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Phospho-EGF Receptor (Tyr1068) (1H12) Mouse mAb (Sepharose® Bead Conjugate) #6625
This product is discontinued
Gallery: Phospho-EGF Receptor (Tyr1068) (1H12) Mouse mAb (Sepharose® Bead Conjugate) #6625
Phospho-EGF Receptor (Tyr1068) (1H12) Mouse mAb (Sepharose® Bead Conjugate) detects endogenous levels of EGF receptor only when phosphorylated at Tyr1068. This antibody does not recognize EGF receptor phosphorylated at other sites, but may cross-react with other activated ErbB family members.
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1068 of human EGF receptor.
This Cell Signaling Technology antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated Sepharose® beads. Phospho-EGF Receptor (Tyr1068) (1H12) Mouse mAb (Sepharose® Bead Conjugate) is useful for the immunoprecipitation of EGF receptor that is phosphorylated at Tyr1068. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-EGF Receptor (Tyr1068) (1H12) Mouse mAb #2236.
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).
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