Recombinant Human Growth Hormone R (GHR) Fc Chimera, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Growth Hormone R (GHR) Fc Chimera, CF Summary

Details of Functionality
Measured by its ability to inhibit GH-induced proliferation of Nb2‑11 rat lymphoma cells. Gout, P.W. et al. (1980) Cancer Res. 40:2433. The ED50 for this effect is 0.4-2.0 ng/mL in the presence of 0.2 ng/mL of rhGH.
Source
Mouse myeloma cell line, NS0-derived human Growth Hormone R/GHR protein
Human GHR
(Ala27-Tyr264)
Accession # P10912
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Ala27
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
GHR
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
54 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.
SDS-PAGE
75-90 kDa, reducing conditions
Publications
Read Publication using
1210-GR 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
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
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 Growth Hormone R (GHR) Fc Chimera, CF

  • GH receptor
  • GHBP
  • GHR
  • growth hormone binding protein
  • Growth Hormone R
  • growth hormone receptor
  • serum binding protein
  • Somatotropin receptor

Background

Growth hormone (GH), also known as somatotropin, is a member of a family of growth factors that includes prolactin, placental lactogens, proliferins and somatolactin (1, 2). It is synthesized primarily by somatotropes in the anterior pituitary and is released as an endocrine hormone. Other cells and tissues, including lymphoid tissues, can also produce GH (3). GH is a pleiotropic molecule which can act directly or indirectly via IGF-I, to regulate growth and metabolism as well as enhance T cell survival and thymic functions (1, 2, 4). GH exerts its biological actions by binding to the GH receptor (GHR) that is present in many cell types (1, 2). Human GHR cDNA encodes a 638 amino acid (aa) residue type I transmembrane protein with an 18 aa putative signal peptide, a 246 aa extracellular domain, a 24 aa transmembrane domain and a 350 aa cytoplasmic domain (5). At least two alternatively spliced isoforms of human GHR, lacking the sequence encoded by exon 3, or lacking most of the cytoplasmic domain, also exist (6, 7). Soluble GH-binding proteins corresponding to extracellular domain of the transmembrane proteins can be generated from the membrane proteins (8). Ligation of GHR by GH has been shown to result in receptor dimerization and activation of the JAK/STAT signaling cascade (9). The soluble GHBP has been shown to interfere with GH signaling by competing with the transmembrane receptor of GH. Alternatively, the GHBP has also been shown to enhance GH action by slowing GH clearance (8, 10).

  1. Goffin, V. et al. (1996) Endocrine Rev. 17:385.
  2. Le Roith, D. et al. (2001) Endocrine Rev. 22:53.
  3. Clark, R. (1997) Endocr. Rev. 18:157.
  4. Welniak, L.A. et al. (2002) J. Leukoc. Biol. 71:381.
  5. Leung, D.W. et al. (1987) Nature 330:537.
  6. Stallings-Mann, J.L. et al. (1996) Proc. Nat. Acad. Sci. 93:12394.
  7. Amit, T. et al. (1997) Endocr. Metab. 82:3813.
  8. Ross, R.J.M., et al. (1997) Molecular Endocrinology 11:265.
  9. Carter-Su, C. et al. (1996) Annu. Rev. Physiol. 58:187.
  10. Postel-Vinay, M.C. and J. Finidori (1995) Eur. J. Endocrinol. 133:654.

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1210-GR
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Publications for Growth Hormone R (1210-GR)(1)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Affinity Chromatography.


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Bioinformatics

Gene Symbol GHR
Uniprot