Johnson & Johnson Clinical Diagnostics, Inc.

Kevin Matthew Gorman

John L Daiss

Carolyn R Hinchman

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

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.

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Rochester, NY, United States of America

Kevin Matthew Gorman