Search Patents
  • Patent number: 5268358
    Abstract: Methods and compositions are provided for treating several acute disease states associated with smooth muscle cell proliferation as well as the chronic process of atherogenesis utilizing oligopeptides corresponding to regions of the PDGF receptor protein. The oligopeptides can be used to block PDGF binding and activation for numerous applications, and can serve as immunogens to raise receptor-specific antibodies.
    Type: Grant
    Filed: May 6, 1991
    Date of Patent: December 7, 1993
    Assignee: Cor Therapeutics, Inc.
    Inventor: Larry J. Fretto
  • Patent number: 5756664
    Abstract: The present invention provides the sequence of the novel bone-related protein OSF-2 which can be obtained from mammalian bone tissues. The invention further provides a method of production of OSF-2 by recombinant techniques.
    Type: Grant
    Filed: April 21, 1995
    Date of Patent: May 26, 1998
    Assignee: Hoechst Japan Limited
    Inventors: Egon Amann, Yoko Otawara-Hamamoto, Reiko Kikuno, Sunao Takeshita, Kenichi Tezuka
  • Patent number: 5264549
    Abstract: A purified protein, factor J, which has inhibitory properties which prevent the formation or the dissociation of Cl complex and a method of purification for said protein. The method including the following sequential chromatography steps: anion exchange, QAE-"SEPHADEX", heparin-"SEPHAROSE" affinity, "MONO Q" and hydroxylapatite.
    Type: Grant
    Filed: April 27, 1992
    Date of Patent: November 23, 1993
    Assignee: The Beth Israel Hospital Association
    Inventor: Anne Nicholson-Weller
  • Patent number: 5268363
    Abstract: A purified protein, factor J, which has inhibitory properties which prevent the formation or the dissociation of Cl complex and a method of purification for said protein. The method including the following sequential chromatography steps: anion exchange QAE-"SEPHADEX", heparin-"SEPHAROSE" affinity, "MONO Q" and hydroxylapatite.
    Type: Grant
    Filed: April 27, 1992
    Date of Patent: December 7, 1993
    Assignee: The Beth Israel Hospital Association
    Inventor: Anne Nicholson-Weller
  • Patent number: 5128453
    Abstract: Purification of human FSH from post-menopausal urine gonadotropin using immunoaffinity chromatography with elution at high pH and reverse-phase HPLC steps yields a biologically active hormone which is free from detectable traces of luteinizing hormone and other urinary proteins.
    Type: Grant
    Filed: February 7, 1989
    Date of Patent: July 7, 1992
    Assignee: Istituto DiRicerca Cesare Serono SpA
    Inventors: Guiseppe Arpaia, Serenella Serani, Antonino Sirna, Stefano Villa
  • Patent number: 5449758
    Abstract: The invention relates to a multidomain protein comprising sites for cleavage of the protein into at least 3 polypeptide domains; nucleic acid encoding the multidomain protein; a protein ladder comprising a collection of protein fragments obtained by the partial cleavage of one or more multidomain proteins by one or more cleaving agents; and methods of using and preparing the protein ladder.
    Type: Grant
    Filed: December 2, 1993
    Date of Patent: September 12, 1995
    Assignee: Life Technologies, Inc.
    Inventor: James L. Hartley
  • Patent number: 5008377
    Abstract: A method for the preparation of a protein in a physiologically active or native form, which method includesproviding a source of protein in a solubilized form,and a cationic exchange medium;contacting the source of protein and cationic exchange medium; andrecovering the protein in a physiologically active form.
    Type: Grant
    Filed: April 21, 1988
    Date of Patent: April 16, 1991
    Assignee: Bunge (Australia) Pty. Ltd.
    Inventors: Joseph J. Patroni, Malcolm R. Brandon
  • Patent number: 5717067
    Abstract: A new substrate of epidermal growth factor receptor and certain other tyrosine kinase receptors denominated eps15, polynucleotides encoding epsl5, antisense eps15 polynucleotide, triple helix eps15 polynucleotide, antibodies to eps15, and assays for determining eps15.
    Type: Grant
    Filed: June 7, 1995
    Date of Patent: February 10, 1998
    Assignee: The United States of America as represented by the Department of Health and Human Services
    Inventors: Pier Paolo DiFiore, Francesca Fazioli
  • Patent number: 5478923
    Abstract: Single-chain analogs of the naturally occurring two-chain peptide monellin retain the sweetening properties of the natural protein and are stable under conditions which would otherwise destabilize the native peptide. A covalent linkage joins peptides corresponding to portions of the A and B chains of the naturally occurring protein.
    Type: Grant
    Filed: March 25, 1994
    Date of Patent: December 26, 1995
    Assignees: The Regents of the University of California, Lucky, Ltd.
    Inventors: Sung-Hou Kim, Joong M. Cho
  • Patent number: 5439886
    Abstract: The present invention relates to a monclonal antibody capable of suppressing the motility of cancer cells, a polypeptide recognizable by said anti-cancer antibody and its fragment peptides which is capable of suppressing the motility of cancer cells.The present invention also relates to a production and a use for preventing the matastasis of cancer thereof.
    Type: Grant
    Filed: June 6, 1994
    Date of Patent: August 8, 1995
    Assignee: Takeda Chemical Industries, Ltd.
    Inventors: Shuichi Ikeyama, Masaru Koyama, Masayuki Miyake, Masaharu Senoo
  • Patent number: 4966963
    Abstract: A method for the preparation of proteins in biologically active form including providing a source of protein solubilized from inclusion bodies with a cationic surfactant; providing a weak denaturing agent; and contacting the solubilized protein with the weak denaturant in water in an amount sufficient to allow the protein to remain in a biologically active form.
    Type: Grant
    Filed: February 11, 1988
    Date of Patent: October 30, 1990
    Assignee: Bunge (Australia) Pty. Ltd.
    Inventor: Joseph J. Patroni
  • Patent number: 5270449
    Abstract: A group of growth factors, designated heparin-binding brain mitogens (HBBMs), is disclosed. The HBBMs are isolated from brain tissue by a sequence of purification steps. The growth factors may be useful in the promotion of angiogenesis, such as in the promotion of wound healing, bone healing and in the treatment of burns, as well as in promoting the formation, maintenance and repair of tissue, in particular, neural tissue.
    Type: Grant
    Filed: September 14, 1992
    Date of Patent: December 14, 1993
    Assignee: American Cyanamid Company
    Inventors: Peter Bohlen, Peter Gautschi-Sova
  • Patent number: 4992531
    Abstract: A method for the recovery of proteins in a solubilized form from host cells including providing a source of host cells incorporating a synthesized or expressed protein; providing a source of at least one cationic surfactant; and treating the host cells with at least one cationic surfactant, in an amount sufficient to effect solubilization of the proteins.
    Type: Grant
    Filed: June 13, 1988
    Date of Patent: February 12, 1991
    Assignee: Bunge (Australia) Pty. Ltd.
    Inventors: Joseph J. Patroni, Malcolm R. Brandon
  • Patent number: 5095094
    Abstract: The proteins of the invention are specifically recognized by polyclonal anti-AC antibodies raised against purified AC preparations, devoid of adenylate cyclase CaM-activable activity and devoid of affinity for CaM.
    Type: Grant
    Filed: February 20, 1990
    Date of Patent: March 10, 1992
    Assignees: Institut Pasteur, Institut National de la Sante et de la Recherche Medicale
    Inventors: Colette Brezin, Hoang-Oanh Nghiem, Jean Luc Boucaud, Jean M. Alonso
  • Patent number: 5241050
    Abstract: From a cDNA library, a nucleotide sequence of a novel gene, called rig, specifically expressed by streptozotocin- or alloxan-nicotinamide-induced rat insulinomas was determined and an amino acid sequence of a protein encoded by the gene was deduced. Further, novel genes with base sequences homologous to rig were found in a BK virus-induced hamster insulinoma and in a surgically removed human insulinoma. The above DNA is transcribed to provide an mRNA. The above novel proteins, DNAs and mRNAs can be efficaciously employed for the medical purposes of pancreatic diseases.
    Type: Grant
    Filed: December 18, 1990
    Date of Patent: August 31, 1993
    Assignee: Tohoku University
    Inventor: Hiroshi Okamoto
  • Patent number: 5415859
    Abstract: The protein doublet H110D, the individual components thereof, and the production and use thereof in a vaccine against a nematode infection. This protein doublet is a plasma membrane-associated protein material of the intestinal microvilli of Haemonchus contortus. H110D has a molecular weight of about 110 kd and reacts with antibodies raised in animals injected with a contortin-enriched fraction. Injection of preparations of the protein doublet H110D or its components induces the production of specific protective antibodies.
    Type: Grant
    Filed: August 14, 1992
    Date of Patent: May 16, 1995
    Inventor: Edward A. Munn
  • Patent number: 5457178
    Abstract: This invention provides a family of insecticidally effective proteins and particular members of that family which may be isolated from the venom of the spider Filistata hibernalis, DNA encoding such proteins, insecticidal compositions of these proteins or the DNA encoding them, and methods for controlling invertebrate pests. Recombinant expression vectors and host cells and methods for producing insecticidally effective peptides are also provided.
    Type: Grant
    Filed: July 7, 1993
    Date of Patent: October 10, 1995
    Assignees: FMC Corporation, NPS Pharmaceuticals, Inc.
    Inventors: John R. H. Jackson, Karen J. Krapcho, Janice H. Johnson, Robert M. Kral, Jr.
  • Patent number: 5075423
    Abstract: Affinity-purified protein A preparations are contacted with a suitable anionic exchange material in order to remove trace contamination. Staphylococcal enterotoxin B (SEB) and other proteinaceous contaminants are removed by passing such affinity-purified protein A preparations through a DEAE-cellulose column and thereafter selectively eluting the protein A to separate the contaminants. Very high purity protein A composition are thus obtained, typically having a contaminant concentration of about 5 weight % or below, with below about 0.001 weight % SEB.
    Type: Grant
    Filed: January 24, 1990
    Date of Patent: December 24, 1991
    Assignee: Imre Corporation
    Inventor: Joseph P. Balint, Jr.
  • Patent number: 4923967
    Abstract: The present invention discloses a new method for solubilizing and refolding recombinant proteins expressed as granules. The method involves sulfitolysis and the formation of a precipitate of protein-S-sulfonate by warming. The precipitate has been found to contain protein in high purity. In addition, proper folding takes place if the desired protein is fully reduced and passed through an intermediate concentration of denaturant which allows for a transition between its folded and unfolded states.
    Type: Grant
    Filed: September 26, 1988
    Date of Patent: May 8, 1990
    Assignee: Eli Lilly and Company
    Inventors: Jesse L. Bobbitt, Joseph Manetta
  • Patent number: 5314993
    Abstract: The invention concerns a process for purifying protein A preparations to high purity with high product yield. Where the protein A is obtained from a Gram-negative recombinant microbe hosting a vehicle containing a gene encoding protein A, the protein A is purified to high purity, and, advantageously, to very low levels of endotoxin. The protein A preparations made via the invention process are useful in therapeutic application, e.g., therapeutic plasma exchange, as well as for other well-known uses of protein A.
    Type: Grant
    Filed: February 10, 1992
    Date of Patent: May 24, 1994
    Assignee: Repligen Corporation
    Inventors: Richard N. Love, Albert T. Profy