Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...
Reexamination Certificate
2006-08-22
2006-08-22
Guzo, David (Department: 1636)
Chemistry: molecular biology and microbiology
Micro-organism, tissue cell culture or enzyme using process...
Recombinant dna technique included in method of making a...
C435S069600, C435S325000, C435S383000, C435S390000
Reexamination Certificate
active
07094574
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: 4767704 (1988-08-01), Cleaveland et al.
patent: 4978616 (1990-12-01), Dean, Jr. et al.
patent: 5122469 (1992-06-01), Mather et al.
patent: 5393668 (1995-02-01), Cinatl et al.
patent: 5633162 (1997-05-01), Keen et al.
patent: 5851800 (1998-12-01), Adamson et al.
patent: 6048728 (2000-04-01), Inlow et al.
patent: 6100061 (2000-08-01), Reiter et al.
patent: 6475725 (2002-11-01), Reiter et al.
patent: 6936441 (2005-08-01), Reiter et al.
patent: 0 666 312 (1995-08-01), None
patent: 3244391 (1991-10-01), None
patent: 5123178 (1993-05-01), None
patent: 7039386 (1995-02-01), None
patent: WO 91/10726 (1991-07-01), 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 97/05240 (1997-02-01), None
patent: WO 98/08934 (1998-03-01), None
patent: WO 98/15614 (1998-04-01), None
patent: WO 00/03000 (2000-01-01), None
Quest International; “Protein derived peptide mixtures can effectively replace serum, glutamine and other free amino acids in cell culture media”; Research Disclosure; Nov. 1998; pp. 1474-1476.
Quest International Product Information; www.sheffield-products.com; Accessed on Nov. 18, 2003; 14 pages.
Fischer B. et al., “coparison of N-Glycan pattern of recombinant human coagulation factors II and IX expressed in Chinese hamster ovary (CHO) and African green monkey (Vero) cells,” J. Thromb. Thrombolysis, 1996, pp. 57-62, vol. 3.
Fischer, B. et al., “Structural analysis of recombinant von Willebrand factor: Identification of hetero- and homodimers,” FEBS Letters, 1994, pp. 345-348, vol. 351.
Harant, H. et al., “Two-dimensional electrophoresis as a tool for control of quality and consistency in production systems using animal cells,” Cytotechnology, 1992, pp. 119-127, vol. 8.
Ito, Y. et al., “Protein-free cell culture on an artificial substrate with covalently immobilized insulin,” Proc. Natl. Acad. Sci. USA, 1998, pp. 3598-3801, vol. 93.
Katinger, H. et al., “Long-term stability of continuously perfused animal cells immobilized on novel macroporous microcarriers,” Advances in Mol. and Cell Biol., 1996, p. 193-207, vol. 15A.
Kaufman, R. et al., “Effect of von Willebrand factor coexpression on the synthesis and secretion of factor VII in Chinese hamster ovary cells,” Mol. & Cell. Biol. 1989, pp. 1233-1242, vol. 9.
Miyaji, J. et al., “Efficient expression of human beta-interferon In namalwa KJM-1 cells adapted to serum-free medium by dhfr gene coamplification method,” Cytotechnology, 1990, pp. 173-180, vol. 4.
Miyaji, J. et al., “Expression of human beta-interferon in namalwa KJM-1 which was adapted to serum-free medium,” Cytotechnology, 1990, pp. 133-140, vol. 37.
Murhammer, D.W. and Gooche, C.F., “Structural features of nonionic polygtycol polymer molecules responsible for the protective effect in sparged animal cell bloreactors,” Biotechnol. Prog., 1990, pp. 142-146, vol. 6.
Nakajima, K. et al., “Medium for producing proteins by recombinant technology,” Japanese Appl. 2696001, Nov. 16, 1992, pp. 1-15.
Paterson, T. et al., “Approaches to maximizing stable expression of α-1-antitrypsin in transformed CHO cells,” Applied Microbiology and Technology, 1994, pp. 691-698, vol. 40.
Reiter, M. et al., “Flow cytometry and two-dimensional electrophoresis (2-DE) for system evaluation of long term continuous perfused animal cell cultures in macroporous beads,” Cytotechnology, 1992, p. 247-253, vol. 9.
Sinacore, M.S. et al., “CHO DUKX cell lineages preadapted to growth in serum-free suspension culture enable rapid development of cell culture process for the manufacture of recombinant proteins,” Biotechn. and Bioengineering, 1996, vol. 52.
Yamauchi, T. et al., “Production of human antithrombin-III in a serum-free culture of CHO cells,” Bioscl. Biotech. Biochem., 1992, pp. 600-604, vol. 56.
Zang, M. et al., “Production of recombinant proteins in Chinese hamster ovary cells using a protein-free cell culture medium,” Biotechnology, 1995, pp. 389-3922, vol. 13.
Dorner Friedrich
Mundt Wolfgang
Reiter Manfred
Baxter Aktiengesellschaft
Guzo David
Townsend and Townsend / and Crew 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-3609280