Recombinant Human EphA4 Protein (Fc Tag) | PKSH032385

Recombinant Human EphA4 Protein (Fc Tag) | PKSH032385 | Gentaur US, UK & Europe Disrtribition

Synonyms: Ephrin type-A receptor 4;HEK8; SEK; TYRO1;EPHA4;Tyrosine-protein kinase receptor SEK;Tyrosine-protein kinase TYRO1;EK8;hEK8;EPH-like kinase 8

Active Protein: N/A

Activity: Recombinant Human Ephrin type A receptor 4 is produced by our Mammalian expression system and the target gene encoding Val20-Thr547 is expressed with a Fc tag at the C-terminus.

Protein Construction: Recombinant Human Ephrin type A receptor 4 is produced by our Mammalian expression system and the target gene encoding Val20-Thr547 is expressed with a Fc tag at the C-terminus.

Fusion Tag: C-Fc

Species: Human

Expressed Host: Human Cells

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 85.6 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of 20mM Tris, 150mM NaCl, pH8.0.

Reconstitution: Please refer to the printed manual for detailed information.

Background: Ephrin type-A receptor 4(EPHA4) belongs to the protein kinase superfamily and Ephrin receptor subfamily. EPHA4 contains 1 Eph LBD domain; 2 fibronectin type-III domains; 1 protein kinase domain and 1 SAM domain. 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.

Research Area: Signal Transduction, Cardiovascular, Neuroscience,