Animal protein free media for cultivation of cells

Chemistry: molecular biology and microbiology – Virus or bacteriophage – except for viral vector or...

Reexamination Certificate

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C435S239000, C435S069100

Reexamination Certificate

active

07955833

ABSTRACT:
The present invention relates to animal protein free cell culture media comprising a combination of non-animal derived peptides derived from soy hydrolysate and yeast hydrolysate. The invention also provides an animal protein free culture process, wherein cells are cultivated, propagated and passaged without animal-derived components. This process is useful for cultivating cells, such as recombinant cells or cells infected with a virus, and for production biological products by cell culture processes under conditions devoid of animal protein components.

REFERENCES:
patent: 4282315 (1981-08-01), Luderer et al.
patent: 4322404 (1982-03-01), Gauri et al.
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: 5753489 (1998-05-01), Kistner et al.
patent: 5789247 (1998-08-01), Ballay 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: 6406909 (2002-06-01), Shibuya et al.
patent: 6475725 (2002-11-01), Reiter et al.
patent: 2002/0182679 (2002-12-01), Reiter et al.
patent: 2003/0203448 (2003-10-01), Reiter et al.
patent: 1659/99 (1999-09-01), None
patent: 78958/98 (1998-10-01), 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: 2001211878 (2001-08-01), 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: 7-039388 (1995-02-01), None
patent: 2-859679 (1999-02-01), None
patent: H01-211488 (1999-08-01), None
patent: WO 85/02810 (1985-06-01), None
patent: WO 86/04920 (1986-08-01), None
patent: WO 88/00987 (1988-02-01), None
patent: WO 89/00192 (1989-12-01), None
patent: WO 91/10726 (1991-07-01), None
patent: WO 91/09122 (1991-08-01), 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 96/26266 (1996-08-01), None
patent: WO 96/40886 (1996-08-01), None
patent: WO 97/05240 (1997-02-01), None
patent: WO 98/08934 (1998-03-01), None
patent: WO98/15614 (1998-04-01), None
patent: WO 98/15614 (1998-04-01), None
patent: WO 96/18734 (1998-08-01), None
patent: WO 98/54296 (1998-12-01), None
patent: WO 99/05268 (1999-02-01), None
patent: WO99/47648 (1999-09-01), None
patent: WO 99/57246 (1999-11-01), None
patent: WO00/03000 (2000-01-01), 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
Quest International, Product Information Sheet, “HY-SOY”, Norwich, NY, 1995.
Sheffield Pharma Ingredients, Technical Manual, “Cell Nutrition, Hydolyzed Proteins & Yeast Extracts”,.
Berg, D.T. et al.; “High-Level Expression of Secreted Proteins from Cells Adapted to Serum-Free Suspension Culture”;BioTechniques; 1998; vol. 14(6); pp. 972-978.
Bielicki, J. et al.; “Recombinant Human Sutphamidase: 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 Amplificiation 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 4D1 inCell&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 7 inCulture 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 Recombiant Genes in Serum-Independent Chinese Hampster 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.
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