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.

Format

Suggested Companion Products

Preparation and Storage

Store undiluted at -20°C.The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.

Product Notices

1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Please refer to www.bdbiosciences.com/pharmingen/protocols for technical protocols.