Anti-Phospho-EGFR (Tyr1173) Rabbit mAb

Primary Antibodies

Uncategorized

Ambient temperature

170

The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand bindingresults in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation.Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the activestate enzyme, and providing a binding surface for substrate proteins. c-Src is involved in phosphorylation of EGFR at Tyr845. The SH2 domainof PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling. Phosphorylation of EGFR at Tyr1045creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation. TheGRB2 adaptor protein binds activated EGFR at phospho-Tyr1068. A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide adocking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation. Phosphorylation of EGFR at specificserine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylatedby CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation.

PBS, Glycerol, BSA

Tyr1173