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Recombinant human GDNF protein

Glial Cell Line-Derived Neurotrophic Factor
Human Glial-Derived Neurotrophic Factor, Recombinant, E. coli
Cat #: G-240
Alternative Name Glial Cell Line-Derived Neurotrophic Factor
Lyophilized Powder yes
  • Bioassay Tested
  • Sterile & Endotoxin Free yes
    Origin Recombinant, E. coli
    MW: 30.1 kDa.
    Endotoxin Level <0.1 EU per 1 µg of the protein by the LAL method.
    Purity: >98% (HPLC)
    Form Lyophilized from a 0.2 µm filtered solution.
    Sequence MSPDKQMAVLPRRERNRQAAAANPENSRGKGRRGQRGKNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCDAAETTYDKILKNLSRNRRLVSDKVGQACCRPIAFDDDLSFLDDNLVYHILRKHSAKRCGCI.
    Structure
    Activity GDNF enhances survival and differentiation of dopaminergic neurons. It is also a potent survival factor for motor neurons1-3.
    References-Activity
    1. Lin, L.F. et al. (1993) Science 260, 1130.
    2. Lin, L.F. et al. (1994) J. Neurochem63, 758.
    3. Henderson, C.E. et al. (1995) Science 266, 1062.
    Shipping and storage Shipped at room temperature. Product as supplied can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.
    Solubility Sterile water at a concentration of at least 1 µg/0.1 ml.
    Centrifuge all product preparations before use (10000 x g 5 min). Repeated freezing/thawing might result in loss of activity.
    Storage of solutions Up to one week at 4°C or four-six weeks at -70°C.
    Our bioassay
    • Alomone Labs Recombinant human GDNF protein induces PKB (Akt) and ERK1/2 MAPK activation in SH-SY5Y cells.
      Alomone Labs Recombinant human GDNF protein induces PKB (Akt) and ERK1/2 MAPK activation in SH-SY5Y cells.
      Cells were serum starved for 2 h and then stimulated with various concentrations of Recombinant human GDNF protein (#G-240) for 10 min. Cell proteins were resolved by SDS-PAGE and probed with anti-phospho(Ser473)-Akt (upper panel) and anti-phospho-ERK1/2 (lower panel).
    References - Scientific background
    1. Airaksinen, M.S. Saarma, M. (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. and Matsuoka, I. (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. and Gash, D.M. (1998) J. Neurol. 245, P35.
    Scientific background

    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 proto-oncogene and one of the four α1-α4 receptors.1

    GDNF promotes survival of various neuronal cells, including motoneurons,2,3 Purkinje cells and sympathetic neurons.4 In embryonic midbrain cultures, GDNF promotes the survival and morphological differentiation of dopaminergic neurons and increases their high-affinity dopamine uptake.5 Cells that express GDNF include Sertoli cells, type 1 astrocytes, Schwann cells,6 neurons, pinealocytes, and skeletal muscle cells.7

    In vivo, following transection of facial motor neuron axons, locally applied GDNF has been shown to rescue virtually all damaged neurons from cell death.8 GDNF may be of clinical relevance in the treatment of Parkinson's disease that is characterized by progressive degeneration of midbrain dopaminergic neurons.9,10

    Net Peptide Content: 100%
    Last update: 15/10/2020

    Recombinant human GDNF protein (#G-240) is a highly pure, recombinant, and biologically active protein.

    For research purposes only, not for human use

    Applications

    Specifications

    Scientific Background

    Citations

    Citations
    Product citations
    1. Joyce, P.I. et al. (2016) Hum. Mol. Genet. 25, 291.
    2. Murakami, K. et al. (2015) Neuroscience 300, 338.
    3. Zahavi, E.E. et al. (2015) J. Cell Sci. 128, 1241.
    4. Zhai, J. et al. (2015) J. Neurosci. 35, 9088.
    5. Kelly, C.E. et al. (2013) PLoS ONE 11, e1001538.
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