An amino terminal sequence of 64 amino acid residues specific to human c-yes was expressed in E. coli as a fused molecule with a bacterial phosphate binding protein. The fused protein was used as both immunogen for mice and antigen to obtain monoclonal antibodies against the c-yes protein. Monoclonal antibodies (MAbs) from two monoclonal hybridomas (1B7: IgG2a, 3H9: IgG1) recognized human p62c-yes in blotting analyses. In addition, MAb3H9 reacted with murine p62c-yes. The p62c-yes immunoprecipitated with MAb1B7 exhibited protein tyrosine kinase and autophosphorylation activities in vitro. Immunohistochemical analysis with MAb1B7 showed that the p62c-yes expression in the kidney was confined to the proximal tubules.
|Number of pages||4|
|Publication status||Published - 1990 Apr|
ASJC Scopus subject areas
- Molecular Biology
- Cancer Research