Phospho-EGF Receptor (Thr678) AntibodyProduct information
|100 µl (10 western blots)||-||Unavailable in your region|
Product Pathways - Tyrosine Kinase / Adaptors
Phospho-EGF Receptor (Thr678) Antibody #14343
|14343S||100 µl (10 western blots)||---||In Stock||---|
|14343||carrier free and custom formulation / quantity||email request|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Species predicted to react based on 100% sequence homology: Mouse, Rat, Pig.
Specificity / Sensitivity
Phospho-EGF Receptor (Thr678) Antibody recognizes endogenous levels of EGFR protein only when phosphorylated at Thr678.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phospho-peptide corresponding to residues surrounding Thr678 of human EGFR protein. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of extracts from serum-starved BT-20 cells, untreated (-) or treated with TPA #4174 (200 nM, 15 min; +), using Phospho-EGF Receptor (Thr678) Antibody (upper) and EGF Receptor (D38B1) XP® Rabbit mAb #4267 (lower).
Immunoprecipitation of phospho-EGF receptor protein from extracts of A549 cells treated with TPA #4174 (200 nM, 15 min). Lane 1 is 10% input, lane 2 is Normal Rabbit IgG #2729, and lane 3 is Phospho-EGF Receptor (Thr678) Antibody. Western blot analysis was performed using Phospho-EGF Receptor (Thr678) Antibody.
The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).
EGFR can be phosphorylated at Thr678 by PKC (11,12). Phosphorylation at this site is important for keeping internalized EGFR in recycling endosomes and away from degradation pathways (13). Phosphorylation at this site has also been shown to be required for EGFR nuclear shuttling (14).
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