Eps8 Mouse, Unlabeled, Clone: 15, BD

Description

• The p97 [Eps8] protein, a substrate for EGF-R tyrosine kinase, contains an SH3 domain, but lacks a functional SH2 domain
• Antibodies to Eps8 recognize the 97 kDa protein and a less abundant 68 kDa protein
• Both forms are tyrosine-phosphorylated following treatment of cells with EGF
• It is likely that p68 [Eps8] is synthesized from an alternatively spliced mRNA since two major Eps8-specific mRNAs are detected by Northern analysis
• Co-immunoprecipitation studies have demonstrated a physical association between the Eps8 protein and the EGF-R both in vivo and in vitro
• For many EGF-R substrates, this interaction is mediated through an SH2 domain of the substrate
• Since Eps8 lacks a well defined SH2 domain and a fusion protein containing the SH2-like region of Eps8 could not bind EGF-R, the mechanism of Eps8-EGF-R association remains unclear
• Overexpression of Eps8 in fibroblasts and hematopoietic cells results in an increased mitogenic response to EGF, suggesting that Eps8 has a role in the modulation of EGF-R function.