineering; vol. 60(6); pp. 656-663.
Faure, T. et al.; “Stable Expression of Coagulation Factors FVIII and Fix in Recombinant Chinese Hamster Ovary Cells”; 1989; Meeting Info. 9thGeneral Meeting of the European Society for Animal Cell Technology; Knokke (Belgium); 1988; pp. 481-488.
Field, R.P. et al.; “Production of a Chimeric Antibody for Tumour Imaging and Therapy From Chinese Hamster Ovary (CHO) and Myeloma Cells”; May 1990;Proceedings of the 10thESACT Meeting; pp. 742-744.
Fischer, B. et al.; “Comparison of N-Glycan Pattern of Recombinant Human Coagulation Factors II and IX Expressed in Chinese Hamster Ovary (CHO) and African Green Monkey (Vero) Cells”; 1996;J. Thrombos. and Trombolys.; vol. 3; pp. 57-62.
Fischer, B.E. et al.; “Biochemical and Functional Characterization of Recombinant von Willebrand Factor Produced on a Large Scale”; 1997;CMLS; vol. 53; pp. 943-950.
Fischer, B.E. et al.; “Structural Analysis of Recombinant von Willebrand Factor Produced at Industrial Scale Fermentation of Transformed CHO Cells Co-expressing Recombinant Furin”; 1995;FEBS Letters; vol. 375; pp. 259-262.
Fischer et al.; “Structural Analysis of Recombinant von Willebrand Factor: Identification of Hetero- and Homo-Dimers”; 1994;FEBS Letters; vol. 351; pp. 345-348.
Franek, F. et al; “Plant Protein Hydrolysates: Preparation of Defined Peptide Fractions Promoting Growth and Production in Animal Cells Cultures”; 2000;Biotechnol. Prog.; vol. 16(5); pp. 688-692.
Freshney, R.I.; “The Culture Environment: Substrate, Gas Phase, Medium, and Temperature”; Chapter 7In Culture of Animal Cells a Manual of Basic Technique, 2ndEdition; 1987; pp. 57-84.
Friedman, J.S. et al.; “High Expression in Mammalian Cells Without Amplification”; Apr. 1989;Biotechnology; vol. 7; pp. 359-362.
Gandor, C.; “Amplification and Expression of Recombinant Genes in Serum-Independent Chinese Hamster Ovary Cells”; 1995;FEBS Letters; vol. 377; pp. 290-294.
Gorfien, S.F. et al.; “Recombinant Protein Production by CHO Cells Cultured in a Chemically Defined Medium”; 1996; presented at JAACT, Yokohama: Japan; 16 pages.
Haldankar, R, et al.; “Stable Production of a Human Growth Hormone Antagonist From CHO Cells Adapted to Serum-Free Suspension Culture”; 1999;Biotechnol. Prog.; vol. 15(3); pp. 336-346.
Ham, R.G.; “Clonal Growth of Mammalian Cells in a Chemically Defined, Synthetic Medium”; 1965;PNAS; vol. 53; pp. 288-293.
Harant, H. et al.; “Two-Dimensional Electrophoresis as a Tool for Control of Quality and Consistency in Production Systems Using Animal Cells”; 1992;Cytotec
Dorner Friedrich
Mundt Wolfgang
Reiter Manfred
Baxter Innovations GmbH
Joike Michele K
Kilpatrick Townsend & Stockton LLP
LandOfFree
Recombinant cell clones having increased stability and... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Recombinant cell clones having increased stability and..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Recombinant cell clones having increased stability and... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-4316710