Upstream / Downstream

Explore pathways related to this product.

Antibody Guarantee

CST Antibody Performance Guarantee

LEARN MORE  

Questions?

Find answers on our FAQs page.

ANSWERS  

Visit PhosphoSitePlus®

PTM information and tools available.

LEARN MORE

Product Includes Quantity Applications Reactivity MW(kDa) Isotype
Phospho-EGF Receptor (Tyr1068) (D7A5) XP® Rabbit mAb 3777 1 x 100 µl
H M R Mk 175 Rabbit IgG
EGF Receptor (D38B1) XP® Rabbit mAb 4267 1 x 100 µl
H M Mk 175 Rabbit IgG

Product Description

PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.


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).


1.  Zwick, E. et al. (1999) Trends Pharmacol Sci 20, 408-12.

2.  Hackel, P.O. et al. (1999) Curr Opin Cell Biol 11, 184-9.

3.  Cooper, J.A. and Howell, B. (1993) Cell 73, 1051-4.

4.  Hubbard, S.R. et al. (1994) Nature 372, 746-54.

5.  Biscardi, J.S. et al. (1999) J Biol Chem 274, 8335-43.

6.  Emlet, D.R. et al. (1997) J Biol Chem 272, 4079-86.

7.  Levkowitz, G. et al. (1999) Mol Cell 4, 1029-40.

8.  Ettenberg, S.A. et al. (1999) Oncogene 18, 1855-66.

9.  Rojas, M. et al. (1996) J Biol Chem 271, 27456-61.

10.  Feinmesser, R.L. et al. (1999) J Biol Chem 274, 16168-73.


Entrez-Gene Id 1956
Swiss-Prot Acc. P00533

Protein Specific References

Heimberger AB et al. (2002) Clin Cancer Res 8, 3496–502

Chen X and Resh MD (2002) J Biol Chem 277, 49631–7

Ravid T et al. (2002) J Biol Chem 277, 31214–9

Westover EJ et al. (2003) J Biol Chem 278, 51125–33

Agazie YM and Hayman MJ (2003) Mol Cell Biol 23, 7875–86

Saito T et al. (2004) Endocrinology 145, 4232–43

Pao W et al. (2004) Proc Natl Acad Sci U S A 101, 13306–11

Mattila E et al. (2005) Nat Cell Biol 7, 78–85

Tanos B and Pendergast AM (2006) J Biol Chem 281, 32714–23

Huang F et al. (2006) Mol Cell 21, 737–48

Wu SL et al. (2006) Mol Cell Proteomics 5, 1610–27

Kannangai R et al. (2006) Mod Pathol 19, 1456–61

Sonnweber B et al. (2006) J Clin Pathol 59, 255–9

Riggins RB et al. (2006) Cancer Res 66, 7007–15

Huang F et al. (2007) Proc Natl Acad Sci U S A 104, 16904–9

Tong J et al. (2009) Mol Cell Proteomics 8, 2131–44

Goh LK et al. (2010) J Cell Biol 189, 871–83

Hall EH et al. (2011) Cell Signal 23, 1972–7

Huang WC et al. (2011) J Biol Chem 286, 20558–68

Cotton CU et al. (2013) Traffic 14, 337–54

Heimberger AB et al. (2002) Clin Cancer Res 8, 3496–502

Chen X and Resh MD (2002) J Biol Chem 277, 49631–7

Ravid T et al. (2002) J Biol Chem 277, 31214–9

Westover EJ et al. (2003) J Biol Chem 278, 51125–33

Agazie YM and Hayman MJ (2003) Mol Cell Biol 23, 7875–86

Saito T et al. (2004) Endocrinology 145, 4232–43

Pao W et al. (2004) Proc Natl Acad Sci U S A 101, 13306–11

Mattila E et al. (2005) Nat Cell Biol 7, 78–85

Tanos B and Pendergast AM (2006) J Biol Chem 281, 32714–23

Huang F et al. (2006) Mol Cell 21, 737–48

Wu SL et al. (2006) Mol Cell Proteomics 5, 1610–27

Kannangai R et al. (2006) Mod Pathol 19, 1456–61

Sonnweber B et al. (2006) J Clin Pathol 59, 255–9

Riggins RB et al. (2006) Cancer Res 66, 7007–15

Huang F et al. (2007) Proc Natl Acad Sci U S A 104, 16904–9

Tong J et al. (2009) Mol Cell Proteomics 8, 2131–44

Goh LK et al. (2010) J Cell Biol 189, 871–83

Hall EH et al. (2011) Cell Signal 23, 1972–7

Huang WC et al. (2011) J Biol Chem 286, 20558–68

Cotton CU et al. (2013) Traffic 14, 337–54


For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
PhosphoPlus® is a trademark of Cell Signaling Technology, Inc.