Chemistry: analytical and immunological testing – Involving an insoluble carrier for immobilizing immunochemicals
Reexamination Certificate
2011-07-19
2011-07-19
Yu, Melanie (Department: 1641)
Chemistry: analytical and immunological testing
Involving an insoluble carrier for immobilizing immunochemicals
C436S524000, C436S527000, C436S528000, C436S532000
Reexamination Certificate
active
07981694
ABSTRACT:
The invention is a method for the isolation of molecules of interest using tubes in which at least a portion of the inner walls of the tube are coated with microbeads that are coated with a capture reagent to bind the molecule of interest. The microbeads may be glass or polymer beads. The invention is a method and apparatus for preparation of the tubes for use in the method of the invention. The invention is a method for determining ratios of guanine nucleotides bound to guanine-nucleotide binding proteins.
REFERENCES:
patent: 4251616 (1981-02-01), Hendriks
patent: 4366242 (1982-12-01), Neumann et al.
patent: 4965087 (1990-10-01), Wolfbeis et al.
patent: 5296347 (1994-03-01), LaMotte, III
patent: 5470609 (1995-11-01), Leach et al.
patent: 5599668 (1997-02-01), Stimpson et al.
patent: 5741635 (1998-04-01), Boss
patent: 6156550 (2000-12-01), Glad
patent: 6294401 (2001-09-01), Jacobson et al.
patent: 6569619 (2003-05-01), Sivaraja
patent: 6699677 (2004-03-01), Schall et al.
patent: 2003/0046717 (2003-03-01), Zhang
patent: 2003/0068616 (2003-04-01), Polansky
patent: 2003/0153010 (2003-08-01), Orth et al.
patent: 2004/0014101 (2004-01-01), Liu et al.
patent: WO 98/56806 (1998-12-01), None
“Affinity Chromatography,” from http:mobitec.de. Publication date unknown, 4 pages.
Albarghouthi, M. et al., “Immobilization of Antibodies on Alginate-Chitosan Beads,” International Journal of Pharmaceutics, 2000, pp. 23-34, vol. 206.
“Attach a Protein Onto Glass, Silica, or Quartz Surface Using a Cleavable Cross-Linker,” Technical Resource, Pierce Biotechnology, Oct. 2002, 7 pages.
Chen et al., High-Efficiency Solid-Phase Capture Using Glass Beads Bonded to Microcentrifuge Tubes: Immnoprecipitation of Proteins from Cell Extracts and Assessment of Ras Activation, Analytical Biochemistry, 2002, pp. 298-304, vol. 302.
“CNBr-activated Sepharose 4B,” Amersham Biosciences, 2002, 12 pages.
“Cross-linking,” Pierce Biotechnology, 2002, [Online] [Retrieved on Jan. 9, 2004] Retrieved from the Internet<URL:http://www.piercenet.com/Objects/View.cfm?type =Page&ID=70485B9B-2585-45C7-846B>.
Denizli, A. et al., “Protein A Immobilized Polyhydroxyethylmethylacrylate Beads for Affinity Sorption of Human Immunoglobulin G,” Journal of Chromatography B, 1995, pp. 13-19, vol. 668.
“Double Agents Cross-linking Reagents Selection Guide,” Pierce Biotechnology, 2003, 32 pages.
“EDC,” Instructions, Pierce Biotechnology, May 2002, 3 pages.
Fahrner, R.L. et al., “Performance Comparison of Protein A Affinity-Chromatography Sorbents for Purifying Recombinant Monoclonal Antibodies,” Biotechnol. Appl. Biochem., 1999, pp. 121-128, vol. 30.
Hale, J.E. et al., Purification of Humanized Murine and Murine Monoclonal Antibodies Using Immobilized Metal-Affinity Chromatography, Analytical Biochemistry, 1994, pp. 29-33, vol. 222.
Hammerl, P. et al., “Particulate Nitrocellulose as a Solid Phase for Protein Immobilization in Immuno-Affinity Chromatography,” Journal of Immunological Methods, 1993, pp. 59-66, vol. 165.
Kim, J. et al., “Protein Immobilization on Plasma-Polymerized Ethylenediamine-Coated Glass Slides,” Analytical Biochemistry, 2003, pp. 41-45, vol. 313.
Krogh, T.N. et al., “Protein Analysis Using Enzymes Immobilized to Paramagnetic Beads,” 1999, pp. 153-162, vol. 274.
Leibl, H. et al., “Separation of Polysaccharide-Specific Human Immunoglobulin G Subclasses Using a Protein A Superose Column with a pH Gradient Elution System,” Journal of Chromatography, 1996, pp. 51-56, vol. 639.
Nisnevitch, M. et al., “The Solid Phase in Affinity Chromatography Strategies for Antibody Attachment,” J. Biochem. Biophys. Methods, 2001, pp. 467-480, vol. 49.
Phillips, T.M. et al., “Isolation and Quantitation of Serum IgE Levels by High Performance Immunoaffinity Chromatography,” Journal of Chromatography, 1985, pp. 205-211, vol. 327.
Phillips, T.M., “Multi-Analyte Analysis of Biological Fluids with a Recycling Immunoaffinity Column Array,” J. Biochem. Biophys. Methods, 2001, pp. 253-262, vol. 49.
Phillips, T.M. et al., “Protein A-Coated Glass Beads: Universal Support Meduim for High-Performance Immunoaffinity Chromatography,” Journal of Chromatography, 1985, pp. 213-219, vol. 327.
Quitadamo, I.J. et al., “Efficient Purification of Mouse Anti-FGF Receptor IgM Monclonal Antibody by Magnetic Beads,” Hybridoma, 1998, pp. 199-207, vol. 17, No. 2.
Scheele, J.S. et al., “Determination of Absolute Amounts of GDP and GTP Bound to Ras in Mammalian Cells: Comparison of Parental and Ras-Overproducing NIH 3T3 Fibroblasts,” Proc. Natl. Acad. Sci. USA, Cell Biology, Feb. 1995, pp. 1097-1100, vol. 92.
Schneider, C. et al., “A One-Step Purification of Membrane Protein Using a High Efficiency Immunomatrix,” The Journal of Biological Chemistry, Sep. 25, 1982, pp. 10766-10769, vol. 257, No. 18.
Walsh, M.K. et al., “Optimizing the Immobilization of Single Stranded DNA onto Glass Beads,” J Biochem Biophys. Methods, 2001, pp. 221-231, vol. 47.
Bos, J.L., “ras-Oncogenes in Human Cancer: a Review,” Cancer Research, 1989, pp. 4682-4689, vol. 49.
Bradford, M.M., “A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein Dye Binding,” Analytical Biochemistry, 1976, pp. 248-254, vol. 72.
Brunk, C. et al., “Assay for Nanogram Quantities of DNA in Cellular Homogenates,” Analytical Biochemistry, 1979, pp. 497-500, vol. 92.
Dupuy, A.J., et al., “Activation of the Rap1 Guanine Nucleotide Exchange Gene, CalDAG-GEF I, in BXH-2 Murine Myeloid Leukemia,” The Journal of Biological Chemistry, Apr. 13, 2001, pp. 11804-11811, vol. 276, No. 15.
Gibbs, J.B. et al., “Identification of Guanine Nucleotides Bound toras-Encoded Proteins in Growing Yeast Cells,” The Journal of Biological Chemistry, Aug. 5, 1987, pp. 10426-10429, vol. 262, No. 22.
Guha, A. et al., “Proliferation of Human Malignant Astrocytomas is Dependent on Ras Activation,” Oncogene, 1997, pp. 2755-2765, vol. 15.
Hall, A., “Rho GTPases and the Actin Cytoskeleton,” Science, 1998, pp. 509-514, vol. 279.
Mul, F.P.J. et al., “An Improved Method for the Purification of Basophilic Granulocytes from Human Blood,” Journal of Immunological Methods, 1992, pp. 207-214, vol. 149.
Müller-Schulte, D. et al., “Novel Magnetic Micro Spheres on the Basis of Poly(vinylalcohol) as Affinity Medium for Quantitative Detection of Glycated Haemoglobin,” Journal of Chromatography, 1995, pp. 53-60, vol. 711.
Murphy, S.J. et al., “An Evaluation of Cell Separation Techniques in a Model Mixed Cell Population,” Journal of Cell Science, 1992, pp. 789-798, vol. 102.
Olofsson, B. “Rho Guanine Dissociation Inhibitors: Pivotal Molecules in Cellular Signalling,” Cell Signal, 1999, pp. 545-554, vol. 11, No. 8.
Olsvik, R. et al., “Magnetic Separation Techniques in Diagnostic Microbiology,” Clinical Microbiology Reviews, Jan. 1994, pp. 43-54, vol. 7, No. 1.
Phillips, T.M et al., “High-Performance Affinity Chromatography: a Rapid Technique for the Isolation and Quantitation of IgG from Cerebral Spinal Fluid,” Journal of Chromatography, 1984, pp. 173-179, vol. 317.
Pilz, R.B. et al., “Isolation and Characterization of HL-60 Cells Resistant to Nitroprusside-induced Differentiation,” The Journal of Biological Chemistry, Dec. 23, 1994, pp. 32155-32161, vol. 269, No. 51.
Pilz, R.B.et al., “Chemically-Induced Murine Erythroleukemia Cell Differentiation is Severely Impaired When cAMP-Dependent Protein Kinase Activity is Repressed by Transfected Genes,” The Journal of Biological Chemistry, Aug. 15, 1992, pp. 16161-16167, vol. 267, No. 23.
Prigent, S.A. et al. “Enhanced Tumorigenic Behavior of Gli
Boss Gerry R.
Chen Jeffrey C.
Hoffman Stephanie
Jones Stephen B.
Kimmerly Adam
Fenwick & West LLP
The Regents of the University of California
Yu Melanie
LandOfFree
Solid phase isolation of proteins, nucleic acids and other... does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Solid phase isolation of proteins, nucleic acids and other..., we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Solid phase isolation of proteins, nucleic acids and other... will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-2716755