Recombinant Human GDNF Protein

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Recombinant Human GDNF (Catalog # 212‑GD) induces SH-SY5Yhuman neuroblastoma cell proliferation in the presence of RecombinantHuman GFR alpha ‑1 Fc Chimera (Catalog # 714‑GR). The ED50 for this effectis ...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

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Recombinant Human GDNF Protein 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 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 with BSA as a carrier protein.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Notes

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

Alternate Names for Recombinant Human GDNF Protein

  • 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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212-GD
Species: Hu
Applications: Binding Activity, Bioactivity

Publications for GDNF (212-GD)(75)

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.


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Bioassay
(70)
Cell Culture Substrate
(1)
ELISA capture
(1)
In Vivo
(2)
Surface Plasmon Resonance
(1)
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Human
(54)
Mouse
(9)
Rat
(3)
Bacteria
(1)
Chicken
(2)
Guinea Pig
(1)
Porcine
(2)
Rabbit
(1)
Synthetic
(1)
All Species
Showing Publications 1 - 10 of 75. Show All 75 Publications.
Publications using 212-GD Applications Species
K Kirino, T Nakahata, T Taguchi, MK Saito Efficient derivation of sympathetic neurons from human pluripotent stem cells with a defined condition Sci Rep, 2018;8(1):12865. 2018 [PMID: 30150715] (Bioassay, Human) Bioassay Human
K Fujimori, M Ishikawa, A Otomo, N Atsuta, R Nakamura, T Akiyama, S Hadano, M Aoki, H Saya, G Sobue, H Okano Modeling sporadic ALS in iPSC-derived motor neurons identifies a potential therapeutic agent Nat. Med., 2018;0(0):. 2018 [PMID: 30127392] (Bioassay, Human) Bioassay Human
S Koyuncu, I Saez, HJ Lee, R Gutierrez-, W Pokrzywa, A Fatima, T Hoppe, D Vilchez The ubiquitin ligase UBR5 suppresses proteostasis collapse in pluripotent stem cells from Huntington&#039;s disease patients Nat Commun, 2018;9(1):2886. 2018 [PMID: 30038412] (Bioassay, Human) Bioassay Human
N Tsuburaya, K Homma, T Higuchi, A Balia, H Yamakoshi, N Shibata, S Nakamura, H Nakagawa, SI Ikeda, N Umezawa, N Kato, S Yokoshima, M Shibuya, M Shimonishi, H Kojima, T Okabe, T Nagano, I Naguro, K Imamura, H Inoue, T Fujisawa, H Ichijo A small-molecule inhibitor of SOD1-Derlin-1 interaction ameliorates pathology in an ALS mouse model Nat Commun, 2018;9(1):2668. 2018 [PMID: 29991716] (Bioassay, Human) Bioassay Human
Y Yehuda, B Blumenfeld, N Mayorek, K Makedonski, O Vardi, L Cohen-Dani, Y Mansour, S Baror-Sebb, H Masika, M Farago, M Berger, S Carmi, Y Buganim, A Koren, I Simon Germline DNA replication timing shapes mammalian genome composition Nucleic Acids Res., 2018;0(0):. 2018 [PMID: 29986092] (Bioassay, Mouse) Bioassay Mouse
G Collo, L Cavalleri, M Zoli, U Maskos, E Ratti, E Merlo Pich Alpha6-Containing Nicotinic Acetylcholine Receptors Mediate Nicotine-Induced Structural Plasticity in Mouse and Human iPSC-Derived Dopaminergic Neurons Front Pharmacol, 2018;9(0):572. 2018 [PMID: 29910731] (Bioassay, Human) Bioassay Human
R Nehme, E Zuccaro, SD Ghosh, C Li, JL Sherwood, O Pietilaine, LE Barrett, F Limone, KA Worringer, S Kommineni, Y Zang, D Cacchiarel, A Meissner, R Adolfsson, S Haggarty, J Madison, M Muller, P Arlotta, Z Fu, G Feng, K Eggan Combining NGN2 Programming with Developmental Patterning Generates Human Excitatory Neurons with NMDAR-Mediated Synaptic Transmission Cell Rep, 2018;23(8):2509-2523. 2018 [PMID: 29791859] (Bioassay, Human) Bioassay Human
K Kakiuchi, K Taniguchi, H Kubota Conserved and non-conserved characteristics of porcine glial cell line-derived neurotrophic factor expressed in the testis Sci Rep, 2018;8(1):7656. 2018 [PMID: 29769589] (Bioassay, Mouse) Bioassay Mouse
MJ Ziller, JA Ortega, KA Quinlan, DP Santos, H Gu, EJ Martin, C Galonska, R Pop, S Maidl, A Di Pardo, M Huang, HY Meltzer, A Gnirke, CJ Heckman, A Meissner, E Kiskinis Dissecting the Functional Consequences of De Novo DNA Methylation Dynamics in Human Motor Neuron Differentiation and Physiology Cell Stem Cell, 2018;0(0):. 2018 [PMID: 29551301] (Bioassay, Human) Bioassay Human
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
Show All 75 Publications.

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Blogs on GDNF.

The identification of dopaminergic neurons using Tyrosine Hydroxylase in Parkinson's research and LRRK2
Tyrosine hydroxylase (TH) is a crucial enzyme involved in the biosynthesis of dopamine, norepinephrine and epinephrine in the brain.  Specifically, TH catalyzes the conversion of l-tyrosine to l-dihydroxyphenylalanine (l-dopa).  The importance of t...  Read full blog post.

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Bioinformatics

Gene Symbol GDNF
Entrez
Uniprot