Eck (D7) Antibodies as Cancer Diagnostic

Changes in protein tyrosine phosphorylation and cell adhesion play an important role in cancer progression. While sites of cell adhesion are the primary localization of tyrosine-phosphorylated proteins, only a few of these proteins have been identified to date.

To identify new proteins, researchers at Purdue University utilized an innovative new approach to generate monoclonal antibodies. The method selected uses tyrosine-phosphorylated proteins enriched within sites of cell adhesion in human breast cancer cells. This generated as many as 430 different antibodies specific for proteins within focal adhesions or adherens junctions. One antibody, D7, recognizes a 130kDa tyrosine phosphorylated protein found with cell-cell junctions. In vitro kinase assays with immunoprecipitated material reveal potent tyrosine kinase activity. D7 is not found within cell-cell junctions of Ras-transformed cells and is not tyrosine phosphorylated. Moreover, expression of the D7 protein is completely absent in breast cancer cells, but is expressed in some other carcinomas. Thus, the function of D7 can be regulated by changes in its phosphorylation, localization, or expression. This suggests that D7 is a tumor suppressor and a sensitive new marker for breast cancer progression.

Advantages:

-Generates as many as 430 different antibodies specific for junction proteins

-Can be used to monitor cancer progression

TRL: 4

Intellectual Property:

Keywords: Protein tyrosine phosphorylation, cell adhesion, cancer progression, monoclonal antibodies, human breast cancer cells, focal adhesions, adherens junctions, tumor suppressor, breast cancer marker, tyrosine phosphorylated protein, Antibodies, Biomarker Discovery, Biomarkers, Biotechnology, Breast Cancer, Kinases, Monoclonal Antibodies