|Reactivity||Human, Mouse, Rat|
|Calculated MW||23720 Da|
|Homology||Rat, mouse - identical.|
|Other Names||Glial cell line-derived neurotrophic factor, hGDNF, Astrocyte-derived trophic factor, ATF, GDNF|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)PEDYPDQFDDVMD, corresponding to amino acid residues 54-66 of human GDNF (precursor) (Accession P39905). Pro-domain of the GDNF protein.The antibody is specific for the pro-domain region of GDNF and will not react with mature GDNF.|
|Peptide Confirmation||Confirmed by mass-spectrography and amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl DDW.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
Glial-Derived Neurotrophic Factor (GDNF) is a member of the TGF-β superfamily. GDNF signals through a multi-component receptor system, composed of a RET protooncogene and one of the four α1-α4 receptors1. GDNF promotes survival of various neuronal cells, including motoneurons2,3, Purkinje cells and sympathetic neurons4. In embryonic midbrain cultures, GDNF promotes the survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake5. Cells that express GDNF include Sertoli cells, type 1 astrocytes, Schwann cells6, neurons, pinealocytes, and skeletal muscle cells7. In vivo, following transection of facial motor neuron axons, locally applied GDNF has been shown to rescue virtually all damaged neurons from death8. GDNF may be of clinical relevance in the treatment of Parkinson's disease that is characterized by progressive degeneration of midbrain dopaminergic neurons9,10. Recently, it has been hypothesized that functional, carboxy-terminally amidated peptides are processed from the GDNF precursor upon proteolytic cleavage by furin-like endopeptidase11,12,13. Those different peptides (a 5-mer and 11-mer) have not been isolated endogenously to date. However, the rat 11-mer sequence (named brain excitatory peptide, BEP) significantly induced synaptic excitability and possessed some dopaminergic activities in vitro (thus named dopamine neuron stimulating peptides, DNSP)13. Furthermore, the human 11-mer sequence (named DNSP-11) exhibits neurotrophic-like properties13. Thus, the role of the full proDomain of GDNF, which is a product of proteolytic cleavage of proGDNF, is not clearly understood yet. Abgent is pleased to offer a highly specific antibody directed against the prodomain of human GDNF. Anti-proGDNF antibody (#AG1167) can be used in Western blot analysis. It has been designed to recognize proGDNF from human, mouse and rat samples.
References 1. Airaksinen, M.S. et al. (2002) Nat. Rev. Neurosci. 3, 383. 2. Henderson, C.E. et al. (1994) Science 266, 1062. 3. Houenou, L.J. et al. (1996) Cell. Tissue Res. 286, 219. 4. Kobayashi, M. et al. (2000) Neuroreport 11, 2541. 5. Tomac, A. et al. (1995) Nature 373, 335. 6. Zhou, F.Q. et al. (2003) Cell 113, 814. 7. Lin, L.F. et al. (1993) Science 260, 1130. 8. Matheson, C.R. et al. (1997) Neuroreport 8, 1739. 9. Brundin, P. (2002) Brain 125, 2149. 10. Grondin, R. et al. (1998) J. Neurol. 245, P35. 11. Bradley, L.H. et al. (2010) PLoS ONE 5, e9752. 12. Immonen, T. et al. (2008) Exp. Neurol. 210, 793. 13. Kelps, K.A. et al. (2011) Neuropeptides 45, 213.
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