Ipamorelin (5mg)

Ipamorelin Research Background

Ipamorelin is a synthetic pentapeptide (Aib-His-D-2-Nal-D-Phe-Lys-NH2) supplied here as a 5 mg lyophilized reference material for in-vitro and preclinical laboratory work. It carries the molecular formula C38H49N9O5 and CAS number 170851-70-4. Structurally it is a short, sequence-defined amidated peptide built partly from non-natural residues — the alpha-aminoisobutyric acid (Aib) cap and the D-configured 2-naphthylalanine and phenylalanine — which distinguish it from a simple linear chain of proteinogenic amino acids. In the research literature Ipamorelin is classified as a growth-hormone secretagogue and is frequently described as one of the more receptor-selective members of that peptide family, which is why it recurs as a comparator compound in mechanistic studies.

Interest in Ipamorelin as a research substance centers on its reported selectivity at the growth-hormone secretagogue receptor (GHSR-1a, the ghrelin receptor) in cell-based systems. It is used on the bench as a tool compound for probing this receptor and associated signaling readouts. The compound has no established consumer application; the surrounding body of work is preliminary and ongoing, and results from receptor assays and rodent-model experiments should not be extrapolated to human or animal outcomes.

What Has Been Studied in Preclinical Models

Published investigations involving Ipamorelin are predominantly in-vitro and rodent-model in nature. Reported experimental lines of inquiry include GHSR-1a receptor-binding and functional-activation assays, comparisons of secretagogue selectivity against related peptides, and measurement of downstream signaling endpoints in cultured pituitary-derived cells. Researchers have also used the peptide in isolated-tissue and rodent-model preparations to characterize dose-response behavior and receptor pharmacology under controlled laboratory conditions.

• Receptor-level assays characterizing binding and functional activation at the ghrelin/GHSR-1a receptor in transfected or pituitary-derived cell lines.
• Comparative selectivity studies against other growth-hormone secretagogue peptides in vitro.
• Rodent-model and isolated-tissue preparations examining secretagogue pharmacology and dose-response relationships.
• Stability and identity assays used to characterize the pentapeptide's behavior in solution.

Analytical Characterization

Each research lot of Ipamorelin is supplied as a lyophilized white powder and characterized before release. Identity and purity are established using orthogonal analytical methods so that the material described on the Certificate of Analysis (COA) matches the sequence and mass expected for this amidated pentapeptide. This dual-method approach separates purity — how much of the sample is the target peptide — from identity, the confirmation that the target is the correct molecule.

• RP-HPLC purity: quantified by peak-area integration and reported on the COA (≥99% for this product). The chromatogram resolves the main peak from process-related impurities and truncated sequences.
• Mass-spectrometry identity: ESI-MS or MALDI-TOF confirms the observed mass against the theoretical value for C38H49N9O5, verifying molecular identity of the pentapeptide.
• Supporting data: appearance, net peptide content, and residual-solvent or water-content checks where applicable.

The COA accompanying each product is the definitive analytical record for that specific lot. Because purity and mass can vary slightly between synthesis batches, researchers should reference the COA tied to the lot number received rather than generic specifications when documenting experimental inputs. Retaining the COA alongside experimental records supports reproducibility and traceability across studies.

Laboratory Handling of Lyophilized Material

As a lyophilized peptide, Ipamorelin is hygroscopic and sensitive to repeated temperature cycling. Standard laboratory practice is to allow the sealed vial to equilibrate to room temperature before opening to minimize condensation, then reconstitute with an appropriate research-grade solvent under aseptic technique. Aliquoting reconstituted stock into single-use portions limits the freeze-thaw cycles that can degrade peptide integrity. Detailed temperature and stability windows for lyophilized, reconstituted, and working solutions appear in the storage table on this page. This handling guidance applies to laboratory storage only and does not imply any human or animal application.