University of Rochester

Eastman-kodak Company

Johnson & Johnson Clinical Diagnostics, Inc.

Ortho-clinical Diagnostics, Inc

Microbplex, Inc.

John L Daiss

Edward M Schwarz

Mark A Sullivan

Edward R Scalice

Theodore W Esders

Kenneth G Christy, Jr

David J Sharkey

Sheila Bello-Irizarry

James Brodell

John J Varrone

Kevin Matthew Gorman

Brian A Snyder

Paul B Contestable

Alan J Lowne

Frances Eun-Hyung Lee

Leonard J Seaberg

Elizabeth A Grogan

Holly L Groth

Stephen E Clark

Frances L Stickley

Alan R Thomson

Carolyn R Hinchman

Sheila N Bello-Irizarry

The present invention is directed to a monoclonal antibody that binds specifically to aglucosaminidase and inhibits in vivo growth of. Also disclosed are monoclonal antibody binding portions, recombinant or hybridoma cell lines, pharmaceutical compositions containing the monoclonal antibody or binding portions thereof, and methods of treatinginfection and osteomyelitis, and methods for introducing an orthopedic implant into a patient using the monoclonal antibody, binding portion, or pharmaceutical composition of the present invention.

Anti-glucosaminidase passive immunization forinfections

Disclosed herein are monoclonal antibodies or binding portion thereof that bind specifically to aspp. autolysin N-acetylmuramoyl-L-alanine amidase catalytic domain and/or cell wall binding domain, as well as pharmaceutical compositions containing the same. Cell lines expressing the monoclonal antibodies, including hybridomas, are also disclosed. Methods of using the monoclonal antibodies for installation of orthopedic implants, grafts or medical devices, treating or preventing ainfection, and treating osteomyelitis are described, as are diagnostic methods for the detection ofin a sample.

Passive immunization forinfections

Disclosed are methods and kits for early detection of antigen exposure through the presence or absence of antigen-specific antibodies.

Media elaborated with newly synthesized antibodies (MENSA) and uses thereof

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The present invention is directed to a monoclonal antibody that binds specifically to aglucosaminidase and inhibits in vivo growth of. Also disclosed are monoclonal antibody binding portions, recombinant or hybridoma cell lines, pharmaceutical compositions containing the monoclonal antibody or binding portions thereof, and methods of treating 5*.infection and osteomyelitis, and methods for introducing an orthopedic implant into a patient using the monoclonal antibody, binding portion, or pharmaceutical composition of the present invention.

The present invention relates to new CRP immunoassay compositions. The compositions include a low affinity anti-human CRP monoclonal antibody, and an antiidiotypic antibody raised against it. The invention further provides a method for obtaining antiidiotypic monoclonal antibody populations directed to an antibody that is specific for a high concentration, high molecular weight target antigen.

Immunoassay for C-reactive protein

Specific binding ligands can be detected with an assay which utilizes an immobilized receptor for the ligand, an immobilized reporter enzyme, an inhibitor antibody and a a water-soluble conjugate of the ligand and an anti-inhibitor antibody. Both antibodies are specific for the reporter enzyme, but the antibodies affect enzymatic activity differently. The inhibitor antibody effectively shuts down the activity of the reporter enzyme when it is complexed thereto. The anti-inhibitor antibody binds to the reporter enzyme, does not affect the enzymatic activity, but prevents the binding of the inhibitor enzyme. This assay provides a direct correlation of the generated signal to the target specific binding ligand.

Specific binding assay using enzyme inhibitor and anti-inhibitor

Monoclonal antibodies have been prepared which are of the IgG isotype and are highly specific for horseradish peroxidase. One group of antibodies inhibits at least about 95% of the normal activity of horseradish peroxidase when bound to the enzyme. A second group of antibodies inhibits less than about 20% of the enzymatic activity when bound to the enzyme, but prevents the binding of the antibodies from the first group. The antibodies in either group can be conjugated to specific binding ligands such as drugs or hormones.

Inhibitor and anti-inhibitor monoclonal antibodies specific for

Antibodies which are specific to a thermostable DNA polymerase can be used to reduce or eliminate the formation of non-specific products in polymerase chain reaction methods. These antibodies and other temperature sensitive inhibitors are effective to inhibit DNA polymerase enzymatic activity at a certain temperature T.sub.1 which is generally below about 85.degree. C. The inhibitors are irreversibly inactivated at temperature T.sub.2 which is generally above about 40.degree. C. T.sub.2 is also greater than T.sub.1. Such inhibitors can be supplied individually or in admixture with the DNA polymerase in a diagnostic test kit suitable for PCR.

Thermostable polymerase specific antibody-containing DNA amplification

Specific binding ligands can be detected with an assay which utilizes an immobilized receptor for the ligand, a reporter enzyme, an inhibitor antibody and an anti-inhibitor antibody. Both antibodies are specific for the reporter enzyme. The inhibitor antibody effectively shuts down the activity of the reporter enzyme when it is complexed thereto. The anti-inhibitor antibody binds to the reporter enzyme, does not affect the enzymatic activity, but prevents the binding of the inhibitor enzyme. This assay provides a direct correlation of the target specific binding ligand to the signal generated without the use of separation or wash steps.

Separation-free specific binding assays using anti-inhibitor antibodies

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Rochester, NY, United States of America

John L Daiss