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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
EGF Receptor (D38B1) XP® Rabbit mAb 4267 40 µl
Western Blotting Immunoprecipitation Immunohistochemistry Immunofluorescence Flow Cytometry
H M Mk 175 Rabbit IgG
Phospho-EGF Receptor (Tyr1068) (D7A5) XP® Rabbit mAb 3777 40 µl
Western Blotting Immunohistochemistry Immunofluorescence Flow Cytometry
H M R Mk 175 Rabbit IgG
Phospho-EGF Receptor (Tyr992) Antibody 2235 40 µl
Western Blotting Immunohistochemistry
H 175 Rabbit 
Phospho-EGF Receptor (Tyr1045) Antibody 2237 40 µl
Western Blotting Immunofluorescence
H R 175 Rabbit 
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
Western Blotting
All Goat 

Product Description

The Phospho-EGF Receptor Antibody Sampler Kit provides an economical means of evaluating the EGF Receptor and several phosphorylation sites that are involved in its activation. The kit contains enough primary and secondary antibodies to perform four Western blot experiments.


Specificity / Sensitivity

Each phospho-EGF Receptor antibody recognizes only the phosphorylated form of EGF Receptor at the indicated sites. The control EGF Receptor antibody recognizes both the phosphorylated and nonphosphorylated forms of EGF receptor.


Source / Purification

Antibodies are produced by immunizing animals with synthetic phosphopeptides corresponding to residues surrounding Tyr992, Tyr1045 or Tyr1068 of human EGF receptor. EGF Receptor Antibody is produced by immunizing animals with a fusion protein containing the cytoplasmic domain of human EGF receptor. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.

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

Product Specific References

Wang, X. et al. (2011) Blood 118, 1255-63.

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

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


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