Sermorelin is the synthetic 29-residue C-terminally amidated peptide corresponding to the N-terminal fragment GHRH(1-29) of human growth-hormone-releasing hormone, the 44-residue hypothalamic peptide first isolated and sequenced in 1982. All residues are natural L-amino acids and the sequence is unmodified, which makes it the reference compound against which substituted GRF(1-29) analogs are compared.

The GHRH(1-29) amide retains the reported receptor-binding determinants of the full-length hormone and is described as an agonist at the class B G-protein-coupled GHRH receptor (GHRHR), which couples through Gs to adenylyl cyclase; cryo-EM structures of the activated receptor have since been reported. Plasma incubation studies describe rapid cleavage between residues 2 and 3 by dipeptidyl peptidase-IV.

Cited in GPCR structural biology and receptor-binding pharmacology, pituitary somatotroph cell models, peptide structure-activity series and analytical chemistry. Supplied as a lyophilized solid.

Research use only. This material is sold for in-vitro laboratory research and development purposes exclusively. It is not a drug, food, or dietary supplement, has not been evaluated by the FDA, and must not be used in humans or animals.