Human Ephrin-A5/EFNA5 (His Tag) recombinant protein

Human Ephrin-A5/EFNA5 (His Tag) recombinant protein

• DataSheet
• Material Safety Data Sheets (MSDS)

Cell surface GPI-bound ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Induces compartmentalized signaling within a caveolae-like membrane microdomain when bound to the extracellular domain of its cognate receptor. This signaling event requires the activity of the Fyn tyrosine kinase. Activates the EPHA3 receptor to regulate cell-cell adhesion and cytoskeletal organization. With the receptor EPHA2 may regulate lens fiber cells shape and interactions and be important for lens transparency maintenance. May function actively to stimulate axon fasciculation. The interaction of EFNA5 with EPHA5 also mediates communication between pancreatic islet cells to regulate glucose-stimulated insulin secretion. Cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion.

Ephrin-A5

EPLG7; AF1; EFL-5; EPHRIN-A5; GLC1M; LERK-7; LERK7; AV158822; EFNA5; EFL5; EPL7; RAGS; AL-1

P52803

EFNA5; EPLG7; LERK7

Human Cells

A DNA sequence encoding the extracellular domain (Met 1-Asn 203) of human Ephrin-A5 (NP_001953.1) precursor was expressed with a C-terminal polyhistidine tag.

Human

The recombinant human Ephrin-A5 consists of 194 amino acids and has a calculated molecular mass of 23 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rhEphrin-A5 is approximately 27 kDa due to glycosylation.

> 90 % as determined by SDS-PAGE

Measured by its binding ability in a functional ELISA. Immobilized human EPHA5 at 20 μg/ml (100 μl/well) can bind human EFNA4 with a linear ranger of 1.28-32 ng/ml.