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EGF Receptor (EGFR1) Mouse mAb (IP Specific) #2256
Western blot analysis of EGF Receptor (EGFR1) Mouse mAb (IP Specific) immunoprecipitated samples from Iressa-treated and untreated HCC827 cell lysates, using Phospho-EGF Receptor (Tyr1068) Antibody (#2234) (upper) and EGF Receptor Antibody (#2232) (lower).Learn more about how we got this image
Gallery: EGF Receptor (EGFR1) Mouse mAb (IP Specific) #2256
EGF Receptor (EGFR1) Mouse mAb (IP Specific) specifically immunoprecipitates endogenous EGF receptors from various cell lysates. This antibody does not cross-react with other EGF receptor family members.Species Reactivity: Human
Monoclonal antibody is produced by immunizing animals with a recombinant protein corresponding to the extracellular domain of human EGF receptor.
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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