The egl-15 antibody is a polyclonal antibody designed to detect EGL-15, the sole FGFR homolog in C. elegans. EGL-15 exists in two major isoforms (5A and 5B) generated by alternative splicing, which differ in their extracellular domains and functions . The antibody recognizes specific epitopes within the receptor:
Crackle antibody: Targets the carboxy-terminal domain of EGL-15 .
Pop antibody: Binds to the acid box region in the extracellular domain .
The antibody has been used to:
Identify EGL-15 isoforms: Western blotting reveals four distinct EGL-15 polypeptides (∼105, 95, 85, and 75 kDa), corresponding to differentially glycosylated forms or splice variants .
Study receptor localization: Immunostaining in C. elegans tissues, including the hypodermis and sex myoblasts .
Investigate protein degradation: EGL-15 activation via the Ras-MAPK pathway triggers proteolysis in muscle cells, a process validated using antibody-based assays .
Protein degradation: Hyperactivation of EGL-15 (via clr-1 mutations) induces muscle proteolysis through the GRB2/Ras/MAPK pathway .
Heparin binding: EGL-15 binds heparin in vitro, with the 105-kDa isoform showing highest affinity .
EGL-15 antibody has elucidated mechanisms such as: