Overview
- Peptide (C)HYLTAVGMGAKVELR, corresponding to amino acid residues 333 - 347 of human EphA2 (Accession P29317). Extracellular, N-terminus.
- Rat and mouse brain membranes; human U87-MG glioblastoma, THP-1 monocytic leukemia, LNCaP prostate adenocarcinoma, and MCF-7 breast adenocarcinoma cell lysates (1:200-1:1000).
Western blot analysis of rat brain membranes (lanes 1 and 3) and mouse brain membranes (lanes 2 and 4):1, 2. Anti-EphA2 (extracellular) Antibody (#AER-019), (1:200).
3, 4. Anti-EphA2 (extracellular) Antibody, preincubated with EphA2 (extracellular) Blocking Peptide (#BLP-ER019).
- Human THP-1 monocytic leukemia cells (2.5 µg).
Erythropoietin-producing hepatocellular receptor A2 (EphA2) is a tyrosine kinase that belongs to the Ephrin (Eph) family of receptors. Members bind to cell surface-associated Ephrin ligands on neighboring cells. This binding generates bidirectional signaling which is a major form of contact-dependent communication between cells1.
Eph receptors are divided into two classes, EphA and EphB, depending on the homology of their extracellular domains. Each extracellular domain is composed of a ligand-binding domain, Sushi domain, epidermal growth factor (EGF)-like domain, and two fibronectin type-III repeats. Eph receptors also contain a transmembrane domain, juxtamembrane region, tyrosine kinase domain, sterile alpha motif (SAM) and postsynaptic density (PSD)-95 protein, Discs large, and Zona occludens tight junction protein (PDZ) domain-binding motif.
The interaction between Ephrin and the Eph receptor results in both “forward signaling” and “reverse signaling,” which are mediated by Eph receptor and Ephrin, respectively2. Forward signaling induces Eph receptor oligomer clustering, cross-phosphorylation of tyrosine residues on the juxtamembrane domain and activation loop and, consequently, activation of the kinase activity.
Eph receptor-ligand interactions mainly regulate cell proliferation and migration during development as well as tissue homeostasis, axon guidance, synapse plasticity, tissue remodeling, bone morphogenesis, and angiogenesis2.
EphA2 is expressed in normal epidermal cells and in various solid tumors, such as breast, ovary, prostate, pancreas, glioblastoma, neck, renal, lung, melanoma, bladder and other types of cancer2.
EphA2 expression in tumors is associated with a more aggressive cancer phenotype and correlates with tumor metastasis and poor patient outcome. In contrast, EphA2 also reduces cancer cell motility and proliferation and hence has both pro- and anti-oncogenic roles, depending on the cellular context3.
Due to its pivotal role in various diseases, EphA2 is an appealing drug target and research is performed in order to control its activity4.
