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Order Information
Key Product Details
Source: | NS0 |
Accession #: | P39905 |
Structure / Form: | Disulfide-linked homodimer |
Applications: | Binding Activity, Bioactivity |
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Product Specifications
Source |
Mouse myeloma cell line, NS0-derived human GDNF protein Arg109-Ile211 Manufactured and tested under cGMP guidelines. |
Purity | >97%, by SDS-PAGE with silver staining, under reducing conditions. |
Endotoxin level | <1.0 EU per 1 μg of the protein by the LAL method. |
N-terminal sequence Analysis | Arg109-Gly-Gln-Arg-Gly-Lys-Asn-Arg-Gly-(Cys) |
Predicted Molecular Mass | 11.6 kDa (monomer) |
Activity |
Measured in a cell proliferation assay using SH‑SY5Y human neuroblastoma cells. The ED50 for this effect is 2-12 ng/mL in the presence of Recombinant Human GFR alpha ‑1/GDNF R alpha ‑1 Fc Chimera (Catalog # 714-GR). The specific activity of recombinant human GDNF is >5.0 x 105 units/mg, which is calibrated against the human GDNF Reference Standard (NIBSC code: 09/266). Measured by its binding ability in a functional ELISA. Immobilized Recombinant Human GFR alpha ‑1/GDNF R alpha ‑1 Fc Chimera (Catalog # 714-GR) at 1 µg/mL can bind Recombinant Human GDNF with an apparent Kd <1 nM. |
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Recombinant Human GDNF GMP Protein Bioactivity GMP-grade Recombinant Human GDNF (Catalog # 212-GMP) stimulates proliferation in the SH-SY5Y human neuroblastoma cell line. The ED50for this effect is 2-12 ng/mL in the presence of Recombinant Human GFRa-1/GDNF Ra-1 Fc Chimera (Catalog # 714-GR). |
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Recombinant Human GDNF GMP Protein SDS-PAGE 1 μg/lane of GMP-grade Recombinant Human GDNF (Catalog # 212-GMP) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing bands at 17 kDa and 33 kDa, respectively. |
Formulation, Preparation and Storage
Carrier Free
What does CF mean?CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
What formulation is right for me?In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 μg/mL in PBS. |
Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Background: GDNF
Native GDNF, a disulfide-linked homodimeric glycoprotein, is a novel member of the TGF-beta superfamily. Human GDNF cDNA encodes a 211 amino acid residue prepropeptide that is processed to yield a dimeric protein. Mature human GDNF was predicted to contain two 134 amino acid residue subunits. NS0 expressed mature human GDNF lacks 31 residues from the amino-terminus of the predicted sequence. This glycosylated recombinant mature human GDNF still contains the seven conserved Cys residues found in all members of the TGF-beta superfamily and is biologically active. The GDNF sequence contains two potential glycosylation sites and insect cell‑expressed recombinant rat GDNF proteins are glycosylated. Mature rat and human GDNF exhibit approximately 93% amino acid sequence identity and show considerable species cross-reactivity. Cells known to express GDNF include Sertoli cells, type 1 astrocytes, Schwann cells, neurons, pinealocytes and skeletal muscle cells.
Item | Value |
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Long Name | Glial Cell line-derived Growth Factor |
Entrez Gene IDs | 2668 (Human); 25453 (Rat) |
Alternate Names | ATF, ATF1, ATF2, Astrocyte-derived trophic factor, GDNF, HFB1-GDNF, HGDNF, HSCR3, glial cell derived neurotrophic factor, glial cell line derived neurotrophic factor, glial cell line-derived neurotrophic factor |
Citations
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