Serial dilutions of Human GDNF Recombinant Protein were added to C6 cells. Cell proliferation was measured and the linear portion of the curve was used to calculate the ED50.
The purity of Human GDNF Recombinant Protein was determined by SDS-PAGE of 1 µg reduced (+) and non-reduced (-) recombinant hGDNF and staining with Coomassie Blue. hGDNF is a disulfide-linked homodimer with a predicted total molecular weight (MW) of 30.4 kDa with each subunit equaling 15.2 kDa.
Human GDNF Recombinant Protein is supplied as lyophilized material that is very stable at -20°C. It is recommended to reconstitute with sterile water at a concentration of 0.1 mg/ml which can be further diluted in aqueous solutions as needed. Addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage.
A greater than or equal to 95% purity was determined by SDS-PAGE.
Endotoxin levels are less than or equal to 1 EU / 1 μg hGDNF.
The bioactivity of recombinant hGDNF was determined in a C6 cell proliferation assay. The ED50 of each lot is less than or equal to 3 μg/ml.
Recombinant human GDNF was expressed in E. coli and is supplied in a lyophilized form.
Glial cell-derived neurotrophic factor (GDNF) plays an important role in the development and maintenance of the central and peripheral nervous system, renal morphogenesis, and spermatogenesis (1). This glycosylated, disulfide-bonded homodimer is a member of the TGF-β superfamily and plays an important role in neuronal survival (2). GDNF and the related GDNF family of ligands (GFLs) neurturin, persephin, and artemin bind to the GDNF family receptor α (GFRα) proteins that signal through the Ret receptor tyrosine kinase (3,4). The effect that GDNF has on degenerating dopamine neurons makes it an important growth factor when studying Parkinson’s disease (PD) (5).
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