Recombinant Rat Growth Hormone R/GHR Fc Chimera (Catalog # 1211-GR)
Perfusion fixed frozen sections of rat thymus
Measured by its ability to neutralize Growth Hormone R/GHR-mediated inhibition of proliferation in the Nb2‑11 rat lymphoma cell line. The Neutralization Dose (ND50) is typically 0.075-0.3 µg/mL in the presence of 10 ng/mL Recombinant Rat Growth Hormone R/GHR Fc Chimera and 0.2 ng/mL Recombinant Human Growth Hormone.
Please Note: Optimal dilutions should be determined by each laboratory for each application.
are available in the Technical Information section on our website.
Growth Hormone R/GHR Inhibition of Growth Hormone-dependent Cell Proliferation and Neutralization by Rat Growth Hormone R/GHR Antibody.
Recombinant Rat Growth Hormone R/GHR Fc Chimera (Catalog # 1211‑GR) inhibits Recombinant Human Growth Hormone (Catalog # 1067‑GH) induced proliferation in the Nb2‑11 rat lymphoma cell line in a dose-dependent manner (orange line). Inhibition of Recombinant Human Growth Hormone (0.2 ng/mL) activity elicited by Recombinant Rat Growth Hormone R/GHR Fc Chimera (10 ng/mL) is neutralized (green line) by increasing concentrations of Goat Anti-Rat Growth Hormone R/GHR Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1211). The ND50 is typically 0.075‑0.3 µg/mL.
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
Reconstitution Buffer Available
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & 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.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
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). Rat GHR cDNA encodes a 638 amino acid (aa) residue type I transmembrane protein with a 18 aa signal peptide, a 247 aa extracellular domain, a 24 aa transmembrane domain and a 349 aa cytoplasmic domain. An alternatively spliced 297 aa isoform of rat GHR also exists. This 279 aa variant corresponds to the serum GH-binding protein and is identical in sequence to the extracellular domain of the transmembrane protein up to Glu262 (5). Ligation of GHR by GH has been shown to result in receptor dimerization and activation of the JAK/STAT signaling cascade (6). 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 (5, 7).
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Clark, R. (1997) Endocr. Rev. 18:157.
Welniak, L.A. et al. (2002)J. Leukoc. Biol. 71:381.
Postel-Vinay, M.C. and J. Finidori (1995) Eur. J. Endocrinol. 133:654.
Carter-Su, C. et al. (1996) Annu. Rev. Physiol. 58:187.
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