Recombinant Human GFR alpha-2 Fc Chimera Protein, CF

Glial cell line-derived growth factor (GDNF), neurturin (NTN), persephin (PSP) and artemin, distant members of theTGF-beta  superfamily, are neurotrophic factors for a variety of neuronal populations in the central and peripheral nervous systems. The bioactivities of GDNF and NTN are mediated through a receptor complex composed of the non ligand-binding signaling subunit (c-Ret receptor tyrosine kinase) and either of two ligand binding subunits (GDNF receptor alpha-1 [GFR alpha-1], also known as Trn R1 or GFR alpha-2, also known as Trn R2). GFR alpha-1 and -2 are members of a family of at least four cysteine-rich glycosyl-phosphatidylinositol (GPI)-linked cell surface proteins that share conserved placements of many of their cysteine residues. Binding of GDNF or NTN to membrane-associated GFR alpha-1 or GFR alpha-2 initiates the association with and activation of the Ret tyrosine kinase.

Human GFR alpha-2 cDNA encodes a 464 amino acid (aa) residue protein with a putative N-terminal 21 aa residue hydrophobic signal peptide. Like other GPI-linked proteins, human GFR alpha-2 has a C-terminal hydrophobic region which is preceded by a three aa residue (GPS) GPI-binding site. Human GFR alpha-2 shares 96.5% amino acid identity with mouse GFR alpha-2. The expression of the various GFR alphas are differentially regulated in the central and peripheral nervous system, suggesting complementary roles for the GFR alphas in mediating the activities of the GDNF family of neurotrophic factors.