Phospho-EphA2 (Ser897) (D9A1) Rabbit mAb #6347
- WB
- IP
- IHC
Supporting Data
| REACTIVITY | H M |
| SENSITIVITY | Endogenous |
| MW (kDa) | 125 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Immunohistochemistry (Paraffin) | 1:8000 |
Storage
For a carrier free (BSA and azide free) version of this product see product #16662.
Protocol
Specificity / Sensitivity
Phospho-EphA2 (Ser897) (D9A1) Rabbit mAb recognizes endogenous levels of EphA2 protein only when phosphorylated at Ser897.
Species Reactivity:
Human, Mouse
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser897 of human EphA2 protein.
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).
It has been demonstrated that ligand-independent promotion of cell migration by EphA2 overexpression requires phosphorylation of EphA2 at Ser897 by Akt. On the other hand, stimulation of EphA2 by its ligand Ephrin-A1 negates Akt activation by growth factors and causes EphA2 dephosphorylation at Ser897 (8).
- Wilkinson, D.G. (2000) Int Rev Cytol 196, 177-244.
- Klein, R. (2001) Curr Opin Cell Biol 13, 196-203.
- Dodelet, V.C. and Pasquale, E.B. (2000) Oncogene 19, 5614-9.
- Holder, N. and Klein, R. (1999) Development 126, 2033-44.
- Brückner, K. et al. (1997) Science 275, 1640-3.
- Palmer, A. et al. (2002) Mol Cell 9, 725-37.
- Kalo, M.S. et al. (2001) J Biol Chem 276, 38940-8.
- Miao, H. et al. (2009) Cancer Cell 16, 9-20.
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