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Phospho-EphA2(S897) Antibody
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, DB, E |
|---|---|
| Primary Accession | P29317 |
| Other Accession | Q03145, Q1KL86 |
| Reactivity | Human |
| Predicted | Monkey, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 108266 Da |
| Gene ID | 1969 |
|---|---|
| Other Names | Ephrin type-A receptor 2, Epithelial cell kinase, Tyrosine-protein kinase receptor ECK, EPHA2, ECK |
| Target/Specificity | This EphA2 Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding S897 of human EphA2. |
| Dilution | WB~~1:1000 DB~~1:500 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Phospho-EphA2(S897) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | EPHA2 |
|---|---|
| Synonyms | ECK |
| Function | Receptor tyrosine kinase which binds promiscuously membrane- bound ephrin-A family ligands residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Activated by the ligand ephrin- A1/EFNA1 regulates migration, integrin-mediated adhesion, proliferation and differentiation of cells. Regulates cell adhesion and differentiation through DSG1/desmoglein-1 and inhibition of the ERK1/ERK2 (MAPK3/MAPK1, respectively) signaling pathway. May also participate in UV radiation-induced apoptosis and have a ligand- independent stimulatory effect on chemotactic cell migration. During development, may function in distinctive aspects of pattern formation and subsequently in development of several fetal tissues. Involved for instance in angiogenesis, in early hindbrain development and epithelial proliferation and branching morphogenesis during mammary gland development. Engaged by the ligand ephrin-A5/EFNA5 may regulate lens fiber cells shape and interactions and be important for lens transparency development and maintenance. With ephrin-A2/EFNA2 may play a role in bone remodeling through regulation of osteoclastogenesis and osteoblastogenesis. |
| Cellular Location | Cell membrane; Single-pass type I membrane protein. Cell projection, ruffle membrane; Single-pass type I membrane protein. Cell projection, lamellipodium membrane; Single-pass type I membrane protein. Cell junction, focal adhesion. Note=Present at regions of cell-cell contacts but also at the leading edge of migrating cells (PubMed:19573808, PubMed:20861311). Relocates from the plasma membrane to the cytoplasmic and perinuclear regions in cancer cells (PubMed:18794797). |
| Tissue Location | Expressed in brain and glioma tissue and glioma cell lines (at protein level). Expressed most highly in tissues that contain a high proportion of epithelial cells, e.g. skin, intestine, lung, and ovary. |
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Provided below are standard protocols that you may find useful for product applications.
Background
EphA2 belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. This gene encodes a protein that binds ephrin-A ligands.
References
Larsen, A.B., et al. Cell. Signal. 22(4):636-644(2010)
Salaita, K., et al. Science 327(5971):1380-1385(2010)
Zhuang, G., et al. Cancer Res. 70(1):299-308(2010)
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