Recombinant Human Growth Hormone 2 Protein Summary
Product Specifications
Phe27-Phe217, with an N-terminal Met
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.
7668-GH
| Formulation | Lyophilized from a 0.2 μm filtered solution in HCl with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 200 μg/mL in 4 mM HCl containing at least 0.1% human or bovine serum albumin. |
| 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.
|
7668-GH/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in HCl. |
| Reconstitution | Reconstitute at 200 μg/mL in 4 mM HCl. |
| 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.
|
Reconstitution Calculator
Background: Growth Hormone 2
Growth Hormone 2 (GH2), also known as Growth Hormone Variant (GH‑V) and Placental Growth Hormone (PGH), is a secreted 22 kDa glycoprotein in the Placental Lactogen/Prolactin peptide hormone family. GH2 shares considerable structural and functional similarity with the pituitary‑derived Growth Hormone (GH) (1‑3). Mouse and rat orthologs of GH2 have not been identified, but human GH2 is bioactive in mice as well as rats (4, 5). Alternative splicing of human GH2 generates a 20 kDa isoform with a deletion of amino acids 32‑46 and isoforms with substituted C‑terminal regions (3, 6). GH2 is secreted by placental syncytiotrophoblasts into the maternal circulation beginning early in gestation and rising throughout pregnancy, as the level of circulating GH concommitantly decreases (1, 3, 7). GH2 is also present at lower concentrations in the fetal circulation and amniotic fluid (8‑10). It is elevated in the amniotic fluid of Down syndrome pregnancies, and maternal and fetal circulating levels may be either elevated or depressed during pre‑eclampsia (10‑12). Like GH, GH2 exerts its activities through the Growth Hormone Receptor (GHR) (13). It promotes trophoblast invasion of the uterine wall and the secretion of maternal IGF‑I (14, 15). Maternal serum levels of GH2 positively correlate with IGF‑I during the third trimester and with fetal birthweight (7, 16). GH2 induces maternal insulin resistance and exerts both somitogenic and anti‑lipogenic activities (4, 5, 13). The 20 kDa isoform of GH2 also binds GHR and shows full anti‑lipogenic activity, reduced somitogenic activity, and reduced diabetogenic activity (5, 13).
- McIntyre, H.D. et al. (2009) Curr. Diabetes Rev. 5:185.
- Igout, A. et al. (1988) Arch. Int. Physiol. Biochim. 96:63.
- Cooke, N.E. et al. (1988) J. Biol. Chem. 263:9001.
- Barbour, L.A. et al. (2002) Am. J. Obstet. Gynecol. 186:512.
- Vickers, M.H. et al. (2009) Am. J. Physiol. Endocrinol. Metab. 297:E629.
- Boguszewski, C.L. et al. (1988) J. Clin. Endocrinol. Metab. 83:2878.
- Fuglsang, J. et al. (2003) J. Clin. Endocrinol. 88:4355.
- Higgins, M.F. et al. (2012) PLoS ONE 7:e29164.
- Mittal, P. et al. (2008) Growth Horm. IGF Res. 18:174.
- Mittal, P. et al. (2007) J. Matern. Fetal Neonatal Med. 20:651.
- Sifakis, S. et al. (2009) Growth Horm. IGF Res. 19:121.
- Mannik, J. et al. (2012) Mol. Cell. Endocrinol. 355:180.
- Solomon, G. et al. (2006) Growth Horm. IGF Res. 16:297.
- Lacroix, M.C. et al. (2005) Endocrinology 146:2434.
- Caufriez, A. et al. (1993) Am. J. Physiol. 265:E572.
- Mannik, J. et al. (2010) J. Clin. Endocrinol. Metab. 95:2433.
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