Glial-Derived Neurotrophic Factor, ATF-1
GDNF is a disulfide-linked, homodimeric neurotrophic factor structurally
related to Artemin, Neurturin and Persephin.
These proteins belong to the cysteine-knot superfamily of growth factors
that assume stable dimeric protein structures.
GDNF signals through a multicomponent receptor system, composed of a RET
and one of the four GFRα (α1-α4) receptors.
GDNF specifically promotes dopamine uptake and survival, and
morphological differentiation of midbrain neurons. Using a Parkinson’s disease mouse model, GDNF
has been shown to improve conditions such as bradykinesia, rigidity, and postural
instability. The functional murine GDNF
ligand is a disulfide-linked homodimer consisting of two 15.1 kDa polypeptide
chains called monomers. Each monomer
contains seven conserved cysteine residues, including Cys-101, which is used
for inter-chain disulfide bridging, and others that are involved in the
intramolecular ring formation known as the cysteine knot configuration. The calculated molecular weight of Recombinant Murine GDNF is 30.2 kDa.
MSPDKQAAAL PRRERNRQAA AASPENSRGK GRRGQRGKNR GCVLTAIHLN VTDLGLGYET KEELIFRYCS GSCESAETMY DKILKNLSRS RRLTSDKVGQ ACCRPVAFDD DLSFLDDNLV YHILRKHSAK RCGCI
Greater than 98% by SDS-PAGE gel and HPLC analyses.
The ED50 was determined by the proliferation of rat C6 cells is ≤ 0.2 ng/ml, corresponding to a specific activity of ≥ 5 x 106 units/mg.
Rat, Mouse, N/A
Country of Origin: