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Recombinant Human Ret Fc Chimera Protein, CF

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When Recombinant Human Ret Fc Chimera (Catalog # 9986-CR) isimmobilized at 1 µg/mL, Recombinant Human GDNF (Catalog # 212-GD) binds with anED50 of 0.02-0.12 μg/mL in the presence of Recombinant Human GFR ...read more
2 μg/lane of Recombinant Human Ret Fc Chimera was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 120-140 kDa and 240-280 kDa, ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human Ret Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human Ret Fc Chimera is immobilized at 1 µg/mL (100 µL/well), Recombinant Human GDNF (Catalog # 212-GD) binds with an ED50 of 0.02-0.12 μg/mL in the presence of Recombinant Human GFR alpha ‑1/GDNF R alpha ‑1 Fc Chimera (Catalog # 714-GR).
Source
Mouse myeloma cell line, NS0-derived human Ret protein
Human Ret
(Leu29-Arg635)
Accession # P07949
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Leu29
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
94 kDa.
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.
SDS-PAGE
120 - 140 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human Ret Fc Chimera Protein, CF

  • CDHF12MTC1
  • CDHR16
  • EC 2.7.10
  • Hirschsprung disease 1
  • Hirschsprung disease)
  • MEN2A
  • MEN2B
  • multiple endocrine neoplasia and medullary thyroid carcinoma 1
  • ret proto-oncogene
  • RET transforming sequence
  • Ret

Background

The GDNF family of neurotrophic factors forms a subfamily within the TGF-beta superfamily. These proteins are potent survival factors for various central and peripheral neurons during development and in the adult animal. The GDNF family members (GDNF, Neurturin, Artemin and Persephin) signal through multicomponent receptors that consist of the Ret receptor tyrosine kinase and one of four glycosyl-phosphatidylinositol (GPI)-linked ligand-binding subunits (GFR alpha -1-4). GFR alpha -1 -2, -3 and -4 are the preferred ligand-binding subunits for GDNF, Neurturin, Artemin and Persephin, respectively. The Ret tyrosine-kinase receptor is encoded by the c-ret proto-oncogene. Mutations of the Ret gene have been associated with various human diseases affecting tissues derived from the neural crest, including Hirschsprung's disease, multiple endocrine neoplasia MEN2A and MEN2B, and familial medullary thyroid carcinoma. Human and mouse Ret share 83% amino acid sequence homology (77% homology in the extracellular domain and 93% homology in the cytoplasmic domain). Although Ret does not bind GDNF ligands directly, the extracellular domain of Ret binds the GDNF-GFR-alpha complex with high affinity and is a potent GDNF antagonist in the presence of soluble GFR-alpha (1-4).
  1. Trupp, M. et al. (1998) Mol. Cell. Neurosci. 11:47.
  2. Enokido, Y. et al. (1998) Curr. Biol. 8:1019.
  3. Carlomagno, F. et al. (1998) Endocrinology 139:3613.
  4. Baloh, R. et al. (1998) Neuron 21:1291.

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