Growth Hormone Releasing Factor, GRF (1-29), amide, human
This hypophysiotropic peptide was isolated from human hypothalamic-hypophysial tissues. Within this 1 to 29 amino acid GRF fragment, amino acids 13 to 21 are more important than 24 to 29 for high affinity receptor binding. Structure–activity studies show that hpGRF(1–29)-NH2 has full intrinsic activity and potency in vitro as the full length GRF in stimulating growth hormone release. Human GRF (1-29) has a high degree (>93%) homology with procine, bovine and ovine GRF (1-29)-NH2.
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Proteins & Peptides
-20°C
Peak Area by HPLC ≥95%
3357.9
Ling, N. et al. Proc Natl Acad Sci USA 81, 4302 (1984)Gaudreau, P. et al. J Med Chem 35, 1864 (1992), doi: 10.1021/jm00088a023 Lance, VA. et al. Biochem Biophys Res Commun 119, 265 (1984), doi: 10.1016/0006-291X(84)91647-4 Lapierre, H. et al. Domest Anim Endocrinol 4, 207 (1987) Mayo, KE. et al. Nature 306, 86 (1983)Rivier, J. et al. Nature 300, 276 (1982), doi:10.1038/300276a0Grossman, A. et al. Clin Endocrinol (Oxf) 21, 321 (1984)
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