Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

Eps8 (D1X1L) Rabbit mAb #43114

No. Size Price
43114S 100 µl ( 10 western blots ) ¥3,250.00 现货查询 购买询价 防伪查询
43114 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat, Endogenous 95 Rabbit IgG
IP 1:50
IHC-P 1:100

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting, IP=Immunoprecipitation, IHC-P=Immunohistochemistry (Paraffin),

Specificity / Sensitivity

Eps8 (D1X1L) Rabbit mAb recognizes endogenous levels of total Eps8 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Arg250 of human Eps8 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using Eps8 (D1X1L) Rabbit mAb.

IP

IP

Immunoprecipitation of Eps8 protein from LoVo cell extracts. Lane 1 is 10% input, lane 2 is Rabbit (DA1E) mAb IgG XP® Isotype Control #3900, and lane 3 is Eps8 (D1X1L) Rabbit mAb. Western blot analysis was performed using Eps8 (D1X1L) Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded LoVo (left) and SH-SY5Y (right) cell pellets using Eps8 (D1X1L) Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human colon carcinoma using Eps8 (D1X1L) Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human lung carcinoma using Eps8 (D1X1L) Rabbit mAb.

IHC-P (paraffin)

IHC-P (paraffin)

Immunohistochemical analysis of paraffin-embedded human ovarian carcinoma using Eps8 (D1X1L) Rabbit mAb.

Background

Epidermal growth factor receptor pathway substrate 8 (Eps8) is an adaptor protein and can be phosphorylated by several receptor tyrosine kinases including EGFR and Src (1,2). Eps8 is composed of an N-terminal PTB domain, followed by an SH3 domain and a C-terminal effector domain. Eps8 controls actin-based motility by capping the barbed end of actin and bundling actin subunits through its C-terminal effector domain (3,4). The C-terminal α hexlical structure of Eps8 interacts directly with actin to exert these capping and bundling functions (5). The actin capping activity requires the release of Eps8 autoinhibitory binding through SH3 domain interaction with an adaptor molecule, such as Abi-1 (6). This SH3 domain of Eps8 also binds to RN-tre to regulate the down stream Rab5-mediated endocytosis pathway (6). Eps8 functions by binding several receptor tyrosine kinases, such as EGFR or FGFR, to enhance receptor mediated mitogenic Rac signaling and Rab5 endocytosis (6,7). The effector region of Eps8 is necessary for this process. By association with Abi-1 and forming the Eps8/Abi-1/Sos-1 complex, Eps8 couples initial growth factor stimulation to actin motility and the Rac activation pathway (8,9). Eps8 has been shown to be important in the cellular function of filopodial protrusions, cell migration, microvilli formation, and focal adhesion (10-13). Research studies have demonstrated that through its involvement in actin related cellular functions, Eps8 plays a role in cancer cell growth, survival, motility, and invasiveness (14-18).

  1. Fazioli, F. et al. (1993) EMBO J 12, 3799-808.
  2. Gallo, R. et al. (1997) Oncogene 15, 1929-36.
  3. Disanza, A. et al. (2004) Nat Cell Biol 6, 1180-8.
  4. Disanza, A. et al. (2006) Nat Cell Biol 8, 1337-47.
  5. Hertzog, M. et al. (2010) PLoS Biol 8, e1000387.
  6. Lanzetti, L. et al. (2000) Nature 408, 374-7.
  7. Auciello, G. et al. (2013) J Cell Sci 126, 613-24.
  8. Scita, G. et al. (1999) Nature 401, 290-3.
  9. Innocenti, M. et al. (2003) J Cell Biol 160, 17-23.
  10. Welsch, T. et al. (2007) Cancer Lett 255, 205-18.
  11. Frittoli, E. et al. (2011) Immunity 35, 388-99.
  12. Zwaenepoel, I. et al. (2012) Mol Biol Cell 23, 1080-94.
  13. Maa, M.C. et al. (2007) J Biol Chem 282, 19399-409.
  14. Xu, M. et al. (2009) Endocrinology 150, 2064-71.
  15. Chen, Y.J. et al. (2008) Mol Cancer Ther 7, 1376-85.
  16. Yap, L.F. et al. (2009) Oncogene 28, 2524-34.
  17. Chen, H. et al. (2010) Cancer Res 70, 9979-90.
  18. Funato, Y. et al. (2004) Cancer Res 64, 5237-44.

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