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E8027 Sigma

EphA2/Fc Chimera from mouse

>95% (SDS-PAGE), recombinant, expressed in NSO cells, lyophilized powder

Synonym: Eck, Myk2, Sek



Related Categories Angiogenesis, Application Index, Biochemicals and Reagents, Cancer Research, Cell Biology,
recombinant   expressed in NSO cells
assay   >95% (SDS-PAGE)
form   lyophilized powder
mol wt   monomer calculated mol wt 84 kDa
  mol wt ~105 kDa by SDS-PAGE (reducing)
impurities   endotoxin, tested
storage temp.   −20°C
Gene Information   mouse ... Epha2(13836)


Analysis Note

The biological activity is measured by its ability to bind recombinant mouse ephrin-A1/Fc in an ELISA assay.

Biochem/physiol Actions

Member of the Eph receptor tyrosine kinase family shown to bind ephrin-A1, ephrin-A2, ephrin-A3, ephrin-A4, and ephrin-A5; involved in pattern formation and morphogenesis. EphA2 is expressed on endothelial cells and in tumor xenographs and may regulate tumor neovascularization.

EPHA2 binds to the ephrin-A ligand and has diverse cellular function. EPHA2 has been shown to be an oncoprotein of importance in a range of cancers. EPHA2 is overexpressed in several human cancer types and promotes malignancy through a mechanism involving RhoA-dependent destabilization of adherens junctions. EPHA2 overexpression induces a FAK-dependent increase in MMP-2 expression and invasiveness and this process that can be reversed by ligation of EPHA2.

Other Notes

Extracellular domain of mouse EphA2 (amino acids 1-535) fused by means of a polypeptide linker to the Fc region of human IgG1 that is histidine-tagged at the C-terminus.

Physical form

Lyophilized from a 0.2 μm filtered solution in 20 mM Tris, pH 8.0.

General description

EPHA2 (ephrin receptor A2) belongs to the Eph family of receptor tyrosine kinases. It is a type I transmembrane protein, and its exoplasmic domain consists of a ligand binding domain in its N-terminal, a cysteine-rich domain, and two fibronectin type III repeats. Its cytoplasmic domain contains a juxtamembrane region, a tyrosine kinase domain, a SAM (sterile-a-motif) motif, and a PDZ-binding domain.

Price and Availability

All labs need water

Biomedical Applications
Safety & Documentation

Safety Information

NONH for all modes of transport
WGK Germany 


Certificate of Analysis

Certificate of Origin

Protocols & Articles
Peer-Reviewed Papers


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