Sermorelin

Sermorelin is a synthetic peptide corresponding to the first 29 amino acids of human growth hormone-releasing hormone (GHRH 1-29). In preclinical research it has been examined as the minimal GHRH fragment that retains GHRH receptor binding activity comparable to the full-length 44-amino-acid peptide.

Sermorelin emerged from research in the late 1970s and early 1980s, when scientists were working to characterize how the hypothalamus controls growth hormone release. The pivotal discovery came in 1982 when Roger Guillemin's team at the Salk Institute in California isolated and characterized the structure of growth hormone-releasing hormone from pancreatic tumors.

Researchers determined that the first 29 amino acids of the 44-amino-acid GHRH molecule retained full in vitro receptor binding activity. This truncated version, named Sermorelin (or GHRH 1-29), became a common research tool because it was easier and more economical to synthesize while preserving the receptor-binding and signaling properties observed for full-length GHRH.

Sermorelin was among the first GHRH analogs extensively studied in preclinical research settings during the 1990s. Its relatively short half-life has made it useful in investigations of pulsatile GH release patterns, and it has appeared in peer-reviewed publications examining the GHRH axis in preclinical models. This product is intended for research use only.

Research peptides are supplied lyophilized (freeze-dried) . Keep sealed vials cool, dry, and protected from light until reconstitution.

After reconstitution, refrigerate prepared solutions and use sterile technique. For general laboratory diluent and handling notes, see lyophilized peptide reconstitution .