U.S. patents available from 1976 to present.
U.S. patent applications available from 2005 to present.

Icon_funbox Bizarre Patents

Patent No. 6711769

Pillow with retractable umbrella

A pillow assembly having a supporting assembly and a retractable umbrella assembly that is easily transportable and allows a user to support his/her head while covering their face from sunlight.

Newsletter  PatentStorm News

Make the Most of PatentStorm

See this month's Top Inventors and Most Cited Patents.

Stay on top of the latest patents by subscribing to an RSS feed.

Got questions? Ask a Patent Expert!

Registered users: Manage your profile, comments and alerts.

 

US Patent 7238488 - Therapeutic and diagnostic applications of perlecan domain I splice variants

US Patent Issued on July 3, 2007
Estimated Patent Expiration Date: Icon_subject September 13, 2022Estimated Expiration Date is calculated based on simple USPTO term provisions. It does not account for terminal disclaimers, term adjustments, failure to pay maintenance fees, or other factors which might affect the term of a patent.
loading...


View Patent Images (PDF)
(Registered users only)

Abstract

A method of producing antibodies comprising the step of encoding a peptide sequence from a Domain I perlecan splice variant, wherein the peptide sequence is used to produce anti-peptide antibodies.

Other References

  • Ailles, et al., “Induction of Perlecan Gene Expression Precedes Amyloid Formation During Experimental Murine AA Amyloidogenesis,” Laboratory Investigation, vol. 69, No. 4, pp. 443-448, 1993.
  • Cohen et al., “Structural Characterization of the Complete Human Perlecan Gene and its Promoter,” Proc. Natl. Acad. Sci USA, vol. 90, pp. 10404-10408, 1993.
  • Dolan et al., “Identification and Sites in Domain I of Perlecan That Regulate Heparan Sulfate Synthesis,” Journal of Bio. Chem, vol. 272, No. 7, pp. 4316-4322, Feb. 14, 1997.
  • Groffen, et al., “Expression and Characterization of Human Perlecan Domains I and II Synthesized by Baculovirus-infected Insect Cells,” European Journal of Biochem., vol. 241, pp. 827-834, 1996.
  • Murdoch et al., “Widespread Expression of Perlecan Proteoglycan in Basement Membranes and Extracellular Matrices of Human Tissues as Detected by a Novel Monoclonal Antibody Against Domain III and by In Situ Hybridization,” The Journal of Histochem. and Cytochem., vol. 42, No. 2, pp. 239-249, 1994.
  • Noonan et al., “Perlecan, the Large Low-density Proteoglycan of Basement Membranes: Structure and Variant Forms,” Kidney International, vol. 43, pp. 53-60, 1993.
  • Sigma Chemical Company, “Biochemicals Organic Compounds for Research and Diagnostic Reagents,” Sigma Chemical Company, 1992, pp. 513 (see products entitle heparan sulfate).
  • Stryer, Biochemsity, W.H. Freeman and Company, San Francisco, 1981, pp. 13-16 and 512-513.
  • Goedert et al., “Assembly of Microtubule-associated Protein Tau into Alzheimer-life Filaments Induced by Sulphated Glycosaminoglycans,” Nature, vol. 383, pp. 550-553, Oct. 1996.
  • Maresh et al., “Detection and Quantitation of Perlecan mRNA Levels in Alzheimer's Disease and Normal Aged Hippocampus by Competitive Reverse Transcription-Polymerase Chain Reaction,” J. Neurochem., vol. 67, No. 3, pp. 1132-1143, 1996.
  • Murdoch et al., “Primary Structure of the Human Heparan Sulfate Proteoglycan from Basement Membrane (HSPG2/Perlecan),” Journal of Bio. Chem., vol. 267, No. 12, pp. 8544-8557, Apr. 25, 1992.
  • Snow et al., “The Presence of Heparan Sulfate Proteoglycans in the Neuritic Plaques and Congophilic Angiopathy in Alzheimer's Disease,” American Journal of Pathology, vol. 133, No. 3, pp. 456-463, Dec. 1988.
  • Snow et al., “Immunolocalization of Heparan Sulfate Proteoglycans to the Prion Protein Amyloid Plaques of Gerstmann-Straussler Syndrome, Creutzfeldt-Jakob Disease and Scrapie,”Laboratory Investigation, vol. 63, No. 5, pp. 601-611, 1990.
  • Snow et al., “Proteoglycans in the Pathogenesis of Alzheimer's Disease and Other Amyloidoses,” Neurobiology of Aging, vol. 10, pp. 481-497, 1989.
  • Snow et al., “Heparan Sulfate Proteoglycans in Diffuse Plaques of Hippocampus but not of Cerebellum in Alzheimer's Disease Brain,” American Journal of Pathology, vol. 144, No. 2, pp. 337-347, Feb. 1994.
  • Snow et al., “Differential Binding of Vascular Cell-Derived Proteoglycans (Perlecan, Biglycan, Decorin, and Versican) to the Beta-Amyloid Protein of Alzheimer's Disease,” Archives of Biochemistry and Biophysics, vol. 320, No. 1, pp. 84-95, Jun. 20, 1995.
  • Brunden et al., “pH-Dependent Binding of Synthetic β-Amyloid Peptides in Glycosaminoglycans,” J. Neurochem., vol. 61, No. 6, pp. 2147-2154, 1993.
  • Snow et al., “An Important Role of Heparan Sulfate Proteoglycan (Perlecan) in a Model System for the Deposition and Persistence of Fibrillar Aβ-Amyloid in Rat Brain,” Neuron, vol. 12, pp. 219-234, Jan. 1994.
  • Gupta-Bansal et al., “Proteoglycan-Mediated Inhibition of Aβ Proteolysis,” Journal of Bio. Chem., vol. 270, No. 31, pp. 18666-18671, 1995.
  • Snow et al., “Early Accumulation of Heparan Sulfate in Neurons and in the Beta-Amyloid Protein-Containing Lesions of Alzheimer's Disease and Down's Syndrome,” American Journal of Pathology, vol. 137, No. 5, pp. 1253-1270, Nov. 1990.
  • Kallunki et al., “Human Basement Membrane Heparan Sulfate Proteoglycan Core Protein: A 467-kD Protein Containing Multiple Domains Resembling Elements of the Low Density Lipoprotein Receptor, Laminin, Neural Cell Adhesion Molecules, and Epidermal Growth Factor,” Journal of Cell Biology, vol. 116, pp. 559-571, 1992.
  • Noonan et al., “The Complete Sequence of Perlecan, a Basement Membrane Heparan Sulphate Proteoglycan, Reveals Extensive Similarity with Laminin A Chain, Low Density Lipoprotein-Receptor, and the Neural Cell Adhesion Molecule,” Journal of Bio. Chem., vol. 266, No. 34, pp. 22939-22947, Dec. 5, 1991.
  • Kato et al., “Basement Membrane Proteoglycan in Various Tissues: Characterization Using Monoclonal Antibodies to the Engelbreth-Holm-Swarm Mouse Tumor Low Density Heparan Sulfate Proteoglycan,” Journal of Cell Biology, pp. 2203-2210, Jun. 1988.
  • Kokenyesi et al., “Formation of Heparan Sulfate or Chondroitin/Dermatan Sulfate on Recombinant Domain I of Mouse Perlecan Expressed in Chinese Hamster Ovary Cells,” Biochemical and Biophysical Research Communications, vol. 211, No. 1, pp. 262-267, Jun. 6, 1995.
  • Nochlin et al., “A Simple Method of Rapid Freezing Adequately Preserves Brain Tissue for Immunocytochemistry Light and Electron Microscopic Examination,” Acta Neuropathol, vol. 86, pp. 645-650, 1993.
  • Jacob et al., “The 5′Splice Site: Phylogenetic Evolution and Variable Geometry of Association with U1RNA,” Nucleic Acids Research, vol. 17, No. 6, pp. 2159-2180, 1989.
  • Jackson et al., “A Reappraisal of Non-Consensus mRNA Splice Sites,” Nucleic Acids Research, vol. 19, No. 14, pp. 3795-3798, 1991.
  • Merrifield, “Solid Phase Synthesis,”Science, vol. 232, pp. 341-347, Apr. 18, 1986.
  • Fields et al., “Solid Phase Peptide Synthesis Utilizing 9-Fluorenylmethoxycarbonyl Amino Acids,” Intl. J. Peptide Protein Res., vol. 35, pp. 161-214, 1990.
  • Hampson et al., “Separation of Radiolabelled Glycosaminoglycan Oligosaccharides by Polyacrylamide-Gel Electrophoresis,” vol. 221, pp. 697-705, 1984.
  • Farach-Carson et al., “Extraction and Isolation of Glycoproteins and Proteoglycans,” BioTechniques, vol. 7, No. 5, pp. 482-493, 1989.
  • Hovingh et al., “Differentially Expressed Patterns of Glycosaminoglycan Structure in Heparan Sulfate Proteoglycans and Free Chains,” Eur. J. Biochem., vol. 211, pp. 771-779, 1993.

Inventors

Application

No. 10244151 filed on 09/13/2002

US Classes:

435/7.1, Involving antigen-antibody binding, specific binding protein assay or specific ligand-receptor binding assay435/7.21, Animal cell435/40.5, Involving fixed or stabilized, nonliving microorganism, cell, or tissue (e.g., processes of staining, stabilizing, dehydrating, etc.; compositions used therefore, etc.)435/40.52, Involving tissue sections436/501, BIOSPECIFIC LIGAND BINDING ASSAY436/503, Utilizing isolate of tissue or organ as binding agent436/547, INVOLVING PRODUCTION OR TREATMENT OF ANTIBODY436/63, BIOLOGICAL CELLULAR MATERIAL TESTED530/326, 15 to 23 amino acid residues in defined sequence530/387.1, Immunoglobulin, antibody, or fragment thereof, other than immunoglobulin antibody, or fragment thereof that is conjugated or absorbed530/402, Chemical modification or the reaction product thereof, e.g., covalent attachment or coupling, etc.530/403, Protein is identified as an antigen, e.g., immunogenic carriers, etc.436/6Corrosion resistance or power

Field of Search

435/7.1, Involving antigen-antibody binding, specific binding protein assay or specific ligand-receptor binding assay435/7.21, Animal cell435/7.9, Assay in which an enzyme present is a label435/7.92, Heterogeneous or solid phase assay system (e.g., ELISA, etc.)435/7.8, Involving nonmembrane bound receptor binding or protein binding other than antigen-antibody binding530/300, PEPTIDES OF 3 TO 100 AMINO ACID RESIDUES436/501, BIOSPECIFIC LIGAND BINDING ASSAY436/504Radioactive label

Examiners

Primary: Chernyshev, Olga N.

Attorney, Agent or Firm

US Patent References

6432636Diagnostic applications of perlecan domain I splice variants
Issued on: 08/13/2002
Inventor: Maresh, et al.

International Classes

G01N 33/53
G01N 33/567
G01N 1/00
G01N 33/48
G01N 33/566
A61K 38/00
C07K 16/00
C07K 1/00
C07K 14/00

Comments

No comments for this page
 
 
Forgot password?
Register here