Overview
- Peptide (C)KEHEQLTYSSTRSK, corresponding to amino acid residues 482-495 of rat EphA6 (Accession P54758). Extracellular, N-terminus.
- Mouse and rat brain membranes; human LNCaP prostate adenocarcinoma cell lysate (1:200-1:2000).
- Western blot analysis of mouse brain membranes (lanes 1 and 3) and rat brain membranes (lanes 2 and 4):1, 2. Anti-EphA6 (extracellular) Antibody (#AER-016), (1:200).
3, 4. Anti-EphA6 (extracellular) Antibody, preincubated with EphA6 (extracellular) Blocking Peptide (#BLP-ER016).
- Rat brain sections (1:200).
- Human THP-1 monocytic leukemia cells (2.5 µg).
EphA6 is an erythropoietin-producing hepatocellular (Eph) receptor that belongs to the tyrosine kinase receptor family. The Eph receptor family consists of 9 EphA receptors and 5 EphB receptors, which serve key roles in normal physiology, including cell migration, cell adhesion, cell proliferation and neuronal synaptic plasticity. These activities depend on the binding of their Eph receptor-interacting (ephrin) proteins, of which include 8 members. Compelling data has demonstrated that Eph receptors and ephrins affect tumor growth, invasiveness, angiogenesis and metastasis1. They are also involved in brain development, learning and memory2.
EphA6 signaling pathways are inhibitory for developing axons and blocking these pathways enhances regeneration following spinal cord and brain injury; rendering EphA6 an appealing drug target3.
Eph receptors contain an extracellular structure consisting of an ephrin binding domain, the juxtamembrane region connects the extracellular portion of the receptor to the intracellular kinase domain. Two Tyrosine residues on the juxtamembrane region mediate autophosphorylation and receptor dimerization mediates the formation of heterocomplexes that are required for signaling4.