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

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

• DataSheet
• Material Safety Data Sheets (MSDS)

Ephrin-A5 also known as EFNA5, is a member of the Ephrin family. The Eph family receptor interacting proteins (ephrins) are a family of proteins that serve as the ligands of the Eph receptor, which compose the largest known subfamily of receptor protein-tyrosine kinases (RTKs). Ephrin subclasses are further distinguished by their mode of attachment to the plasma membrane: ephrin-A ligands bind EphA receptors and are anchored to the plasma membrane via a glycosylphosphatidylinositol (GPI) linkage, whereas ephrin-B ligands bind EphB receptors and are anchored via a transmembrane domain. Ephrin-A5/EFNA5 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. Ephrin-A5/EFNA5 also serves as a cognate/functional ligand for EPHA7, their interaction regulates brain development modulating cell-cell adhesion and repulsion.

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

Human Cells

A DNA sequence encoding the extracellular domain (Met 1-Asn 203) of human Ephrin-A5 (NM_001962.1) precursor was expressed with the C-terminal fused Fc region of human IgG1.

Human

The recombinant human Ephrin-A5/Fc chimera is a disulfide-linked homo-dimeric protein. The reduced monomer consists of 421 amino acids and has a calculated molecular mass of 47.9 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of the monomer is approximately 50-55 kDa due to glycosylation.

> 97 % as determined by SDS-PAGE