Monoclonal antibodies to the amino-terminal sequence of the c-yes gene product as specific probes of its expression

Jun Sukegawa, Toshitaka Akatsuka, Isamu Sugawara, Shigeo Mori, Tadashi Yamamoto, Kumao Toyoshima

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)611-614
Number of pages4
JournalOncogene
Volume5
Issue number4
Publication statusPublished - 1990 Apr

ASJC Scopus subject areas

  • Molecular Biology
  • Cancer Research
  • Genetics

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