Recombinant Human EphA1 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human EphA1 Fc Chimera is coated at 2 μg/mL (100 μL/well), the concentration of Biotinylayed Recombinant Mouse Ephrin‑A1 Fc Chimera (Catalog # BT602) that produces 50% of the optimal binding response is typically 10-50 ng/mL.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<0.01 EU per 1 μg of the protein by the LAL method.
83.5 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
100-110 kDa, reducing conditions
Read Publication using 7146-A1 in the following applications:
EphA1, also known as Eph and Esk, is a 120‑130 kDa glycosylated member of the Eph family of transmembrane receptor tyrosine kinases. The A and B classes of Eph proteins are distinguished by Ephrin ligand binding preference but have a common structural organization. Eph‑Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression (1‑3). Mature mouse EphA1 consists of a 524 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 408 aa cytoplasmic domain. The ECD contains an N-terminal globular domain, a cysteine-rich domain, and two fibronectin type III domains. The cytoplasmic domain contains a juxtamembrane motif with two tyrosine residues which are the major autophosphorylation sites, a kinase domain, and a conserved sterile alpha motif (SAM) (4). Within the ECD, human EphA1 shares 84% aa sequence identity with mouse and rat EphA1. EphA1 can form pH sensitive cis-homodimers on the cell surface (5). Membrane-bound or clustered Ephrin ligands interact with EphA1 and activate its kinase domain which is capable of Ser, Thr, and Tyr phosphorylation (6). Reverse signaling is propagated through the Ephrin ligand (7). EphA1 is widely expressed in differentiated epithelial cells, particularly in bone marrow, spleen, thymus, and testes (6, 8). It is additionally expressed on CD4+ T cells and a subpopulation of CD19+ B cells (9, 10). On CD4+ T cells, EphA1 interacts with EphA4, induces Tyr phosphorylation of PYK2, and promotes chemokine-induced chemotaxis (9, 10). EphA1 is up‑regulated or down‑regulated in a variety of human carcinomas and is implicated in tumor invasiveness (3, 7, 11). The region of Fibronectin including type I repeats #10‑12 interacts with EphA1, and this interaction plays a role in VEGF-dependent in vitro angiogenesis (12).
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