Recombinant Human GDNF Protein, CF

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Recombinant Human GDNF (Catalog # 212‑GD/CF) induces SH-SY5Y human neuroblastoma cell proliferation in the presence of Recombinant Human GFR alpha ‑1 Fc Chimera (Catalog # 714‑GR). The ED50 for this effect ...read more
1 ug/lane of Recombinant Human GDNF was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing single bands at 17 kDa and 34 kDa, respectively.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity, Bioactivity
Format
Carrier-Free

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Recombinant Human GDNF Protein, CF Summary

Details of Functionality
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 approximately 3.1 x 103 units/μg, which is calibrated against recombinant 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 K<1 nM.
Source
Mouse myeloma cell line, NS0-derived human GDNF protein
Arg109-Ile211
Accession #
N-terminal Sequence
Arg109
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
GDNF
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
11.6 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Publications
Read Publications using
212-GD/CF in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human GDNF Protein, CF

  • Astrocyte-derived trophic factor
  • ATF
  • ATF1
  • ATF2
  • GDNF
  • glial cell derived neurotrophic factor
  • glial cell line derived neurotrophic factor
  • glial cell line-derived neurotrophic factor
  • HFB1-GDNF
  • hGDNF
  • HSCR3

Background

Glial Cell Line-derived Neurotrophic Factor (GDNF) is a neurotrophic factor that has been shown to promote the survival of various neuronal subpopulations in both the central as well as the peripheral nervous systems at different stages of their development. Neuronal subpopulations that have been shown to be affected by GDNF include motoneurons, midbrain dopaminergic neurons, Purkinje cells and sympathetic neurons.

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.

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Publications for GDNF (212-GD/CF)(59)

We have publications tested in 9 confirmed species: Human, Mouse, Rat, Bacteria, Chicken, Guinea Pig, Porcine, Rabbit, Synthetic.

We have publications tested in 5 applications: Bioassay, Cell Culture Substrate, ELISA capture, In Vivo, Surface Plasmon Resonance.


Filter By Application
Bioassay
(54)
Cell Culture Substrate
(1)
ELISA capture
(1)
In Vivo
(2)
Surface Plasmon Resonance
(1)
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Human
(41)
Mouse
(6)
Rat
(3)
Bacteria
(1)
Chicken
(2)
Guinea Pig
(1)
Porcine
(2)
Rabbit
(1)
Synthetic
(1)
All Species
Showing Publications 1 - 10 of 59. Show All 59 Publications.
Publications using 212-GD/CF Applications Species
R Jalili, J Horecka, JR Swartz, RW Davis, HHJ Persson Streamlined circular proximity ligation assay provides high stringency and compatibility with low-affinity antibodies Proc. Natl. Acad. Sci. U.S.A., 2018;0(0):. 2018 [PMID: 29339495] (Bioassay) Bioassay
N Avaliani, U Pfisterer, A Heuer, M Parmar, M Kokaia, M Andersson Directly Converted Human Fibroblasts Mature to Neurons and Show Long-Term Survival in Adult Rodent Hippocampus Stem Cells Int, 2017;2017(0):5718608. 2017 [PMID: 29317869] (Bioassay, Human) Bioassay Human
EA Newman, S Chukkapall, D Bashllari, TT Thomas, RA Van Noord, ER Lawlor, MJ Hoenerhoff, AW Opipari, VP Opipari Alternative NHEJ pathway proteins as components of MYCN oncogenic activity in human neural crest stem cell differentiation: implications for neuroblastoma initiation Cell Death Dis, 2017;8(12):3208. 2017 [PMID: 29238067] (Bioassay, Human) Bioassay Human
O Awad, LM Panicker, RM Deranieh, MP Srikanth, RA Brown, A Voit, T Peesay, TS Park, ET Zambidis, RA Feldman Altered Differentiation Potential of Gaucher&#039;s Disease iPSC Neuronal Progenitors due to Wnt/?-Catenin Downregulation Stem Cell Reports, 2017;9(6):1853-1867. 2017 [PMID: 29198828] (Bioassay, Human) Bioassay Human
T Ruetz, U Pfisterer, B Di Stefano, J Ashmore, M Beniazza, TV Tian, DF Kaemena, L Tosti, W Tan, JR Manning, E Chantzoura, DR Ottosson, S Collombet, A Johnsson, E Cohen, K Yusa, S Linnarsson, T Graf, M Parmar, K Kaji Constitutively Active SMAD2/3 Are Broad-Scope Potentiators of Transcription-Factor-Mediated Cellular Reprogramming Cell Stem Cell, 2017;0(0):. 2017 [PMID: 29174331] (Bioassay, Human) Bioassay Human
A Taguchi, R Nishinakam Higher-Order Kidney Organogenesis from Pluripotent Stem Cells Cell Stem Cell, 2017;0(0):. 2017 [PMID: 29129523] (Bioassay, Human) Bioassay Human
M Ferreira, S Boens, C Winkler, K Szekér, I Verbinnen, A Van Eynde, M Fardilha, M Bollen The protein phosphatase 1 regulator NIPP1 is essential for mammalian spermatogenesis Sci Rep, 2017;7(1):13364. 2017 [PMID: 29042623] (Bioassay, Mouse) Bioassay Mouse
M Höllerhage, C Moebius, J Melms, WH Chiu, JN Goebel, T Chakroun, T Koeglsperg, WH Oertel, TW Rösler, M Bickle, GU Höglinger Protective efficacy of phosphodiesterase-1 inhibition against alpha-synuclein toxicity revealed by compound screening in LUHMES cells Sci Rep, 2017;7(1):11469. 2017 [PMID: 28904388] (Bioassay, Human) Bioassay Human
J Liu, D Shang, Y Xiao, P Zhong, H Cheng, R Zhou Isolation and characterization of string-forming female germline stem cells from ovaries of neonatal mice J. Biol. Chem., 2017;0(0):. 2017 [PMID: 28827310] (Bioassay, Mouse) Bioassay Mouse
J Drouin-Oue, S Lau, PL Brattås, D Rylander O, K Pircs, DA Grassi, LM Collins, R Vuono, A Andersson, G Westergren, C Graff, L Minthon, H Toresson, RA Barker, J Jakobsson, M Parmar REST suppression mediates neural conversion of adult human fibroblasts via microRNA-dependent and -independent pathways EMBO Mol Med, 2017;9(8):1117-1131. 2017 [PMID: 28646119] (Bioassay, Human) Bioassay Human
Show All 59 Publications.

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Bioinformatics

Gene Symbol GDNF
Entrez
Uniprot