Recombinant Human Growth Hormone R (GHR) Fc Chimera, CF
Recombinant Human Growth Hormone R (GHR) Fc Chimera, CF Summary
Product Specifications
| Human GHR (Ala27-Tyr264) Accession # P10912 |
IEGRMD | Human IgG1 (Pro100-Lys330) |
| N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
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.
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.
1210-GR
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
| Shipping | The product is shipped at ambient temperature. 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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Reconstitution Calculator
Background: Growth Hormone R/GHR
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).
- Goffin, V. et al. (1996) Endocrine Rev. 17:385.
- Le Roith, D. et al. (2001) Endocrine Rev. 22:53.
- Clark, R. (1997) Endocr. Rev. 18:157.
- Welniak, L.A. et al. (2002) J. Leukoc. Biol. 71:381.
- Leung, D.W. et al. (1987) Nature 330:537.
- Stallings-Mann, J.L. et al. (1996) Proc. Nat. Acad. Sci. 93:12394.
- Amit, T. et al. (1997) Endocr. Metab. 82:3813.
- Ross, R.J.M., et al. (1997) Molecular Endocrinology 11:265.
- Carter-Su, C. et al. (1996) Annu. Rev. Physiol. 58:187.
- Postel-Vinay, M.C. and J. Finidori (1995) Eur. J. Endocrinol. 133:654.
Citation for Recombinant Human Growth Hormone R (GHR) Fc Chimera, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
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Highly efficient ribosome display selection by use of purified components for in vitro translation.
Authors: Villemagne D, Jackson R, Douthwaite JA
J. Immunol. Methods, 2006-05-11;313(1):140-8.
Species: Human
Sample Types: Recombinant Protein
Applications: Bioassay
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Average Rating: 4.5 (Based on 2 Reviews)
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Reason for Rating: Works consistently well for our binding assay.
