EphA4 was detected in immersion fixed frozen sections of embryonic rat rib cartilage primordium (E15) using 5 µg/mL Goat Anti-Mouse EphA4 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF641) ...read more
Detects mouse EphA4 in direct ELISAs and Western blots. In direct ELISAs, approximately 50% cross-reactivity with recombinant human EphA4 is observed, and less than 5% cross-reactivity with recombinant mouse (rm) EphA3, rmEphA6, rmEphA7, and rmEphA8 is observed.
Immunogen affinity purified
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Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.
Immunogen affinity purified
Reconstitute at 0.2 mg/mL in sterile PBS.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for EphA4 Antibody
EPH receptor A4
EPH-like kinase 8
ephrin type-A receptor 4
receptor protein-tyrosine kinase HEK8
TYRO1 protein tyrosine kinase
Tyrosine-protein kinase receptor SEK
Tyrosine-protein kinase TYRO1
EphA4, also known as Sek, Sek1, Cek8, Hek8, and Tyro1 (1), is a member of the Eph receptor family which binds members of the ephrin ligand family. There are two classes of receptors, designated A and B. Both the A and B class receptors have an extracellular region consisting of a globular domain, a cysteine-rich domain, and two fibronectin type III domains. This is followed by the transmembrane region and cytoplasmic region. The cytoplasmic region contains a juxtamembrane motif with two tyrosine residues, which are the major autophosphorylation sites, a kinase domain, and a conserved sterile alpha motif (SAM) in the carboxy tail which contains one conserved tyrosine residue. Activation of kinase activity occurs after ligand recognition and binding. EphA4 has been shown to bind ephrin-A5, ephrin-A1, ephrin‑A3, ephrin-A2, ephrin-B2, ephrin-B3, and ephrin-A4 (2, 3). The extracellular domains of mouse and human EphA4 share greater than 95% amino acid identity. Only membrane-bound or Fc-clustered ligands are capable of activating the receptor in vitro. While soluble monomeric ligands bind the receptor, they do not induce receptor autophosphorylation and activation (2). In vivo, the ligands and receptors display reciprocal expression (3). It has been found that nearly all receptors and ligands are expressed in developing and adult neural tissue (3). The Eph/ephrin families also appear to play a role in angiogenesis (3).
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