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REACTIVITY MW (kDa)

Figure 1. Target map of the PathScan® EGFR Signaling Antibody Array Kit (Fluorescent Readout) #12785. † A reduction in a signal associated with E746-A750 deletion mutant was observed after treatment of cells with the small molecule inhibitors Gefitinib #4765 and Erlotinib #5083.

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Figure 2. A-431 cells were grown to 90% confluency and then serum-starved overnight. Cells were stimulated with Human Epidermal Growth Factor (hEGF) #8916 (100 ng/ml, 5 min). Cell extracts were prepared and analyzed using the PathScan® EGFR Signaling Antibody Array Kit (Fluorescent Readout) #12785. Panel A shows images that were acquired using the LI-COR® Biosciences Odyssey® imaging system. Panel B shows raw values of quantified fluorescence intensity. Pixel intensity was quantified using the LI-COR® Image Studio v2.0 array analysis software.

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Figure 3. Calu-3 cells were grown to 90% confluency and lysed using a buffer containing (P) or devoid of (NP) phosphatase inhibitors. Cell extracts were prepared and analyzed using the PathScan® EGFR Signaling Antibody Array Kit (Fluorescent Readout) #12785. Panel A shows images that were acquired using the LI-COR® Biosciences Odyssey® imaging system. Panel B shows raw values of quantified fluorescence intensity for a selected set of targets. Pixel intensity was quantified using the LI-COR® Image Studio v2.0 array analysis software.

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Figure 4. HCC827 and H3255 are two non-small cell lung cancer (NSCLC) cell lines carrying two different gefitinib-sensitive mutants of EGFR: E746-A750 deletion in exon 19 and L858R point mutation, respectively. Cells were grown to 90% confluency and then lysed using a buffer containing (P) or devoid of (NP) phosphatase inhibitors. Cell extracts were prepared and analyzed using the PathScan® EGFR Signaling Antibody Array Kit (Fluorescent Readout) #12785. Images were acquired using the LI-COR® Biosciences Odyssey® imaging system. Fluorescence intensity was quantified using the LI-COR® Image Studio v2.0 array analysis software. Heatmap analysis was generated using MultiExperiment Viewer (MeV) analysis software (14) using the raw fluorescence intensity values.

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Figure 5. (A) HCC827 cells were treated with Gefitinib #4765, Erlotinib #5083, Crizotinib #4401, or Foretinib, as indicated, for 16 hours. The total amounts of EGFR (wt and mutant) or the EGFR (E746-A750) deletion mutant were quantified using the PathScan® EGFR Signaling Antibody Array Kit (Fluorescent Readout) #12785 (bar graph). The same samples were also analyzed by western blot using EGF Receptor (E746-A750del Specific) 6B6 XP® Rabbit mAb #2085 (upper) and EGF Receptor (15F8) Rabbit mAb #4405 (lower). Note: The western blot shows that sandwich immunoassay detection in the EGFR (E746-A750) deletion mutant specific assay (bar graph) may be sensitive to EGFR inhibitors targeting the active site. (B) HCC827 cells were treated with increasing concentrations of Gefitinib #4765 for 2.5 hours. Tyrosine phosphorylation levels of the indicated sites in EGFR or the EGFR (E746-A750) deletion mutant were quantified using the PathScan® EGFR Signaling Antibody Array Kit (Fluorescent Readout) #12785.

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Image
Product Includes Quantity
Array Slides - EGFR Signaling Array Kit  2 Ea
Detection Ab Cocktail A(10X) - EGFR Signaling Array Kit 150 µl
Detection Ab Cocktail B(10X) - EGFR Signaling Array Kit 150 µl
16-Well Gasket 2 Ea
Sealing Tape 2 sheets
20X Array Wash Buffer 15 ml
Array Blocking Buffer 5 ml
Array Diluent Buffer 15 ml
DyLight 680TM-linked Streptavidin (10X) 300 µl
Cell Lysis Buffer (10X) 9803 15 ml

Product Usage Information

Storage: Kit should be stored at 4°C with the exception of Lysis Buffer, which is stored at –20°C (packaged separately).

Product Description

The PathScan® EGFR Signaling Antibody Array Kit (Fluorescent Readout) uses glass slides as the planar surface and is based upon the sandwich immunoassay principle. The array kit allows for the simultaneous detection of phosphorylated EGFR, HER2, c-Met on distinct sites as well as a number of key signaling nodes found downstream of these RTKs. Target-specific capture antibodies have been spotted in duplicate onto nitrocellulose-coated glass slides. Each kit contains two slides allowing for the interrogation of 16 different samples. To improve assay performance the content of this array is split between two sub-arrays. The pads on left-hand side of each slide belong to sub-array A while the pads on the right-hand side of each slide belong to sub-array B. Cell lysates are incubated on the slide followed by a biotinylated detection antibody cocktail A or cocktail B (each cocktail for the corresponding sub-array). Streptavidin-conjugated DyLight® 680 is then used to visualize the bound detection antibody. A fluorescent image of the slide can then be captured with a digital imaging system and spot intensities quantified using array analysis software.


Specificity / Sensitivity

PathScan® EGFR Signaling Antibody Array Kit (Fluorescent Readout) detects the target proteins as specified on the Array Target Map. No substantial cross-reactivity has been observed between targets. This kit is optimized for cell lysates diluted to a total protein concentration between 0.2 and 1 mg/ml (see kit protocol). All capture antibodies have been validated for human and mouse-derived samples.

Note: Detection in the EGFR (E746-A750) deletion mutant specific assay may be sensitive to EGFR inhibitors targeting the active site. (See Figure 5).


The Epidermal Growth Factor Receptor (EGFR) is a receptor tyrosine kinase (RTK) that constitutes an important disease driver, as well as a validated drug target. The potency of EGFR in driving tumorigenesis can be attributed to its pleiotropic intracellular signaling. Activated EGFR initiates a wide range of signaling modules and switches such as the Ras - Erk/MAP kinase, Akt, Src, Stat, and PKC. Two of the most common EGFR mutations ocurring in lung cancer are the E746-A750 deletion and L858R point mutation. This array utilizes unique antibodies made by Cell Signaling Technology that are sensitive to each of these EGFR mutants, allowing specific target detection in cell extracts.

EGFR can interact and heterodimerize with other RTKs. HER2 (also known as ErbB2) is an oncogenic RTK belonging to the EGFR/HER family of RTKs and is an important heterodimerization partner of all HER family members. Another prominent heterodimerization partner of EGFR is c-Met. c-Met is an RTK serving as a receptor for the hepatocyte growth factor (HGF). c-Met can induce cell scattering, migration, and invasion. It has been shown that c-Met is responsible for some cases of tumor resistance to EGFR-targeted therapies and is a contributing factor to tumor metastasis.

PLCγ is a phosphoinositide-specific phospholipase. EGFR can activate PLCγ that, in turn, hydrolyzes phosphoinositide phospholipids residing within the inner leaflet of the plasma membrane. This hydrolysis generates two important second messengers: inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG). IP3 causes calcium mobilization from intracellular storage pools, while DAG (together with calcium) activates PKC. MEK1 is a dual-specificity protein kinase and serves as the MAP kinase kinase for Erk1 and Erk2. Upon EGFR activation, MEK1 is phosphorylated by Raf and, in turn, phosphorylates the Erk kinases at Thr202 and Tyr204, leading to their activation. Activated Erk MAP kinase is a major signaling node with a multitude of substrates and primarily transmits growth and proliferation signals. Akt is another important protein kinase downstream of EGFR. Akt is activated by many RTKs and has a large number of intracellular substrates. Akt generates anabolic growth and survival signals. Stat3 is activated in response to EGFR stimulation, as well as in response to activation of a variety of cytokine receptors. Stat3 is a well-established oncogene that is also a transcription factor.

The oncogenic signals generated by activated EGFR are a focus of intense drug discovery efforts. It has become clear that in many cases a single agent inhibiting only one target is unable to cause tumor cell death in vivo. To monitor the blockade of EGFR signals alongside markers of cell death, cleaved PARP is included in this array. PARP is an enzyme involved in DNA repair. As a part of the apoptotic process, PARP is irreversibly inactivated by endoproteolytic cleavage executed by activated cell death proteases, such as caspase-3 and caspasae-7.


1.  Yarden, Y. (2001) Eur J Cancer 37 Suppl 4, S3-8.

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

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

4.  Avraham, R. and Yarden, Y. (2011) Nat Rev Mol Cell Biol 12, 104-17.

5.  Levitzki, A. (2003) Lung Cancer 41 Suppl 1, S9-14.

6.  Sharma, S.V. and Settleman, J. (2009) Exp Cell Res 315, 557-71.

7.  Knowles, L.M. et al. (2009) Clin Cancer Res 15, 3740-50.

8.  Hudelist, G. et al. (2003) Breast Cancer Res Treat 80, 353-61.

9.  Engelman, J.A. et al. (2007) Science 316, 1039-43.

10.  Comoglio, P.M. (2001) Nat Cell Biol 3, E161-2.

11.  Benedettini, E. et al. (2010) Am J Pathol 177, 415-23.

12.  Guo, A. et al. (2008) Proc Natl Acad Sci U S A 105, 692-7.

13.  Klein, S. and Levitzki, A. (2009) Curr Opin Cell Biol 21, 185-93.

14.  Saeed, A.I. et al. (2003) Biotechniques 34, 374-8.


Entrez-Gene Id 207, 208, 10000, 1956, 5595, 5594, 2064, 5604, 5605, 4233, 142, 5335, 6774
Swiss-Prot Acc. P31749, P31751, Q9Y243, P00533, P27361, P28482, P04626, Q02750, P36507, P08581, P09874, P19174, P40763

Protein Specific References

Germack R and Dickenson JM (2000) Br J Pharmacol 130, 867–74

Wick MJ et al. (2000) J Biol Chem 275, 40400–6

Rane MJ et al. (2001) J Biol Chem 276, 3517–23

Guizzetti M and Costa LG (2001) Neuroreport 12, 1639–42

Brognard J et al. (2001) Cancer Res 61, 3986–97

Maira SM et al. (2001) Science 294, 374–80

Schönherr E et al. (2001) J Biol Chem 276, 40687–92

Hill MM et al. (2001) J Biol Chem 276, 25643–6

Dhawan P et al. (2002) Cancer Res 62, 7335–42

Conus NM et al. (2002) J Biol Chem 277, 38021–8

Sano H et al. (2002) J Biol Chem 277, 19439–47

Egawa K et al. (2002) J Biol Chem 277, 38863–9

Kisseleva MV et al. (2002) J Biol Chem 277, 6266–72

Barry FA and Gibbins JM (2002) J Biol Chem 277, 12874–8

Ikonomov OC et al. (2002) Endocrinology 143, 4742–54

Rani MR et al. (2002) J Biol Chem 277, 38456–61

Ho R et al. (2002) Cancer Res 62, 6462–6

Wan X and Helman LJ (2003) Oncogene 22, 8205–11

Fukuda T et al. (2003) J Biol Chem 278, 51324–33

Kim HH et al. (2003) FASEB J 17, 2163–5

Min YH et al. (2004) Cancer Res 64, 5225–31

Tazzari PL et al. (2004) Br J Haematol 126, 675–81

Matsuzaki H et al. (2004) Biochemistry 43, 4284–93

Wolfrum S et al. (2004) Arterioscler Thromb Vasc Biol 24, 1842–7

Kaneko Y et al. (2004) J Cell Sci 117, 407–15

Esfandiarei M et al. (2004) J Virol 78, 4289–98

Baudhuin LM et al. (2004) FASEB J 18, 341–3

Dietze EC et al. (2004) Oncogene 23, 3851–62

Wu T et al. (2004) Mol Cancer Ther 3, 299–307

Honjo S et al. (2005) DNA Cell Biol 24, 141–7

Karlsson HK et al. (2005) Diabetes 54, 1459–67

Viniegra JG et al. (2005) J Biol Chem 280, 4029–36

Le XF et al. (2005) J Biol Chem 280, 2092–104

Smith E and Frenkel B (2005) J Biol Chem 280, 2388–94

Edwards LA et al. (2005) Oncogene 24, 3596–605

Karlsson HK et al. (2005) Diabetes 54, 1692–7

Kippenberger S et al. (2005) J Biol Chem 280, 3060–7

Jung HS et al. (2005) Mol Endocrinol 19, 2748–59

Khundmiri SJ et al. (2006) Am J Physiol Cell Physiol 291, C1247–57

Hers I and (2007) Blood 110, 4243–52

Ananthanarayanan B et al. (2007) J Biol Chem 282, 36634–41

Zunder ER et al. (2008) Cancer Cell 14, 180–92

Grenegård M et al. (2008) J Biol Chem 283, 18493–504

Abubaker J et al. (2009) Mol Cancer 8, 51

Chen PL and Easton AS (2011) Curr Neurovasc Res 8, 14–24

Van Aller GS et al. (2011) Biochem Biophys Res Commun 406, 194–9

Uesugi A et al. (2011) Cancer Res 71, 5765–78

Ou YH et al. (2011) Mol Cell 41, 458–70

Wang S et al. (2012) PLoS One 7, e37427

Glidden EJ et al. (2012) J Biol Chem 287, 581–8

Shih MC et al. (2012) Oncogene 31, 2389–400

Misra UK and Pizzo SV (2012) J Cell Biochem 113, 1488–500

Germack R and Dickenson JM (2000) Br J Pharmacol 130, 867–74

Wick MJ et al. (2000) J Biol Chem 275, 40400–6

Rane MJ et al. (2001) J Biol Chem 276, 3517–23

Guizzetti M and Costa LG (2001) Neuroreport 12, 1639–42

Brognard J et al. (2001) Cancer Res 61, 3986–97

Maira SM et al. (2001) Science 294, 374–80

Schönherr E et al. (2001) J Biol Chem 276, 40687–92

Hill MM et al. (2001) J Biol Chem 276, 25643–6

Dhawan P et al. (2002) Cancer Res 62, 7335–42

Conus NM et al. (2002) J Biol Chem 277, 38021–8

Sano H et al. (2002) J Biol Chem 277, 19439–47

Egawa K et al. (2002) J Biol Chem 277, 38863–9

Kisseleva MV et al. (2002) J Biol Chem 277, 6266–72

Barry FA and Gibbins JM (2002) J Biol Chem 277, 12874–8

Ikonomov OC et al. (2002) Endocrinology 143, 4742–54

Rani MR et al. (2002) J Biol Chem 277, 38456–61

Ho R et al. (2002) Cancer Res 62, 6462–6

Wan X and Helman LJ (2003) Oncogene 22, 8205–11

Fukuda T et al. (2003) J Biol Chem 278, 51324–33

Kim HH et al. (2003) FASEB J 17, 2163–5

Min YH et al. (2004) Cancer Res 64, 5225–31

Tazzari PL et al. (2004) Br J Haematol 126, 675–81

Matsuzaki H et al. (2004) Biochemistry 43, 4284–93

Wolfrum S et al. (2004) Arterioscler Thromb Vasc Biol 24, 1842–7

Kaneko Y et al. (2004) J Cell Sci 117, 407–15

Esfandiarei M et al. (2004) J Virol 78, 4289–98

Baudhuin LM et al. (2004) FASEB J 18, 341–3

Dietze EC et al. (2004) Oncogene 23, 3851–62

Wu T et al. (2004) Mol Cancer Ther 3, 299–307

Honjo S et al. (2005) DNA Cell Biol 24, 141–7

Karlsson HK et al. (2005) Diabetes 54, 1459–67

Viniegra JG et al. (2005) J Biol Chem 280, 4029–36

Le XF et al. (2005) J Biol Chem 280, 2092–104

Smith E and Frenkel B (2005) J Biol Chem 280, 2388–94

Edwards LA et al. (2005) Oncogene 24, 3596–605

Karlsson HK et al. (2005) Diabetes 54, 1692–7

Kippenberger S et al. (2005) J Biol Chem 280, 3060–7

Jung HS et al. (2005) Mol Endocrinol 19, 2748–59

Khundmiri SJ et al. (2006) Am J Physiol Cell Physiol 291, C1247–57

Hers I and (2007) Blood 110, 4243–52

Ananthanarayanan B et al. (2007) J Biol Chem 282, 36634–41

Zunder ER et al. (2008) Cancer Cell 14, 180–92

Grenegård M et al. (2008) J Biol Chem 283, 18493–504

Abubaker J et al. (2009) Mol Cancer 8, 51

Chen PL and Easton AS (2011) Curr Neurovasc Res 8, 14–24

Van Aller GS et al. (2011) Biochem Biophys Res Commun 406, 194–9

Uesugi A et al. (2011) Cancer Res 71, 5765–78

Ou YH et al. (2011) Mol Cell 41, 458–70

Wang S et al. (2012) PLoS One 7, e37427

Glidden EJ et al. (2012) J Biol Chem 287, 581–8

Shih MC et al. (2012) Oncogene 31, 2389–400

Misra UK and Pizzo SV (2012) J Cell Biochem 113, 1488–500

Germack R and Dickenson JM (2000) Br J Pharmacol 130, 867–74

Wick MJ et al. (2000) J Biol Chem 275, 40400–6

Rane MJ et al. (2001) J Biol Chem 276, 3517–23

Guizzetti M and Costa LG (2001) Neuroreport 12, 1639–42

Brognard J et al. (2001) Cancer Res 61, 3986–97

Maira SM et al. (2001) Science 294, 374–80

Schönherr E et al. (2001) J Biol Chem 276, 40687–92

Hill MM et al. (2001) J Biol Chem 276, 25643–6

Dhawan P et al. (2002) Cancer Res 62, 7335–42

Conus NM et al. (2002) J Biol Chem 277, 38021–8

Sano H et al. (2002) J Biol Chem 277, 19439–47

Egawa K et al. (2002) J Biol Chem 277, 38863–9

Kisseleva MV et al. (2002) J Biol Chem 277, 6266–72

Barry FA and Gibbins JM (2002) J Biol Chem 277, 12874–8

Ikonomov OC et al. (2002) Endocrinology 143, 4742–54

Rani MR et al. (2002) J Biol Chem 277, 38456–61

Ho R et al. (2002) Cancer Res 62, 6462–6

Wan X and Helman LJ (2003) Oncogene 22, 8205–11

Fukuda T et al. (2003) J Biol Chem 278, 51324–33

Kim HH et al. (2003) FASEB J 17, 2163–5

Min YH et al. (2004) Cancer Res 64, 5225–31

Tazzari PL et al. (2004) Br J Haematol 126, 675–81

Matsuzaki H et al. (2004) Biochemistry 43, 4284–93

Wolfrum S et al. (2004) Arterioscler Thromb Vasc Biol 24, 1842–7

Kaneko Y et al. (2004) J Cell Sci 117, 407–15

Esfandiarei M et al. (2004) J Virol 78, 4289–98

Baudhuin LM et al. (2004) FASEB J 18, 341–3

Dietze EC et al. (2004) Oncogene 23, 3851–62

Wu T et al. (2004) Mol Cancer Ther 3, 299–307

Honjo S et al. (2005) DNA Cell Biol 24, 141–7

Karlsson HK et al. (2005) Diabetes 54, 1459–67

Viniegra JG et al. (2005) J Biol Chem 280, 4029–36

Le XF et al. (2005) J Biol Chem 280, 2092–104

Smith E and Frenkel B (2005) J Biol Chem 280, 2388–94

Edwards LA et al. (2005) Oncogene 24, 3596–605

Karlsson HK et al. (2005) Diabetes 54, 1692–7

Kippenberger S et al. (2005) J Biol Chem 280, 3060–7

Jung HS et al. (2005) Mol Endocrinol 19, 2748–59

Khundmiri SJ et al. (2006) Am J Physiol Cell Physiol 291, C1247–57

Hers I and (2007) Blood 110, 4243–52

Ananthanarayanan B et al. (2007) J Biol Chem 282, 36634–41

Zunder ER et al. (2008) Cancer Cell 14, 180–92

Grenegård M et al. (2008) J Biol Chem 283, 18493–504

Abubaker J et al. (2009) Mol Cancer 8, 51

Chen PL and Easton AS (2011) Curr Neurovasc Res 8, 14–24

Van Aller GS et al. (2011) Biochem Biophys Res Commun 406, 194–9

Uesugi A et al. (2011) Cancer Res 71, 5765–78

Ou YH et al. (2011) Mol Cell 41, 458–70

Wang S et al. (2012) PLoS One 7, e37427

Glidden EJ et al. (2012) J Biol Chem 287, 581–8

Shih MC et al. (2012) Oncogene 31, 2389–400

Misra UK and Pizzo SV (2012) J Cell Biochem 113, 1488–500

Johnson AL et al. (2001) Biol Reprod 64, 1566–74

Zhang M and Riedel H (2009) J Cell Biochem 107, 65–75

Johnson AL et al. (2001) Biol Reprod 64, 1566–74

Zhang M and Riedel H (2009) J Cell Biochem 107, 65–75

Johnson AL et al. (2001) Biol Reprod 64, 1566–74

Zhang M and Riedel H (2009) J Cell Biochem 107, 65–75

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

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

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