Product Pathways - Tyrosine Kinase / Adaptors
EGF Receptor (D38B1) XP® Rabbit mAb (Sepharose Bead Conjugate) #5735
|IP||H M Mk||Endogenous||175||Rabbit IgG|
Reactivity Key: H=Human M=Mouse Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Specificity / Sensitivity
EGF Receptor (D38B1) XP® Rabbit mAb (Sepharose Bead Conjugate) detects endogenous levels of total EGF receptor protein. The antibody does not cross-react with other proteins of the ErbB family.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a fusion protein containing the cytoplasmic domain 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. EGF Receptor (D38B1) XP® Rabbit mAb (Sepharose Bead Conjugate) is useful for immunoprecipitation assays. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated EGF Receptor (D38B1) XP® Rabbit mAb #4267.
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).
- Hackel, P.O. et al. (1999) Curr Opin Cell Biol 11, 184-9.
- Zwick, E. et al. (1999) Trends Pharmacol Sci 20, 408-12.
- Cooper, J.A. and Howell, B. (1993) Cell 73, 1051-4.
- Hubbard, S.R. et al. (1994) Nature 372, 746-54.
- Biscardi, J.S. et al. (1999) J Biol Chem 274, 8335-43.
- Emlet, D.R. et al. (1997) J Biol Chem 272, 4079-86.
- Levkowitz, G. et al. (1999) Mol Cell 4, 1029-40.
- Ettenberg, S.A. et al. (1999) Oncogene 18, 1855-66.
- Rojas, M. et al. (1996) J Biol Chem 271, 27456-61.
- Feinmesser, R.L. et al. (1999) J Biol Chem 274, 16168-73.
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