Recombinant Human Growth Hormone 2 Protein, CF Summary
Details of Functionality |
Measured in a cell proliferation assay using Nb2‑11 rat lymphoma cells. Gout, P.W. et al. (1980) Cancer Res. 40:2433. The ED50 for this effect is 0.2-1.2 ng/mL. |
Source |
E. coli-derived human Growth Hormone 2 protein Phe27-Phe217, with an N-terminal Met |
Accession # |
|
N-terminal Sequence |
Met |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
GH2 |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Endotoxin Note |
<1.0 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
22.4 kDa. 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 |
20 kDa, reducing conditions |
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 HCl. |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions |
Reconstitute at 200 μg/mL in 4 mM HCl. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Growth Hormone 2 Protein, CF
Background
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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