Anti-EGFR (N-terminal region) Antibody

The epidermal growth factor receptor (EGFR) is a transmembrane glycoprotein with an extracellular ligand-binding domain and a cytoplasmic domain with intrinsic tyrosine kinase activity. The cytoplasmic domain has a C-terminal region with multiple autophosphorylation sites (Tyr-992, 1068, 1086, 1148, and 1173) . These sites are important for downstream signaling and rapid internalization. In addition, EGFR activation leads to c-Src mediated phosphorylation of Tyr-845 and Tyr-1101. The former site is required for mitogenic responses to EGFR activation, while the latter may be an SH2 binding site. Phosphorylation of EGFR on serine and threonine residues is thought to represent a mechanism for regulation of receptor kinase activity and internalization. These sites include a PKC site (Thr-654), CAMKII sites (Ser-1046, 1047, 1057, and 1142), and constitutively phosphorylated sites (Ser-967 and Ser-1002) . Thus, the regulation of EGFR activity involves a complex series of phosphorylation events at multiple sites throughout the intracellular portion of the receptor.

Our EGFR (N-terminal region) rabbit polyclonal primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat EGFR (N-terminal region) and is antigen affinity purified. It is great for use in WB, ICC.

EGFR synthetic peptide (coupled to KLH) corresponding to amino acid residues from the N-terminal region of human EGFR (ErbB-1) . This human EGFR sequence has high homology to rat and mouse EGFR, and low homology to other ErbB family members.

For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.