EGFR, or Epidermal Growth Factor Receptor is a member of the ErbB family, a tyrosine kinase receptor known to affect cellular growth and differentiation. EGFR antibodies are widely used in cancer research, as mutations of the protein can lead to uncontrolled cell division, a precursor of tumour formation.
EGFR is activated by epidermal growth factor (EGF) and transforming growth factor α (TGFα). Binding of these protein ligands induces EGFR to switch from an inactive monomer to an active homodimer form, via autophosphorylation of several tyrosine residues, among them Tyr 992, 1045, 1068, 1148, 1173 and 1086. There is some evidence that EGFR may also bind with another member of the ErbB family to create an active heterodimer. The EGFR kinase domain can also phosphorylate the residues of other receptors it is associated with, becoming activated in this way.
Phosphorylation induces downstream signalling by the activation of several other proteins. Activity occurs following binding to appropriate phosphorylated tyrosine residues via phosphotyrosine-binding SH2 domains. For example, Tyr 992 phosphorylation induces downstream signalling by creating a binding site for the PLC-gamma (phospholipase C-gamma) SH2 domain.
EGFR downstream signalling activates a number of other proteins on our antibody database, predominantly those concerning the MAPK, Akt and JNK cascade pathways. These proteins trigger DNA synthesis and cell division, as well as modulating areas like cell adhesion, proliferation and migration. Genetic mutations in these pathways can cause tumours to form, in addition to which EGFR mutation can lead to overexpression of these proteins, leading to uncontrolled cell growth, cell migration etc.
EGFR is an oncogene known to contribute to a number of cancers, EGFR antibodies have been used to develop a number of targeted cancer therapies, including the EGFR-inhibitors Gefitinib, erlotinib, and lapatinib. We at Novus Biologicals have over 350 antibodies, proteins and peptides in our antibody catalog matching EGFR.