Recombinant Rat Growth Hormone R (GHR) Fc Chimera, CF
Recombinant Rat Growth Hormone R (GHR) Fc Chimera, CF Summary
Product Specifications
| Rat GHR (Phe19 - Arg265) Accession # P16310 |
RIEGRMD | 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.
1211-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). 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).
- 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.
- Postel-Vinay, M.C. and J. Finidori (1995) Eur. J. Endocrinol. 133:654.
- Carter-Su, C. et al. (1996) Annu. Rev. Physiol. 58:187.
- Frick, G.P. et al. (1998) Endocrinology 139:2824.
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