Laboratory Corporation of America Holdings

Monogram Biosciences, Inc.

Other

Gerald J Wallweber

Sharat Singh

John William Winslow

Tracy J Matray

Hossein Salimi-Moosavi

Jeff Sperinde

Xueguang Jin

Hrair Kirakossian

Vincent S Hernandez

Syed Hasan Tahir

Mojgan Haddad

Michael R Bates

Weidong Huang

Jodi Weidler

Po-Ying Chan-Hui

Gordon Parry

Ali Mukherjee

Gundo Diedrich

Stephen J Williams

Laurie Goodman

Jennifer W Cook

Hasan Tahir

Hrair Kirakosssian

Michael Bates

Provided are methods of detecting and quantitatively measuring protein-protein interactions between proteins present on the surface of different cells using a sensitive antibody-based assay. Antibodies specific for each target protein are either directly labeled, or are detected by labeled secondary antibodies. The antibodies are labeled with detectable tags that are releasable when the target proteins are within proximity to each other. Also provided are methods for facilitating diagnosis, prognosis, and treatment of cancer using this assay to detect protein-protein interactions between target proteins of interest. Methods of screening test agents that impact the protein-protein interaction are also provided.

Methods of assessing protein interactions between cells

The present invention relates generally to methods of accurately quantifying HER2 and/or p95 expression in subjects with a HER2 positive cancer and indicating the risk of brain relapse in such patients.

Methods for determining the likelihood of survival and for predicting likelihood of metastasis in cancer patients

Provided are methods of detecting and quantitatively measuring protein-protein interactions between proteins present on the surface of different cells using a sensitive antibody based assay. Antibodies specific for each target protein are either directly labeled, or are detected by labeled secondary antibodies. The antibodies are labeled with detectable tags that are releasable when the target proteins are within proximity to each other. Also provided are methods for facilitating diagnosis, prognosis, and treatment of cancer using this assay to detect protein-protein interactions between target proteins of interest. Methods of screening test agents that impact the protein-protein interaction are also provided.

The disclosure provides methods of making antibodies specific for p95.

Methods of producing antibodies specific for p95

Compositions, kits, and methods are disclosed for determining one or more target polypeptides in a sample where the target polypeptides have undergone a post-translational modification. The compositions can include a first reagent including a cleavage-inducing moiety and a first binding agent for a binding site that includes a post-translational modification of a target polypeptide.

Methods and compositions for analyzing proteins

Methods, compositions and kits are disclosed for determining one or more target polypeptides in a sample where the target polypeptides have undergone a post-translational modification.

Compositions for analyzing proteins

The invention provides methods of measuring and/or quantifying the presence and/or amount of p95 and/or p95 complex in a sample. The invention also provides antibodies specific for p95.

Methods and assays for measuring p95 and/or p95 complexes in a sample and antibodies specific for p95

Methods are provided for detecting the formation of complexes of molecules, especially proteins, in a sample, such as a cell or tissue lysate. In one aspect, a cleaving probe specific for a first protein in a complex and one or more binding compounds specific for one or more second proteins in a complex are provided. Upon binding, the cleaving probe is induced to generate an active species, such as singlet oxygen, that cleaves molecular tags attached to the binding compounds only in the local region of the cleaving probe. The released molecular tags are separated from the assay mixture and from one another to provide a readout that is related to the number and types of proteins present in the complex.

Detecting and profiling molecular complexes

Methods, compositions and kits are disclosed for determining one or more target polypeptides in a sample where the target polypeptides have undergone a post-translational modification. A mixture comprising the sample and a first reagent comprising a cleavage-inducing moiety and a first binding agent for a binding site on a target polypeptide is subjected to conditions under which binding of respective binding moieties occurs. The binding site is the result of post-translational modification activity involving the target polypeptide. The method may be employed to determine the target polypeptide itself. In another embodiment the presence and/or amount of the target polypeptide is related to the presence and/or amount and/or activity of an agent such as an enzyme involved in the post-translational modification of the target polypeptide. The interaction between the first binding agent and the binding site brings the cleavage-inducing moiety into close proximity to a cleavable moiety, which is associated with the polypeptide and is susceptible to cleavage only when in proximity to the cleavage-inducing moiety. In this way, an electrophoretic tag for each of the polypeptides may be released. Released electrophoretic tags are separated and the presence and/or amount of the target polypeptides are determined based on the corresponding electrophoretic tags.

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Foster City, CA, United States of America

Gerald J Wallweber