Cell Signaling Technology
XP Monoclonal Antibody

Product Pathways - Tyrosine Kinase / Adaptors

EphA2 (D4A2) XP® Rabbit mAb #6997

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP IF-IC H M R Mk Endogenous 125 Rabbit IgG

Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IF-IC=Immunofluorescence (Immunocytochemistry)
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

EphA2 (D4A2) XP® Rabbit mAb recognizes endogenous levels of total EphA2 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the amino terminus of human EphA2 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using EphA2 (D4A2) XP® Rabbit mAb

IF-IC

IF-IC

Confocal immunofluorescent analysis of A549 cells (left) and SK-MEL-28 cells (right) using EphA2 (D4A2) XP® Rabbit mAb (green). Blue pseudocolor = DRAQ5® #4084 (fluorescent DNA dye).

Background

The Eph receptors are the largest known family of receptor tyrosine kinases (RTKs). They can be divided into two groups based on sequence similarity and on their preference for a subset of ligands: EphA receptors bind to a glycosylphosphatidylinositol-anchored ephrin A ligand; EphB receptors bind to ephrin B proteins that have a transmembrane and cytoplasmic domain (1,2). Research studies have shown that Eph receptors and ligands may be involved in many diseases including cancer (3). Both ephrin A and B ligands have dual functions. As RTK ligands, ephrins stimulate the kinase activity of Eph receptors and activate signaling pathways in receptor-expressing cells. The ephrin extracellular domain is sufficient for this function as long as it is clustered (4). The second function of ephrins has been described as "reverse signaling", whereby the cytoplasmic domain becomes tyrosine phosphorylated, allowing interactions with other proteins that may activate signaling pathways in the ligand-expressing cells (5). Various stimuli can induce tyrosine phosphorylation of ephrin B, including binding to EphB receptors, activation of Src kinase, and stimulation by PDGF and FGF (6). Tyr324 and Tyr327 have been identified as major phosphorylation sites of ephrin B1 in vivo (7).

EphA2 is overexpressed in various tumor cells, and it has been suggested that EphA2 may promote malignancy. However, several studies demonstrate that EphA2 plays an important role in tumor suppression (8). The role of EphA2 in tumor development may depend upon regulation of its tyrosine kinase activity.

  1. Wilkinson, D.G. (2000) Int. Rev. Cytol. 196, 177-244.
  2. Klein, R. (2001) Curr. Opin. Cell Biol. 13, 196-203.
  3. Dodelet, V.C. and Pasquale, E.B. (2000) Oncogene 19, 5614-5619.
  4. Holder, N. and Klein, R. (1999) Development 126, 2033-2044.
  5. Brückner, K. et al. (1997) Science 275, 1640-1643.
  6. Palmer, A. et al. (2002) Mol. Cell 9, 725-737.
  7. Kalo, M.S. et al. (2001) J. Biol. Chem. 276, 38940-38948.
  8. Guo, H. et al. (2006) Cancer Res 66, 7050-7058.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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